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Gene therapy, regulatory mechanisms, and protein function in vision

Published online by Cambridge University Press:  04 February 2010

James F. McGinnis
James F. McGinnis*
Affiliation:
Department of Anatomy and Cell Biology, University of California, Los Angeles, Los Angeles, CA 90024. ianwjfm@mvs.oac.ucla.edu
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Abstract

Hereditary retinal degeneration due to mutations in visual genes may be amenable to therapeutic interventions that modulate, either positively or negatively, the amount of protein product. Some of the proteins involved in phototransduction are rapidly moved by a lightdependent mechanism between the inner segment and the outer segment in rod photoreceptor cells, and this phenomenon is important in phototransduction.

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Behavioral and Brain Sciences , Volume 18 , Special Issue 3: An International Journal of Current Research and Theory with Open Peer Commentary , September 1995, pp. 481 - 482
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Copyright © Cambridge University Press 1995

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References

Abeliovich, A., Chen, C., Goda, Y., Silva, A. J., Stevens, C. F. & Tonegawa, S. (1993a) Modified hippocampal long term potentiation in PKC-gamma mutant mice. Cell 75: 1253–62. [aZX]10.1016/0092-8674(93)90613-UCrossRefGoogle ScholarPubMed
Abeliovich, A., Paylor, R., Chen, C., Kim, J. J., Wehner, J. M. & Tonegawa, S. (1993b) PKC gamma mutant mice exhibit mild deficits in spatial and contextual learning. Cell 75: 1263–71. [aZX]10.1016/0092-8674(93)90614-VCrossRefGoogle ScholarPubMed
Abrams, T. W. (1985) Activity-dependent presynaptic facilitation: An associative mechanism in Aplysia. Cellular and Molecular Neurobiology 5: 123–45. [TWA]10.1007/BF00711089CrossRefGoogle ScholarPubMed
Abrams, T. W., Bernier, L., Hawkins, R. D. & Kandel, E. R. (1984) Possible roles of Ca2+ and cAMP in activity-dependent facilitation, a mechanism for associative learning in Aplysia. Society for Neuroscience Abstracts 10:269. [TWA]Google Scholar
Abrams, T. W. & Galun, J. (1993) Temporal aspects of activation of a Ca2+/CaM-sensitive adenylyl cyclase: Possible contribution to detection of CS-US pairing during conditioning. Society for Neuroscience Abstracts 19: 1065. [TWA]Google Scholar
Abrams, T. W., Jarrard, H. E. & Yovell, Y. (1994) Calcium accelerates adenylyl cyclase deactivation contributing to CS-US sequence requirement during conditioning in Aplysia. Submitted. [TWA]Google Scholar
Abrams, T. W. & Kandel, E. R. (1988) Is contiguity detection in classical conditioning a system or a cellular property? Learning in Aplysia suggests a possible molecular site. Trends in Neuroscience 11: 128–35. [TWA]10.1016/0166-2236(88)90137-3CrossRefGoogle ScholarPubMed
Abrams, T. W, Karl, K. A. & Kandel, E. R. (1991a) Biochemical studies of stimulus convergence during classical conditioning in Aplysia: Dual regulation of adenylate cyclase by Ca2+/calmodulin and transmitter. Journal of Neuroscience 11: 2655–65. [aZX, WH]10.1523/JNEUROSCI.11-09-02655.1991CrossRefGoogle ScholarPubMed
Adamus, G., Ortega, H., Witkowska, D. & Polans, A. (1994) Recovorin: A potent uveitogen for the induction of photoreceptor degeneration in Lewis rats. Experimental Eye Research 59: 447–56. [ASP]10.1006/exer.1994.1130CrossRefGoogle Scholar
Adamus, G., Zam, Z. S., Arendt, A., Palczewski, K., McDowell, J. H. & Hargrave, P. A. (1991) Anti-rhodopsin monoclonal antibodies of defined specificity: Characterization and application. Vision Research 31: 17–31 [aPAH]10.1016/0042-6989(91)90069-HCrossRefGoogle ScholarPubMed
Agranoff, B. W., Davis, R. E. & Brink, J. J. (1965) Memory fixation in the goldfish. Proceedings of the National Academy of Sciences USA 54: 788– 93. [EDR]10.1073/pnas.54.3.788CrossRefGoogle ScholarPubMed
Aguirre, G., Farber, D. Lolley, R., Fletcher, R. T. & Chader, C. (1978) Rodcone dysplasia in Irish setters: A defect in cyclic GMP metabolism in visual cells. Science 201: 1133–34. [MWK]10.1126/science.210508CrossRefGoogle Scholar
Ahlijanian, M. K., Halford, M. K. & Cooper, D. M. F. (1987) Ca2+/ calmodulin distinguishes between guanyl-5'-yl-imidodiphosphate- and opiate-mediated inhibition of rat striatal adenylate cyclase. Journal of Neurochemistry 49: 1308–15. [MMR]10.1111/j.1471-4159.1987.tb10025.xCrossRefGoogle ScholarPubMed
Ahmad, I., Korbmacher, C., Segal, A. S., Cheung, P., Boulpaep, E. L. & Barnstable, C. J. (1992) Mouse cortical collecting duct cells show nonselective cation channel activity and express a gene related to the cGMP-gated rod photorecoptor channel. Proceedings of the National Academy of Sciences USA 89: 10262–66. [aRSM]10.1073/pnas.89.21.10262CrossRefGoogle Scholar
Ahmad, I., Redmond, L. J. & Barnstable, C. J. (1990) Developmental and tissue-specific expression of rod photoreceptor cGMP-gated ion channel gene. Biochemical and Biophysical Research Communications 173:463–70. [aRSM]10.1016/S0006-291X(05)81081-2CrossRefGoogle ScholarPubMed
Akita, H., Tanis, S. P., Adams, M., Balogh-Nair, V. & Nakanishi, K. (1980) Nonbleachable rhodopsins retaining the full natural chromophore. Journal of the American Chemical Society 102: 6370–72. [aPAH]10.1021/ja00540a047CrossRefGoogle Scholar
Al-Maghtheh, A., Kim, R. Y., Inglehearn, C. & Bhattacharya, S. S. (1994a) A 150 bp insert in the rhodopsin gene of an autosomal dominant retinitis pigmentosa family. Human Molecular Cenetics 3: 205–6. [aSPD]10.1093/hmg/3.1.205CrossRefGoogle Scholar
Al-Maghtheh, M., Inglehearn, C. F., Keen, T. J., Evans, K., Moore, A. T., Jay, M., Bird, A. C. & Bhattacharya, S. S. (1994) Identification of a sixth locus for autosomal dominant retinitis pigmentosa on chromosome 19. Human Molecular Genetics 3: 351–54. [aSPD]10.1093/hmg/3.2.351CrossRefGoogle ScholarPubMed
Al-Maghtheh, M., Inglehearn, C., Lunt, P., Jay, M., Bird, A. & Bhattacharya, S. (1994) Two new rhodopsin transversion mutations (C40R; M216K) in families with autosomal dominant retinitis pigmentosa. Human Mutation 3: 409–10. [aSPD]10.1002/humu.1380030417CrossRefGoogle Scholar
Albert, A. D. & Litman, B. J. (1978) Independent structural domains in the membrane protein bovine rhodopsin. Biochemistry 17: 3893–3900. [ADA]10.1021/bi00612a001CrossRefGoogle ScholarPubMed
Alexander, K. A., Cimler, B. M., Meier, K. E. & Storm, D. R. (1987) Regulation of cahmodulin binding to P-57. Journal of Biological Chemistry 262: 6108–13. [aZX]10.1016/S0021-9258(18)45544-5CrossRefGoogle ScholarPubMed
Allen, J. P. & Feher, G. (1991). Crystallization of reaction centers from Rhodobacter sphaervides. In: Crystallization of membrane proteins, ed. Michel, H.. CRC Press. [aPAH]Google Scholar
Altenhnfen, W., Ludwig, J., Eismann, E., Kraus, W., Bönigk, W. & Kaupp, U. B. (1991) Control of ligand specificity in cyclic nucleotide-gated channels from rod photoreceptors and olfactory epithelium. Proceedings of the National Academy of Sciences USA 88: 9868–72. [aRSM]10.1073/pnas.88.21.9868CrossRefGoogle Scholar
Ames, J. B., Porumbo, T., Tanaka, T., Ikura, M. & Stryer, L. (1995) Aminoturminal myristoylation induces cooperative calcium binding to recoverin. Journal of Biological Chemistry 270: 4526–33. [rJBH]10.1074/jbc.270.9.4526CrossRefGoogle ScholarPubMed
Amos, L. A., Henderson, R. & Unwin, P. N. T. (1982) Three-dimensional structure determination by electron microscopy of 2-D crystals. Progress in Biophysics and Molecular Biology 39: 183–231. [aPAH]10.1016/0079-6107(83)90017-2CrossRefGoogle Scholar
Anant, J. S. & Fung, B. K.-K. (1992) In vivo farnesylation of rat rhodopsin kinase. Biochemical and Biophysical Research Communications 183: 468–73. [aMDB]10.1016/0006-291X(92)90505-FCrossRefGoogle ScholarPubMed
Anant, J. S., Ong, O. C, Xie, H., Clarke, S., O'Brien, P. J. & Fung, B. K.-K. (1992) In vivo differential prenylation of retinal cyclic GMP phosphodiesterase catalytic subunits. Journal of Biological Chemistry 267: 687–90. [aMDB]10.1016/S0021-9258(18)48336-6CrossRefGoogle ScholarPubMed
Andersson, L. & Porath, J. (1986) Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatography. Analytical Biochemistry 154: 250– 54. [aPAH]10.1016/0003-2697(86)90523-3CrossRefGoogle ScholarPubMed
Andrade, R. (1993) Neuron 10: 83–88. [MMR]10.1016/0896-6273(93)90244-LCrossRefGoogle Scholar
Andreasen, T. J., Luetje, C. W., Heideman, W. & Storm, D. R. (1983) Purification of a novel calmodulin binding protein from bovine cerebral cortex membranes. Biochemistry 22: 4615–18. [aZX]10.1021/bi00289a001CrossRefGoogle ScholarPubMed
Andréasson, S., Ehinger, B., Abrahamson, M. & Fex, G. (1992) A six-generation family with autosomal dominant retinitis pigmentosa and a rhodopsin gene mutation (arginine-135-leucine). Ophthalmic Pediatrics and Genetics 13: 145–53. [aSPD]10.3109/13816819209046483CrossRefGoogle Scholar
Angleson, J. K. & Wensel, T. G. (1993) A GTPase-accelerating factor for transducin, distinct from its effector cGMP phosphodiesterase, in rod outer segment membranes. Neuron 11: 939–49. [aMDB]10.1016/0896-6273(93)90123-9CrossRefGoogle ScholarPubMed
Angleson, J. K. & Wensel, T. G. (1994) Enhancement of rod outer segment GTPase accelerating protein activity by the inhibitory subunit of cGMP phosphodiesterase. Journal of Biological Chemistry 269: 16290–96. [arMDB]10.1016/S0021-9258(17)34006-1CrossRefGoogle ScholarPubMed
Antonny, B., Otto-Bruc, A., Chabre, M. & Minh Vuong, T. (1993) GTP hydrolysis by purified α-subunit of transducin and its complex with the cyclic GMP phosphodiesterase inhibitor. Biochemistry 32: 8646– 53. [arMDB, BMW]10.1021/bi00084a036CrossRefGoogle ScholarPubMed
Apel, E. D., Byford, M. F., Au, D., Walsh, K. A. & Storm, D. R. (1990) Identification of the protein kinase C phosphorylation site in neuromodulin. Biochemistry 29: 2330–35. [aZX]10.1021/bi00461a017CrossRefGoogle ScholarPubMed
Apfelstedt-Sylla, E., Kunisch, M., Horn, M., Ruther, K., Gal, A. & Zrenner, E. (1992) Diffuse loss of rod function in autosomal dominant retinitis pigmentosa with pro-347-leu mutation of rhodopsin. German Journal of Ophthalmology 1: 319–27. [aSPD]Google ScholarPubMed
Applebury, M. A. (1991) Molecular determinants of visual pigment function. Current Opinion in Neurobiology 1: 263–69. [aPAH]10.1016/0959-4388(91)90088-OCrossRefGoogle ScholarPubMed
Applebury, M. L. & Hargrave, P. A. (1986) Molecular biology of the visual pigments. Vision Research 26: 1881–95. [aPAH]10.1016/0042-6989(86)90115-XCrossRefGoogle ScholarPubMed
Arikawa, K., Molday, L. L., Molday, R. S. & Williams, D. (1992) Localization of peripherin/rds in the disk membranes of cone and rod photoreceptors: Relationship to disk membrane morphogenesis and retinal degeneration. Journal of Cell Biology 116: 659–67. [aSPD]10.1083/jcb.116.3.659CrossRefGoogle ScholarPubMed
Arnoux, B., Ducruix, A., Reiss-Husson, F., Lutz, M., Norris, J., Schiffer, M. & Chang, C. G. (1989) Structure of spheroidene in the photosynthetic reaction center from Y Rhodobacter sphaeroides . FEBS Letters 258: 47–50. [aPAH]10.1016/0014-5793(89)81612-6CrossRefGoogle ScholarPubMed
Arshavsky, V. Y., Antoch, M. P., Dizhoor, A. M., Rakhilin, S. V. & Philippov, P. P. (1987) Interaction of visual transduction enzymes in a detergent solution. In: Retinal proteins, ed. Ovchinnikov, Y. A.. Utrecht: VNU Science Press. [aMDB]Google Scholar
Arshavsky, V. Y., Antoch, M. P., Lukjanov, K. A. & Philippov, P. P. (1989) Transducin GTPase provides for rapid quenching of the cGMP cascade in rod outer segments. FEBS Letters 250: 353–56. [aMDB]10.1016/0014-5793(89)80754-9CrossRefGoogle ScholarPubMed
Arshavsky, V. Y. & Bownds, M. D. (1992) Regulation of deactivation of photoreceptor G protein by its target enzyme and cGMP. Nature 357: 416–17. [aMDB]10.1038/357416a0CrossRefGoogle ScholarPubMed
Arshavsky, V. Y., Dizhoor, A. M., Shestakova, I. K. & Philippov, P. P. (1985) The effect of rhodopsin phosphorylation on the light-dependent activation of phosphodiesterase from bovine rod outer segments. FEBS Letters 181: 264–66. [aMDB]10.1016/0014-5793(85)80272-6CrossRefGoogle ScholarPubMed
Arshavsky, V. Y., Dumke, C. L. & Bownds, M. D. (1992) Non-catalytic cGMP binding sites of amphibian rod cCMP phosphodiesterase control interaction with its inhibitory gamma-subunits—a putative regulatory mechanism of the rod photoresponse. Journal of Biological Chemistry 267: 24501–7. [aMDB]10.1016/S0021-9258(18)35793-4CrossRefGoogle Scholar
Arshavsky, V. Y., Dumke, C. L. & Bownds, M. D.(1995) Manuscript in preparation. [aMDB]Google Scholar
Arshavsky, V. Y., Dumke, C. L., Zhu, Y., Artemyev, N. O., Skiba, N. P., Hamm, H. E. & Bownds, M. D. (1994) Regulation of transducin GTPase activity in bovine rod outer segments. Journal of Biological Chemistry 269: 19882–87. [arMDB]10.1016/S0021-9258(17)32102-6CrossRefGoogle ScholarPubMed
Arshavsky, V. Y., Gray-Keller, M. P. & Bownds, M. D. (1991) cGMP suppresses GTPase activity of a portion of transducin equimolar to phosphodiesterase in frog rod outer segments. Light-induced cGMP decreases as a putative feedback mechanism of the photoresponse. Journal of Biological Chemistry 266: 18530–37. [aMDB]Google ScholarPubMed
Artlich, A., Horn, M., Lorenz, B., Bhattacharya, S. & Gal, A. (1992) Recurrent 3-bp deletion at codon 255/256 of the rhodopsin gene in a German pedigree with autosomal dominant retinitis pigmentosa. American Journal of Human Genetics 50: 876–78. [aSPD]Google Scholar
Aton, B. R., Litman, B. J. & Jackson, M. L. (1984) Isolation and Identification of the phosphorylated species of rhodopsin. Biochemistry 23: 1737– 41. [aPAH]10.1021/bi00303a024CrossRefGoogle ScholarPubMed
Bacskai, B. J., Hochner, B., Mahaut-Smith, M., Adams, S. R., Kaang, B. K., Kandel, E. R. & Tsien, R. Y. (1993) Spatially resolved dynamics of cAMP and protein kinase A subunits in Aplysia sensory neurons. Science 260: 222–26. [aZX]10.1126/science.7682336CrossRefGoogle ScholarPubMed
Baehr, W., Gorczyca, W., Subbaraya, I., Ohguro, H., Johnson, R. S., Walsh, K. A., Gray-Keller, M. P., Detwiler, P. B., Crabb, J. & Palezewski, K. (1994) Isolation, cloning, and functional characterization of bovine retina guanylate cyclase activating protein (GCAP). Investigative Ophthalmology and Visual Science 35: 1486. [aMDB]Google Scholar
Baehr, W., Morita, E. A., Swanson, R. J. & Applebury, M. L. (1982) Characterization of bovine rod outer segment G-protein. Journal of Biological Chemistry 257: 6452–60. [aMDB]10.1016/S0021-9258(20)65163-8CrossRefGoogle ScholarPubMed
Bakalyar, H. A. & Reed, R. R. (1990) Identification of a specialized adenylyl cyclase that may mediate odorant detection. Science 250: 1403–6. [aZX]10.1126/science.2255909CrossRefGoogle ScholarPubMed
Baldwin, J. M. (1993) The probable arrangement of the helices in G proteincoupled receptors. EM BO Journal 12: 1693–1703. [aSPD, SOS]Google Scholar
Baldwin, P. A. & Hubbell, W. L. (1985a) Effects of lipid environment on the light-induced conformational changes of rhodopsin: 1. Absence ofmetarhodopsin II production in dimyristoylphosphatidylcholine recombinant membranes. Biochemistry 24: 2624–32. [ADA]10.1021/bi00332a006CrossRefGoogle ScholarPubMed
Baldwin, P. A. & Hubbell, W. L. (1985b) Effects of lipid environment on the light-induced conformational changes of rhodopsin: 2. Roles of lipid chain length, unsaturation, and phase state. Biochemistry 24: 2633–39. [ADA]10.1021/bi00332a007CrossRefGoogle ScholarPubMed
Barker, D., Schafer, M. & White, R. (1984) Restriction sites containing CpG show a higher frequency of polymorphism in human DNA. Cell 6: 131– 38. [aSPD]10.1016/0092-8674(84)90081-3CrossRefGoogle Scholar
Bascom, R. A., Manara, S., Collins, L., Molday, R. S., Kalnins, V. I. & Mclnnes, R. R. (1992) Cloning of the cDNA for a novel photoreceptor membrane protein (rom-1) identifies a disk rim protein family implicated in human retinopathies. Neuron 8: 1171–84. [aSPD]10.1016/0896-6273(92)90137-3CrossRefGoogle ScholarPubMed
Baudier, J., Bronner, C., Kligman, D. & Cole, R. D. (1989) Protein kinase C substrates from bovine brain: Purification and characterization of neuromodulin, a neuron-specific calmodulin binding protein. Journal of Biological Chemistry 264: 1824–28. [EDR]10.1016/S0021-9258(18)94262-6CrossRefGoogle ScholarPubMed
Bauer, P. H., Müller, S., Puzicha, M., Pippig, S., Obermaier, B., Helmreich, E. J. M. & Lohse, M. J. (1992) Phosducin is a protein kinase A-regulated G-protein regulator. Nature 358: 73–76. [BMW]10.1038/358073a0CrossRefGoogle ScholarPubMed
Baumann, A., Frings, S., Godde, M., Seifert, R. & Kaupp, U. B. (1994) Primary structure and functional expression of a Drosphila cyclic nucleotide-gated channel present in eyes and antennae. EMBO Journal 13: 5040–50. [rRSM]10.1002/j.1460-2075.1994.tb06833.xCrossRefGoogle Scholar
Baylor, D. A. (1987) Photoreceptor signals and vision. Investigative Ophthalmology and Visual Science 28: 34–49. [aPAH]Google Scholar
Baylor, D. A. & Hodgkin, A. L. (1974) Changes in time scale and sensitivity in turtle photoreceptors. Journal of Physiology (London) 242: 729–58. [aMDB]10.1113/jphysiol.1974.sp010732CrossRefGoogle ScholarPubMed
Baylor, D. A., Lamb, T. D. & Yau, K.-W. (1979a) The membrane current of single rod outer semgments. Journal of Physiology (London) 288: 589–611. [aMDB]Google Scholar
Baylor, D. A., Lamb, T. D. & Yau, K.-W. (1979b) Responses of retinal rods to single photons. Journal of Physiology (London) 288: 613–34. [aMDB]Google ScholarPubMed
Baylor, D. A., Matthews, G. & Yau, K.-W. (1980) Two components of electrical dark noise in toad retinal rod outer segments. Journal of Physiology (London) 309: 591–621. [aMDB]10.1113/jphysiol.1980.sp013529CrossRefGoogle ScholarPubMed
Beaudet, A. L. & Tsui, L.-C. (1993) A suggested nomenclature for designating mutations. Human Mutation 2: 245–48. [aSPD]10.1002/humu.1380020402CrossRefGoogle ScholarPubMed
Bell, C., Converse, C. A., Collins, M. F., Esakowitz, L., Kelly, K. F. & Haites, N. E. (1992) Autosomal dominant retinitis pigmentosa (ADRP): A rhodopsin mutation in a Scottish family. Journal of Medical Genetics 29: 667–68. [aSPD]10.1136/jmg.29.9.667CrossRefGoogle Scholar
Bennett, A. E., Ok, J. H., Griffin, R. G. & Vega, S. (1992) Chemical shift correlation specetroscopy in rotating solids: Radio frequency-driven dipolar recoupling and logitudinal exchange. Journal of Chemical Physics 96: 8624–27. [SOS]10.1063/1.462267CrossRefGoogle Scholar
Bennett, N. & Clere, A. (1989) Activation of cGMP phosphodiesterase in retinal rods: Mechanism of interaction with the GTP-binding protein (transducin). Biochemistry 28: 7418–24. [aMDB]10.1021/bi00444a040CrossRefGoogle Scholar
Bennett, N. & Sitaramayya, A. (1988) Inactivation of photoexcited rhodopsin in retinal rods: The roles of rhodopsin kinase and 48-KDa protein(arrestin). Biochemistry 27: 1710–15. [aMDB]10.1021/bi00405a049CrossRefGoogle Scholar
Benowitz, L. I. & Routtenberg, A. (1987) A membrane phosphoprotein associated with neural development axonal regeneration, phospholipid metabolism, and synaptic plasticity. Trends in Neuroscience 10: 527– 32. [aZX]10.1016/0166-2236(87)90135-4CrossRefGoogle Scholar
Berson, E. L. (1993) Retinitis pigmentosa—The Friedenwald Lecture. Investigative Ophthamology and Visual Science 34: 1659–76. [aSPD, aPAH]Google Scholar
Berson, E. L., Rosner, B., Sandberg, M. A. & Dryja, T. P. (1991) Ocular findings in patients with autosomal dominant retinitis pigmentosa and a rhodopsin gene defect (Pro-23-His). Archives of Ophthalmology 109: 92–101. [aSPD]10.1001/archopht.1991.01080010094039CrossRefGoogle Scholar
Berson, E. L., Rosner, B., Sandberg, M. A., Weigel-DiFranco, C. & Dryja, T. P. (1991a) Ocular findings in patients with autosomal dominant retinitis pigmentosa and rhodopsin, Proline-347-Leucine. American Journal of Ophthalmology 111: 614–23. [aSPD]10.1016/S0002-9394(14)73708-0CrossRefGoogle ScholarPubMed
Berson, E. L., Sandberg, M. A. & Dryja, T. P. (1991b) Autosomal dominant retinitis pigmentosa with rhodopsin, valine-345-methionine. Transcripts of the American Ophthalmological Society 89: 117–30. [aSPD]Google ScholarPubMed
Bhattacharya, S. S., Ridge, K. D., Knox, B. E. & Khorana, H. G. (1992) Light-stable rhodopsin: 1. A rhodopsin analog reconstituted with a nonisomerizable ll-cis retinal derivative. Journal of Biological Chemistry 267: 6763–69. [aPAH]10.1016/S0021-9258(19)50491-4CrossRefGoogle ScholarPubMed
Bhattacharya, S. S., Wright, A. F., Clayton, J. F., Price, W. U., Phillips, C. I., McKeown, C. M. E., Jay, M., Bird, A. C, Pearson, P. L., Southern, E. M. & Evans, H. J. (1984) Close genetic linkage between X-linked retinitis pigmentosa and a restriction fragment length polymorphism identified by recombinant DNA probe Ll.28. Nature 309: 253–55. [aSPD]10.1038/309253a0CrossRefGoogle Scholar
Biel, M., Altenhofen, W., Hullin, R., Ludwig, J., Freichel, M., Flocherzi, V., Dascal, N., Kaupp, U. B. & Hofmann, F. (1993) Primary structure and functional expression of a cyclic nucleotide-gated channel from rabbit aorta. FEBS Letters 329: 134–38. [aRSM]10.1016/0014-5793(93)80209-DCrossRefGoogle ScholarPubMed
Biel, M., Zong, X., Distler, M., Bosse, R., Klugbauer, N., Murakami, M., Flockerzi, V. & Hoffmann, F. (1994) Another member of the cyclic nucleotide-gated channel family expressed in testis, kidney and heart. Proceedings of the National Academy of Sciences USA 91: 3505–9. [rRSM]10.1073/pnas.91.9.3505CrossRefGoogle Scholar
Biernbaum, M. S., Binder, B. M. & Bownds, M. D. (1991) Dim background light and Cerenkov radiation from 32P block reversal of rhodopsin phosphorylation in intact frog retinal rods. Visual Neuroscience 7: 499–503. [aMDB]10.1017/S0952523800009780CrossRefGoogle ScholarPubMed
Biernbaum, M. S. & Bownds, M. D. (1985) Light-induced changes in GTP and ATP in frog rod photoreeeptors: Comparison with recovery of dark current and light sensitivity during dark adaptation. Journal of General Physiology 85: 107–21. [aMDB]10.1085/jgp.85.1.107CrossRefGoogle ScholarPubMed
Binder, B. M., Biernbaum, M. S. & Bownds, M. D. (1990) Light activation of one rhodopsin molecule causes the phosphorylation of hundreds of others. A reaction observed in electropermeabilized frog rod outer segments exposed to dim illumination. Journal of Biological Chemistry 265: 15333–40. [aMDB]10.1016/S0021-9258(18)77260-8CrossRefGoogle ScholarPubMed
Binder, B. M., Brewer, E. & Bownds, M. D. (1989) Stimulation of protein phosphorylations in frog rod outer segments by protein kinase activators: Suppression of light-induced changes in membrane current and cGMP by protein kinase C activators. Journal of Biological Chemistry 264: 8857– 64. [aMDB]10.1016/S0021-9258(18)81872-5CrossRefGoogle ScholarPubMed
Bitensky, M. W, Wheeler, M. A., Yamazaki, A., Rasenick, M. M. & Stein, P. J. (1981) Cyclic nucleotide matabolism in vertebrate photoreceptors: A remarkable analogy and an unraveling enigma. Current Topics in Membrane Transportation 15: 237–71. [TGW]10.1016/S0070-2161(08)60505-5CrossRefGoogle Scholar
Blanton, S. H., Heckenlively, J. R., Cottingham, A. W, Friedman, J., Sadler, L. A., Wagner, M., Friedman, L. H. & Daiger, S. P. (1991) Linkage mapping of autosomal dominant retinitis pigmentosa (adRP) to the pericentric region of human chromosome 8. Genomics 11: 857–69. [aSPD]10.1016/0888-7543(91)90008-3CrossRefGoogle Scholar
Blatt, C., Eversole-Cire, P., Colin, V. H., Zollman, S. et al. (1988) Chromosomal localization of genes encoding guanine nuclcotide-binding protein subunits in mouse and human. Proceedings of the National Academy of Sciences USA 85: 7642–46. [aSPD]10.1073/pnas.85.20.7642CrossRefGoogle ScholarPubMed
Bodoia, R. D. & Detwiler, P. B. (1985) Patch-clamp recordings of the lightsensitive dark noise in retinal rods from the lizard and frog. Journal of Physiology 367: 183–216. [aRSM]CrossRefGoogle Scholar
Boekema, E. J., Van Heel, M. G. & Van Bruggen, E. F. J. (1986) Preparation of two-dimensional crystals of complex 1 and image analysis. Methods in Enzymology 126: 344–53. [aPAH]10.1016/S0076-6879(86)26034-6CrossRefGoogle Scholar
Boesze-Battaglia, K. & Albert, A. (1990) Cholesterol modulation of photoreceptor function in bovine rod outer segments. Journal of Biological Chemistry 265: 20727–30. [ADA]10.1016/S0021-9258(17)45275-6CrossRefGoogle Scholar
Bönigk, W., Altenhofen, W., Muller, F., Dose, A., Illing, M., Molday, R. S. & Kaupp, U. B. (1993) Rod and cone photoreceptor cells express distinct genes for cyclic GMP-gated channels. Neuron 10: 865–77. [aRSM]10.1016/0896-6273(93)90202-3CrossRefGoogle Scholar
Bornancin, F., Pfister, C. & Chabre, M. (1989) The transitory complex between photoexcited rhodopsin and transducin: Reciprocal interaction between the retinal site in rhodopsin and the nucleotide site in transducin. European Journal of Biochemistry 184: 687–98. [aPAH]10.1111/j.1432-1033.1989.tb15068.xCrossRefGoogle ScholarPubMed
Bourne, H. R. & Nicoll, R. (1993a) Molecular machines integrate coincident synaptic signals. Cell 72: 65–75. [aZX]10.1016/S0092-8674(05)80029-7CrossRefGoogle ScholarPubMed
Bourne, H. R. & Nicoll, R. (1993b) Molecular machines integrate coincident synaptic signals. Neuron 10(Suppl.):65–75. [TWA]Google Scholar
Bourne, H. R., Sanders, D. A. & McCormick, F. (1990) The GTPase superfamily: A conserved switch for diverse cell functions. Nature 348: 125–32. [aMDB]10.1038/348125a0CrossRefGoogle ScholarPubMed
Bourne, H. R., Sanders, D. A. & McCormick, F. (1991) The GTPase superfamily: Conserved structure and molecular mechanism. Nature 349: 117–27. [aMDB]10.1038/349117a0CrossRefGoogle ScholarPubMed
Bowes, C., Li, T., Danciger, M., Baxter, L. C, Applebury, M. L & Farber, D. B. (1990) Retinal degeneration in the rd mouse is caused by a defect in the β subunit of rod cGMP-phosphodiesterase. Nature 347: 677–80. [aSPD, MWK]10.1038/347677a0CrossRefGoogle ScholarPubMed
Bowes, C., Li, T., Frankel, W. N., Danciger, M., Coffin, J. M., Applebury, M. L. & Farber, D. B. (1993) Localization of a retroviral element within the rd gene coding for the beta subunit of cGMP phosphodiesterase. Proceedings of the National Academy of Sciences USA 90: 2955–59. [aSPD]10.1073/pnas.90.7.2955CrossRefGoogle ScholarPubMed
Bowie, J. U., Lüthy, R. & Eisenberg, D. (1991) A method to identify protein sequences that fold into a known three-dimensional structure. Science 253: 164–70. [RMC]10.1126/science.1853201CrossRefGoogle ScholarPubMed
Bownds, D., Dawes, J., Miller, J. & Stahlman, M. (1972) Phosphorylation of frog photoreceptor membranes induced by light. Nature New Biology 237: 125–27. [aMDB]10.1038/newbio237125a0CrossRefGoogle Scholar
Bownds, M. D., Arshavsky, V. Y., Calvert, P. D. & Dumke, C. I. (1992) Rod outer segment concentration and structure influence the apparent kinetics of cGMP phosphodiesterase. Investigative Ophthalmology and Visual Science 33: 873. [aMDB]Google Scholar
Bownds, M. D. & Thomson, D. (1988) Control of the sensitivity and kinetics of the vertebrate photoresponse during light adaptation—calculations from simple molecular models. In: Molecular physiology of retinal proteins, ed. Hara, T.. Osaka: Japan Scientific Society Press. [aMDB]Google Scholar
Bradley, J., Li, J., Davidson, N., Lester, H. A. & Zinn, K. (1994) Heteromeric olfactory cyclic nucleotide-gated channels: A subunit that confers increased sensitivity to cAMP. Proceedings of the National Academy of Sciences USA 91: 8890–94. [rRSM]10.1073/pnas.91.19.8890CrossRefGoogle Scholar
Brann, M. R. & Cohen, L. V. (1987) Diurnal expression of tranducin mRNA and translocation of transducin in rods of rat retina. Science 235: 585–88. [JFM]10.1126/science.3101175CrossRefGoogle Scholar
Breer, H. & Boekhoff, I. (1992) Second messenger signalling in olfaction. Current Opinion in Neurobiology 2: 439–43. [aMDB]10.1016/0959-4388(92)90177-MCrossRefGoogle ScholarPubMed
Bressler, N. M., Bressler, S. B. & Fine, S. L. (1988) Age-related macular degeneration. Survey of Ophthalmology 32: 375–413. [aSPD]10.1016/0039-6257(88)90052-5CrossRefGoogle ScholarPubMed
Brown, N. G., Fowles, C., Sharma, R. & Akhtar, M. (1993) Quantitative characterization of the structure of rhodopsin in disc membrane by means of Fourier transform infrared spectroscopy. Journal of Biological Chemistry 268: 2403–9. [ADA]Google Scholar
Brown, R. L., Bert, R. J., Evans, F. E. & Karpen, J. W. (1993) Activation of retinal rod cGMP-gated channels: What makes for an effective 8-snbstitutecl derivative of cGMP? Biochemistry 32: 10089–95. [RLB]10.1021/bi00089a026CrossRefGoogle ScholarPubMed
Brown, R. L., Cerber, W. V. & Karpen, J. W. (1993) Specific labeling and permanent activation of the retinal rod cGMP-activated channel by the photaffinity analog 8-p-azidophcnacylthio-cGMP. Proceedings of the National Academy of Sciences USA 90: 5369–73. [aRSM, RLB]10.1073/pnas.90.11.5369CrossRefGoogle Scholar
Brown, R. L., Cramling, R., Bert, R. J. & Karpen, J. W. (in press) Cyclic GMP contact points within the 63-kDa subunit and a 240-kDa associated protein of retinal rod cGMP-activated channels. Biochemistry. [RLB]Google Scholar
Brown, R. L. & Karpen, J. W. (1994) Dissecting the activation mechanism of retinal rod cGMP-gated channels using covalently tethered ligands. Biophysics Journal 66: A350. [RLB, TGW]Google Scholar
Buczylko, J., Gutmann, C. & Palezewski, K. (1991) Regulation of rhodopsin kinase by autophosphorylation. Proceedings of the National Academy of Sciences USA 88: 2568–72. [aMDB]10.1073/pnas.88.6.2568CrossRefGoogle ScholarPubMed
Bunge, S., Wedemann, H., David, D., Terwilliger, D. J., Van Den Bom, L. I., Aulehla-Scholz, C., Sammons, C., Horn, M., Ott, J., Schwinger, E., Schinzel, A., Denton, M. J. & Gal, A. (1993) Molecular analysis and genetic mapping of the retinitis pigmentosa gene in families with autosomal dominant retinitis pigmentosa. Genomics 17: 230–33. [aSPD]10.1006/geno.1993.1309CrossRefGoogle ScholarPubMed
Burks, C., Cinkosky, M. J., Fischer, W. M., Gilna, P., Hayden, J. E.-D., Keen, G. M., Kelly, M., Kristofferson, D. & Lawrence, J. (1992) GenBank. Nucleic Acids Research 20: 2065–69. [aSPD]10.1093/nar/20.suppl.2065CrossRefGoogle ScholarPubMed
Byrne, J. H. (1987) Presynaptic facilitation as a mechanism for behavioral sensitization in Aplysia. Physiology Review 67: 329–439. [aZX]10.1152/physrev.1987.67.2.329CrossRefGoogle Scholar
Cali, J. F., Zwaagstra, J. C., Mons, N., Cooper, D. M. F. & Krupinski, J. (1994) Type VIII adenylyl cyclase. Journal of Biological Chemistry 269: 12190–95. [aZX]10.1016/S0021-9258(17)32700-XCrossRefGoogle ScholarPubMed
Campbell, J. W., Duee, E., Hodgson, G., Mercer, W. D., Stammers, D. K., Wendell, P. L., Muirhead, H. & Watson, H. C. (1971) X-ray diffraction studies on enzymes in the glycolytic pathway. Cold Spring Harbor Symposium on Quantitative Biology 36: 165–70. [aPAH]10.1101/SQB.1972.036.01.023CrossRefGoogle Scholar
Caretta, A. & Cavaggioni, A. (1983) Fast ionic flux activated by cyclic GMP in the membrane of cattle rod outer segments. European Journal of Biochemistry 132: 1–8. [TGW]10.1111/j.1432-1033.1983.tb07317.xCrossRefGoogle ScholarPubMed
Caretta, A., Cavaggioni, A., Grimaldi, R. & Sorbi, R. (1988) Regulation of cyclic GMP binding to retinal rod membranes by calcium. European Journal of Biochemistry 177: 139–46. [aRSM]10.1111/j.1432-1033.1988.tb14354.xCrossRefGoogle ScholarPubMed
Caretta, A., Cavaggioni, A. & Sorbi, R. T. (1979) Cyclic GMP and the permeability of the disks of the frog photoreceptors. Journal of Physiology 295: 171–78. [TGW]10.1113/jphysiol.1979.sp012959CrossRefGoogle ScholarPubMed
Castellucci, V. F., Blumenfeld, H., Goelet, P. & Kandel, E. R. (1989) Inhibitor of protein synthesis blocks long-term behavioral sensitization in the isolated gill-withdrawal reflex of Aplysia. Journal of Neurobiology 20: 1–9. [aZX]10.1002/neu.480200102CrossRefGoogle ScholarPubMed
Castellucci, V. F. & Kandel, E. R.(1976) Presynaptic facilitation as a mechanism for behavioral sensitization in Aplysia. Science 194: 1176–78. [aZX]10.1126/science.11560CrossRefGoogle ScholarPubMed
Cavaggioni, A. & Sorbi, R. T. (1981) Cyelie GMP releases calcium from disc membranes of vertebrate photoreceptors. Proceedings of the National Academy of Science USA 78: 3964–68. [TGW]10.1073/pnas.78.6.3964CrossRefGoogle ScholarPubMed
Caviness, V. S. Jr, So, D. K. & Sidman, R. L. (1972) The hybrid reeler mouse. Journal of Heredity 63: 341–46. [DW]10.1093/oxfordjournals.jhered.a108286CrossRefGoogle ScholarPubMed
Cervetto, L., Torre, V., Pasino, E., Marroni, P. & Capovilla, M. (1984) Recovery from light-desensitization in toad rods. In: Photoreceptors, ed. Borcellino, A. & Cervetto, L.. Plenum. [arMDB]Google Scholar
Chabre, M. (1985) Molecular mechanism of visual phototransduction in retinal rod cells. Annual Review of Biophysics and Biophysical Chemistry 14: 331–60. [aPAH]Google Scholar
Chabre, M. & Deterre, P. (1989) Molecular mechanism of visual transduction. European Journal of Biochemistry 179: 255–66. [aMDB, aPAH, aRSM]10.1111/j.1432-1033.1989.tb14549.xCrossRefGoogle ScholarPubMed
Chakraborty, R. (1993) Generalized occupancy problem and its applications in population genetics. In: Genetics of cellular, individual, family, and population variability, ed. Sing, C. F. & Hanis, C. L.. Oxford University Press. [aSPD]Google Scholar
Chang, B., Heckenlively, J. R., Hawes, N. L. & Roderick, T. H. (1993) New mouse primary retinal degeneration (rd-3). Genomics 16: 45–49. [MWK]10.1006/geno.1993.1138CrossRefGoogle Scholar
Chang, G.-Q., Hao, Y. & Wong, F. (1993) Apoptosis: Final common pathway of photoreceptor death in rd, rds, and rhodopsin mutant mice. Neuron 11: 595–605. [aSPD, MT]10.1016/0896-6273(93)90072-YCrossRefGoogle ScholarPubMed
Charbonneau, H., Prusti, R. K., LeTrong, , Sonnenburg, W. K., Mullancy, P. J., Walsh, K. A. & Beavo, J. A. (1990) Identification of a noncatalytic cGMP-binding domain conserved in both the cGMP-stimulated and photoreceptor cyclic nucleotide phosphodiesterase. Proceedings of the National Academy of Sciences USA 87: 288–92. [aMDB]10.1073/pnas.87.1.288CrossRefGoogle Scholar
Chen, C.-K. & Hurley, J. B. (1994) Calcium-dependent recoverin/rhodopsin kinase interaction. Investigative Ophthalmology and Visual Science 35: 1485. [aMDB, aJBH, AY]Google Scholar
Chen, S., Fry, C. H., Illner, H., Kickenweiz, E., McGuigan, J. A. S., Powell, T. & Twist, V. W. (1992) Measurement of intracellular free magnesium in isolated guinea-pig papillary muscles and ventricular myocytes. Journal of Physiology (London) 452: 194 p.[RLH]Google Scholar
Chen, T. -Y, Illing, M., Molday, L. L., Hsu, T.-T, Yau, K.-W. & Molday, R. S. (1994) subunit 2 (or β) of retinal rod cGMP-gated cation channel is a component of the 240-kDa channel-associated protein and mediates Ca2+-ealmodulin modulation. Proceedings of the National Academy of Sciences USA 91: 11757–61. [rRSM, RLB, DDO]10.1073/pnas.91.24.11757CrossRefGoogle ScholarPubMed
Chen, T.-Y, Peng, Y.-W, Dhallan, R. S., Ahamed, B., Reed, R. R. & Yau, K.-W. (1993) A new subunit of the cyclic nucleotide-gated cation channel in retinal rods. Nature 362: 764–67. [arRSM, RLB, LWH, RLH, DDO]10.1038/362764a0CrossRefGoogle ScholarPubMed
Chen, T.-Y. & Yau, K.-W. (1994) Direct modulation by Ca-calmodulin of cyclic nucleotide-activated channel of rat olfactory receptor neurons. Nature 368: 545–48. [rRSM]10.1038/368545a0CrossRefGoogle Scholar
Chetkovich, D. M., Gray, R., Johnston, D. & Sweatt, J. D. (1991) N-methyl- D-aspartate receptor activation increases cAMP levels and voltage gated Ca2+ channel activity in area CA1 of hippocampus. Proceedings of the National Academy of Sciences USA 88: 6467–71. [aZX, EDR]10.1073/pnas.88.15.6467CrossRefGoogle ScholarPubMed
Chevkovich, D. M. & Sweatt, J. D. (1993) NMDA receptor activation increases cyclic AMP in area CA1 of the hippocampus via calcium/calmodulin stimulation of adenylyl cyclase. Journal of Neurochemistry 61: 1933–42. [aZX, EDR]10.1111/j.1471-4159.1993.tb09836.xCrossRefGoogle Scholar
Cheung, W. Y. & Storm, D. R. (1982) Calmodulin regulation of cAMP metabolism. Handbook of Experimental Pharmacology 58: 301–17. [aZX]10.1007/978-3-642-68111-0_7CrossRefGoogle Scholar
Choi, E. J., Wong, S. T, Dittman, A. H. & Storm, D. R. (1993). Phorbol ester stimulation of the type I & type III adenylyl cyclases in whole cells. Biochemistry 32: 1891–94. [aZX]10.1021/bi00059a001CrossRefGoogle ScholarPubMed
Choi, E. J., Wong, S. T., Hinds, T. J. & Storm, D. R. (1992a) Calcium and muscarinic agonist stimulation of type I adenylyl cyclase in whole cells. Journal of Biological Chemistry 267: 12440–42. [aZX]10.1016/S0021-9258(18)42296-XCrossRefGoogle ScholarPubMed
Choi, E. J., Xia, Z. & Storm, D. R. (1992b) Stimulation of the type III olfactory adenylyl cyclase by calcium and calmodulin. Biochemistry 31: 6492–98. [arZX]10.1021/bi00143a019CrossRefGoogle ScholarPubMed
Cimler, B. M., Andreasen, T. J., Andreasen, K. I. & Storm, D. R. (1985) P–57 is a neural specific calmodulin-binding protein. Journal of Biological Chemistry 260: 10784–88. [aZX]10.1016/S0021-9258(19)85150-5CrossRefGoogle ScholarPubMed
Clack, J. W. & Pepperberg, D. R. (1982) Desensitization of skate photoreceptor by bleaching and background light. Journal of General Physiology 80: 863–83. [aMDB]10.1085/jgp.80.6.863CrossRefGoogle ScholarPubMed
Clack, J. W. & Stein, P. J. (1988) Opsin exhibits cCMP-activated single channel activity. Proceedings of the National Academy of Sciences USA 85: 9806–10. [aRSM]10.1073/pnas.85.24.9806CrossRefGoogle ScholarPubMed
Clore, G. M. & Gronenborn, A. M. (1994a) Structures of larger proteins, protein-ligand and protein-DNA complexes by multidimensional heteronuclear NMR: Young investigator award lecture. Protein Science 3: 372–90. [RKC]10.1002/pro.5560030302CrossRefGoogle ScholarPubMed
Clore, G. M. & Gronenborn, A. M. (1994b) Structures of larger proteins, protein-ligand and protein-DNA complexes by multidimensional heteronuclear NMR. Protein Science 3: 372–90. [rPAH]10.1002/pro.5560030302CrossRefGoogle ScholarPubMed
Coleman, D. L. (1981) Inherited obesity-diabetes syndromes in the mouse. In: Mammalian genetics and cancer. Liss. [DW]Google Scholar
Coles, J. A. & Yamane, S. (1975) Effects of adapting lights on the time course of the receptor potential of the anuran retinal rod. Journal of Physiology (London) 247: 189–207. [arMDB]10.1113/jphysiol.1975.sp010927CrossRefGoogle ScholarPubMed
Collingridge, G. (1987) Synaptic plasticity: The role of NMDA receptors in learning and memory. Nature 330: 604–5. [TWA]10.1038/330604a0CrossRefGoogle ScholarPubMed
Cone, R. A. (1972) Rotational diffusion of rhodopsin in the visual receptor membrane. Nature New Biology 236: 39–43. [aPAH]10.1038/newbio236039a0CrossRefGoogle ScholarPubMed
Connell, G., Bascom, R., Molday, L., Reid, D., Mclnnes, R. R. & Molday, R. S. (1991) Photoreceptor peripherin is the normal product of the gene responsible for retinal degeneration in the rds mouse. Proceedings of the National Academy of Sciences USA 38: 723–36. [aSPD, MWK]10.1073/pnas.88.3.723CrossRefGoogle Scholar
Cook, N. J., Hanke, W. & Kaupp, U. B. (1987) Identification, purification and functional reconstitution of the cyclic GMP-dependent channel from rod photoreceptors. Proceedings of the National Academy of Sciences USA 84: 585–89. [aRSM, RLB, RLH, TGW]10.1073/pnas.84.2.585CrossRefGoogle ScholarPubMed
Cook, N. J., Molday, L. L., Reid, D., Kaupp, U. B. & Molday, R. S. (1989) The cGMP- gated channel of bovine rod phororeceptors is localized exclusively in the plasma membrane. Journal of Biological Chemistry 264: 6996–99. [aRSM, RLH, TGW]10.1016/S0021-9258(18)83530-XCrossRefGoogle Scholar
Corless, J. M., McCaslin, D. R. & Scott, B. L. (1982) Two-dimensional rhodopsin crystals from disk membranes of frog retinal rod outer segments. Proceedings of the National Academy of Sciences USA 79:1116–20. [aPAH EAD]10.1073/pnas.79.4.1116CrossRefGoogle ScholarPubMed
Cornwall, M. C. & Fain, G. L. (1992) Bleaching of rhodopsin in isolated rods causes a sustained activation of PDE and cyclase which is reversed by pigment regeneration. Investigative Ophthalmology and Visual Science 33: 1103. [aMDB]Google Scholar
Cornwall, M. C. & Fain, G. L. (1994) Bleached pigment activates transduction in isolated rods of the salamander retina. Journal of Physiology (London) 480: 261–279. [rMDB]10.1113/jphysiol.1994.sp020358CrossRefGoogle ScholarPubMed
Cornwall, M. C. & Fain, G. L. (1994) Bleached pigment activates transduction in isolated rods of the salamander retina. Journal of Physiology 480: 261–79. [RKC]10.1113/jphysiol.1994.sp020358CrossRefGoogle ScholarPubMed
Cornwall, M. C. & Pan, W.-Z. (1985). Spatial resolution of bleaching and background adaptation in rod photoreceptors of Ambystoma tigrinum. In: The visual system, ed. Fein, A. & Levine, J.. Liss, Alan R.. [RKC]Google Scholar
Cornwall, M. C, Fein, A. & MacNichol, E. F. (1990) Cellular mechanisms that underlie bleaching and background adaptation. Journal of General Physiology 96: 345–72. [RKC]10.1085/jgp.96.2.345CrossRefGoogle ScholarPubMed
Cornwall, M. C, Fein, A. & MacNichol, E. F. (1983) Spatial localization of bleaching adaptation in isolated vertebrate rod photoreceptors. Proceedings of the National Academy of Sciences USA 80: 2785–88. [RKC]10.1073/pnas.80.9.2785CrossRefGoogle ScholarPubMed
Corson, D. W., Cornwall, M. C, MaeNichol, E. F., Jin, J., Johnson, R., Derguini, F., Crouch, R. K. & Nakanishi, K. (1990) Sensitization of bleached rod photoreceptors by 11-cis-locked analogues of retinal. Proceedings of the National Academy of Sciences USA 87: 6823–27. [RKC]10.1073/pnas.87.17.6823CrossRefGoogle ScholarPubMed
Corson, D. W., Cornwall, M. C, MaeNichol, E. F., Tsang, S., Derguini, F., Crouch, R. K. & Nakanishi, K. (1994a) Relief of opsin desensitization and prolonged excitation of rod photoreceptors by 9-desmethyl retinal. Proceedings of the National Academy of Sciences USA 91: 6952–58. [RKC]10.1073/pnas.91.15.6958CrossRefGoogle Scholar
Corson, D. W., Cornwall, M. C. & Pepperberg, D. R. (1994b) Evidence for the prolonged photoactivated lifetime of an analogue visual pigment containing 11-cis 9-desmethylretinal. Visual Neuroscience 11: 91–98. [RKC]10.1017/S0952523800011135CrossRefGoogle ScholarPubMed
Cote, R. H. & Brunnock, M. A. (1993) Intracellular cGMP concentration in rod photoreceptors is regulated by binding to high and moderate affinity cGMP binding sites. Journal of Biological Chemistry 268: 17190– 98. [aMDB]10.1016/S0021-9258(19)85321-8CrossRefGoogle ScholarPubMed
Cote, R. H., Bownds, M. D. & Arshavsky, V. Y. (1994) cGMP binding sites on photoreceptor phosphodiesterase: Role in feedback regulation of visual transduction. Proceedings of the National Academy of Sciences USA 91: 4845–49. [arMDB, BMW]10.1073/pnas.91.11.4845CrossRefGoogle ScholarPubMed
Creuzet, F., McDermott, A., Gebhard, R., van der Hoef, K., Spijker-Assink, M., Herzfeld, J., Lugtenburg, J., Levitt, M. H. & Griffin, R. G. (1991) Determination of membrane protein structure by rotational resonance NMR: Bacteriorhodopsin. Science 251: 783–86. [SOS]10.1126/science.1990439CrossRefGoogle ScholarPubMed
Davis, S., Butcher, S. P. & Morris, R. G. (1992) The NMDA receptor antagonist D-2-amino-5-phosphonopentanoate (D-AP5) impairs spatiallearning and LTP in vivo at intracerebral concentrations comparable to those that block LTP in vitro. Journal of Neuroscience 12: 21–34. [aZX, TWA]10.1523/JNEUROSCI.12-01-00021.1992CrossRefGoogle Scholar
Dawis, S. M. (1991) A molecular basis for Weber's law. Visual Neuroscience 7: 285–320. [aMDB]10.1017/S0952523800004806CrossRefGoogle ScholarPubMed
Dawis, S. M., Graeff, R. M., Heyman, R. A., Walseth, T. F. & Goldberg, N. D. (1988) Regulation of cyclic GMP metabolism in toad photoreceptors. Journal of Biological Chemistry 263: 8771–85. [arMDB]10.1016/S0021-9258(18)68373-5CrossRefGoogle ScholarPubMed
de Crip, W. J. (1982a) Purification of bovine rhodopsin over concanavalin A-sepharose. Methods in Enzymology 81: 197–207. [aPAH]10.1016/S0076-6879(82)81032-XCrossRefGoogle Scholar
de Crip, W. J. (1982b) Thermal stability of rhodopsin and opsin in some novel detergents. Methods in Enzymology 81: 256–65. [aPAH]10.1016/S0076-6879(82)81040-9CrossRefGoogle Scholar
de Grip, W. J., Olive, J. & Bovee-Geurts, P. H. M. (1983) Reversible modulation of rhodopsin photolysis in pure phosphatidylserine membranes. Biochimica et Biophysica Ada 734: 168–79. [aPAH]10.1016/0005-2736(83)90115-3CrossRefGoogle Scholar
de Grip, W. J., van Oostrum, J., Bovee-Geurts, P. H. M., van der Steen, R., van Amsterdam, L. J. P., Groesbeek, M. & Lugtenburg, J. (1990) 10,20-methanorhodopsins: (7E.9E, 13E)- 10,20, methanorhodopsin and (7E.9Z, 13Z)-10,20-methanorhodopsin: 11-cis-locked rhodopsin analog pigments with unusual thermal and photo-stability. European Journal of Biochemistry 191: 211–20. [aPAH]10.1111/j.1432-1033.1990.tb19112.xCrossRefGoogle Scholar
de Grip, W. J., van Oostrum, J. & De Caluw, C. L. J. (1992) Studies towards the crystallization of the rod visual pigment rhodopsin. Journal of Crystal Growth 122: 375–84. [aPAH]10.1016/0022-0248(92)90272-KCrossRefGoogle Scholar
Deese, A. J., Dratz, E. A., Dahlquist, F. W. & Paddy, M. R. (1981) Interaction of rhodopsin with two unsaturated phosphatidylcholines: A deuterium nuclear magnetic resonance study. Biochemistry 20: 6420–27. [aPAH]10.1021/bi00525a021CrossRefGoogle ScholarPubMed
Deisenhofer, J. & Michel, H. (1989) The photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis . Science 245: 1463–73. [aPAH]10.1126/science.245.4925.1463CrossRefGoogle ScholarPubMed
Demin, V. V., Yurkova, E. V., Kuzin, A. P., Barnakov, A. N. & Abdulaev, N. G. (1987). Crystallization of bovine retinal rhodopsin. In: Retinal proteins. VNU Science Press. [aPAH]Google Scholar
Dencher, N. A., Dresselhaus, D., Zaccai, G. & Boldt, G. (1989) Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction. Proceedings of the National Academy of Sciences USA 86: 7876–79. [aPAH]10.1073/pnas.86.20.7876CrossRefGoogle ScholarPubMed
Derguini, F. & Nakanishi, K. (1986) Synthetic rhodopsin analogs. Photobiochemistry & Photobiophysics 13: 259–83. [aPAH]Google Scholar
Deterre, P., Bigay, J., Forguet, F., Robert, M. & Chabre, M. (1988) cGMP of phosphodiesterase of retinal rods is regulated by two inhibitory subunits. Proceedings of the National Academy of Sciences USA 85: 2424–28. [aMDB]10.1073/pnas.85.8.2424CrossRefGoogle ScholarPubMed
Detwiler, P. B. & Gray-Keller, M. P. (1992) Some unresolved issues in the physiology and biochemistry of phototransduction. Current Opinion in Neurobiology 2: 433–38. [aMDB]10.1016/0959-4388(92)90176-LCrossRefGoogle ScholarPubMed
Dhallan, R. S., Macke, J. P., Eddy, R. L., Shows, T. B., Reed, R. R., Yau, K. W. & Nathans, J. (1992) Human rod photoreceptor cGMP-gated channel: Amino acid sequence, gene structure, and functional expression. Journal of Neuroscience 12: 3248–56. [aRSM]10.1523/JNEUROSCI.12-08-03248.1992CrossRefGoogle ScholarPubMed
Dhallan, R. S., Yau, K. W, Schrader, K. A. & Reed, R. R. (1990) Primary structure and functional expression of a cyclic nucleotide-activated channel from olfactory neurons. Nature 347: 184–87. [aRSM]10.1038/347184a0CrossRefGoogle ScholarPubMed
Dittman, A. H., Weber, J. P., Hinds, T. R., Choi, E. J., Migeon, J. C., Nathanson, N. M. & Storm, D. R. (1994) A novel mechanism for coupling of m4 muscarinic acetylcholine receptors to calmodulin-sensitive adenylyl cyclases: Cross-over from G protein coupled inhibition to stimulation. Biochemistry 33: 943–51. [aZX]10.1021/bi00170a013CrossRefGoogle Scholar
Dizhoor, A. M., Chen, C.-K., Olshevskaya, E., Sinelnikova, V. V., Philipov, P. & Hurley, J. B. (1993) Role of the acylated amino terminus of recoverin in Ca+2-dcpendcnt membrane iuteraction. Science 259: 829–32. [aJBH, SK]10.1126/science.8430337CrossRefGoogle Scholar
Dizhnor, A. M., Ericsson, L. H., Johnson, R. S., Kumar, S., Olshevakaya, E., Zozulya, S., Neubert, T. A., Stryer, L., Hurley, J. B. & Walsh, K. A. (1992) The NH2 terminus of retinal recoverin is acylated by a small family of fatty acids. Journal of Biological Chemistry 267: 16033–36. [aJBH, KS]10.1016/S0021-9258(18)41959-XCrossRefGoogle Scholar
Dizhoor, A. M., Lowe, D. C, Olshevskaya, E. V., Laura, R. P. & Hurley, J. B. (1994) The human photorcceptor membrane guanylyl cyclase, RetGC, is present in outer segments and is regulated by calcium and a soluble activator. Neuron 12: 1345–52. [aMDB]10.1016/0896-6273(94)90449-9CrossRefGoogle Scholar
Dizhoor, A. M., Ray, S., Kumar, S., Niemi, C., Spencer, M., Brolley, D., Walsh, K. A., Philipov, P. P., Hurley, J. B. & Stryer, L. (1991) Recoverin: A calcium sensitive activator of retinal rod guanylate cyclase. Science 251: 915–18. [aMDB, aJBH, SK, JFM, ASP]10.1126/science.1672047CrossRefGoogle ScholarPubMed
Dorset, D. L., Engel, A., Honor, M., Massalski, A. & Rosenbusch, J. P. (1983) Two-dimensional crystal packing of matrix porin. Journal of Molecular Biology 165: 701–10. [aPAH]10.1016/S0022-2836(83)80275-7CrossRefGoogle ScholarPubMed
Downer, N. W. (1985) Cross-linking of dark-adapted frog photoreceptor disk membranes: Evidence for monomeric rhodopsin. Biophysical Journal 47: 285–93. [aPAH]10.1016/S0006-3495(85)83918-7CrossRefGoogle ScholarPubMed
Dratz, E. A., Furstenau, J., Hamm, H. E. & Hargrave, P. A. (1990) Probing the molecular mechanism of visual excitation using bioactive peptide sequences. Investigative Ophthalmology and Visual Science 31: 79. [EAD]Google Scholar
Dratz, E. A., Furstenau, J., Lambert, C. G., Thireault, D. L., Rarick, H., Schepers, T., Pakhlevaniants, S. & Hamm, H. E. (1993) NMR structure of a receptor-bound G-protein peptide. Nature 363: 276–81. [EAD]10.1038/363276a0CrossRefGoogle ScholarPubMed
Dratz, E. A., Hamm, H. E., Zwolinski, R., Furstenau, J. & Lambert, C. (1991) The 3D structure of the active interface between rhodopsin and G-protein determined using 2D NMR. Biophysical Journal 59:189a. [EAD]Google Scholar
Dratz, E. A. & Hargrave, P. A. (1983) The structure of rhodopsin and the rod outer segment disk membrane. Trends in Biochemical Sciences 8: 128–31. [aPAH, EAD]10.1016/0968-0004(83)90235-9CrossRefGoogle Scholar
Dratz, E. A., Lewis, J. W., Schaechter, L. E., Parker, K. R. & Kliger, D. S. (1987) Retinal rod GTPase turnover rate increases with concentration: A key to the control of visual excitation? Biochemical and Biophysical Research Communications 146: 379–86. [aMDB]10.1016/0006-291X(87)90540-7CrossRefGoogle Scholar
Dratz, E. A., VanBreeinen, J. F. L., Kamps, K. M. P., Keegstra, W. & VanBruggon, E. F. J. (1985) Two-dimensional crystallization of bovine rhodopsin. Biochimica ct Biophysica Acta 832:337–42. [aPAH, EAD]10.1016/0167-4838(85)90268-7CrossRefGoogle ScholarPubMed
Dryer, S. E. & Henderson, D. (1991) A cyclic GMP-activated channel in dissociated cells of the chick pineal gland. Nature 353: 756–58. [aRSM]10.1038/353756a0CrossRefGoogle ScholarPubMed
Dryja, T. P. (1992) Doyne lecture: Rhodopsin and autosomal dominant retinitis pigmentosa. Eye 6: 1–10. [aPAH, aSPD]10.1038/eye.1992.2CrossRefGoogle ScholarPubMed
Dryja, T. P., Berson, E. L., Rao, V. & Oprian, D. D. (1993) Heterozygous missense mutation in the rhodopsin gene as the cause of congenital stationary night blindness. Nature Genetics 4:280–83. [aSPD]10.1038/ng0793-280CrossRefGoogle ScholarPubMed
Dryja, T. P., Hahn, L. B., McGee, T. L., Cowley, G. S. & Berson, E. L.(1991) Mutation spectrum of the rhodopsin gene in patients with autosomal dominant retinitis pigmentosa. Proceedings of the National Academy of Sciences USA 88: 9370–74. [aSPD]10.1073/pnas.88.20.9370CrossRefGoogle ScholarPubMed
Dryja, T. P., McGee, T. I., Hahn, L. B., Cowley, G. S., Olsson, J. E., Keichel, E., Sandberg, M. A. & Berson, E. L. (1990) Mutations within the rhodopsin gene in patients with autosomal dominant retinitis pigmentosa. New England Journal of Medicine 323: 1302–7. [aSPD]10.1056/NEJM199011083231903CrossRefGoogle ScholarPubMed
Dryja, T. P., McGee, T. I., Reichel, E., Hahn, L. B., Cowley, G. S., Yandell, D. W., Sandberg, M. A. & Berson, E. L. (1990a) A point mutation of the rhodopsin gene in one form of retinitis pigmentosa. Nature 343(6256):364–66. [aSPD]10.1038/343364a0CrossRefGoogle ScholarPubMed
Duclai, V. (1988) Neurogenetic dissection of learning and short-term memory in Drosophila. Annual Review of Neuroscience 11: 537–63. [aZX]Google Scholar
Dudai, Y. & Zvi, S. (1984) Adenylate cyclase in the Drosophila memory mutant rutabaga displays an altered Ca2+ sensitivity. Neuroscience Letters 47: 19–24. [aZX, TWA]10.1016/0304-3940(84)90416-6CrossRefGoogle ScholarPubMed
Dudai, Y. & Zvi, S. (1985) Multiple defects in the activity of adenylyl cyclase from the Drosophila memory mutant rutabaga. Journal of Neurochemistry 45: 355–64. [aZX]10.1111/j.1471-4159.1985.tb03996.xCrossRefGoogle ScholarPubMed
Dumke, C. L., Arshavsky, V. Y., Calvert, P. D., Pugh, E. N. & Bownds, M. D. (1994) Rod outer segment structure influences the apparent kinetic parameters of cGMP phosphodiesterase. Journal of General Physiology 103: 1071–98. [aMDB]10.1085/jgp.103.6.1071CrossRefGoogle Scholar
Durell, S. R. & Guy, R. (1992) Atomic scale structure and functional models of voltage-gated potassium channels. Biophysics Journal 62: 238–50. [aRSM]10.1016/S0006-3495(92)81809-XCrossRefGoogle ScholarPubMed
Eisman, E., Bönigk, W. & Kaupp, U. B. (1993) Structural features of cyclic nucleotide-gated channels. In: Cellular physiology and biochemistry, ed. Lang, F.. Karger, S. AC. [rRSM]Google Scholar
Eismann, E., Müller, F., Heinemann, S. H. & Kaupp, U. B. (1994) A single negative charge within the pore region of a cGMP-gated channel controls rectification, Ca2+ blockage and ionic selectivity. Proceedings of the National Academy of Sciences USA 91: 1109–13. [rRSM]10.1073/pnas.91.3.1109CrossRefGoogle ScholarPubMed
Erickson, M. A., Robinson, P. & Lisman, J. (1992) Deactivation of visual transduction without guanosine triphosphate hydrolysis by G protein. Science 257: 1255–58. [aMDB, AY]10.1126/science.1519062CrossRefGoogle ScholarPubMed
Fahmy, K. & Sakmar, T. P. (1993) Regulation of rhodopsin-transducin interaction by a highly conserved carboxylic acid group. Biochemistry 32: 7229–36. [aSPD]10.1021/bi00079a020CrossRefGoogle ScholarPubMed
Fain, G. L. (1976) Sensitivity of toad rods: Dependence on wavelength and background illumination. Journal of Physiology (London) 261:71–101. [aMDB]10.1113/jphysiol.1976.sp011549CrossRefGoogle Scholar
Fain, G. L. & Cornwall, M. C. (1993) Light and dark adaptation in vertebrate photoreceptors. In: Contrast Sensitivity from receptors to clinic, ed. Shapley, R. & Lam, D.-K.. MIT Press. [RKC]Google Scholar
Fain, G. L., Lamb, T. D., Matthews, H. R. & Murphy, R. L. W. (1989) Cytoplasmic calcium concentration as the messenger for light adaptation in salamander rods. Journal of Physiology 416: 215–43. [HRM]10.1113/jphysiol.1989.sp017757CrossRefGoogle ScholarPubMed
Fain, G. L. & Lisman, J. E. (1993) Photoreceptor degeneration in vitamin A deprivation and retinitis pigmentosa: The equivalent light hypothesis. Experimental Eye Research 57: 335–40. [aMDB]10.1006/exer.1993.1132CrossRefGoogle ScholarPubMed
Fain, G. L. & Matthews, H. R. (1990) Calcium and the mechanism of light adaptation in vertebrate photoreceptors. Trends in Neuroscience 13: 378– 84. [HRM]10.1016/0166-2236(90)90023-4CrossRefGoogle ScholarPubMed
Farber, D. B., Seager, , Danciger, J. & Aguirre, G. (1992) The β subunit of cyclic GMP phosphodiesterase mRNA is deficient in canine rod-cone dysplasia l. Neuron 9: 349–56. [MWK]10.1016/0896-6273(92)90173-BCrossRefGoogle Scholar
Famsworth, C. & Dratz, E. A. (1976) Oxidative damage of retinal rod outer segment membranes and the role of vitamin E. Biochimica et Biophysica Acta 443: 556–70. [aPAH]Google Scholar
Farrar, G. J., Findlay, J. B. C, Kumar-Singh, R., Kenna, P., Humphries, M. M., Sharpe, E. & Humphries, P. (1992) Autosomal dominant retinitis pigmentosa: A novel mutation in the rhodopsin gene in the original 3q linked family. Human Molecular Cenetics 1: 769–71. [aSPD]10.1093/hmg/1.9.769CrossRefGoogle ScholarPubMed
Farrar, G. J., Jordan, S. A., Kenna, P., Humphries, N. M., Kumar-Singh, R., McWilliams, P., Allamand, V., Sharp, E. & Humphries, P. (1991) Autosomal dominant retinitis pigmentosa: Localization of a disease gene (RP6) to the short arm of chromosome 6. Cenomics 11: 870–4. [aSPD]Google Scholar
Farrar, G. J., Kenna, P., Redmond, R., McWilliams, P., Bradley, D. G., Humphries, M. M., Sharp, E. M., Inglehearn, C. F., Bashir, R., Jay, M., Waytty, A., Ludwig, M., Schinzel, A., Samanns, C., Gal, A., Bhattacharya, S. & Humphries, P. (1990) Autosomal dominant retinitis pigmentosa: Absence of the rhodopsin proline—histidine substitution (codon 23) in pedigrees from Europe. American Journal of Human Genetics 47: 941–45. [aSPD]Google ScholarPubMed
Farrar, G. J., Kenna, P., Redmond, R., Shiels, D., McWilliams, P., Humphries, M. M., Sharp, E. M., Jordan, S., Kumar-Singh, R. & Humphries, P. (1991a) Autosomal dominant retinitis pigmentosa: A mutation in codon 178 of the rhodopsin gene in two families of Celtic origin. Cenomics 11: 1170–71. [aSPD]Google ScholarPubMed
Farrar, G. J., McWilliams, P., Bradley, D. G., Kenna, P., Lawler, M., Sharp, E. M., Humphries, N. M., Eiberg, H., Conneally, P. M., Trofatter, J. A. & Humphries, P.(1990) Autosomal dominant retinitis pigmentosa: Linkage to rhodopsin and evidence for genetic heterogeneity. Genomics 8:35–40. [aSPD]10.1016/0888-7543(90)90223-HCrossRefGoogle ScholarPubMed
Feany, M. B. (1990) Rescue of the learning defect in dunce, a Drosophila learning mutant, by an allele of rutabaga, a second learning mutant. Proceedings of the National Academy of Sciences USA 87: 2795–99. [aZX]10.1073/pnas.87.7.2795CrossRefGoogle ScholarPubMed
Federman, A. D., Conklin, B. R., Schrader, K. A., Reed, R. R., Bourne, H. R. (1992) Hormonal stimulation of adenylyl cyclase through G,-protein beta gamma subunits. Nature 356: 159–61.10.1038/356159a0CrossRefGoogle ScholarPubMed
Feher, G., Atten, J. P., Okamura, M. Y. & Rees, D. C. (1989) Structure and function of bacterial photosynthetic reaction centers. Nature 339: 111– 16. [aPAH]10.1038/339111a0CrossRefGoogle Scholar
Feinstein, P. G., Schrader, A., Bakalyar, H. A., Tang, W. J., Krupinski, J., Oilman, A. G. & Reed, R. R. (1991) Molecular cloning and characterization of a calcium calmodulin insensitive adenylyl cyclase (typell) from rat brain. Proceedings of the National Academy of Sciences USA 88: 10173– 77. [aZX]10.1073/pnas.88.22.10173CrossRefGoogle Scholar
Ferrell, R. E., Hittner, H. M. & Antoszyk, J. H. (1983) Linkage of atypical vitelliform macular dystrophy (GPT1) locus. American Journal of Human Genetics 35: 78–84. [aSPD]Google ScholarPubMed
Fesenko, E. E., Kolensnikov, S. S. & Lyubarsky, A. L. (1985) Induction by cyclic GMP of cationic conductance in plasma membrane of retinal rod outer segments. Nature 313: 310–13. [aRSM, DDO, TGW]10.1038/313310a0CrossRefGoogle Scholar
Findlay, J. B. C. (1986). The biosynthetic, functional, and evolutionary implications of the structure of rhodopsin. In: The molecular mechanismof photoreception. Springor-Verlag. [aPAH]Google Scholar
Firestein, S. (1991) A noseful of odor receptors. Trends in Neuroscience 14:270–72. [aMDB]10.1016/0166-2236(91)90135-HCrossRefGoogle ScholarPubMed
Fishman, G. A. (1990) Inherited macular dystrophies: A clinical overview. Australia and New Zealand Journal of Ophthalmology 18:123–28. [aSPD]Google ScholarPubMed
Fishman, G. A. (1978) Retinitis pigmentosa: Genetic percentages. Archives of Ophthalmology 96:822–26. [aSPD]10.1001/archopht.1978.03910050428005CrossRefGoogle ScholarPubMed
Fishman, G. A., Alexander, K. R. & Anderson, R. J. (1985) Autosomal dominant retinitis pigmentosa: A method of classification. Archives of Ophthalmology 103:366–74. [aSPD]10.1001/archopht.1985.01050030062023CrossRefGoogle ScholarPubMed
Fishman, G. A., Stone, E. M., Gilbert, L. D., Kenna, P. & Sheffield, V. C. (1991) Ocular findings associated with a rhodopsin gene codon 58 transversion mutation in autosomal dominant retinitis pigmentosa. Archives of Ophthalmology 109:1387–93. [aSPD]10.1001/archopht.1991.01080100067044CrossRefGoogle ScholarPubMed
Fishman, G. A., Stone, E. M., Gilbert, L. D. & Sheffield, V. C. (1992) Ocular findings associated with a rhodopsin gene codon 106 mutation glycine-to-arginine change in autosomal dominant retinitis pigmentosa. Archives of Ophthalmology 110:646–53. [aSPD]10.1001/archopht.1992.01080170068026CrossRefGoogle ScholarPubMed
Fishman, G. A., Stone, E. M., Sheffield, V. C., Gilbert, L. D. & Kimura, A. E. (1992a) Ocular findings associated with rhodopsin gene eodon 17 and codon 182 transition mutation in dominant retinitis pigmentosa. Archives of Ophthalmology 110:54–62. [aSPD]10.1001/archopht.1992.01080130056026CrossRefGoogle ScholarPubMed
Fishman, G. A., Vandenburgh, K., Stone, E. M., Gilbert, L. D., Alexander, K. R. & Sheffield, V. C. (1992b) Ocular findings associated with rhodopsin gene codon 267 and codon 190 mutations in dominant retinitispigmentosa. Archives of Ophthalmology 110:1582–88. [aSPD]10.1001/archopht.1992.01080230082026CrossRefGoogle Scholar
Flaherty, K. M., Zozulya, S., Stryer, L. & McKay, D. B. (1993) Three dimensional structure of recoverin, a calcium sensor in vision. Cell 75:709–16 [aMDB, aJBH, KWK]10.1016/0092-8674(93)90491-8CrossRefGoogle ScholarPubMed
Flieslcr, S. J. & Anderson, R. E. (1983) Chemistry and metabolism of lipids in the vertebrate retina. Progress in Lipid Research 22:79–131. [aMDB]10.1016/0163-7827(83)90004-8CrossRefGoogle Scholar
Fong, S.-L., Tsin, A. T. C., Bridges, C. D. B. & Lion, G. I. (1982) Detergents for extraction of visual pigments: Types, solubilization, and stability. Methods in Enzymology 81:133–40. [aPAH]10.1016/S0076-6879(82)81022-7CrossRefGoogle ScholarPubMed
Forti, S., Menini, A., Rispoli, G. & Torre, V. (1989) Kinetics of phototransduction in retinal rods of the newt Triturus cristatus . Journal of Physiology (London) 419:265–95. [aMDB]10.1113/jphysiol.1989.sp017873CrossRefGoogle ScholarPubMed
Fowles, C., Charma, R. & Akhtar, M. (1988) Mechanistic studies on the phosphorylation of photoexcited rhodopsin. FEBS Letters 238:56–60. [aMDB]10.1016/0014-5793(88)80224-2CrossRefGoogle ScholarPubMed
Franke, R. R., Konig, B., Sakmar, T. P., Khorana, H. G. & Hofmann, K. P. (1990) Rhodopsin mutants that bind but fail to activate transducin. Science 250:123–25. [aPAH, EAD]10.1126/science.2218504CrossRefGoogle ScholarPubMed
Franke, R. R., Sakmar, T. P., Graham, R. M. & Khorana, H. G. (1992) Structure and function in rhodopsin: Studies of the interaction between the rhodopsin cytoplasmic domain and transducin. Journal of Biological Chemistry 267:14767–74. [aPAH]10.1016/S0021-9258(18)42106-0CrossRefGoogle ScholarPubMed
Franke, R. R., Sakmar, T. P., Oprian, D. D. & Khorana, H. G. (1988) A single amino acid substitution in rhodopsin (Lysine 248 Leucine) prevents activation of transducin. Journal of Biological Chemistry 263:2119–22. [aSPD]10.1016/S0021-9258(18)69178-1CrossRefGoogle ScholarPubMed
Frey, U., Huang, Y. Y. & Kandel, E. R. (1993) Effects of cAMP simulate a late stage of LTP in hippocampal CA1 neurons. Science 260:1661–64. [aZX, EDR]10.1126/science.8389057CrossRefGoogle ScholarPubMed
Frey, U., Krug, M., Reynumn, K. G. & Matthies, H. (1988) Anisomyein, an inhibitor of protein synthesis, blocks late phases of LTP phenomena in the hippocampal CA1 region in vitro. Brain Research 45:257–65. [EDR, aZX]Google Scholar
Frey, U., Matthies, H., Reymann, K. G. & Matthies, H. (1991). The effect of dopaminergic D1 receptor blockade during totalization on the expression of long-term potentiation in the rat CA1 region in vitro. Neuroscience Letters 29:111–14. [aZX]10.1016/0304-3940(91)90732-9CrossRefGoogle Scholar
Frost, W. N., Castellucei, V. F., Hawkins, R. D. & Kandel, E. R. (1985) Monosynaptic connections from the sensory neurons of the gill- and siphon-withdrawal reflex in Aplysia participate in the storage of long-term memory for sensitization. Proceedings of the National Academy of Sciences USA 82:8266–69. [aZX]10.1073/pnas.82.23.8266CrossRefGoogle Scholar
Fryxell, K. J. & Meyerowitz, E. M. (1991) The evolution of rhodopsins and neurotransmitter receptors. Journal of Molecular Evolution 33:367–68. [aSPD]10.1007/BF02102867CrossRefGoogle ScholarPubMed
Fujiki, K., Hotta, Y., Hayakawa, M., Sakuma, H., Shiono, T., Noro, M., Shakuma, T., Tamai, M., Hikiji, K., Kawaguchi, R. & Hoshi, A. (1992) Point mutations of rhodopsin gene found among Japanese families with antosomal dominant retinitis pigmentosa (ADRP). Japanese Journal of Human Genetics 37:125–32. [aSPD]Google Scholar
Fukuda, M. N., Papermaster, D. S. & Hargrave, P. A. (1979) Rhodopsin carbohydrate: Structure of small oligosaecharides attached at two sites near the NH2 terminus. Journal of Biological Chemistry 254:8201–7. [aPAH]10.1016/S0021-9258(19)86876-XCrossRefGoogle ScholarPubMed
Fukada, Y., Schichida, Y., Yoshizawa, T., Ito, M., Kodama, A. & Tsukida, K. (1984) Studies on structure and function of rhodopsin by use of cyclopentatrienylidene 11-cis-locked-rhodopsin. Biochemistry 23:5826–32. [aPAH]10.1021/bi00319a023CrossRefGoogle ScholarPubMed
Fukada, Y., Takao, T., Ohguor, H., Yoshizawa, T., Akino, T. & Shimonishi, Y. (1990) Farnesylated gamma subunit of photoreceptor G protein indispensable for GTP-binding. Nature 346:658–60. [aMDB]10.1038/346658a0CrossRefGoogle ScholarPubMed
Fung, B. K.-K. (1993) Characterization of transducin from bovine retinal rod outer segments: 1. Separation and reconstitution of the subunits. Journal of Biological Chemistry 258:10495–502. [rM DB]10.1016/S0021-9258(17)44483-8CrossRefGoogle Scholar
Fung, B. K.-K. & Griswold-Prenner, I. (1989) G-protein-effector coupling: Binding of rod phosphodiesterase inhibitory subunit to transducin. Biochemistry 28:3133–37. [AY]10.1021/bi00434a003CrossRefGoogle Scholar
Fung, B. B.-K., Hurley, J. B. & Stryer, L. (1981) Flow of information in the light-triggered cyclic nucleotide cascade of vision. Proceedings of the National Academy of Sciences USA 78:152–56. [aM DB, AY]10.1073/pnas.78.1.152CrossRefGoogle Scholar
Fung, B. K.-K., Young, J. H., Yamane, H. K. & Griswold-Prenner, I. (1990) Subunit stoichiometry of retinal rod cGMP phosphodiesterase. Biochemistry 29:2657–64. [aMDB]10.1021/bi00463a006CrossRefGoogle ScholarPubMed
Furman, R. E. & Tanaka, J. C. (1990) Monovalent selectivity of the cyclic guanosine monophosphatu-activated ion channel. Journal of General Physiology 96:57–82. [aRSM]10.1085/jgp.96.1.57CrossRefGoogle ScholarPubMed
Gal, A., Artlich, A., Ludwig, M., Niemeyer, C., Olek, K., Schwinger, E. & Schinzel, A. (1991) Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant retinitis pigmentosa. Genomics 11:468–70. [aSPD]10.1016/0888-7543(91)90159-CCrossRefGoogle ScholarPubMed
Gal, A., Orth, U., Baehr, W., Schwinger, E., & Rosenberg, T. (1994) Heterozygous missense mutation in the rod cGMP phosphodiesterase G-subunit gene in autosomal dominant stationary night blindness. Nature Genetics 7, 551:64–67. [aSPD]10.1038/ng0594-64CrossRefGoogle Scholar
Gannon, A. M., Rodriguez, J. A., Humphries, P., Birch, D. G., Heckenlively, J. R. & Daiger, S. P. (1993) Mutations in peripherin/RDS in patients with retinitis pigmentosa: A 12 base-pair deletion in exon 2. American Journal of Human Genetics 53:1160. [aSPD]Google Scholar
Gao, B. & Gilman, A. (1991) Cloning and expression of a widely distributed (type IV) adenylyl cyclase. Proceedings of the National Academy of Sciences USA 88:10178–82. [aZX]10.1073/pnas.88.22.10178CrossRefGoogle ScholarPubMed
Garavito, R. M. (1991). Crystallizing membrane proteins: Experiments on different systems. In: Crystallization of membrane proteins, ed. Michel, H.. CRC Press. [aPAH]Google Scholar
Garavito, R. M. (in press) Strategies for crystallizing membrane proteins. Journal of Bioenergetics and Biomembranes. [RMG]Google Scholar
Garavito, R. M. & Picot, D. (1990) The art of membrance protein crystallization. Methods: A Companion to methods in Enzymology 1:57–69. [RMG]10.1016/S1046-2023(05)80147-1CrossRefGoogle Scholar
Gery, I., Chanaud, N. P. III & Anglade, E. (1994) Recover in is highly uveitogenic in Lewis rats. Investigative Ophthalmology and Visual Science 35:3342–45. [ASP]Google Scholar
Ghirardi, M., Braha, O., Hochner, B., Montarolo, P. G., Kandel, E. R. & Dale, N. (1992) Roles of PKA and PKC in facilitation of evoked and spontaneous transmitter release at depressed and nondepressed synapsesin Aplysia sensory neurons. Neuron 9:479–89. [aZX, TWA]10.1016/0896-6273(92)90185-GCrossRefGoogle Scholar
Gibson, F., Walsh, J., Mburu, P., Varela, A., Brown, K. A., Antonio, M., Belsel, K. W., Steel, K. P. & Brown, S. D. M. (1995) A type VII myosin encoded by the mouse deafness gene shaker-1. Nature 374:62–64. [rSPD]10.1038/374062a0CrossRefGoogle ScholarPubMed
Gillespie, P. G. & Beavo, J. A. (1988) Characterization of a bovine cone photoreceptor phosphodiesterase purified by cyclic GMP-sepharose chromatography. Journal of Biological Chemistry 263:8133–41. [aMDB]10.1016/S0021-9258(18)68452-2CrossRefGoogle ScholarPubMed
Gillespie, P. G. & Beavo, J. A. (1989) cGMP is tightly bound to bovine retinal rod phosphodiesterase. Proceedings of the National Acadenuj of Sciences USA 86:4311–15. [aMDB]10.1073/pnas.86.11.4311CrossRefGoogle ScholarPubMed
Glatt, C. E. & Snyder, S. H. (1993) Cloning and expression of an adenylyl cyclase localized to the corpus striatum. Nature 363:679–80. [aZX]10.1038/363679b0CrossRefGoogle Scholar
Gnegy, M., Muirhead, N., Roberts-Lewis, J. M. & Treisman, G. (1984) Calmodulin stimulates adenylyl cyclase activity and increases dopamine activation in bovine retina. Journal of Neuroscience 4:2712–17. [aZX]10.1523/JNEUROSCI.04-11-02712.1984CrossRefGoogle ScholarPubMed
Gnegy, M. & Treisman, G. (1981) Effect of calmodulin on dopamine-sensitive adenylate cyclase activity in rat striatal membranes. Molecular Pharmacology 19:256–63. [aZX]Google ScholarPubMed
Gold, G. H. & Korenbrot, J. J. (1980) Light-induced calcium release by intact retinal rods. Proceedings of the National Academy of Sciences USA 77:5557–61. [TGW]10.1073/pnas.77.9.5557CrossRefGoogle ScholarPubMed
Goldberg, M. F. (1994) Molecular heterogeneity in retinitis pigmentosa. Ophthalmic Genetics 15(2):47–50 [AB]10.3109/13816819409098863CrossRefGoogle ScholarPubMed
Goldsmith, B. A. & Abrams, T. W. (1991) Reversal of synoptic depression by serotonin ut Aplysia sensory neuron synapses involves activation of adenylate cyclase. Proceedings of the National Academy of Sciences USA 88:9021–25. [TWA]10.1073/pnas.88.20.9021CrossRefGoogle Scholar
Gorczyca, W. A., Gray-Keller, M. P., Detwiler, P. B. & Palczewski, K. (1994) Purification and physiological evaluation of a guanylate eyclase activating protein from retinal rods. Proceedings of the National Academy of Sciences USA 91:4014–18. [aMDB]10.1073/pnas.91.9.4014CrossRefGoogle ScholarPubMed
Gordon, J. I., Duronio, R. J., Rudnick, D. A., Adams, S. P. & Gokel, G. W. (1991) Protein N-myristoylation. Journal of Biological Chemistry 266:8647–50. [KS]10.1016/S0021-9258(18)31490-XCrossRefGoogle ScholarPubMed
Gordon, S. E., Brautigan, D. L. & Zimmerman, A. L. (1992) Protein phosphatases modulate the apparent agonist affinity of the ligand regulated ion channel of retinal rods. Neuron 8:739–48. [aMDB, aRSM, RLB. LWH, TGW]10.1016/0896-6273(92)90036-DCrossRefGoogle Scholar
Gordon, S. E., Downing-Park, J. & Zimmerman, A. L. (in press) Modulation of the cGMP-gated ion channel in frog rods by calmodulin and an endogenous inhibitory factor. Journal of Physiology. [MPG-K, rRSM]Google Scholar
Gordon, S. E. & Zimmerman, A. L. (1994) Modulation of the rod cCMP-gated ion channel by calmodulin and an endogenous factor distinct from calmodulin. Biophysics Journal 66:A355. [MSS, TCW]Google Scholar
Gorodovikova, E. N. & Philippov, P. P. (1993) The presence of a calcium sensitive p26-containing complex in bovine retinal rod cells. FEBS Letters 335:277–79. [SK]10.1016/0014-5793(93)80746-HCrossRefGoogle Scholar
Goslin, K., Schreyer, D. J., Skene, J. H. P. & Banker, G. (1988) Development of neuronal polarity: GAP-43 distinguishes axonal from dendritic growth cones. Nature 336:672–74. [EDR]10.1038/336672a0CrossRefGoogle ScholarPubMed
Golliding, E. H., Ngai, J., Kramer, R. H., Colicos, S., Axel, R., Siegelbaum, S. A. & Chess, A. (1992) Molecular cloning and single channel properties of the cyclic nuclco tide-gated channel from catfish olfactory neurons. Neuron 8:45–58. [aRSM]10.1016/0896-6273(92)90107-OCrossRefGoogle Scholar
Golliding, E. H., Tibbs, G. R., Liu, D. & Siegelbaum, S. A. (1993) Role of the H5 domain in determining pore diameter and ion permeation through cyclic nuclcotide-gated channels. Nature 364:61–64. [aRSM]10.1038/364061a0CrossRefGoogle Scholar
Golliding, E. H., Tibbs, G. R. & Siegelbaum, S. A. (1994) Molecular mechanism of cyclic-nucleotide-gated channel activation. Nature 372:369–74. [rRSM]10.1038/372369a0CrossRefGoogle Scholar
Grant, S. G. N., O'Dell, T. J., Karl, K. A., Stein, P. L., Soriano, P. & Kandel, E. R. (1992) Impaired long-term potentiation, spatial learning and hippocampal development in fyn mutant mice. Science 258:1903–92. [aZX]10.1126/science.1361685CrossRefGoogle ScholarPubMed
Gray-Keller, M. P., Bienibaiim, M. S. & Bownds, M. D. (1990) Transducin activation in electropermeabilized frog rod outer segments is highly amplified, and a portion equivalent to phosphodiesterase remains membrane-bound. Journal of Biological Chemistry 265:15323–32. [aMDB]10.1016/S0021-9258(18)77259-1CrossRefGoogle Scholar
Gray-Keller, M. P. & Detwiler, P. B. (1994a) Intracellular calcium measurements in isolated rod photoreceptors. Investigative Ophthalmology and Visual Science 35:1486. [aMDB]Google Scholar
Gray-Keller, M. P. & Detwiler, P. B. (1994b) Tlie calcium feedback signal in the phototransduction cascade of vertebrate rods. Neuron 13(4):849–61. [MPC-K, MSS, TCW, rMDB]10.1016/0896-6273(94)90251-8CrossRefGoogle Scholar
Gray-Keller, M. P., Polans, A. S. Palczewski, K. & Derwiler, P. B. (1993) The effect of recoverin-like calcium-binding proteins on the photoresponse of retinal rods. Neuron 10:523–31. [aMDB, aJBH, MPC-K, LWH]10.1016/0896-6273(93)90339-SCrossRefGoogle ScholarPubMed
Grecksch, G. & Matthies, H. (1980) Two sensitive periods for the amnesic effect of anisomycin. Pharmacology and Biochemistry of Behavior 12:663–65. [aZX]10.1016/0091-3057(80)90145-8CrossRefGoogle ScholarPubMed
Greenberg, J., Goliath, R., Brighton, P., & Raniesar, R. (1994) A new locus for autosomal dominant retinitis pitmentosa on the short arm of chromosome 17. Human Molecular Genetics 6:915–18. [aSPD]10.1093/hmg/3.6.915CrossRefGoogle Scholar
Greenberg, S. M., Castellueci, V. F., Bayley, H. & Schwartz, J. H. (1987) A molecular mechanism for long-term sensitization in Aplysia. Neuron 329:62–65. [aZX]Google ScholarPubMed
Greengard, P. (1979) Cyclic nucleotides, phosphorylated proteins, and the nervous system. Federation Proceedings 38:2208–17. [TWA]Google ScholarPubMed
Groskoph, S. L., Hammett, D. J. & Cote, R. H. (1992) Nucleotide energy metabolism in electropormeabilizcd rod photoreceptors. Investigative Ophthalmology and Visual Science 33:1008. [aM DB]Google Scholar
Gullion, T. & Schaefer, J. (1989) Detection of weak heteronuclear dipolar coupling by rotational echo double resonance nuclear magnetic resonance. In: Advances in magnetic resonance, vol. 13., ed. Warren, W. S.. Academic Press. [SOS]Google Scholar
Gustafsson, B., Wigstrom, H., Abraham, W. C. & Huang, Y. Y. (1987) Longterm potentiation in the hippocampus using depolarizing current pulses as the conditioning stimulus to single volley synaptic potentials. Journal of Neuroscience 7:774–80. [TWA]10.1523/JNEUROSCI.07-03-00774.1987CrossRefGoogle Scholar
Hagiwara, M., Brindle, P., Harootunian, A., Armstrong, R., Rivier, J., Vale, J., Tsien, R. & Montminy, M. R. (1993) Coupling of hormonal stimulation and transcription via the cAMP responsive factor CREB is rate limited by nuclear entry of protein kinase A. Molecular and Cellular Biology 13:4852–59. [aZX]Google ScholarPubMed
Hakki, S. & Sitaramayya, A. (1990) Guanylate cyclase from bovine rod outer segments: Solubilization, partial purification, and regulation by inorganic pyrophosphate. Biochemistry 29:1088–94. [KWK]10.1021/bi00456a035CrossRefGoogle ScholarPubMed
Hall, M. D., Hoon, M. A., Ryba, N. J. P., Pottinger, J. D. D., Keen, J. N., Sabil, H. R. & Findlay, J. B. C. (1991) Molecular cloning and primary structure of squid (Loligo forbesi) rhodopsin, a phospholipase C-directed C-protein-linked receptor. Biochemistry Journal 274:35–40. [aPAH]10.1042/bj2740035CrossRefGoogle ScholarPubMed
Halloran, S. L. (1985) A multidisciplinary analysis of retinitis pigmentosa: Genetic, cpidemiological and clinical parameters. Doctoral thesis, Virginia Commonwealth University. [aSPD]Google Scholar
Hamm, H. (1990) Regulation by light of cyclic nucleotide-dependent protein kinases and their substrates in frog rod outer segments. Journal of General Physiology 95:545–67. [aMDB]10.1085/jgp.95.3.545CrossRefGoogle ScholarPubMed
Hamm, H. E. & Bownds, M. D. (1986) Protein complement of rod outer segments of frog retina. Biochemistry 25:4512–23. [aMDB]10.1021/bi00364a010CrossRefGoogle ScholarPubMed
Hamm, H. E., Deretic, D., Arendt, A., Hargrave, P. A., Koenig, B. & Hofmann, K. P. (1988) Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit. Science 241:832–35. [EAD]10.1126/science.3136547CrossRefGoogle ScholarPubMed
Hamm, H. E. & Rarick, H. M. (1994) Use of synthetic peptides for mapping G protein interaction sites with receptors. Methods in Enzymology 237:423–36. [RKC]10.1016/S0076-6879(94)37079-6CrossRefGoogle Scholar
Han, M., DeDecker, B. & Smith, S. O. (1993) Localization of the retinal protonated schiff base counterion in rhodopsin. Biophysics Journal 65:899–926. [SOS]10.1016/S0006-3495(93)81117-2CrossRefGoogle ScholarPubMed
Han, M. & Smith, S. O. (in press) NMR constraints on the location of the retinal chromophore in rhodopsin and bathorhodopsin. Biochemistry. [SOS]Google Scholar
Harbison, G. S., Smith, S. O., Pardoen, J. A., Winkel, D. C., Lugtenburg, J., Herzfeld, J., Mathies, R. & Griffln, R. G. (1984) Dark-adapted Bacteriorhodopsin contains 13-cis, 15-syn and all-trans, 15-anti retinal schiff bases. Proceedings of the National Academy of Sciences USA 81:1706–9. [SOS]10.1073/pnas.81.6.1706CrossRefGoogle ScholarPubMed
Hardie, R. C. & Minke, B. (1992) The trp gene is essential for a light activated Ca2+ channel in Drosophila photoreceptors. Neuron 8:643–51. [aRSM]10.1016/0896-6273(92)90086-SCrossRefGoogle ScholarPubMed
Hargrave, P. A. & Fong, S.-L. (1977) The amino-and carboxyl-terminal sequence of bovine rhodopsin. Journal of Supramolecular Structure 6:559–70. [rPAH]10.1002/jss.400060409CrossRefGoogle ScholarPubMed
Hargrave, P. A., Hamm, H. E. & Hofmann, K. P. (1993) Interaction of rhodopsin with the G-protein, transducin. BioEssays 15:43–50. [aPAH]10.1002/bies.950150107CrossRefGoogle ScholarPubMed
Hargrave, P. A. & McDowell, J. H. (1992a) Rhodopsin and phototransduction: A model system for G protein-linked receptors. FASEB Journal 6:2323–31. [aMDB, aSPD, aPAH]10.1096/fasebj.6.6.1544542CrossRefGoogle Scholar
Hargrave, P. A. & McDowell, J. H. (1992b) Rhodopsin and phototransduction. International Review of Cytology 137B:49–97. [aSPD]Google ScholarPubMed
Hargrave, P. A. & McDowell, J. H. (1993) Rhodopsin and phototransduction. International Review of Cytology 137B:49–97. [aPAH]10.1016/S0074-7696(08)62600-5CrossRefGoogle Scholar
Hargrave, P. A., McDowell, J. H., Feldmann, R. J., Atkinson, P. H., Rao, J. K. M. & Argos, P. (1984) Rhodopsin's protein and carbohydrate structure: Selected aspects. Vision Research 24:1487–99. [aPAH]10.1016/0042-6989(84)90311-0CrossRefGoogle ScholarPubMed
Hargrave, P. A. & O'Brien, P. J. (1991) Speculations of the molecular basis of retinal degeneration in retinitis pigmentosa. In: Retinal degeneration, ed. Hollyfield, J. G., Anderson, R. E. & LaVail, M. M.. CRC Press. [aSPD]Google Scholar
Hayakawa, M., Hotta, Y., Imai, Y., Fujiki, K., Nakamura, A., Yanashima, K. & Kanai, A. (1993) Clinical features of autosomal dominant retinitis pigmentosa with rhodopsin gene codon 17 mutation and retinal neovascularization. American Journal of Ophthalmology 115:168–73. [aSPD]10.1016/S0002-9394(14)73920-0CrossRefGoogle ScholarPubMed
Hayashi, F. (1994) Light-dependent in vivo phosphorylation of an inhibitory subunit of cGMP-phosphodiesterase in frog rod photoreceptor outer segments. FEBS Letters 338:203–6. [aMDB]10.1016/0014-5793(94)80365-XCrossRefGoogle ScholarPubMed
Hayashi, F., Lin, G. Y., Matsumoto, H. & Yamazaki, A. (1991) Phosphatidylinositol-stimulated phosphorylation of an inhibitory subunit of cGMP phosphodiesterase in vertebrate rod photoreceptors. Proceedings of the National Academy of Sciences USA 88:4333–37. [aMDB]10.1073/pnas.88.10.4333CrossRefGoogle ScholarPubMed
Haynes, L. W. (1992) Block of the cyclic CMP-gated channel of vertebrate rod and cone photoreeeptors by L-cis-diltiazem. Journal of General Physiology 100:783–801. [LWH]10.1085/jgp.100.5.783CrossRefGoogle ScholarPubMed
Haynes, L. W. & Yau, K.-W. (1985) Cyclic GMP-sensitive conductance in outer segment membrane of catfish cones. Nature 317:61–64. [aRSM]10.1038/317061a0CrossRefGoogle ScholarPubMed
Hearst, E. (1988) Fundamentals of learning and conditioning. In: Steven's handbook of experimental psychology, ed. Atkinson, R. C., Herrnstein, R. J., Lindzey, G. & Luce, R. D.. Wiley Interscience. [TWA]Google Scholar
Hebert, H., Xian, Y., Hacksell, I. & Mårdh, S. (1992) Two-dimensional crystals of membrane-bound gastric H, K-ATPase. FEBS Letters 299:159–62. [aPAH]10.1016/0014-5793(92)80237-BCrossRefGoogle ScholarPubMed
Heck, M. & Hofmann, K. P. (1993) G-protein-effector coupling: A real-time light-scattering assay for transducin-phosphodiesterase interaction. Biochemistry 32:8220–27. [aMDB]10.1021/bi00083a024CrossRefGoogle ScholarPubMed
Heckenlively, J. R. (1988) Retinitis pigmentosa. Lippincott. [aSPD]Google ScholarPubMed
Heckenlively, J. R., Rodriguez, J. A. & Daiger, S. P. (1990) Autosomal dominant sectoral retinitis pigmentosa: Two families with transversion mutation in codon 23 of rhodopsin. Archives of Ophthalmology 109:84–91. [aSPD]10.1001/archopht.1991.01080010086038CrossRefGoogle Scholar
Heginbotham, L., Abramson, T. & MacKinnon, R. (1992) A functional connection between the pores of distantly-related ion channels as revealed by mutant K+ channels. Science 258:1152–55. [aRSM]10.1126/science.1279807CrossRefGoogle ScholarPubMed
Heinonen, E. & Akerman, K. E. (1987) Intracellular free magnesium in synaptosomes measured with entrapped eriochrome blue. Biochimica et Biophysica Acta 898:331–37. [RLH]10.1016/0005-2736(87)90074-5CrossRefGoogle ScholarPubMed
Hekman, M., Bauer, P. H., Sohlemann, P. & Lohse, M. J. (1994) Phosducin inhibits receptor phosphorylation by the β-adrenergic receptor kinase in a PKA-regulated manner. FEBS Letters 343:120–24. [BMW]10.1016/0014-5793(94)80302-1CrossRefGoogle Scholar
Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E. & Downing, K. H. (1990) Model for the structure of baeteriorhodopsin based on high-resolution electron cryomicroscopy. Journal of Molecular Biology 213:899–929. [aPAH, EAD. RMG]10.1016/S0022-2836(05)80271-2CrossRefGoogle Scholar
Henderson, R. & Unwin, P. N. T. (1975) Three-dimensional model of purple membrane obtained by electron microscopy. Nature (London) 275:28–32. [RMG]Google Scholar
Hermolin, J., Karell, M. A., Hamm, H. E. & Bownds, M. D. (1982) Calcium and cyclic GMP regulation of light-sensitive protein phosphorylation in frog photoreceptor membranes. Journal of General Physiology 79:633–55. [aMDB]10.1085/jgp.79.4.633CrossRefGoogle ScholarPubMed
Hidaka, H. & Okazaki, K. (1993) Neurocalcin family: A novel calcium-binding protein abundant in bovine central nervous system. Neuroscience Research 16:73–77. [KT]10.1016/0168-0102(93)90074-ZCrossRefGoogle ScholarPubMed
Hille, B. (1992) Ionic channels of excitable membranes, 2d ed. Sinauer. [TWA]Google Scholar
Hodgkin, A. L., McNaughton, P. A. & Nunn, B. J. (1985) The ionic selectivity and calcium dependence of the light-sensitive pathway in toad rods. Journal of Physiology 358:447–68. [aRSM]10.1113/jphysiol.1985.sp015561CrossRefGoogle ScholarPubMed
Hodgkin, A. L. & Nunn, B. J. (1988) Control of light-sensitive current in salamander rods. Journal of Physiology (London) 403:439–71. [aMDB]10.1113/jphysiol.1988.sp017258CrossRefGoogle ScholarPubMed
Hofmann, K. P. (1986) Photoproducts of rhodopsin in the disc membrane. Photochemistry & Photobiophysics 13:309–27. [aPAH]Google Scholar
Hofmann, K. P., Pulvermuller, A., Buczylko, J., Van Hooser, P. & Palczewski, K. (1992) The role of arrestin and retinoids in the regeneration pathway of rhodopsin. Journal of Biological Chemistry 267:15701–6. [aMDB, RKC]10.1016/S0021-9258(19)49592-6CrossRefGoogle ScholarPubMed
Hong, K. & Hubbell, W. L. (1973) Lipid requirements for rhodopsin regenerability. Biochemistry 12:4517–23. [aPAH]10.1021/bi00746a033CrossRefGoogle ScholarPubMed
Hopkins, W. F. & Johnston, D. (1988) Noradrenergic enhancement of long-term potentiation at mossy fiber synapses in the hippocampus. Journal of Neurophysiology 59:667–87. [aZX]10.1152/jn.1988.59.2.667CrossRefGoogle ScholarPubMed
Horn, M., Humphries, P., Kunisch, M., Marchese, C., Apfelstedt-Sylla, E., Fugi, L., Zrenner, E., Kenna, P., Gal, A. & Farrar, J. (1992) Deletions in exon 5 of the human rhodopsin gene causing a shift in reading frame and autosomal dominant retinitis pigmentosa. Human Genetics 90:255–57. [aSPD]10.1007/BF00220073CrossRefGoogle ScholarPubMed
Hotta, Y., Shiono, T., Hakawa, M., Hashimoto, T., Kanai, A., Nakajima, A., Noro, M., Sakuma, T. & Fujiki, K. (1992) Molecular biological study of the rhodopsin gene in Japanese patients with autosomal dominant retinitis pigmentosa. Nippon Canka Gakkai Zasshi 96:237–42. [aSPD]Google ScholarPubMed
Hovmuller, S., Slaughter, M., Berriman, J., Karlsson, B., Weiss, H. & Leonard, K. (1983) Structural studies of cytochrome reductase: Improved membrane crystals of the enzyme complex and crystallization of a subcomplex. Journal of Molecular Biology 165:401–6. [aPAH]10.1016/S0022-2836(83)80264-2CrossRefGoogle Scholar
Hsu, Y.-T. & Molday, R. S. (1993) Modulation of the cGMP-gated channel of rod photoreceptor cells by calmodulin. Nature 361:76–79. [aMDB, aJBH, aZX, MPG-K, LWH, DDO]10.1038/361076a0CrossRefGoogle ScholarPubMed
Hsu, Y.-T. & Molday, R. S. (1994) Interaction of calmodulin with the cyclic GMP-gated channel of rod photoreceptor cells. Journal of Biological Chemistry 269:29765–70. [rRSM]10.1016/S0021-9258(18)43947-6CrossRefGoogle ScholarPubMed
Hu, S., Franklin, P. J., Wang, J., Ruiz Silva, B. E., Derguini, F. & Nakanishi, K. (1994) Unbleachable rhodopsin with an 11-cis-locked eightmembered ring retinal: The visual transduction process. Biochemistry 33:408–16. [aPAH]10.1021/bi00168a004CrossRefGoogle Scholar
Huang, P. C., Gaitan, A. E., Hao, Y., Petters, R. M. & Wong, F. (1993) Cellular interactions implicated in the mechanism of photoreceptor degeneration in transgenic mice expressing a mutant rhodopsin gene. Proceedings of the National Academy of Sciences USA 90:8484–88. [MWK]10.1073/pnas.90.18.8484CrossRefGoogle ScholarPubMed
Humphries, P., Farrar, G. J. & Kenna, P. (1993) Autosomal dominant retinitis pigmentosa: Molecular, genetic and clinical aspects. Progress in Retinal Research 12:231–45. [aSPD]10.1016/0278-4327(93)90011-HCrossRefGoogle Scholar
Humphries, P., Kenna, P. & Farrar, G. J. (1992) On the molecular genetics of retinitis pigmentosa. Science 256:804–8. [aSPD]10.1126/science.256.5058.804CrossRefGoogle ScholarPubMed
Hundal, S. P., Difrancesco, D., Mangoni, M., Grammar, W. J. & Conley, E. C. (1993) An iso form of the cGMP-gated retinal photoreceptor channel gene expressed in the sinoa trial node (pacemaker) region of rabbit heart. Biochemical Society Transcripts 21:119S. [aRSM]10.1042/bst021119sCrossRefGoogle Scholar
Hurley, J. B. (1992) Signal transduction enzymes of vertebrate photoreceptors. Journal of Bioenergetics and Biomembranes 24:219–26. [aMDB]10.1007/BF00762680CrossRefGoogle ScholarPubMed
Hurley, J. B., Dizhoor, A. M., Ray, S. & Stryer, L. (1993) Recovering role: Conclusion withdrawn. Science 260:740. [aMDB, aJBH]10.1126/science.8097896CrossRefGoogle Scholar
Hurley, J. B. & Stryer, L. (1982) Purification and characterization of the gamma regulatory subunit of the cGMP phosphodiesterase from retinal rod outer segments. Journal of Biological Chemistry 257:11094–99. [aMDB]10.1016/S0021-9258(18)33937-1CrossRefGoogle Scholar
Hurwitz, R. & Holcombe, V. (1991) Affinity purification of the photoreceptor cGMP- gated cation channel. Journal of Biological Chemistry 266:7975–77. [aRSM, RLH, TGW]10.1016/S0021-9258(18)92925-XCrossRefGoogle ScholarPubMed
Illing, M., Colville, D. A., Williams, A. J. & Molday, R. S. (1994) Sequencing, cloning and characterization of the cyclic nucleotide-gated channel complex of rod outer segments. Investigative Ophthalmology and Visual Science [Abstract 1022] 35:1474. [rRSM]Google Scholar
Impey, S., Wayman, G., Wu, Z. & Storm, D. R. (in press) The type I adenylyl cyclase functions as a coincidence detector for control of CRE-mediated transcription by Ca2+ and isoproterenol. Molecular and Cellular Biology.Google Scholar
Inglehearn, C. F., Bashir, R., Lester, D. H., Jay, M., Bird, A. C. & Bhattacharya, S. S. (1991) A 3-bp deletion in the rhodopsin gene in a family with autosomal dominant retinitis pigmentosa. American Journal of Human Genetics 48:26–30. [aSPD]Google Scholar
Inglehearn, C. F., Carter, S. A., Keen, T. J., Lindsey, J., Stephenson, A. M., Bashir, R., Al-Maghtheh, M., Moore, A. T., Jay, M., Bird, A. C. & Bhattacharya, S. S. (1993) A new locus for autosomal dominant retinitis pigmentosa (adRP) on chromosome 7p. Nature Genetics 4:51–53. [aSPD]10.1038/ng0593-51CrossRefGoogle ScholarPubMed
Inglehearn, C. F., Keen, T. J., Bashir, R., Jay, M., Fitzke, F., Bird, A. C., Crombie, A. & Bhattacharya, S. S. (1992) A complete screen for mutations of the rhodopsin gene in a panel of patients with autosomal dominant retinitis pigmentosa. Human Molecular Genetics 1:41–45. [aSPD]10.1093/hmg/1.1.41CrossRefGoogle Scholar
Inglese, J., Freedman, N. J., Koch, W. J. & Lefkowitz, R. J. (1993) Structure and mechanism of the G protein-coupled receptor kinases. Journal of Biological Chemistry 268:23735–38. [KT]10.1016/S0021-9258(20)80439-6CrossRefGoogle ScholarPubMed
Ishikawa, Y., Katsushika, S., Chen, L., Halnon, N. J., Kawabe, J. & Homey, C. J. (1992) Isolation and characterization of a novel cardiac adenylyl cyclase cDNA. Journal of Biological Chemistry 267:13553–57. [aZX]10.1016/S0021-9258(18)42247-8CrossRefGoogle Scholar
Ito, M., Kodama, A., Tsukida, K., Fukada, Y., Shichida, Y. & Yoshizawa, T. (1982) A novel rhodopsin analogue possessing the cyclopentatrienylidene structure as the 11-cis-locked and the full planar chromophore. Chemical & Pharmaceutical Bulletin 30:1913–16. [aPAH]10.1248/cpb.30.1913CrossRefGoogle Scholar
Itoh, S., Takshima, A. & Macda, Y. (1992) Protective effect of cerulein on memory impairment induced by protein synthesis inhibitors in rats. Peptides 13:1007–12. [EDR]10.1016/0196-9781(92)90063-9CrossRefGoogle ScholarPubMed
Jacobowitz, O., Chen, J., Premont, R. T. & Iyengar, R. (1993) Stimulation of specific types of Gs-stimulated adenylyl cyclases by phorbol ester treatment. Journal of Biological Chemistry 268:3829–32. [aZX]10.1016/S0021-9258(18)53547-XCrossRefGoogle ScholarPubMed
Jacobson, F. A. S. & Baseom, G. I. (1993) Phosducin as a candidate gene for retinitis pigmentosa and Usher syndrome type H. InvestigativeOphthalmology and Visual Science 34:1458. [aSPD]Google Scholar
Jacobson, S. G., Kemp, C. M., Cideciyan, A. V., Macke, J. P., Sung, C.-H. & Nathans, J. (1994) Phenotypes of stop codon and splice site rhodopsin mutations causing retinitis pigmentosa. Investigative Ophthalmology and Visual Science 35:2521–34. [aSPD, AB]Google ScholarPubMed
Jacobson, S. G., Kemp, C. M., Sung, C.-H. & Nathans, J. (1991) Retinal function and rhodopsin levels in autosomal dominant retinitis pigmentosa with rhodopsin mutations. American Journal of Ophthalmology 112:256–71. [aSPD]10.1016/S0002-9394(14)76726-1CrossRefGoogle ScholarPubMed
Jan, L. Y. & Jan, Y. N. (1989) Voltage-sensitive ion channels. Cell 56:13–25. [aRSM]10.1016/0092-8674(89)90979-3CrossRefGoogle ScholarPubMed
Jan, L. Y. & Jan, Y. N. (1990) A superfamily of ion channels. Nature 345:672. [aRSM]10.1038/345672a0CrossRefGoogle ScholarPubMed
Jansen, J. J. M., Mulder, W. R., De Caluw, G. L. J., Vlak, J. M. & DeGrip, W. J. (1991) In vitro expression of bovine opsin using recombinant baculovirus: The role of glutamic acid (134) in opsin biosynthesis and glycosylation. Biochimica et Biophysica Acta 1089:68–76. [aPAH]10.1016/0167-4781(91)90086-2CrossRefGoogle ScholarPubMed
Jin, J., Crouch, R. K., Corson, D. W., Katz, B. M., MacNichol, E. F. & Cornwall, M. C. (1993) Noncovalent occupancy of the retinal-binding pocket of opsin diminishes bleaching adaptation of retinal cones. Neuron 11:513–22. [aMDB, RKC]10.1016/0896-6273(93)90155-KCrossRefGoogle ScholarPubMed
Johnson, R. S., Ohguro, H., Palczewski, K., Hurley, J. B., Walsh, K. A. & Neubert, T. A. (1994) Heterogeneous N-acylation is a tissue- and speciesspecific posttranshitional modification. Journal of Biological Chemistry 269:21067–71. [KS]10.1016/S0021-9258(17)31930-0CrossRefGoogle Scholar
Jones, G. J., Crouch, R. K., Wiggcrt, B., Cornwall, M. C. & Ghader, G. J. (1989) Retinoid requirements for recovery of sensitivity after visual pigment bleaching in isolated photoreccptors. Proceedings of the National Academy of Sciences USA 86:9606–10. [RKC]10.1073/pnas.86.23.9606CrossRefGoogle Scholar
Jordan, S. A., Farrar, C. J., Kenna, P., Humphries, N. M., Shells, D. M., Kumar-Singh, R., Sharp, E. M., Ayuso, C., Benitez, J. & Humphries, P. (1993) Localization of an autosomal dominant retinitis pigmentosa gene to chromosome 7q. Nature Cenctics 4:54–58. [aSPD]10.1038/ng0593-54CrossRefGoogle ScholarPubMed
Jordan, S. A., Farrar, G. J., Kumar-Singh, R., Kenna, P., Humphries, M. M., Allamand, V., Sharp, E. M. & Humphries, P. (1992) Autosomal dominant retinitis pigmentosa (adRP; RP6): Cosegregation of RP6 and the peripherin-RDS locus in a late-onset family of Irish origin. American Journal of Human Genetics 50:634–39. [aSPD]Google Scholar
Kanng, B. K., Kandel, E. R. & Grant, S. G. (1993) Activation of cAMP-responsive genes by stimuli that produce long-term facilitation in Aplysia sensory neurons. Neuron 10:427–35. [aZX]10.1016/0896-6273(93)90331-KCrossRefGoogle Scholar
Kahlert, M. & Hofmann, K.-P. (1991) Reaction rate and collisioal efficiency of the rhodopsin-transducin system in intact retinal rods. Biophysical Journal 59:375–86. [KWK]10.1016/S0006-3495(91)82231-7CrossRefGoogle ScholarPubMed
Kahlert, M., Pepperberg, D. R. & Hofmann, K. P. (1990) Effect of bleached rhodopsin on signal amplification in rod visual receptors. Nature 345:537–39. [aMDB]10.1038/345537a0CrossRefGoogle ScholarPubMed
Kajimoto, Y., Shirai, Y., Mukai, H., Kuno, T. & Tanaka, C. (1993) Molecular cloning of two additional members of the neural visinin-like Ca2+- binding protein gene family. Journal of Neurochemistry 61:1091–96. [KT]10.1111/j.1471-4159.1993.tb03624.xCrossRefGoogle Scholar
Kajiwara, K., Berson, E. L. & Dryja, T. P. (1994) Digenic retinitis pigmentosa due to mutations at the unlinked pheripherin/RDS and ROM-1 loci. Science 264:1604–8. [aSPD, AB]10.1126/science.8202715CrossRefGoogle Scholar
Kajiwara, K., Huhn, L. B., Mukai, S., Travis, G. H., Berson, E. L. & Dryja, T. P. (1991) Mutations in the human retinal degeneration slow gene in autosomal dominant retinitis pigmentosa. Nature 354:480–3. [aSPD]10.1038/354480a0CrossRefGoogle ScholarPubMed
Kajiwara, K., Sandberg, M. A., Berson, E. L. & Dryja, T. P. (1993) A null mutation in the human periphcrin/RDS gene in a family with autosomal dominant retinitis punctata albescens. Nature Genetics 3:208–12. [aSPD]10.1038/ng0393-208CrossRefGoogle Scholar
Kandel, E. R., Abrams, T., Bernier, L., Caruw, T. J., Hawkins, R. D. & Schwartz, J. H. (1983) Classical conditioning and sensitization share aspects of the same molecular cascade in Aplysia. Cold Spring Harbor Symposium on Quantitative Biology 2:821–30. [TWA]10.1101/SQB.1983.048.01.085CrossRefGoogle Scholar
Kandel, E. R. & Schwartz, J. H. (1982) Molecular biology of learning: Modulation of transmitter release. Science 218:433–43. [aZX, TWA]10.1126/science.6289442CrossRefGoogle ScholarPubMed
Kaplan, J., Gerber, S., Bonneau, D., Rozet, J., Briard, M., Dufler, J., Munnich, A. & Frezal, J. (1991) Probable location of Usher type I gene on chromosome 14q by linkage with D14S13 (MLJ14 probe). Cytogenetics and Cell Genetics 58:1988. [aSPD]Google Scholar
Karnik, S. S. & Khorana, H. C. (1990) Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187. Journal of Biological Chemistry 265:17520–24. [aSPD]10.1016/S0021-9258(18)38195-XCrossRefGoogle ScholarPubMed
Kauer, J. A., Malenka, R. C. & Nicoll, R. A. (1988) NMDA application potentiates synaptic transmission in the hippocampus. Nature 334:250–52. [aZX]10.1038/334250a0CrossRefGoogle ScholarPubMed
Kaupp, U. B. (1991) The cyclic nucleotide-gated channels of vertebrate photoreccptors and olfactory epithelium. Trends in Neuroscience 14:150–57. [aRSM, DDO]10.1016/0166-2236(91)90087-BCrossRefGoogle ScholarPubMed
Kaupp, U. B. & Koch, K.-W. (1992) Role of cCMP and Ca2+ in vertebrate photoreceptor excitation and adaptation. Annual Review of Physiology 54:153–75. [aMDB, aRSM]10.1146/annurev.ph.54.030192.001101CrossRefGoogle Scholar
Kaupp, U. B., Niidoine, T., Tanabe, T., Terada, S., Bönigk, W., Stuhmer, W., Cook, N. J., Kangawa, K., Matsuo, H., Hirose, T., Miyata, T. & Numa, S. (1989) Primary structure and functional expression from complementary DNA of the rod photoreceptor cyclic GMP-gated channel. Nature 342:762–66. [aRSM, LWH, TGW]CrossRefGoogle ScholarPubMed
Kawaniura, S. (1983) Involvement of ATP in activation and inactivation sequence of phosphodicsterase in frog rod outer segments. Biochimica Biophysica Acta 732:276–81. [SK]10.1016/0005-2736(83)90212-2CrossRefGoogle Scholar
Kawaniura, S. (1992) Light-sensitivity modulating protein in frog rods. Photochemistry and Photohiology. 56:1173–80. [SK]10.1111/j.1751-1097.1992.tb09742.xCrossRefGoogle Scholar
Kawaniura, S. (1993) Rhodopsin phosphorylation as a mechanism of cyclic GMP phosphodiesterase regulation by S-modulin. Nature 362:855–57. [aMDB, aJBH, aRSM, SK, KT, AY]10.1038/362855a0CrossRefGoogle Scholar
Kawaniura, S. (1994) Photoreceptor light-adaptation mediated by S-modulin, a member of a possible regulatory protein family of protein phosphorylation in signal transduction. Neuroscience Research 20:293–98. [SK, KT]10.1016/0168-0102(94)90050-7CrossRefGoogle Scholar
Kawamura, S. & Bownds, M. D. (1981) Light adaptation of the cyclic GMP phosphodiesterase of frog photoreceptor membranes mediated by ATP and calcium ions. Journal of General Physiology 77:571–91. [aMDB]10.1085/jgp.77.5.571CrossRefGoogle Scholar
Kawamura, S., Cox, J. A. & Nef, P. (1994) Inhibition of rhodopsin phosphorylation by non-myristoylated recombinated recoverin. Biochemical and Biophysical Research Communications 203:121–27. [SK]10.1006/bbrc.1994.2157CrossRefGoogle Scholar
Kawamura, S., Hisatomi, O., Kayada, S., Tokunaga, F. & Kuo, C. H. (1993) Recoverin has S-modulin activity in frog rods. Journal of Biological Chemistry 268:14579–82. [aJBH, KT, AY]10.1016/S0021-9258(18)82369-9CrossRefGoogle ScholarPubMed
Kawamura, S. & Murakami, M. (1991) Calcium-dependent regulation of cyclic GMP phosphodiesterase by a protein from frog retinal rods. Nature 349:420–23. [aMDB, aJBH, JFM, SK, ASP, KT, AY]10.1038/349420a0CrossRefGoogle ScholarPubMed
Kawamura, S., Takamatsu, K. & Kitamura, K. (1992) Purification and characterization of S-modulin, a calcium-dependent regulator on cGMP phosphodiesterase in frog rod photoreceptors. Biochemical and Biophysical Research Communications 186:411–17. [aMDB, SK]10.1016/S0006-291X(05)80823-XCrossRefGoogle ScholarPubMed
Keen, T. J., Inglehearn, C. F., Lester, D. H., Bashir, R., Jay, M., Bird, A. C., Jay, B. & Bhattacharya, S. S. (1994) Autosomal dominant retinitis pigmentosa: Four new mutations in rhodopsin, one of them in the retinal attachment site. Genomics 11:199–205. [aSPD]10.1016/0888-7543(91)90119-YCrossRefGoogle Scholar
Khan, S. M. A., Bolen, W., Hargrave, P. A., Santoro, M. M. & McDowell, J. H. (1991) Differential scanning calorimetry of bovine rhodópsin in rod outer segment disk membranes. European Journal of Biochemisty 200:53–59. [aPAH]10.1111/j.1432-1033.1991.tb21047.xCrossRefGoogle ScholarPubMed
Khorana, H. G. (1992) Rhodopsin, photoreceptor of the rod cell: An emerging pattern for structure and function. Journal of Biological Chemistry 267:1–4. [aMDB, aPAH]10.1016/S0021-9258(18)48444-XCrossRefGoogle ScholarPubMed
Kim, R. Y., Al-Maghtheh, M., Fitzke, F. W., Arden, G. B., Jay, M., Bhattacharya, S. S. & Bird, A. C. (1993) Dominant retinitis pigmentosa associated with two rhodopsin gene mutations. Leu-40-Arg and an insertion disrupting the 5'-splice junction of exon 5. Archives of Ophthalmology 111:1518–24. [aSPD]10.1001/archopht.1993.01090110084030CrossRefGoogle Scholar
Kimberling, W. J., Moller, C. G., Davenport, S., Priluck, A., Beighton, P. H., Greenberg, J., Reardon, W., Weston, M. D., Kenyon, J. B., Grunkemeyer, J. A., Dahl, S. P., Overbeck, L. D., Blackwood, D. J., Brower, A. M., Hoover, D. M., Rowland, P. & Smith, R. J. H. (1992) Linkage of Usher syndrome type I gene (USH1B) to the long arm of chromosome 11. Genomics 14:988–94. [aSPD]10.1016/S0888-7543(05)80121-1CrossRefGoogle Scholar
Kimberling, W. J., Weston, M. D., Moller, C., Davenport, S. L. H., Shugart, Y. Y., Priluck, I. A., Martini, A., Milani, M. & Smith, R. J. (1990) Localization of Usher syndrome type II to chromosome lq. Genomics 7:245–49. [aSPD]10.1016/0888-7543(90)90546-7CrossRefGoogle Scholar
Kjelsberg, M. A., Cotecchia, S., Ostrowski, J., Caron, M. G. & Lelkowitz, R. J. (1992) Constitutive activation of the alpha-lB-adrenergic receptor by all amino acid substitutions at a single site: Evidence for a region which constrains receptor activation. Journal of Biological Chemistry 267:1430–33. [aPAH]10.1016/S0021-9258(18)45962-5CrossRefGoogle Scholar
Klann, E., Chen, S.-J. & Sweatt, J. D. (1991) Persistent protein kinase activation in the maintenance phase of long-term potentiation. Journal of Biological Chemistry 266:24253–56. [EDR]10.1016/S0021-9258(18)54221-6CrossRefGoogle ScholarPubMed
Klann, E., Chen, S.-J. & Sweatt, J. D. (1992) Increased phosphorylation of a 17-kDa protein kinase C substrate in long-term potentiation. Journal of Neurochemistry 58:1576–79. [EDR]10.1111/j.1471-4159.1992.tb11382.xCrossRefGoogle ScholarPubMed
Klann, E., Chen, S.-J. & Sweatt, J. D. (1993) Mechanism of protein kinase C activation during the induction and maintenance of long-term potentiation probe using a selective peptide substrate. Proceedings of the National Academy of Sciences USA 90:8337–41. [EDR]10.1073/pnas.90.18.8337CrossRefGoogle Scholar
Klausner, R. D. & Sitia, R. (1990) Protein degradation in the endoplasmic reticulum. Cell 62:611–14. [aSPD]10.1016/0092-8674(90)90104-MCrossRefGoogle ScholarPubMed
Knowles, J. A., Shugart, Y., Banerjee, P., Gilliam, T. C., Lewis, C. A., Jacobson, S. G. & Ott, J. (1994) Identification of a locus, distinct from RDS-peripherin, for autosomal recessive retinitis pigmeutosa on chromosome 6p. Human Molecular Genetics 3:1401–3. [rSPD]10.1093/hmg/3.8.1401CrossRefGoogle ScholarPubMed
Kobayashi, M., Takamatsu, K., Saitoh, S. & Noguchi, T. (1993) Myristoylation of hippocalcin is linked to its calcium-dependent membrane association properties. Journal of Biological Chemistry 268:18898–904. [KT]10.1016/S0021-9258(17)46711-1CrossRefGoogle ScholarPubMed
Kobayashi, M., Takamatsu, K., Saitoh, S., Miura, M. & Noguchi, T. (1992) Molecular cloning of hippocalcin, a novel calcium-binding protein of the recoverin family exclusively expressed in hippocampus. Biochemical and Biophysical Research Communications 189:511–17. [aJBH, KT]10.1016/0006-291X(92)91587-GCrossRefGoogle ScholarPubMed
Koch, K.-W. (1991) Purification and identification of photoreeeptor guanylate cyclase. Journal of Biological Chemistry 266:8634–37. [KWK]10.1016/S0021-9258(18)93021-8CrossRefGoogle ScholarPubMed
Koch, K.-W. (1992) Biochemical mechanism of light adaptation in vertebrate photoreceptors. Trends in Biochemical Science 17:307–11. [aMDB]10.1016/0968-0004(92)90442-CCrossRefGoogle ScholarPubMed
Koch, K.-W. (1994) Calcium as modulator of phototransduction in vertebrate photoreceptor cells. Reviews of Physiology, Biochemistry and Pharmacology 125:149–92. [KWK]Google ScholarPubMed
Koch, K.-W., Eckstein, F. & Stryer, L. (1990) Stereochemical course of the reaction catalyzed by guanylate cyclase from bovine retinal rod outer segments. Journal of Biological Chemistry 265:9659–63. [KWK]10.1016/S0021-9258(19)38720-4CrossRefGoogle ScholarPubMed
Koch, K.-W. & Kaupp, U. B. (1985) Cyclic GMP directly regulates a cationic conductance in membranes of bovine rods by a cooperative mechanism. Journal of Biological Chemistry 260:6788–6800. [aRSM, TGW]10.1016/S0021-9258(18)88849-4CrossRefGoogle ScholarPubMed
Koch, K.-W. & Stryer, L. (1988) Highly cooperative feedback control of retinal rod guanylate cyclase by calcium ions. Nature 334:64–66. [arMDB, aJBH, aRSM]10.1038/334064a0CrossRefGoogle ScholarPubMed
Kohn, H. (1980) Light-and GTP-regulated interaction of CTPase and other proteins with bovine photoreceptor membranes. Nature 283:587–89. [aPAH]10.1038/283587a0CrossRefGoogle Scholar
Kohn, H. & McDowell, J. H. (1977) Isoelectric focusing of phosphorylated cattle rhodopsin. Biophysics of Structure and Mechanism 3:199–203. [aPAH]10.1007/BF00535820CrossRefGoogle Scholar
Kohnken, R. E., Chafouleas, J. G., Eadie, D. M., Means, A. R. & McConnell, D. G. (1981) Calmodulin in bovine rod outer segments. Journal of Biological Chemistry 256:12517–22. [aRSM]10.1016/S0021-9258(18)43305-4CrossRefGoogle ScholarPubMed
Kokame, K., Fukada, Y., Yoshizawa, T., Takao, T. & Shimonishi, Y. (1992) Lipid modification at the N terminus of photoreceptor G-protein α-subunit. Nature 359:749–52. [KS]10.1038/359749a0CrossRefGoogle Scholar
Konig, B., Arendt, A., McDowell, J. H., Kahlert, M., Hargrave, P. A. & Hofmann, K. P. (1989) Three cytoplasmic loops of rhodopsin interact with transducin. Proceedings of the National Academy of Sciences USA 86:6878–82. [aSPD, aPAH, EAD]10.1073/pnas.86.18.6878CrossRefGoogle ScholarPubMed
Korenbrot, J. I., Brown, D. T. & Cone, R. A. (1973) Membrane characteristics and osmotic behavior of isolated rod outer segments. Journal of Cell Biology 56:389–98. [aMDB]10.1083/jcb.56.2.389CrossRefGoogle ScholarPubMed
Koutalos, Y., Nakatani, L. & Yau, K.-W. (1994) Modulation of the cGMP-gated channel of retinal rods by Ca2+. Investigative Ophthalmology and Visual Science [Abstract 1023] 35:1474. [HRM, rRSM]Google Scholar
Koutalos, Y. & Yau, K.-W. (1993) A rich complexity emerges in phototransduction. Current Opinion in Neurobiology 3:513–19. [aMDB]10.1016/0959-4388(93)90049-5CrossRefGoogle ScholarPubMed
Kramer, R. H. & Siegelbaum, S. A. (1992) Intracellular Ca2+ regulates the sensitivity of cyclic nucleotide-gated channels in olfactory receptor neurons. Neuron 9:897–906. [aRSM, MSS]10.1016/0896-6273(92)90242-6CrossRefGoogle ScholarPubMed
Kranich, H., Bartkowski, S., Denton, M. J., Krey, S., Dickinson, P., Duvigneau, C. & Gal, A. (1993) Autosotnal dominant “sector” retinitis pigmentosa due to a point mutation predicting an Asn-15-Ser substitution of rhodopsin. Human Molecular Genetics 2:813–14. [aSPD]10.1093/hmg/2.6.813CrossRefGoogle ScholarPubMed
Krebs, E. G. & Beavo, J. A (1979) Phosphorylation-dephosphorylation of enzymes. Annual Review of Biochemistry 48:923–59. [aZX]10.1146/annurev.bi.48.070179.004423CrossRefGoogle ScholarPubMed
Kremer, H., Pinckers, A., van den Helm, B., Deutman, A. F., Ropers, H. H. & Mariman, E. C. M. (1994) Localization of the gene for dominant cystoid macular dystrophy on chromosome 7p. Human Molecular Genetics 3:299–302. [aSPD]10.1093/hmg/3.2.299CrossRefGoogle ScholarPubMed
Krug, M., Lossner, B. & Ott, T. (1984) Anisomycin blocks the late phase of long-term potentiation in the dentate gyrus of freely moving rats. Brain Research Bulletin 13:39–42. [aZX]10.1016/0361-9230(84)90005-4CrossRefGoogle ScholarPubMed
Krupinski, J., Coussen, F., Bakalyar, H. A., Tang, W. J., Feinstein, P. G., Orth, K., Slaughter, C., Reed, R. R. & Gilman, A. G. (1989) Adenylyl cyclase amino acid sequence: Possible channel- or transporter-like structure. Science 244:1558–64. [aZX]10.1126/science.2472670CrossRefGoogle ScholarPubMed
Krupnick, J. G., Gurevich, V. V., Schepers, T., Hamm, H. E. & Benovic, J. L. (1994) Arrestin-rhodopsin interaction: Multi-site binding delineated by peptide inhibition. Journal of Biological Chemistry 269:3226–32. [ADA]10.1016/S0021-9258(17)41852-7CrossRefGoogle ScholarPubMed
Kühlbrandt, W. (1984) Three-dimensional structure of the light-harvesting chlorophyl a/b-protein complex. Nature 307:478–80. [aPAH]10.1038/307478a0CrossRefGoogle Scholar
Kühlbrandt, W. (1988) Three-dimensional crystallization of membrane proteins. Quarterly Reviews of Biophysics 21:429–77. [aPAH, RMG]10.1017/S0033583500004625CrossRefGoogle ScholarPubMed
Kühlbrandt, W. (1992) Two-dimensional crystallization of membrane proteins. Quarterly Reviews of Biophysics 25:1–49. [aPAH, RMG]10.1017/S0033583500004716CrossRefGoogle ScholarPubMed
Kühlbrandt, W., Wang, D. N. & Fujiyoshi, Y. (1994) Atomic model of plant light-harvesting complex by electron crystallography. Nature 367:614–21. [aPAH, RMG]10.1038/367614a0CrossRefGoogle ScholarPubMed
Kuhn, H. (1980) Light- and CTP-regulated interaction of GTPase and other proteins with bovine photoreceptor membranes. Nature 283:587–89. [AY]10.1038/283587a0CrossRefGoogle Scholar
Kumar, V. D. & Weber, I. T. (1992) Molecular model of the cyclic GMP-binding domain of the cyclic GMP-gated ion channel. Biochemistry 31:4643–49. [RLB]10.1021/bi00134a015CrossRefGoogle ScholarPubMed
Kumar-Singh, R., Farrar, G. J., Mansergh, F., Kenna, P., Bhattacharya, S., Gal, S. & Humphries, P. (1993) Exclusion of the involvement of all known retinitis pigmentosa loci in the disease present in a family of Irish origin provides evidence for a sixth autosomal dominant locus (RP8). Human Molecular Genetics 2:875–78. [aSPD]10.1093/hmg/2.7.875CrossRefGoogle Scholar
Kure, S., Tominago, T., Yoshimoto, T., Tada, K. & Narisawa, K. (1991) Glutamate triggers internucleosomal DNA cleavage in neuronal cells. Biochemical and Biophysical Research Communications 179:39–45. [MT]10.1016/0006-291X(91)91330-FCrossRefGoogle ScholarPubMed
Kutuzov, M. & Pfister, C. (1994) Activation of the retinal cGMP-specific phosphodiesterase by the GDP-loaded α-subunit of transducin. European Journal of Biochemistry 220:963–71. [rMDB]10.1111/j.1432-1033.1994.tb18700.xCrossRefGoogle ScholarPubMed
Lagnado, L. & Baylor, D. (1992) Signal flow in visual transduction. Neuron 8:995–1002. [aMDB, aJBH]10.1016/0896-6273(92)90122-TCrossRefGoogle ScholarPubMed
Lagnado, L. & Baylor, D. (1994) Calcium controls light-triggered formation of catalytically active rhodopsin. Nature 367:273–77. [aMDB, RKC, MPG-K, SK, MSS, KT]10.1038/367273a0CrossRefGoogle ScholarPubMed
Lagnado, L., Cervetto, L. & McNaughton, P. (1992) Calcium homeostasis in the outer segment of retinal rods from the tiger salamander. Journal of Physiology (London) 455:111–42. [aMDB, KWK]10.1113/jphysiol.1992.sp019293CrossRefGoogle ScholarPubMed
Lagnado, L. & McNaughton, P. A. (1990) Electrogenic properties of the Na:Ca exchange. Journal of Membrane Biology 113:177–91. [PPMS]10.1007/BF01870070CrossRefGoogle ScholarPubMed
Lakshmi, K. V., Auger, M., Raap, J., Lugtenburg, J., Griffin, R. G., & Herzfeld, J. (1993) Solid-state 13C NMR rotational resonance distance measurement in the M photointermediate of bacteriorhodopsin: Determination of the configuration about the Schiff base. Biophysics Journal 64:A212. [SOS]Google Scholar
Lamb, T. D. (1984) Effects of temperature changes on toad rod photocurrents. Journal of Physiology (London) 346:557–78. [aMDB]10.1113/jphysiol.1984.sp015041CrossRefGoogle ScholarPubMed
Lamb, T. D. (1990) Dark adaptation: A re-examination. In: Night vision: Basic, clinical and applied aspects, ed. Hess, R. F., Sharp, L. T. & Nordby, K.. Cambridge University Press. [RKC]Google Scholar
Lamb, T. D., Matthews, H. R. & Torre, V. (1986) Incorporation of calcium buffers into salamander retinal rods: A rejection of the calcium hypothesis of phototransduction. Journal of Physiology (London) 372:315–49. [aMDB]10.1113/jphysiol.1986.sp016011CrossRefGoogle ScholarPubMed
Lamb, T. D., McNaughton, P. A. & Yau, K.-W. (1981) Spatial spread of activation and background desensitization in toad rod outer segments. Journal of Physiology (London) 319:463–96. [aMDB]10.1113/jphysiol.1981.sp013921CrossRefGoogle ScholarPubMed
Lamb, T. D. & Pugh, E. N. Jr (1992) A quantitative account of the activation steps involved in phototransduction in amphibian photoreceptors. Journal of Physiology (London) 449:719–58. [aMDB]10.1113/jphysiol.1992.sp019111CrossRefGoogle ScholarPubMed
Lamba, O. P., Borchman, D. & O'Brien, P. J. (1994) Fourier transform infrared study of the rod outer segment disk and plasma membranes of vertebrate retina. Biochemistry 33:1704–12. [ADA]10.1021/bi00173a012CrossRefGoogle ScholarPubMed
Lambrecht, H. G. & Koch, K.-W. (1991) A 26 kd calcium binding protein from bovine rod outer segments as modulator of photoreceptor guanylate cyclase. EMBO Journal 10:793–98. [aMDB, aJBH, ASP]10.1002/j.1460-2075.1991.tb08011.xCrossRefGoogle ScholarPubMed
Lambrecht, H. G. & Koch, K.-W. (1992) Recoverin, a novel calcium-binding protein from vertebrate photoreceptors. Biochimica et Biophysica Acta 1160:63–66. [aJBH]10.1016/0167-4838(92)90038-FCrossRefGoogle ScholarPubMed
Lambright, D. G., Noel, J. P., Hamm, H. E. & Sigler, P. B. (1994) Structural determinants for activation of the alpha subunit of a heterotrimeric G protein. Nature 369:621–28. [aMDB, EAD]10.1038/369621a0CrossRefGoogle ScholarPubMed
Lee, R. H., Brown, B. M. & Lolley, R. N. (1984) Light-induced dephosphorylation of a 33K protein in rod outer segments of rat retina. Biochemistry 23:1972–77. [BMW]10.1021/bi00304a014CrossRefGoogle ScholarPubMed
Lee, R. H., Brown, B. M. & Lolley, R. N. (1990) Protein kinase A phosphorylates retinal phosducin on serine 73 in situ. Journal of Biological Chemistry 265:15860–66. [BMW]10.1016/S0021-9258(18)55478-8CrossRefGoogle ScholarPubMed
Lee, R. H., Fowler, A., McCinnis, J. F., Lolley, R. N. & Craft, C. M. (1990a) Amino acid and cDNA sequence of bovine phosducin, a soluble phosphoprotein from photoreceptor cells. Journal of Biological Chemistry 265:15867–73. [aMDB]10.1016/S0021-9258(18)55479-XCrossRefGoogle ScholarPubMed
Lee, R. H., Lieberman, B. S. & Lolley, R. N. (1987) A novel complex from bovine visual cells of a 33,000-dalton phosphoprotein with beta and gamma transducin: Purification and subunit structure. Biochemistry 28:3983–90. [aMDB]10.1021/bi00387a036CrossRefGoogle Scholar
Lee, R. H., Lieberman, B. S. & Lolley, R. N. (1990b) Retinal accumulation of the phosducin/Tgamma and transducin complexes in developing normal mice and in mice and dogs with inherited retinal degeneration. Experimental Eye Research 51:325–33. [aMDB]10.1016/0014-4835(90)90029-TCrossRefGoogle Scholar
Lee, R. H., Ting, T. D., Lieberman, B. S., Tobias, D. E., Lolley, R. N. & Ho, Y.-K. (1992) Regulation of retinal cGMP cascade by phosducin in bovine rod photoreceptor cells. Journal of Biological Chemistry 267:25104–12. [BMW]10.1016/S0021-9258(19)74012-5CrossRefGoogle ScholarPubMed
Lee, R. H., Whelan, J. P., Lolley, R. N. & McGinnis, J. F. (1988) The photoreceptor-specific 33 kDa phosphoprotein of mammalian retina: Generation of monospecific antibodies and localization by immunocytochemistry. Experimental Eye Research 46:829–40. ]aMDB]10.1016/S0014-4835(88)80035-6CrossRefGoogle ScholarPubMed
Lee, S. M. & Bressler, R. (1981) Prevention of diabetic nephropathy by diet control in the db/db mouse. Diabetes 30:106–11. [DW]10.2337/diab.30.2.106CrossRefGoogle ScholarPubMed
Leibrock, C. S., Reuter, T. & Lamb, T. D. (1994) Dark adaptation of toad rod photorcceptors following small bleaches. Vision Research 34:2787–2800. [rMDB]10.1016/0042-6989(94)90048-5CrossRefGoogle ScholarPubMed
Lenz, S. E., Henschel, Y., Zopf, D., Voss, B. & Gundelfinger, E. D. (1992) VILIP, a cognate protein of the retinal calcium binding proteins visinin and recoverin, is expressed in the developing chicken brain. Brain Research 15:133–40. [aJBH]Google ScholarPubMed
Levin, L. R., Han, P. L., Hwang, P. M., Feinstein, P. C., Davis, R. L. & Reed, R. R. (1992) The Drosophila learning and memory gene rutabaga encodes a Ca2+/calmodulin-responsive adenylyl cyclase. Cell 68:479–89. [aZX, TWA]10.1016/0092-8674(92)90185-FCrossRefGoogle ScholarPubMed
Levine, M. A., Modi, W. S. & O'Brien, S. J. (1990) Chromosomal localization of the genes encoding two forms of the G protein β polypeptide, β1 and β3, in man. Genomics 8:380–86. [aSPD]10.1016/0888-7543(90)90296-7CrossRefGoogle Scholar
Lewis, R. A., Otterud, B., Stauffer, D., Lalouel, J.-M. & Leppert, M. (1990) Mapping recessive ophthalmic diseases: Linkage of the locus for Usher syndrome type III to a DNA marker on chromosome lq. Genomics 7:250–56. [aSPD]10.1016/0888-7543(90)90547-8CrossRefGoogle Scholar
Li, H., Volpp, K. & Applebury, M. L. (1990) Bovine cone photoreceptor cGMP phosphodiesterase structure deduced from a cDNA clone. Proceedings of the National Academy of Sciences USA 87:293–97. [aMDB]10.1073/pnas.87.1.293CrossRefGoogle ScholarPubMed
Liang, C.-J., Yamashita, K., Muellenberg, C. G., Shichi, H. & Kobata, A. (1979) Structure of the carbohydrate moieties of bovine rhodopsin. Journal of Biological Chemistry 254:6414–18. [aPAH]10.1016/S0021-9258(18)50382-3CrossRefGoogle ScholarPubMed
Liebman, P. A. & Entine, G. (1968) Visual pigments of frog and tadpole. Vision Research 8:761–75. [aMDB]10.1016/0042-6989(68)90128-4CrossRefGoogle ScholarPubMed
Liebman, P. A., Parker, K. R. & Dratz, E. A. (1987) The molecular mechanism of visual excitation and its relation to the structure and composition of the rod outer segment. Annual Review of Physiology 491:765–91. [aMDB, aPAH]10.1146/annurev.ph.49.030187.004001CrossRefGoogle Scholar
Liebman, P. A. & Pugh, E. N. (1979) The control of phosphodiesterase in rod disk membranes: Kinetics, possible mechanisms and significance for vision. Vision Research 19:375–80. [aMDB]10.1016/0042-6989(79)90097-XCrossRefGoogle ScholarPubMed
Liebman, P. A. & Pugh, E. N. (1980) ATP mediates rapid reversal of cyclic GMP phosphodiesterase activation in visual receptor membranes. Nature 287:734–37. [aMDB]10.1038/287734a0CrossRefGoogle ScholarPubMed
Light, D. B., Corbin, J. D. & Stanton, B. A. (1990) Dualion-channel regulation by cyclic GMP and cyclic GMP-dependent protein kinase. Nature 344:336–39. [aRSM]10.1038/344336a0CrossRefGoogle ScholarPubMed
Liman, E. R. & Buck, L. B. (1994) A second subunit of the olfactory cyclic nucleotide-gated channel confers high sensitivity to cAMP. Neuron 13:611–21. [rRSM]10.1016/0896-6273(94)90029-9CrossRefGoogle Scholar
Linden, D. J. & Routtceberg, A. (1989) The role of protein kinase C in longterm potentiation: A testable model. Brain Research Reviews 14:279–96. [aZX]10.1016/0165-0173(89)90004-0CrossRefGoogle Scholar
Litman, B. J. (1982) Purification of rhodopsin by concanavalin A affinity chromatography. Methods in Enzymology 81:150–53. [aPAH]10.1016/S0076-6879(82)81025-2CrossRefGoogle ScholarPubMed
Litman, B. J., Aton, B. & Hartley, J. B. (1982) Functional domains of rhodopsin. Vision Research 22:1439–42. [ADA]10.1016/0042-6989(82)90206-1CrossRefGoogle ScholarPubMed
Liu, M., Chen, T.-Y., Ahamed, B., Li, J. & Yau, K.-W. (1994) Calciumcalmodulin modulation of the olfactory cyclic nucleotide-gated cation channel. Science 266:1348–54. [rRSM]10.1126/science.266.5189.1348CrossRefGoogle Scholar
Liu, Y. L. & Storm, D. R. (1989) Dephosphorylation of neuromodulin by calcineurin. Journal of Biological Chemistry 264:12800–4. [aZX]10.1016/S0021-9258(18)51557-XCrossRefGoogle ScholarPubMed
Liu, Y. L. & Storm, D. R. (1990) Regulation of free calmodulin levels in neurons by neuromodulin: Relationship to neuron growth and regeneration. Trends in Pharmacological Sciences 11:107–11. [aZX]Google Scholar
Livingston, M. S. (1985) Genetic dissection of Drosophila adenylyl cyclase. Proceedings of the National Academy of Sciences USA 82:5992–96. [aZX]10.1073/pnas.82.17.5992CrossRefGoogle Scholar
Livingston, M. S., Sziber, P. P. & Quinn, W. G. (1984). Loss of calcium/calmodulin responsiveness in adenylyl cyclase of rutabaga, a Drosophila learning mutant. Cell 37:205–15. [aZX, TWA]10.1016/0092-8674(84)90316-7CrossRefGoogle Scholar
Lolley, R. N., Farber, D. B., Rayborn, M. E. & Hollyfield, J. G. (1977) Cyclic GMP accumulation causes degeneration of photoreceptor cells: Simulation of an inherited disease. Science 196:664–66. [aSPD]10.1126/science.193183CrossRefGoogle ScholarPubMed
Lolley, R. N., Rong, H. & Craft, C. M. (1994) Linkage of photoreceptor degeneration by apoptosis with inherited defect in phototransduction. Investigative Ophthalmology and Visual Science 35:358–62. [aSPD]Google ScholarPubMed
Ludwig, J., Marglit, T., Eismann, E., Lancet, D. & Kaupp, U. B. (1990) Primary structure of a cAMP-gated channel from bovine olfactory epithelium. FEBS Letters 270:24–29. [aRSM]10.1016/0014-5793(90)81226-ECrossRefGoogle ScholarPubMed
Lyness, A. L., Ernst, W., Quinlan, M. P., Clover, G. M., Arden, G. B., Carter, R. M., Bird, A. C. & Parker, J. A. (1985) A clinical, psychophysical and electroretinographic survey of patients with autosomal dominant retinitis pigmentosa. British Journal of Ophthalmology 69:326–39. [aSPD]10.1136/bjo.69.5.326CrossRefGoogle ScholarPubMed
Macke, J. P., Davenport, C. M., Jacobson, S. G., Hennessey, J. C., Gonzales-Fernandez, F., Conway, B. P., Heckenlively, J., Palmer, R., Maumenee, I. H., Sieving, P., Gouras, P., Good, W. & Nathans, J. (1993) Identification of novel rhodopsin mutations responsible for retinitis pigmentosa: Implications for the structure and function of rhodopsin. American Journal of Human Genetics 53:80–89. [aSPD]Google ScholarPubMed
Mackler, S. A., Brooks, B. P. & Eberwine, J. H. (1992) Stimulus-induced coordinate changes in mRNA abundance in single postsynaptic hippocampal CA1 neurons. Neuron 9:539–48. [EDR]10.1016/0896-6273(92)90191-FCrossRefGoogle ScholarPubMed
MacNicol, M. & Schulman, H. (1992) Cross-talk between protein kinase C and multifunctional Ca2+/calmodulin-dependent protein kinase. Journal of Biological Chemistry 267:12197–201. [aZX]10.1016/S0021-9258(19)49824-4CrossRefGoogle ScholarPubMed
Madison, D. V., Malenka, R. C. & Nicoll, R. A. (1991) Mechanisms underlying long-term potentiation of synaptic transmission. Annual Review of Neuroscience 14:379–97. [TWA]10.1146/annurev.ne.14.030191.002115CrossRefGoogle ScholarPubMed
Malenka, R. C., Kauer, J. A., Perkel, D. J., Mauk, M. D., Kelly, P. T., Nicoll, R. A. & Waxham, M. N. (1989) An essential role for postsynaptic calmodulin and protein kinase activity in long-term potentiation. Nature 340:554–57. [TWA]10.1038/340554a0CrossRefGoogle ScholarPubMed
Malenka, R. C., Kauer, J. A., Zucker, R. S. & Nicoll, R. A. (1988) Postsynaptic calcium is sufficient for potentiation of hippocampal synaptic transmission. Science 242:81–84. [aZX]10.1126/science.2845577CrossRefGoogle ScholarPubMed
Malinow, R., Schulman, H. & Tsien, R. W. (1989) Inhibition of postsynaptic PKC or CaMKII blocks induction but not expression of LTP. Science 245:862–66. [TWA]10.1126/science.2549638CrossRefGoogle Scholar
Mangels, L. A. & Gnegy, M. E. (1990) Muscarinic receptor mediated transolocation of calmodulin in SK-N-SH human neuroblastoma cells. Molecular Pharmacology 37:820–26. [aZX]Google Scholar
Mangini, N. J., Gamer, G. L., Okajima, T.-L. L., Donoso, L. A. & Pepperberg, D. R. (1994) Effect of hydroxylamine on the subcellular distribution of arrestin (S-antigen) in rod photoreceptors. Visual Neuroscience 11:561–68. [rMDB]10.1017/S0952523800002467CrossRefGoogle Scholar
Mangini, N. J. & Pepperberg, D. R. (1988) Immunolocalization of 48K in rod photoreceptors: Light and ATP increase OS labeling. Investigative Ophthamology and Visual Science 29:1221–34. [JFM]Google ScholarPubMed
Mariuzza, R. A., Phillips, S. E. V. & Poljak, R. J. (1987) The structural basis of antigen-antibody recognition. Annual Review of Biophysics and Biophysical Chemistry 16:139–59. [aPAH]10.1146/annurev.bb.16.060187.001035CrossRefGoogle ScholarPubMed
Massof, R. W. & Finkelstein, D. (1981) Two forms of autosomal dominant primary retinitis pigmentosa. Documenta Ophthalmologica 51:289–346. [aSPD]10.1007/BF00143336CrossRefGoogle ScholarPubMed
Matesic, D. & Liebman, P. A. (1987) cGMP-dependent cation channel of retinal rod outer segments. Nature 326:600–3. [uRSM]10.1038/326600a0CrossRefGoogle ScholarPubMed
Matsuoka, S., Nicoll, D. A., Reilly, R. F., Hilgemann, D. W. & Philipson, K. D. (1993) Initial localization of regulatory regions of the cardiac sarcolemmal Na+-Ca2+ exchanger. Proceedings of the National Academy of Sciences USA 90:3870–74. [PPMS]10.1073/pnas.90.9.3870CrossRefGoogle ScholarPubMed
Matthews, G. (1986) Spread of the light response along the rod outer segment: An estimate from patch-clamp recordings. Vision Research 26:535–41. [aMDB]10.1016/0042-6989(86)90002-7CrossRefGoogle ScholarPubMed
Matthews, H. R. (1992a) Effects of lowered cytoplasmic calcium concentration and light on the responses of rod photoreceptors isolated from the retina of the tiger salamander. Journal of Physiology 446:109 p.[HRM]Google Scholar
Matthews, H. R. (1992b) Inability of light to accelerate the dim flash response without lowered calcium concentration in rod photoreceptors isolated from the retina of the tiger salamander. Journal of Physiology 44:559 p.[HRM]Google Scholar
Matthews, H. R. (in press) Effects of lowered cytoplasmic calcium concentration and light on the responses of salamander rod photoreceptors. Journal of Physiology. [HRM]Google Scholar
Matthews, H. R., Murphy, R. L. W., Fain, G. L. & Lamb, T. D. (1988) Photoreceptor light adaptation is mediated by cytoplasmic calcium concentration. Nature 334:67–69. [aMDB, aRSM, KWK, HRM]10.1038/334067a0CrossRefGoogle ScholarPubMed
Matthies, H., Frey, U., Reymann, K., Krug, M., Jork, R. & Schroeder, H. (1990) Different mechanisms and multiple stages of LTP. Advances in Experimental Medical Biology 268:359–68. [aZX]10.1007/978-1-4684-5769-8_39CrossRefGoogle ScholarPubMed
May, D., Ross, E., Gilman, A. & Smigel, M. (1985). Reconstitution of catecholamine-stimulatcd adenylate cyclase activity using three purified proteins. Journal of Biological Chemistry 260:15829–33. [aZX]10.1016/S0021-9258(17)36333-0CrossRefGoogle ScholarPubMed
McCarthy, S. T., Younger, J. P. & Owen, W. G. (1993) Disc structure, buffering and kinetics of cytosolic free calcium in bullfrog rod outer segments. Investigative Ophthalmology and Visual Science 34:1327. [aMDB]Google Scholar
McCarthy, S. T., Younger, J. P. & Owen, W. G. (1994) Free calcium concentrations in bulfrog rods determined in the presence of multiple forms of Fura-2. Biophysics Journal 67:2076–89. [rMDB]10.1016/S0006-3495(94)80691-5CrossRefGoogle Scholar
McDowell, J. H. (1993) Preparing rod outer segment membranes, regenerating, and determining rhodopsin concentration. In: Photoreceptor cells, ed. Hargrave, P. A.. Academic Press. [aPAH]Google Scholar
McDowell, J. H., Khan, S. M. A., Bolen, D. W., Santoro, M. M. & Hargrave, P. A. (1992) Structural stability of rhodopsin and opsin studied by differential scanning calorimetry. In: Signal transduction in photoreceptor cells, ed. Hargrave, P. A., Hofmann, K. P. & Kaupp, U. B.. Springer-Verlag. [aPAH]Google Scholar
McDowell, J. H., Nawrocki, J. P. & Hargrave, P. A. (1993) Phosphorylation sites in bovine rhodopsin. Biochemistry 32:4968–74. [aMDB]10.1021/bi00069a036CrossRefGoogle ScholarPubMed
McFall-Ngai, M. J. & Horwitz, J. (1990) A comparative study of the thermal stability of the vertebrate eye lens: Antarctic ice fish to the desert iguana. Experimental Eye Research 50:703–9. [aPAH]10.1016/0014-4835(90)90117-DCrossRefGoogle Scholar
McGee, T. L., Berson, E. L. & Dryja, T. P. (1992) Search for point mutations in the interstitial retinoid binding protein gene in patients with hereditary retinal degenerations. Investigative Ophthalmology and Visual Science 33:1396. [aSPD]Google Scholar
McCee, T. L., Lin, D., Berson, E. L. & Dryja, T. P. (1994) Defects in the rod cGMP-gated gene in patients with retinits pigmentosa. Investigative Ophthalmology and Visual Science 35:1716. [aSPD]Google Scholar
McGinnis, J. F., Austin, B. J., Klisak, I., Heinzmann, C., Kojis, J., Sparkes, R. S., Bateman, B. J. & Lerious, V. (1995) Chromosomal assignment of the human gene for the cancer associated retinopathy protein (recoverin). Journal of Neuroscience Research 40:165–168. [JFM]10.1002/jnr.490400204CrossRefGoogle Scholar
McGinnis, J. F., Lerious, V., Pazik, J. & Elliott, R. W. (1993) Chromosomal assignment of the recoverin gene and cancer-associated retinopathy. Mammalian. Genome 4:43–45. [JFM]10.1007/BF00364662CrossRefGoogle ScholarPubMed
McGinnis, J. F. & Leveille, P. J. (1985) Soluble proteins associated with photoreceptor cell death in the rd mouse. Current Eye Research 4:1127–35. [JFM]10.3109/02713688509003359CrossRefGoogle ScholarPubMed
McGinnis, J. F., Stepanik, P. L., Baehr, W., Subbaraya, I. & Lerious, V. (1992a) Cloning and sequencing of the 23 kDa mouse photoreceptor cellspecific protein. FEBS Letters 302:172–76. [JFM]10.1016/0014-5793(92)80433-HCrossRefGoogle Scholar
McGinnis, J. F., Whelan, J. P. & Donoso, L. A. (1992b) Transient, cyclic changes in mouse visual cell gene products during the light-dark cycle. Journal of Neuroscience Research 31:584–90. [JFM]10.1002/jnr.490310325CrossRefGoogle ScholarPubMed
McGuire, R. E., Sullivan, L. S., Blanton, S. H., Church, M., Heckenlively, J. R. & Daiger, S. P. (in press) X-linked dominant cone-rod dystrophy: Linkage mapping of a new locus (CORD3) to Xp22.13—p22.11. American Journal of Human Genetics. [rSPD]Google Scholar
McKusick, V. A. (1994) Mendelian inheritance in man, 11th ed. The Johns Hopkins University Press. [arSPD]Google Scholar
McLaughlin, M. E., Sandberg, M. A., Berson, E. L. & Dryja, T. P. (1993) Recessive mutations in the gene encoding the β-subunit of rod phosphodiesterase in patients with retinitis pigmentosa. Nature Genetics 4:130–34. [aSPD]10.1038/ng0693-130CrossRefGoogle ScholarPubMed
McNaughton, P. A. (1990) Light response of vertebrate photoreceptors. Physiological Reviews 70:847–84. [aMDB]10.1152/physrev.1990.70.3.847CrossRefGoogle ScholarPubMed
McWilliams, P., Farrar, G. J., Kenna, P., Bradley, D. G., Humphries, M. M., Sharp, E. M., McConnell, D. J., Lawler, M., Shiels, D., Ryan, C., Stephens, K., Daiger, S. P. & Humphries, P. (1989) Autosomal dominant retinitis pigmentosa (ADRP): Localization of an ADRP gene to the long arm of chromosome 3. Genomics 5:619–22. [aSPD]10.1016/0888-7543(89)90031-1CrossRefGoogle Scholar
Michel, H. (1982) Characterization and crystal packing of three-dimension bacteriorhodopsin crystals. EMBO Journal 1:1267–71. [RMG]10.1002/j.1460-2075.1982.tb00023.xCrossRefGoogle Scholar
Michel, H. (1991) General and practical aspects of membrane protein crystallization. In: Crystallization of membrane proteins, ed. Michel, H.. CRC Press. [aPAH]Google Scholar
Michel, H. & Oesterhelt, D. (1980) Three-dimensional srystals of membrane proteins: Bacteriorhodopsin. Proceedings of the National Academy of Sciences USA 77:1283–85. [RMG]10.1073/pnas.77.3.1283CrossRefGoogle Scholar
Milam, A. H., Dacey, D. M. & Dizhoor, A. M. (1992) Recoverin immunoreactivity in mammalian cone bipolar cells. Visual Neuroscience 10:1–12. [aJBH]10.1017/S0952523800003175CrossRefGoogle Scholar
Miljanich, G. P., Brown, M. F., Mabry-Gaud, S., Dratz, E. A. & Sturtevant, J. M. (1985) Thermotropic behavior of retinal rod membranes and dispersions of extracted phospholipids. Journal of Membrane Biology 85:79–86. [aPAH]10.1007/BF01872007CrossRefGoogle ScholarPubMed
Miller, C. (1989) Genetic manipulation of ion channels: A new approach to structure and mechanism. Neuron 2:1195–1205. [aRSM]10.1016/0896-6273(89)90304-8CrossRefGoogle ScholarPubMed
Miller, C. (1991) Annus mirabilis of potassium channels. Science 252:1092–96. [aRSM]10.1126/science.252.5009.1092CrossRefGoogle ScholarPubMed
Miller, J. L., Fox, D. A. & Litman, B. J. (1986) Amplification of phosphodiesterase activation is greatly reduced by rhodopsin phosphorylation. Journal of Biological Chemistry 25:4983–88. [aMDB]Google ScholarPubMed
Miller, J. L. & Korenbrot, J. I. (1993) In retinal cones, membrane depolarization in darkness activates the cGMP-dependent conductance. Journal of General Physiology 101:933–61. [KWK]10.1085/jgp.101.6.933CrossRefGoogle ScholarPubMed
Miller, K. R. & Jacobs, J. S. (1983) Two-dimensional crystals formed from photosynthetic reaction centers. Journal of Cell Biology 97:1266–70. [aPAH]10.1083/jcb.97.4.1266CrossRefGoogle ScholarPubMed
Min, K. C., Zvyaga, T. A., Cypess, A. M. & Sakmar, T. P. (1993) Characterization of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa: Mutations on the cytoplasmic surface affect transducin activation. Journal of Biological Chemistry 268:9400–4. [aSPD]10.1016/S0021-9258(18)98364-XCrossRefGoogle ScholarPubMed
Minocherhomjee, A. M., Selfe, S., Flowers, N. W. & Storm, D. R. (1987) Interaction between the catalytic subunit of the calmodulin sensitive adenylate cyclase with [125I] and [125I] calcodulin. Biochemistry 26:4444–48. [aZX]10.1021/bi00388a038CrossRefGoogle Scholar
Mitchell, D. C., Straume, M. & Litman, B. J. (1992) Role of sn-1-saturated, sn-2-polyunsaaturated phospholipids in control of membrane receptor conformational equilibrium: Effects of cholesterol and acyl chain unsaturation on the metarhodopsin I—Metarhodopsin II equilibrium. Biochemistry 31:662–70. [aPAH]10.1021/bi00118a005CrossRefGoogle Scholar
Mitchell, D. C., Straume, M., Miller, J. L. & Litman, B. J. (1990) Modulation of metarhodopsin formation by cholesterol-induced ordering of bilayer lipids. Biochemistry 29:9143. [ADA]10.1021/bi00491a007CrossRefGoogle ScholarPubMed
Mitchell, P. J. & Tjian, R. (1989) Transcriptional regulation in mammalian cells by sequence specific DNA binding proteins. Science 245:371–78. [aZX]10.1126/science.2667136CrossRefGoogle ScholarPubMed
Moench, S. J., Terry, C. E. & Dewey, T. G. (1994) Fluorescence labeling of the palmitoylation sites of rhodopsin. Biochemistry 33:5783–89. [ADA]10.1021/bi00185a016CrossRefGoogle ScholarPubMed
Molday, L. L., Cook, N. J., Kaupp, U. B. & Molday, R. S. (1990) The cGMP gated cation channel of bovine rod photoreceptor cells is associated with a 240 kDa protein exhibiting immunochemical cross-reactivity with spectrin. Journal of Biological Chemistry 265:18690–95. [aRSM, TGW]10.1016/S0021-9258(17)44807-1CrossRefGoogle ScholarPubMed
Molday, R. S. (1989) Monoclonal antibodies to rhodopsin and other proteins of rod outer segments. Progress in Retinal Research 8:173–209. [aPAH]10.1016/0278-4327(88)90025-9CrossRefGoogle Scholar
Molday, R. S. & Molday, L. L. (1987) Differences in the protein composition of bovine retinal rod outer segment disk and plasma membranes isolated by a ricin-gold-dextran density perturbation method. Journal of Cell Biology 105:2589–2601. [TGW]10.1083/jcb.105.6.2589CrossRefGoogle ScholarPubMed
Molday, R. S., Molday, L. L., Dose, A., Clark-Lewis, I., Illing, M., Cook, N. J., Eismann, E. & Kaupp, U. B. (1991) The cGMP-gated channel of the rod photoreceptor cell: Characterization and orientation of the amino terminus. Journal of Biological Chemistry 266:21917–22. [aRSM, RLH]10.1016/S0021-9258(18)54724-4CrossRefGoogle ScholarPubMed
Molday, R. S., Reid, D. M., Connell, G. & Molday, L. L. (1992) Molecular properties of the cGMP-gated channel of rod photoreceptor cells as probed with monoclonal antibodies. In: Signal transduction in photoreceptor cells, ed. Hargrave, P. A., Hofmann, K. P. & Kaupp, U. B.. Springer-Verlag. [aRSM]Google Scholar
Mollner, S. & Pfeuffer, T. (1988) Two different adenylyl cyclases in brain distinguished by monoclonal antibodies. European Journal of Biochemistry 171:265–71. [aZX]10.1111/j.1432-1033.1988.tb13785.xCrossRefGoogle ScholarPubMed
Mollner, S., Simmoteit, R., Palm, D. & Pfeuffer, T. (1991) Monoclonal antibodies against various forms of the adenylyl cyclase catalytic subunit and associated proteins. European Journal of Biochemistry 195:281–86. [aZX]10.1111/j.1432-1033.1991.tb15704.xCrossRefGoogle ScholarPubMed
Montarolo, P. G., Goelet, P., Castellucci, V. F., Morgan, J., Kandel, E. R. & Schacher, S. (1986) A critical period for macromolecular synthesis in long-term heterosynaptic facilitation in Aplysia. Science 234:1249–54. [aZX]10.1126/science.3775383CrossRefGoogle ScholarPubMed
Moore, A. T., Fitzke, F. W., Kemp, C. M., Arden, C. B., Keen, T. J., Inglehearn, C. F., Bhattacharya, S. S. & Bird, A. C. (1992) Abnormal dark adaptation kinetics in autosomal dominant sector retinitis pigmentosa due to rhodopsin mutation. British Journal of Ophthalmology 76:465–69. [aSPD]10.1136/bjo.76.8.465CrossRefGoogle Scholar
Morris, R. G. (1990) Toward a representational hypothesis of the role of hippocampal synaptic plasticity in spatial and other forms of learning. Cold Spring Harbor Symposium on Quantative Biology 50:161–73. [aZX]10.1101/SQB.1990.055.01.019CrossRefGoogle Scholar
Morris, R. G., Anderson, E., Lynch, C. S. & Baudry, M. (1986) Selective impairment of learning and blockade of long-term potentiation by an N-methyl-D-aspartate receptor antagonist, AP5. Nature 319:774–76. [aZX]10.1038/319774a0CrossRefGoogle ScholarPubMed
Morris, R. G., Garrud, P., Rawlins, J. N. & O'Keefe, J. (1982) Place navigation impaired in rats with hippocampal lesions. Nature 297:681–83. [aZX]10.1038/297681a0CrossRefGoogle ScholarPubMed
Mullen, R. J., Eicher, E. M. & Sidman, R. L. (1976) Purkinje cell degeneration, a new neurological mutation in the mouse. Proceedings of the National Academy of Sciences USA 73:208–12. [MWK]10.1073/pnas.73.1.208CrossRefGoogle ScholarPubMed
Musarella, M. A. (1992) Gene mapping of ocular diseases. Survey of Ophthalmology 36:285–312. [aSPD]10.1016/0039-6257(92)90096-CCrossRefGoogle ScholarPubMed
Musarella, M. A., Anson-Cartwright, L., Leal, S. M., Gilbert, L. D., Worton, R. G., Fishman, G. A. & Ott, J. (1990) Multipoint linkage analysis and heterogeneity testing in 20 X-linked retinitis pigmentosa families. Genomics 8:286–96. [aSPD]10.1016/0888-7543(90)90284-2CrossRefGoogle ScholarPubMed
Naash, M. I., Hollyfield, J. G., Al-Ubaidi, M. R. & Baehr, W. (1993) Simulation of human autosomal dominant retinitis pigmentosa in transgenic mice expressing a mutated murine opsin gene. Proceedings of the national Academy of Sciences USA 90:5499–5503. [MWK]10.1073/pnas.90.12.5499CrossRefGoogle ScholarPubMed
Nairn, A. C., Hemmings, H. C. & Greengard, P. (1985) Protein kinases in the brain. Animal Review of Biochemistry 54:931–76. [aZX]10.1146/annurev.bi.54.070185.004435CrossRefGoogle Scholar
Nakamura, T. & Gold, G. H. (1987) A cyclic nucleotide-gated conductance in olfactory receptor cilia. Nature 325:342–44. [aRSM]10.1038/325442a0CrossRefGoogle ScholarPubMed
Nakano, A., Terasawa, M., Watanabe, M., Usuda, N., Morita, T. & Hidaka, H. (1992) Neurocalcin, a novel calcium binding protein with three EF-hand domains, expressed in retinal amacrine cells and ganglion cells. Biochem, Biophys, Res.Commun. 186:1207–11. [aJBH]10.1016/S0006-291X(05)81534-7CrossRefGoogle ScholarPubMed
Nakatani, K., Koutalos, Y. & Yau, K.-W. (1995) Ca+2 modultion of the cGMP-dated channel of bullfrog retinal rod photoreceptors. Journal of Physiology 484:1:69–76. [MPC-K]10.1113/jphysiol.1995.sp020648CrossRefGoogle Scholar
Nakatani, K., Tamura, T. & Yau, K.-W. (1991) Light adaptation in retinal rods of the rabbit and two other nonprimate mammals. Journal of General Physiology 97:413–35. [aMDB, KWK]10.1085/jgp.97.3.413CrossRefGoogle ScholarPubMed
Nakatani, K. & Yau, K.-W. (1988a) Calcium and light adaptation in retinal rods and cones. Nature 334:69–71. [aMDB, KWK, HRM]10.1038/334069a0CrossRefGoogle ScholarPubMed
Nakatani, K. & Yau, K.-W. (1988b) Guanosine 3'-5'-cyclic monophosphate-activatcd conductance studied in a truncated rod outer segment of the toad. Journal of Physiology (London) 395:731–53. [aMDB]10.1113/jphysiol.1988.sp016943CrossRefGoogle Scholar
Nakazawa, M., Kikawa-Araki, E., Shiono, T. & Tamai, M. (1991) Analysis of rhodopsin gene in patients with retinitis pigmentosa using allele-specific polymerase chain reaction. Japanese Journal of Ophthalmology 35:386–93. [aSPD]Google ScholarPubMed
Näirfström, K. (1983) Hereditary progressive retinal atrophy in the Abyssinian cat. The Journal of Heredity 74:273–76. [MWK]10.1093/oxfordjournals.jhered.a109782CrossRefGoogle Scholar
Nathans, J. (1990) Determinants of visual pigment absorbance: Role of charged amino acids in the putative transmembrane segment. Biochemistry 29:937–42. [aPAH]10.1021/bi00456a013CrossRefGoogle Scholar
Nathans, J. (1992) Rhodopsin: Structure, function, and genetics. Biochemistry 31:4923–31. [aMDB, aSPD, aPAH]10.1021/bi00136a001CrossRefGoogle Scholar
Nathans, J., Maumenee, I. H., Zrenner, E., Sadowski, B., Sharpe, L. T., Lewis, R. A., Hansen, E., Rosenberg, T. et al. (1993) Genetic heterogeneity among blue-cone monochromats. American Journal of Human Genetics 53:987–1000. [aSPD]Google ScholarPubMed
Nathans, J., Merbs, S. L., Sung, C.-H., Weitz, C. J. & Wang, Y. (1992a) Molecular genetics of human visual pigments. Annual Review of Genetics 26:403–24. [aSPD]10.1146/annurev.ge.26.120192.002155CrossRefGoogle ScholarPubMed
Nathans, J., Weitz, C. J., Agarwal, N., Nir, I. & Papermaster, D. S. (1989) Production of bovine rhodopsin by mammalian cell lines expressing cluned cDNA: Spectrophotometry and subcellular localization. Vision Research 29:907–14. [aPAH]10.1016/0042-6989(89)90105-3CrossRefGoogle ScholarPubMed
Natsukari, N., Hanai, H., Matsunaga, T. & Fujita, M. (1990) Synergistic activation of brain adenylate cyclase by calmodulin, and either GTP or catecholamines including dopamine. Brain Research 534:170–76. [aZX]10.1016/0006-8993(90)90126-VCrossRefGoogle ScholarPubMed
Nawy, S. & Jahr, C. E. (1990) Suppression by glutamate of cGMP-activated conductance in retinal bipolar cells. Nature 346:269–71. [aRSM]10.1038/346269a0CrossRefGoogle ScholarPubMed
Nef, S., De Castro, E., Martone, M. E., Edelman, V. M., Ellisman, M. H., Fiumelli, H., Comte, M., Cox, J. A., Lenz, S. E., Kawamura, S. & Nef, P. (in press) Relgulation of receptor phosphorylation by a novel family of neuronal calcium sensors (NCS) and distribution of NCS-1 in the avian and rodent nervous systen. Neuron. [SK]Google Scholar
Nef, S., Fiumelli, H., De Castro, E., Raes, M. B. & Nef, P. (in press) Identification of a neuronal calcium sensor (NCS-1) possibly involved in the regulation of receptor phosphorylation. Journal of Receptor Research [KT]Google Scholar
Nei, M. (1987) Molecular evolutionary genetics. Columbia University Press. [aSPD]10.7312/nei-92038CrossRefGoogle Scholar
Nelson, R. B. & Routtenberg, A. (1985) Characterization of protein Fl: A kinase C substrate directly related to neural plasticity. Experimental Neurology 89:213–24. [aZX]10.1016/0014-4886(85)90277-8CrossRefGoogle Scholar
Nestler, E. J. & Greengard, P. (1983) Protein phosphorylation in the brain. Nature 305:583–88. [aZX]10.1038/305583a0CrossRefGoogle Scholar
Neubert, T. A., Johnson, R. S., Hurley, J. B. & Walsh, K. A. (1992) The rod transducin a subunit amino terminus is heterogeneously fatty acylated. Journal of Biological Chemistry 267:18274–77. [aMDB, aJBH, KS]10.1016/S0021-9258(19)36955-8CrossRefGoogle ScholarPubMed
Newton, A. C. & Williams, D. S. (1991) Involvement of protein kinase C in the phosphorylation of rhodopsin. Journal of Biological Chemistry 266:17725–28. [aMDB]10.1016/S0021-9258(18)55183-8CrossRefGoogle ScholarPubMed
Newton, A. C. & Williams, D. S. (1993) Rhodopsin is the major in situ substrate of protein kinase C in rod outer segments of photoreceptors. Journal of Biological Chemistry 268:18181–86. [aMDB]10.1016/S0021-9258(17)46827-XCrossRefGoogle ScholarPubMed
Nicol, G. D. & Bownds, M. D. (1989) Calcium regulates some, but not all, aspects of light adaptation in rod photoreceptors. Journal of General Physiology 94:233–59. [aMDB]10.1085/jgp.94.2.233CrossRefGoogle Scholar
Nicol, G. D., Kaupp, U. B. & Bownds, M. D. (1987) Transduction persists in rod photoreceptors after depletion of intracellular calcium. Journal of General Physiology 89:297–319. [aMDB]10.1085/jgp.89.2.297CrossRefGoogle ScholarPubMed
Nicoll, R. A., Kauer, J. A. & Malenka, R. C. (1988) The current excitement in long-term potentiation. Neuron 1:97–103. [aZX]10.1016/0896-6273(88)90193-6CrossRefGoogle ScholarPubMed
Nichols, B. E., Sheffield, V. C., Vandenburgh, K., Drack, A. V., Kimura, A. E. & Stone, E. M. (1993) Butterfly-shaped pigment dystrophy of the fovea caused by a point mutation in codon 167 of the RDS gene. Nature Genetics 3:202–6. [aSPD]10.1038/ng0393-202CrossRefGoogle ScholarPubMed
Niemeyer, G., Trub, P., Schinzel, A. & Gal, A. (1992) Clinical and ERG data in a family with autosomal dominant RP and Pro-347-Arg mutation in the rhodopsin gene. Documenta Ophthalmologica 79:303–11. [aSPD]10.1007/BF00160945CrossRefGoogle Scholar
Nigg, E. A., Hilz, H., Eppenberger, H. M. & Dutly, F. (1985) Rapid and reversible translocation of the catalytic subunit of cAMP-dependent protein kinase type II from the Golgi complex to the nucleus. EMBO Journal 4:2801–6. [aZX]10.1002/j.1460-2075.1985.tb04006.xCrossRefGoogle ScholarPubMed
Noel, J. P., Hamm, H. E. & Sigler, P. B. (1993) The 2.2 Å crystal structure of transducin- complexed with GTPgammaS. Nature 366:654–63. [aMDB, RKC, EAD]10.1038/366654a0CrossRefGoogle Scholar
Noro, Y., Ishiguro, S.-I. & Tamal, M. (1994) Accumulation of glutamate-like reactivity in the rds/rds mouse retina. Investigative Ophthalmology and Visual Science 35:1362. [MT]Google Scholar
Nussberger, S., Dörr, K., Wang, D. N. & Kühlbrandt, W. (1993) Lipid-protein interactions in crystals of plant light-harvesting complex. Journal of Molecular Biology 234:347–56. [RMG]10.1006/jmbi.1993.1591CrossRefGoogle ScholarPubMed
O'Brien, P. J., StJules, R. S., Reddy, T. S., Bazan, N. G. & Zatz, M. (1987) Acylation of disc membrane rhodopsin may be nonenzymatic. Journal of Biological Chemistry 262:5210–15. [aPAH]10.1016/S0021-9258(18)61175-5CrossRefGoogle ScholarPubMed
O'Brien, P. J. & Zatz, M. (1984) Acylation of bovine rhodopsin by [3H]palmitic acid. Journal of Biological Chemistry 259:5054–57. [aPAH]10.1016/S0021-9258(17)42954-1CrossRefGoogle Scholar
Ocorr, K. A., Walters, E. T. & Byrne, J. H. (1985) Associative conditioning analog selectively increases cAMP levels of tail sensory neurons in Aplysia. Proceedings of the National Academy of Sciences USA 82:2548–52. [TWA]10.1073/pnas.82.8.2548CrossRefGoogle ScholarPubMed
Ohguro, H., Fukada, Y., Takao, T., Shimonishi, Y., Yoshizawa, T. & Akino, T. (1991) Carboxyl methylation and farnesylation of transducin gammasubunit synergistically enhance its coupling with metarhodopsin II. EMBO Journal 10:3669–74. [aMDB]10.1002/j.1460-2075.1991.tb04934.xCrossRefGoogle Scholar
Ohguro, H., Palczewski, K., Ericsson, L. H., Walsh, K. A. & Johnson, R. S. (1993) Sequential phosphorylation of rhodopsin at multiple sites. Biochemistry 32:5718–24. [aMDB]10.1021/bi00072a030CrossRefGoogle ScholarPubMed
Okazaki, K., Watanabe, M., Ando, Y., Hagiwara, M., Terasawa, M. & Hidaka, H. (1992) Full sequence of neurocalcin, a novel calcium-binding protein abundant in central nervous system. Biochemical and Biophysical Research Communications 185:147–53. [aJBH]10.1016/S0006-291X(05)80968-4CrossRefGoogle ScholarPubMed
Oprian, D. D. (1992) The ligand-binding domain of rhodopsin and other G protein-linked receptors. Journal of Bioenergetics & Biomembranes 24:211–17. [aPAH]10.1007/BF00762679CrossRefGoogle ScholarPubMed
Oprian, D. D., Molday, R. S., Kaufman, R. J. & Khorana, H. G. (1987) Expression of a synthetic bovine rhodopsin gene in monkey kidney cells. Proceedings of the National Academy of Sciences USA 84:8874–78. [aPAH]10.1073/pnas.84.24.8874CrossRefGoogle ScholarPubMed
Orth, U., Samanns, C., Gusseck, H., Niemeyer, G., Ludwig, M., Meitinger, T., Schinzel, A., Schwinger, E. & Gal, A. (1991) Autosomal dominant hereditary retinopathia pigmentosa with genetic heterogeneity. Fortschritte der Opththalmologie. 88:455–59. [aSPD]Google ScholarPubMed
Ott, J., Bhattacharya, S. S., Chen, J. D., Denton, M. J., Donald, J., DuBay, C., Farrar, G. J., Fishman, G. A. et al. (1990) Localizing multiple X chromosome-linked retinitis pigmentosa loci using multilocus homogeneity tests. Proceedings of the National Academy of Sciences USA 87:701–4. [aSPD]10.1073/pnas.87.2.701CrossRefGoogle ScholarPubMed
Ovchinnikov, Y. A., Abdulaev, N. G. & Bogachuk, A. S. (1988) Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated. FEBS Letters 230:1–5. [aPAH]10.1016/0014-5793(88)80628-8CrossRefGoogle ScholarPubMed
Ovchinnikov, Y. A., Abdulaev, N. G., Zolotarev, A. S., Artamonov, I. D., Bespalov, I. A., Dergachev, A. E & Tsuda, M. (1988) Octopus rhodopsin: Amino acid sequence deduced from cDNA. FEBS Letters 232:69–72. [aPAH]10.1016/0014-5793(88)80388-0CrossRefGoogle ScholarPubMed
Pagés, F., Deterre, P. & Pfister, C. (1992) Enhanced GTPase activity of transducin when bound to cGMP phosphodiesterase in bovine retinal rods. Journal of Biological Chemistry 267:22018–21. [aMDB]10.1016/S0021-9258(18)41629-8CrossRefGoogle ScholarPubMed
Pagés, F., Deterre, P. & Pfister, C. (1993) Enhancement by phosphodiesterase subunits of the rate of GTP hydrolysis by transducin in bovine retinal rods. Essential role of the phosphodiesterase catalytic core. Journal of Biological Chemistry 268:26358–64. [arMDB, BMW]10.1016/S0021-9258(19)74323-3CrossRefGoogle ScholarPubMed
Palczewski, K., Buczylko, J., Kaplan, M. W., Polans, A. S. & Crabb, J. W. (1991) Mechanism of rhodopsin kinase activation. Journal of Biological Chemistry 266:12949–55. [aMDB]10.1016/S0021-9258(18)98787-9CrossRefGoogle ScholarPubMed
Palczewski, K., Jager, S., Buczylko, J., Crouch, R. K., Bredberg, D. L., Hofmann, K. P., Asson-Batres, M. A. & Saari, J. C. (1994) Rod outer segment retinol dehydrogenase: Substrate specificity and role in phototransduction. Biochemistry 38:13741–50. [RKC]10.1021/bi00250a027CrossRefGoogle Scholar
Palczewski, K., McDowell, J. H. & Hargrave, P.A. (1988a) Purification and characterization of rhodopsin kinase. Journal of Biological Chemistry 263:14067–73. [aMDB]10.1016/S0021-9258(18)68185-2CrossRefGoogle ScholarPubMed
Palczewski, K., McDowell, J. H. & Hargrave, P.A. (1988b) Rhodopsin kinase: Substrate specificity and factors that influence activity. Biochemistry 27:2306–12. [aMDB]10.1021/bi00407a010CrossRefGoogle ScholarPubMed
Palczewski, K., Rispoli, G. & Detwiler, P. B. (1992) The influence of arrestin (48K protein) and rhodopsin kinase on visual transduction. Neuron 8:117–26. [aMDB]10.1016/0896-6273(92)90113-RCrossRefGoogle ScholarPubMed
Palczewski, K., Subbaraya, I., Gorczyca, W. A., Helekar, B. S., Ruiz, C. C., Ohguro, H., Huang, J., Zhao, X., Crabb, J. W., Johnson, R. S., Walsh, K. A., Gray-Keller, M. P., Detwiler, P. B. & Baehr, W. (1994) Molecular cloning and characterization of retinal photoreceptor guanylyl cyclaseactivating protein. Neuron 13:395–404. [KS]10.1016/0896-6273(94)90355-7CrossRefGoogle Scholar
Papac, D. I., Oatis, J. E. Jr, Crouch, R. K. & Knapp, D. R. (1993) Mass spectrometric identification of phosphorylation sites in bleached bovine rhodopsin. Biochemistry 32:5930–34. [aMDB]10.1021/bi00074a002CrossRefGoogle ScholarPubMed
Papac, D. I., Thornburg, K. R., Bullesbach, E. E., Crouch, R. K. & Knapp, D. R. (1992) Palmitylation of a G-protein coupled receptor: Direct analysis by tandem mass spectrometry. Journal of Biological Chemistry 267:16889–94. [aPAH]10.1016/S0021-9258(18)41868-6CrossRefGoogle ScholarPubMed
Papermaster, D. S. & Dreyer, W. J. (1974) Rhodopsin content in the outer segment membranes of bovine and frog retinal rods. Biochemistry 13:2438–44. [aPAH]10.1021/bi00708a031CrossRefGoogle ScholarPubMed
Pearson, P. L., Matheson, N. W., Flescher, D. C., Robbins, F. J. (1992) The GDB[TM] human genome data base anno 1992. Nucleic Acids Research 20:2201–6. [aSPD]10.1093/nar/20.suppl.2201CrossRefGoogle ScholarPubMed
Peng, Y.-W., Robishaw, J. D., Levine, M. A. & Yau, K.-W. (1992) Retinal rods and cones have distinct G protein β and γ subunits. Proceedings of the National Academy of Sciences USA 89:10882–86. [aSPD]10.1073/pnas.89.22.10882CrossRefGoogle ScholarPubMed
Pepperberg, D. R., Cornwall, M. C., Kahlert, M., Hofmann, K. P., Jin, J., Jones, G. J. & Ripps, H. (1992) Light-dependent delay in the falling phase of the retinal rod photoresponse. Visual Neuroscience 8:9–18. [aMDB, RKC]10.1017/S0952523800006441CrossRefGoogle ScholarPubMed
Pepperberg, D. R., Jin, J. & Jones, G. J. (1994) Modulation of transduction gain in light adaptation of retinal rods. Visual Neuroscience 11:53–62. [aMDB, RKC]10.1017/S095252380001110XCrossRefGoogle ScholarPubMed
Perez-Sala, D., Tan, E. W., Canada, F. J. & Rando, R. R. (1991) Methylation and demethylation reactions of guanine nucleotide-binding proteins of retinal rod outer segments. Proceedings of the National Academy of Sciences USA 88:3043–46. [aMDB]10.1073/pnas.88.8.3043CrossRefGoogle ScholarPubMed
Perlman, J. I., Nodes, B. R. & Pepperberg, D. R. (1982) Utilization of retinoids in the bullfrog retina. Journal of General Physiology 80:885–913. [RKC]10.1085/jgp.80.6.885CrossRefGoogle ScholarPubMed
Pfenninger, K. H., Ellis, L., Johnson, M. P., Friedman, L. B. & Somlo, S. (1983) Nerve growth cones isolated from fetal rat brain: Subcellular fractionation and characterization. Cell 35:573–84. [aZX]10.1016/0092-8674(83)90191-5CrossRefGoogle ScholarPubMed
Pfister, C., Bennett, N., Bruckert, F., Catty, P., Clerc, A., Pagès, F. & Deterre, P. (1993) Interactions of a G-protein with its effector: Transducin and cGMP phosphodiesterase in retinal rods. Cellular Signalling 5:235–51. [aMDB]10.1016/0898-6568(93)90015-ECrossRefGoogle ScholarPubMed
Philip, N. J., Chang, W. & Long, K. (1987) Light-stimulated movement in rod photoreceptor cells of the rat retina. FEBS Letters 225:127–31. [JFM]10.1016/0014-5793(87)81144-4CrossRefGoogle Scholar
Phillips, W. J. & Cerione, R. A. (1994) A C-terminal peptide of bovine rhodopsin binds to the transducin alpha-subunit and facilitates its activation. Biochemical Journal 299(Pt 2):351–57. [ADA]10.1042/bj2990351CrossRefGoogle Scholar
Piascik, M. T., Piascik, M. F., Hitzemann, R. J. & Potter, J. D. (1981) Ca2+ -dependent regulation of rat caudate nucleus adenylate cyclase and effects on the response to dopamine. Mol Pharmacol. 20, 2: 319–25. [aZX]Google Scholar
Picones, A. & Korenbrot, J. I. (1992) Permeation and interaction of monovalent cations with the cGMP-gated channel of cone photoreceptors. Journal of Ceneral Physiology 100:647–73. [aRSM]10.1085/jgp.100.4.647CrossRefGoogle ScholarPubMed
Pistorius, A. M. & deGrip, W. J. (1994) Rhodopsin's secondary structure revisited: Assignment of structural elements. Biochemical and Biophysical Research Communications 3:1040–45. [ADA]10.1006/bbrc.1994.1148CrossRefGoogle Scholar
Pittler, S. J. & Baehr, W. (1991) Identification of a nonsense mutation in the rod photoreceptor cGMP phosphodiesterase β-subunit gene of the rd mouse. Proceedings of the National Academy of Sciences USA 88:8322–26. [aSPD, MWK]10.1073/pnas.88.19.8322CrossRefGoogle ScholarPubMed
Pittler, S. J., Keeler, C. E., Sidman, R. L. & Baehr, W. (1993) PCR analysis of DNA from 70-year-old sections of rodless retina demonstrates identity with the mouse rd defect. Proceedings of the National Academy of Sciences USA 90:9616–19. [aSPD]10.1073/pnas.90.20.9616CrossRefGoogle ScholarPubMed
Pittler, S. J., Lee, A. K., Altherr, M. R., Howard, T. A., Seldin, M. F., Hurwitz, R. L., Wasmuth, J. J. & Baehr, W. (1992) Primary structure and chromosomal localization of human and mouse rod photoreceptor cGMP-gated cation channel. Journal of Biological Chemistry 267:6257–62. [aRSM]10.1016/S0021-9258(18)42689-0CrossRefGoogle ScholarPubMed
Plantner, J. J., Le, M.-L. & Kean, E. L. (1991) Enzymatic deglycosylation of bovine rhodopsin. Experimental Eye Research 53:269–74. [aPAH]10.1016/0014-4835(91)90083-QCrossRefGoogle ScholarPubMed
Pober, J. S. & Stryer, L. (1975) Light dissociates enzymatically-cleaved rhodopsin into two different fragments. Journal of Molecular Biology 95:477–81. [rPAH]10.1016/0022-2836(75)90204-1CrossRefGoogle ScholarPubMed
Polans, A. S., Buczylko, J., Crabb, J. & Palczewski, K. (1991) A photoreceptor calcium binding protein is recognized by autoantibodies obtained from patients with cancer-associated retinopathy. Journal of Cell Biology 112:981–89. [aJBH, JFM, ASP]10.1083/jcb.112.5.981CrossRefGoogle ScholarPubMed
Polans, A. S., Burton, M. D., Haley, T. L., Crabb, J. W. & Palczewski, K. (1993) Recoverin, but not visinin, is an autoantigen in the human retina identified with a cancer-associated retinopathy. Investigative Ophthalmology and Visual Science 34:81–90. [aJBH, ASP]Google Scholar
Polans, A. S., Hermolin, J. & Bownds, M. D. (1979) Light-induced phosphorylation of two proteins in frog rod outer segments. Journal of General Physiology 74:595–613. [aMDB]10.1085/jgp.74.5.595CrossRefGoogle ScholarPubMed
Pongs, O., Lindemeier, J., Zhu, X. R., Theil, T., Engelkamp, D., Krah-Jentgens, I., Lambrecht, H. G., Koch, K. W., Schwemer, J., Rivosecchi, R., Mallart, A., Galceran, J., Canal, I., Barbas, J. A. & Ferrus, A. (1993) Frequenin: A novel calcium-binding protein that modulates synaptic efficacy in the Drosophila nervous system. Neuron 11:15–28. [KT]10.1016/0896-6273(93)90267-UCrossRefGoogle ScholarPubMed
Popova, J. S., Johnson, G. L. & Rasenick, M. M. (1994) Journal of Biological Chemistry 269:21748–54. [MMR]10.1016/S0021-9258(17)31868-9CrossRefGoogle Scholar
Poulain, C., Ferrus, A. & Mallart, A. (1994) Modulation of type A K+ current in Drosophila larval muscle by internal Ca2+; effects of the overexpression of frequenin. European Journal of Physiology 427:71–79. [KT]10.1007/BF00585944CrossRefGoogle Scholar
Probst, W. C., Snyder, L. A., Schuster, D. I., Brosius, J. & Sealfon, S. C. (1992) Sequence alignment of the G-protein coupled receptor superfamily. DNA and Cell Biology 11:1–20. [aPAH]10.1089/dna.1992.11.1CrossRefGoogle ScholarPubMed
Pugh, E. N. Jr & Lamb, T. D. (1990) Cyclic GMP and calcium: The internal messengers of excitation and adaptation in vertebrate photoreceptors. Vision Research 30:1923–48. [aMDB]10.1016/0042-6989(90)90013-BCrossRefGoogle ScholarPubMed
Pugh, E. N. Jr & Lamb, T. D. (1993) Amplification and kinetics of the activation steps in phototransduction. Biochimica et Biophysica Acta 1141:111–49. [aMDB, KWK]10.1016/0005-2728(93)90038-HCrossRefGoogle ScholarPubMed
Pullen, N., Brown, N. C., Sharma, R. P. & Akhtar, M. (1993) Cooperativity during multiple phosphorylations chatlyzed by rhodopsin kinase: Supporting evidence using synthetic phosphopeptides. Biochemistry 32:3958–64. [ADA]10.1021/bi00066a016CrossRefGoogle ScholarPubMed
Pulvermuller, A., Palczewski, K. & Hofmann, K. P. (1993) Interaction between photoaetivated rhodopsin and its kinase: Stability and kinetics of complex formation. Biochemistry 32:14082–88. [aMDB]10.1021/bi00214a002CrossRefGoogle ScholarPubMed
Quamme, G. A. & Rabkin, S. W. (1990) Cytosolic free magnesium in cardiac myocytes: Identification of a Mg2+ influx pathway. Biochemical and Biophysical Research Communications 167:1406–12. [RLH]10.1016/0006-291X(90)90679-HCrossRefGoogle ScholarPubMed
Radmacher, M., Fritz, M., Hansma, H. C. & Hansma, P. K. (1994) Direct observation of enzyme activity with the atomic force microscope. Science 265:1577–79. [ADA]10.1126/science.8079171CrossRefGoogle ScholarPubMed
Raju, B., Murphy, E., Levy, L. A., Hall, R. D. & London, R. E. (1989) A fluorescent indicator for measuring cytosolic free magnesium. American Journal of Physiology 256:C540–48. [RLH]10.1152/ajpcell.1989.256.3.C540CrossRefGoogle ScholarPubMed
Raleigh, D. P., Levitt, M. H. & Griffin, R. G. (1988) Rotational resonance in solid state NMR. Chemistry & Physics Letters 146:71–76. [SOS]10.1016/0009-2614(88)85051-6CrossRefGoogle Scholar
Rao, V. R., Cohen, G. B. & Oprian, D. D. (1994) Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness. Nature 367:639–42. [aSPD]10.1038/367639a0CrossRefGoogle Scholar
Ratan, R. R., Murphy, T. H. & Baraban, J. M. (1994) Oxidative stress induces apoptosis in embryonic cortical neurons. Journal of Neurochemistry 62:376–79. [MT]10.1046/j.1471-4159.1994.62010376.xCrossRefGoogle ScholarPubMed
Ratto, G. M., Payne, R., Owen, W. G. & Tsien, R. Y. (1988) The concentration of cytosolic free calcium in vertebrate rod outer segments measured with Fura-2. Journal of Neuroscience 8:3240–46. [aMDB]10.1523/JNEUROSCI.08-09-03240.1988CrossRefGoogle ScholarPubMed
Ray, S., Zozulya, S., Niemi, G. A. et al. (1992) Cloning, expression and crystallization of recoverin, a calcium sensor in vision. Proceedings of the National Academy of Sciences USA 89:5705–9. [aJBH]10.1073/pnas.89.13.5705CrossRefGoogle ScholarPubMed
Reig, C., Llecha, N., Antich, J., Gaen, E., Tejada, I., Molina, M., Revents, J. & Carballa, M. (1994) A missense mutation (211HisArg) and a silent (160Thr) mutation within the rhodopsin gene in a Spanish autosomal dominant retinitis pigmentosa family. Human Molecular Genetics 3:195–96. [aSPD]10.1093/hmg/3.1.195CrossRefGoogle Scholar
Represa, A., Deloulme, J. C., Sensenbrenner, M., Ben-Ari, Y. & Baudier, J. (1990) Neurogranin: Immunocytochemical localization of a brain specific protein kinase C substrate. Journal of Neuroscience 10:3782–92. [EDR]10.1523/JNEUROSCI.10-12-03782.1990CrossRefGoogle ScholarPubMed
Rescorla, R. A. (1988) Behavioral studies of Pavlovian conditioning. Annual Review of Neuroscience 11:329–52. [TWA]10.1146/annurev.ne.11.030188.001553CrossRefGoogle ScholarPubMed
Restagno, C., Maghtheh, M., Ghattacharya, S., Ferrone, M., Garnersoe, S., Samuelly, R. & Carbonara, A. (1992) A large deletion at the 3' end of the rhodopsin gene in an Italian family with a diffuse form of autosomal dominant retinitis pigmentosa. Human Molecular Genetics 2:207–8. [aSPD]10.1093/hmg/2.2.207CrossRefGoogle Scholar
Richards, J. E., Kuo, C. Y., Boehnke, M. & Sieving, P. A. (1991) Rhodopsin Thr58Arg mutation in a family with autosomal dominant retinitis pigmentosa. Ophthalmology 98:1797–1805. [aSPD]10.1016/S0161-6420(91)32047-5CrossRefGoogle Scholar
Ridge, K. D., Bhattacharya, S., Nakayama, T. A. & Khorana, H. G. (1992) Light-stable rhodopsin: 2. An opsin mutant (Trp-265 → Phe) and a retinal analog with a nonisomerizable 11-Cis configuration form a photostable chromophore. Journal of Biological Chemistry 267:6770–75. [aPAH]10.1016/S0021-9258(19)50492-6CrossRefGoogle Scholar
Ridge, K. D., Lee, S. S. J. & Yao, L. L. (in press) In vivo assembly of rhodopsin from expressed polypeptide fragments. Proceedings of the National Academy of Sciences USA. [rPAH]Google Scholar
Ricke, F. & Schwartz, E. A. (1994) A cGMP-gated current can control exocytosis at cone synapses. Neuron 13:863–73. [TGW]10.1016/0896-6273(94)90252-6CrossRefGoogle Scholar
Ringens, P. J., Fang, M., Shinohara, T., Bridges, C. D., Lerea, C. L., Berson, E. L. & Dryja, T. P. (1990) Analysis of genes coding for S-antigen, interstitial retinol binding protein, and the alpha-subunit of cone transducin in patients with retinitis pigmentosa. Investigative Ophthalmology and Visual Science 31:1421–26. [aSPD]Google ScholarPubMed
Rispoli, C. & Detwiler, P. B. (1989) Light adaptation in Gecko rods may involve changes in both the initial and terminal stage of the transduction cascade. Biophysical Journal 55:380. [aMDB]Google Scholar
Rispoli, C. & Detwiler, P. B. (1991) Interactions between calcium and cGMP in dialyzed detached retinal rod outer segments. In: Signal transduction in photoreceptor cells, ed. Hargrave, P. A. & Hofmann, K. P.. Springer-Verlag. [aMDB]Google Scholar
Rispoli, G., Sather, W. A. & Detwiler, P. B. (1993) Visual transduction in dialysed detached rod outer segments from lizard retina. Journal of Physiology (London) 465:513–37. [aMDB]10.1113/jphysiol.1993.sp019691CrossRefGoogle ScholarPubMed
Robinson, P. R., Cohen, G. B., Zhukovsky, E. A. & Oprian, D. D. (1992) Constitutively active mutants of rhodopsin. Neuron 9:719–25. [aMDB, aSPD, aPAH]10.1016/0896-6273(92)90034-BCrossRefGoogle ScholarPubMed
Robinson, P. R., Kawamura, S., Abramson, B. & Bownds, M. D. (1980) Control of the cyclic GMP phosphodiesterase of frog photoreceptor membranes. Journal of General Physiology 76:631–45. [aMDB]10.1085/jgp.76.5.631CrossRefGoogle ScholarPubMed
Rodriquez, J. A., Herrera, C. A., Birch, D. C. & Daiger, S. P. (1993) A leucine to arginine amino acid substitution at codon 46 of rhodopsin is responsible for a severe form of autosomal dominant retinitis pigmentosa. Human Mutation 2:205–13. [aSPD]10.1002/humu.1380020309CrossRefGoogle Scholar
Rodriguez, J. A., Herrera, C. A., Birch, D. G., Heckenlively, J. R. & Daiger, S. P. (1993a) Rhodopsin mutations in patients with retinitis pigmentosa. American Journal of Human Genetics 53:1224. [aSPD]Google Scholar
Ronnett, G. V. & Snyder, S. H. (1992) Molecular messengers of olfaction. Trends in Neuroscience 15:508–13. [aMDB]10.1016/0166-2236(92)90104-GCrossRefGoogle ScholarPubMed
Roof, D. J., Adamian, M. & Hayes, A. (1994) Rhodopsin accumulation at abnormal sites in retinas of mice with a human P23H rhodopsin transgene. Investigative Ophthalmology and Visual Science 35:4049–62. [MWK]Google ScholarPubMed
Root, M. J. & MacKinnon, R. (1993) Identification of an external divalent cation-binding site in the pore of a cGMP-activated channel. Neuron 11:459–66. [arRSM]10.1016/0896-6273(93)90150-PCrossRefGoogle ScholarPubMed
Rosenberg, C.B., Minocherhomjee, A. & Storm, D. R. (1987b) Reconstitution of calmodulin-sensitive adenylate cyclase. Methods in Enzymology 139:776–79. [aZX]10.1016/0076-6879(87)39126-8CrossRefGoogle ScholarPubMed
Rosenberg, G. B. & Storm, D. R. (1987a) Immunological distinction between calmodulin-sensitive and calmodulin-insensitive adenylyl cyclases. Journal of Biological Chemistry 262:7623–28. [oZX]10.1016/S0021-9258(18)47611-9CrossRefGoogle Scholar
Rosenfeld, P. J., Cowley, G. S., McGee, T. L., Sandberg, M. A., Berson, E. L. & Dryja, T. P. (1992) A null mutation in the rhodopsin gene causes rod photoreceptor dysfunction and autosomal recessive retinitis pigmentosa. Nature Genetics 1:209–13. [aSPD]10.1038/ng0692-209CrossRefGoogle Scholar
Ross, E. M. & Gilman, A. G. (1980) Biochemical properties of hormonesensitive adenylyl cyclase. Annual Review of Biochemistry 49:533–64. [aZX]10.1146/annurev.bi.49.070180.002533CrossRefGoogle Scholar
Roth, N. S., Campbell, P. T., Caron, M. G., Lefkowitz, R. J. & Lohse, M. J. (1991) Comparative rates of desensitization of β-adrenergic receptors by the β-adrenergic receptor kinase and the cyclic AMP-dependent protein kinase. Proceedings of the National Academy of Sciences USA 88:6201–4. [aMDB]10.1073/pnas.88.14.6201CrossRefGoogle ScholarPubMed
Routtenberg, A. (1995) Phosphoprotein regulation of memory formation: enhancement and control of synaptic plasticity by protein kinase C and F1 . Annual of the New York Academy of Sciences 444:203–11.10.1111/j.1749-6632.1985.tb37590.xCrossRefGoogle Scholar
Roychowdhury, S. & Rasenick, M. M. (1994) Tubulin-G protein associations stabilizes GTP binding and activates GTPase. Biochemistry 33:9800–5. [MMR]10.1021/bi00198a052CrossRefGoogle ScholarPubMed
Roychowdhury, S., Wang, N. & Rasenick, M. M. (1993) Biochemistry 32:4955–61. [MMR]10.1021/bi00069a034CrossRefGoogle Scholar
Ryba, N. J. P. & Marsh, D. (1992) Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation-transfer electron spin resonance. Biochemistry 31:7511–18. [aPAH]10.1021/bi00148a011CrossRefGoogle ScholarPubMed
Saga, M., Mashima, Y., Kawashima, S., Akeo, K., Oguchi, Y., Kudoh, J. & Shimizu, N. (1993) Rhodopsin gene analysis for Japanese autosomal dominant retinitis pigmentosa patients. Investigative Ophthalmology and Visual Science 34:1459. [aSPD]Google Scholar
Saitoh, S., Takamatsu, K., Kobayashi, M. & Noguchi, T. (1993) Distribution of hippocalcin mRNA and immunoreactivity in rat brain. Neuroscience Letters 157:107–10. [KT]10.1016/0304-3940(93)90654-4CrossRefGoogle ScholarPubMed
Saitoh, S., Takamatsu, K., Kobayashi, M. & Noguchi, T. (1994) Immunohistochemical localization of neural visinin-like Ca2+-binding protein 2 in adult rat brain. Neuroscience Letters 171:155–58. [KT]10.1016/0304-3940(94)90628-9CrossRefGoogle Scholar
Sakmar, T. P., Franke, R. R. & Khorana, H. G. (1989) Glutamic acid-113 serves as the retinylidine schiff base counterion in bovine rhodopsin. Proceedings of the National Academy of Sciences USA 86:8309–13. [aPAH]10.1073/pnas.86.21.8309CrossRefGoogle Scholar
Salter, R. S., Krinks, M. H., Klee, C. B. & Neer, E. J. (1981) Calmodulin activates the isolated catalytic unit of brain adenylate cyclase. Journal of Biological Chemistry 256:9830–33. [aZX]10.1016/S0021-9258(19)68703-XCrossRefGoogle ScholarPubMed
Sanada, K., Kokame, K., Yoshizawa, T., Takao, T. & Fukada, Y. (1995) Role of heterogeneneous N-terminal acylation of recoverin in rhodopsin phosphorylation. Journal of Biological Chemistry 267:18274–18277 Google Scholar
Sankila, E.-M., Pakarinen, L., Kääriäinen, H., Aittomäki, K., Karjalainen, S., Sistonen, P. & de la Chapelle, A. (1995) Assignment of an Usher syndrome type III (USH3) gene to chromosome 3q. Human Molecular Genetics 4:93–98. [rSPD]10.1093/hmg/4.1.93CrossRefGoogle ScholarPubMed
Sano, M. (1985) Calmodulin-dependent adenylate cyclase in rat retina and the response to dopamine. Brain Research 345:337–40. [aZX]10.1016/0006-8993(85)91012-1CrossRefGoogle Scholar
Sather, W. A. & Detwiler, P. B. (1987) Intracellular biochemical manipulation of phototransduction in detached rod outer segments. Proceedings of the National Academy of Sciences USA 84:9290–94. [aM DB]10.1073/pnas.84.24.9290CrossRefGoogle ScholarPubMed
Schacher, S., Castellucci, V. F. & Kandel, E. R. (1988) cAMP evokes longterm facilitation in Aplysia sensory neurons that requires new protein synthesis. Science 240:1667–69. [aZX]10.1126/science.2454509CrossRefGoogle Scholar
Schafmeister, C. E., Miercke, L. J. W. & Stroud, R. M. (1993) Structure at 2.5 Å of a designed peptide that maintains solubility of membrane proteins. Science 262:734–39. [RKC]10.1126/science.8235592CrossRefGoogle ScholarPubMed
Schertler, G. F. X. (1992) Overproduction of membrane proteins. Current Opinion in Structural Biology 2:53444. [aPAH]10.1016/0959-440X(92)90083-JCrossRefGoogle Scholar
Schertler, G. F. X., Bartunik, H. D., Michel, H. & Oesterhelt, D. (1993) Orthorhombic crystal form of bacteriorhodopsin nucleated on benzamidine diffracting to 3.6 Å resolution. Journal of Molecular Biology 234:156–64. [RMG]10.1006/jmbi.1993.1570CrossRefGoogle ScholarPubMed
Schertler, G. F. X. & Hargrave, P. A. (in press) Projection structures of frog rhodopsin in two crystal forms. Proceedings of the National Academy of Sciences USA. [raPAH]Google Scholar
Schertler, G. F. X., Villa, C. & Henderson, R. (1993) Projection structure of rhodopsin. Nature 362:770–72. [aPAH, EAD, RMG]10.1038/362770a0CrossRefGoogle ScholarPubMed
Schnetkamp, P. P. M. (1989) Na-Ca or Na-Ca-K exchange in the outer segments of vertebrate rod photoreceptors. Progress in Biophysics and Molecular Biology 54:1–29. [PPMS]10.1016/0079-6107(89)90007-2CrossRefGoogle ScholarPubMed
Schnetkamp, P. P. M. (1990) Cation selectivity of and cation binding to the cGMP-dependent channel in bovine rod outer segment membranes. Journal of General Physiology 96:517–34. [aRSM]10.1085/jgp.96.3.517CrossRefGoogle Scholar
Schnetkamp, P. P. M., Li, X-.B., Basu, D. K. & Szerencsei, R. T. (1991) Regulation of free cytosolic Ca2+ concentration in the outer segments of bovine retinal rods by Na-Ca-K exchange measured with Fluo-3. Journal of Biological Chemistry 266:22975–82. [PPMS]10.1016/S0021-9258(18)54450-1CrossRefGoogle ScholarPubMed
Schnetkamp, P. P. M. & Szerencsei, R. T. (1993) Intracellular Ca2+ sequestration and release in intact bovine retinal rod outer segments. Journal of Biological Chemistry 268:12449–57. [PPMS]10.1016/S0021-9258(18)31410-8CrossRefGoogle ScholarPubMed
Scholz, K. P. & Byrne, J. H. (1988) Intracellular injection of cAMP induces a long-term reduction of neuronal K+ currents. Science 240:1664–66. [aZX]10.1126/science.2837826CrossRefGoogle ScholarPubMed
Schulte, T. H. & Marchesi, V. T. (1979) Conformation of the human erythrocyte glycophorin A and its constituent peptides. Biochemistry 18:275–80. [ADA]10.1021/bi00569a006CrossRefGoogle ScholarPubMed
Scott, K., Sieving, P. A., Bingham, E., Bhagat, V. J., Sullivan, J., Alpern, M. & Richards, J. E. (1993) Rhodopsin mutations associated with autosomal dominant retinitis pigmentosa. American Journal of Human Genetics 53:147. [aSPD]Google Scholar
Shapley, R. & Enroth-Cugell, C. (1984) Visual adaptation and retinal gain controls. Progress in Retinal Research 3:263–46. [aMDB]10.1016/0278-4327(84)90011-7CrossRefGoogle Scholar
Sheffield, V. C., Fishman, G. A., Beck, J. S., Kimura, A. E. & Stone, E. M. (1991) Identification of novel rhodopsin mutations associated with retinitis pigmentosa by GC-damped denaturing gradient gel electrophoresis. American Journal of Human Genetics 49:699–706. [aSPD]Google ScholarPubMed
Shichi, H., Lewis, M. S., Irreverre, F. & Stone, A. L. (1969) Biochemistry of visual pigments: 1. Purification and properties of bovine rhodopsin. Journal of Biological Chemistry 244:529–36. [aPAH]10.1016/S0021-9258(18)94389-9CrossRefGoogle Scholar
Shinozawa, T., Sokabe, M., Terada, S., Matsusaka, H. & Yoshizawa, T. (1987) Detection of cyclic GMP binding protein and ion channel activity in frog rod outer segments. Journal of Biochemistry 102:281–20. [aRSM]10.1093/oxfordjournals.jbchem.a122052CrossRefGoogle ScholarPubMed
Shiono, T., Hotta, Y., Noro, M., Sakuma, T., Tamai, M., Hayakawa, M., Hashimoto, T., Fujiki, K., Kanai, A. & Nakajima, A. (1992) Clinical features of Japanese family with autosomal dominant retinitis pigmentosa caused by a single point mutation in codon 347 of rhodopsin gene. Japanese Journal of Ophthalmology 36:69–75. [aSPD]Google ScholarPubMed
Shnyrov, V. L. & Berman, A. L. (1988) Calorimetric study of thermal denaturation of vertebrate visual pigments. Biomedica et Biochimica Acta 47:355–62. [aPAH]Google ScholarPubMed
Shuster, T. A. & Farber, D. B. (1984) Phosphorylation in sealed rod outer segments: Effects of cyclic nucleotides. Biochemistry 23:515–21. [aMDB]10.1021/bi00298a018CrossRefGoogle ScholarPubMed
Shuster, T. A., Nagy, A. K., Conly, D. C. & Farber, D. B. (1992) Direct zinc binding to purified rhodopsin and disc membranes. Biochemical Journal 282:123–28. [aPAH]10.1042/bj2820123CrossRefGoogle ScholarPubMed
Sidman, R. L. & Green, M. D. (1965) Retinal degeneration in the mouse: Location of the rd locus in linkage group XVII. Journal of Heredity 56:23–29. [MWK]10.1093/oxfordjournals.jhered.a107364CrossRefGoogle ScholarPubMed
Sidman, R. L. & Green, M. D. (1970) Nervous, a new mutant mouse with cerebellar disease. In: Les mutants pathologiques chez l'animal, ed. Sabourdy, M.. Centre National de la Recherche Scientifique. [MWK]Google Scholar
Sieving, P. A., Richards, J. E., Bingham, E. L. & Naarendorp, F. (1992) Dominant congenital complete nyctalopia and Gly90Asp rhodopsin mutation. Investigative Ophthalmology and Visual Science 33:1397. [aSPD]Google Scholar
Silva, A. J., Paylor, R., Wehner, J. M. & Tanegawa, S. (1992) Impaired spatial learning in a-calcium-calmodulin kinase II mutant mice. Science 257:206–211. [aZX, TWA, EDR]10.1126/science.1321493CrossRefGoogle ScholarPubMed
Silva, A. J., Stevens, C. F., Tonegawa, S. & Wang, Y. (1992) Deficient hippocampal long-term potentiation in alpha-calmodulin kinase II mutant mice. Science 257:201–6. [aZX, EDR]10.1126/science.1378648CrossRefGoogle Scholar
Sitaramayya, A. (1986) Rhodopsin kinase prepared from bovine rod disk membranes quenches light activation of cGMP phosphodiesterase in a reconstituted system. Biochemistry 25:5460–68. [aMDB]10.1021/bi00367a017CrossRefGoogle Scholar
Sitaramayya, A. & Liebman, P. A. (1983a) Mechanism of ATP quench of phosphodiesterase activation in rod disc membranes. Journal of Biological Chemistry 258:1205–9. [aMDB]10.1016/S0021-9258(18)33179-XCrossRefGoogle ScholarPubMed
Sitaramayya, A. & Liebman, P. A. (1983b) Phosphorylation of rhodopsin and quenching of cyclic GMP phosphodiesterase activation by ATP at weak bleaches. Journal of Biological Chemistry 258:12106–9. [aMDB]10.1016/S0021-9258(17)44137-8CrossRefGoogle ScholarPubMed
Skene, J. H. P. (1989) Axonal growth-associated proteins. Annual Review of Neuroscience 12:127–56. [aZX]10.1146/annurev.ne.12.030189.001015CrossRefGoogle ScholarPubMed
Skene, J. H. P., Jacobson, R. D., Snipes, G. J., McGuire, C. B., Norden, J. J. & Freeman, J. A. (1986) A protein induced during nerve growth (GAP-43) is a major component of growth-cone membranes. Science 233:783–86. [aZX]10.1126/science.3738509CrossRefGoogle ScholarPubMed
Skene, J. H. P. & Willard, M. J. (1981a) Changes in axonally transported proteins during axon regeneration in toad retinal ganglion cells. Journal of Cell Biology 89:86–95. [aZX]10.1083/jcb.89.1.86CrossRefGoogle ScholarPubMed
Slack, J. R. & Pockett, S. (1991) Cyclic AMP induces long-term increase in synaptic efficacy in CA1 region of rat hippocampus. Neuroscience Letters 130:69–72. [aZX]10.1016/0304-3940(91)90229-MCrossRefGoogle ScholarPubMed
Small, K. W., Weber, J. L., Roses, A., Lennon, F., Vance, J. M. & Pericak-Vance, N. U. (1992) North Carolina macular dystrophy is assigned to chromosome 6. Genomics 13:681–85. [aSPD]10.1016/0888-7543(92)90141-ECrossRefGoogle ScholarPubMed
Smigel, M. D. (1986) Purification of brain adenylyl cyclase using forskolin affinity chromatography and WGA-Sepharose. Journal of Biological Chemistry 261:1976–82. [aZX]10.1016/S0021-9258(17)36039-8CrossRefGoogle Scholar
Smith, R. J. H., Lee, E. C., Kimberling, W. J., Daiger, S. P., Pelias, M. Z., Keats, B. J. B., Jay, M. L., Bird, A., Reardon, W., Guest, M., Agyagri, R. & Hejtmancik, F. (1992) Localization of two genes for Usher syndrome type I to chromosome 11. Genomics 14:995–1002. [aSPD]10.1016/S0888-7543(05)80122-3CrossRefGoogle ScholarPubMed
Smith, S. J. & Augustine, G. J. (1988) Calcium ions, active zones and synaptic transmitter release. Trends in Neuroscience 11:458–64. [aZX]10.1016/0166-2236(88)90199-3CrossRefGoogle ScholarPubMed
Smith, S. O., Courtin, J., de Groot, H., Gebhard, R. & Lugtenburg, J. (1991) 13C magic angle spinning NMR studies of bathorhodopsin, the primary photoproduct of rhodopsin. Biochemistry 30:7409–15. [SOS]10.1021/bi00244a007CrossRefGoogle ScholarPubMed
Smith, S. O., de Groot, H., Gebhard, R. & Lugtenburg, J. (1992) Magic angle spinning NMR studies on the metarhodopsin II intermediate of bovine rhodopsin: Evidence for an unprotonated Scruff base. Photochemistry & Photobiology 56:1035–39. [SOS]10.1111/j.1751-1097.1992.tb09726.xCrossRefGoogle Scholar
Smith, S. O. & Peersen, O. B. (1992) Solid-state NMR approaches for studying membrane protein structure. Annual Review of Biophysical and Biomolecular Structure 21:25–47. [SOS]10.1146/annurev.bb.21.060192.000325CrossRefGoogle ScholarPubMed
Sneyd, J. & Tranchina, D. (1989) Phototransduction in cones: An inverse problem in enzyme kinetics. Bulletin of Mathematical Biology 51:749–84. [aMDB]10.1007/BF02459659CrossRefGoogle ScholarPubMed
Somlyo, A. P. & Walz, B. (1985) Elemental distribution in rana pipiens retinal rods: Quantitative electron probe analysis. Journal of Physiology (London) 358:183–95. [RLH]10.1113/jphysiol.1985.sp015547CrossRefGoogle ScholarPubMed
Sowadski, J. M. (1994) Crystallization of membrane proteins. Current Opinion in Structural Biology 4:761–64. [RMG]10.1016/S0959-440X(94)90176-7CrossRefGoogle Scholar
Squire, L. R. & Davis, H. P. (1981) The pharmacology of memory: A neurobiological perspective. Annual Review of Pharmacology and Toxicology 21:323–56. [aZX]10.1146/annurev.pa.21.040181.001543CrossRefGoogle ScholarPubMed
Srivastava, D., Fox, D. A. & Hurwitz, R. L. (in press) The role of magnesium in the hydrolysis of cGMP by the bovine retinal rod cGMP phosphodiesterase. Biochemical Journal. [RLH]Google Scholar
Srivastava, D., Hurwitz, R. L. & Fox, D. A. (submitted) Effects of magnesium on cyclic GMP hydrolysis by the bovine retinal rod cyclic GMP phosphodiesterase. [RLH]Google Scholar
Stanton, P. K. & Sarvey, J. M. (1985a) The effect of high-frequency electrical stimulation and norepinephrine on cyclic AMP levels in normal versus norepinephrine-depleted rat hippocampal slices. Brain Research 358:343–48. [aZX]10.1016/0006-8993(85)90981-3CrossRefGoogle ScholarPubMed
Stanton, P. K. & Sarvey, J. M. (1985b) Depletion of norepinephrine, but not serotonin, reduces long-term potentiation in the dentate gyrus of rat hippocampal slices. Journal of Neuroscience 5:2169–76. [aZX]10.1523/JNEUROSCI.05-08-02169.1985CrossRefGoogle Scholar
Steinberg, R. H., Fisher, S. K. & Anderson, D. H. (1980) Disc morphogenesis in vertebrate photoreceptors. Journal of Comparative Neurology 190:501–18. [aMDB]10.1002/cne.901900307CrossRefGoogle ScholarPubMed
Stepanik, P. L., Lerious, V. & McGinnis, J. F. (1993) Developmental appearance, species and tissue specificity of mouse 23-kDa, a retinal calcium-binding protein (recoverin). Experimental Eye Research 57:189–97. [JFM]10.1006/exer.1993.1114CrossRefGoogle Scholar
Stern, J. H., Kaupp, U. B. & MacLeish, P. R. (1986) Control of the light regulated current in rod photoreceptors by cyclic GMP, calcium and L-cis-diltiazem. Proceedings of the National Academy of Sciences USA 83:1167. [aRSM]10.1073/pnas.83.4.1163CrossRefGoogle ScholarPubMed
Stone, E. M., Kimura, A. E., Nichols, B. E., Khadivi, P., Fishman, G. A. & Sheffield, V. C. (1991) Regional distribution of retinal degeneration in patients with proline to histidine mutation in codon-23 of the rhodopsin gene. Ophthalmology 98:1806–13. [aSPD]10.1016/S0161-6420(91)32046-3CrossRefGoogle ScholarPubMed
Stone, E. M., Nichols, B. E., Streb, L. M., Kimura, A. E. & Sheffield, V. C. (1992a) Genetic linkage of vitelliform macular degeneration (Best's disease) to chromosome llql3. Nature Cenetics 1:246–50. [aSPD]10.1038/ng0792-246CrossRefGoogle Scholar
Stone, E. M., Vandenburgh, K., Kimura, A. E., Lam, B. L., Fishman, G. A., Heckenlively, J. R., Castillo, T. A. & Sheffield, V. C. (1993) Novel mutations in the peripherin (RDS) and rhodopsin genes associated with autosomal dominant retinitis pigmentosa (ADRP). Investigative Ophthalmology and Visual Science 34:1149. [aSPD]Google Scholar
Straume, M., Mitchell, D., Miller, J. & Litman, B. J.. (1990) Interconversions of metarhodopsins I and II: A branched photointermediate decay model. Biochemistry 29:9135–42. [ADA]10.1021/bi00491a006CrossRefGoogle Scholar
Stryer, L. (1986) Cyclic GMP cascade of vision. Annual Review of Neuroscience 9:87–119. [aSPD, aRSM]10.1146/annurev.ne.09.030186.000511CrossRefGoogle Scholar
Stryer, L. (1991) Visual excitation and recovery. Journal of Biological Chemistry 266:10711–14. [aMDB, aJBH, aRSM]10.1016/S0021-9258(18)99072-1CrossRefGoogle ScholarPubMed
Subbaraya, I., Qin, N., McGinness, J. F. & Baehr, W. (1994) Cloning and expression of frog recoverin and its interaction with rhodopsin kinase. Investigative Ophthalmology and Visual Science 35:1485. [aJBH, JFM, AY]Google Scholar
Suber, M. L., Pittler, S. J., Qin, N., Wright, G. C., Holcombe, V., Lee, R. H., Craft, C. M., Lolley, R. N., Baehr, W. & Hurwitz, R. L. (1993) Irish setter dogs affected with rod/cone dysplasia contain a nonsense mutation in the rod cGMP phosphodiesterase β-subunit gene. Proceedings of the National Academy of Sciences USA 90:3968–72. [aSPD, MWK]10.1073/pnas.90.9.3968CrossRefGoogle ScholarPubMed
Subramaniam, S., Gerstein, M., Osterhelt, D. & Henderson, R. (1993) Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO Journal 12:1–8. [aPAH, RMG]10.1002/j.1460-2075.1993.tb05625.xCrossRefGoogle ScholarPubMed
Sugimoto, Y., Yatsunami, K., Tsujimoto, M., Khorana, H. G. & Ichikawa, A. (1991) The amino acid sequence of a glutamic acid-rich protein from bovine retina as deduced from the cDNA sequence. Proceedings of the National Academy of Sciences USA 88:3116–19. [rRSM]10.1073/pnas.88.8.3116CrossRefGoogle ScholarPubMed
Suh, K. H. & Hamm, H. (1988) Components I and II form a complex with the beta gamma subunils of G protein in frog rod outer segments. Investigative Ophthalmology and Visual Science 28: 218. [aMDB]Google Scholar
Sullivan, J. M., Makris, G. S., Dickinson, P., Mulhall, L. E. M., Sc, D. A., Forrest, S., Cotton, R. G. H. & Loughnan, M. S. (1993) A new codon 15 rhodopsin gene mutation in autosomal dominant retinitis pigmentosa is associated with sectorial disease. Archives of Ophthalmology 111: 1512–17. [aSPD]10.1001/archopht.1993.01090110078029CrossRefGoogle ScholarPubMed
Sullivan, J. M., Scott, K. M., Falls, B. E., Richards, J. E. & Sieving, P. A. (1993) A novel rhodopsin mutation at the retinal binding site (LYS-296-MET) in ADRP. Investigative Ophthalmology and Visual Science 34: 1149. [aSPD]Google Scholar
Sung, C.-H., Davenport, C. M., Hennessy, J. C., Maumenee, I. H., Jacobson, S. G., Heckenlively, J. R., Nowakowski, R., Fishman, G., Gouras, P. & Nathans, J. (1991) Rhodopsin mutations in autosomal dominant retinitis pigmentosa. Proceedings of the National Academy of Sciences USA 88:6481–85. [aSPD]10.1073/pnas.88.15.6481CrossRefGoogle ScholarPubMed
Sung, C.-H., Davenport, C. M. & Nathans, J. (1993) Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa. Clustering of functional classes along the polypeptide chain. Journal of Biological Chemistry 268: 26645–49. [aSPD]10.1016/S0021-9258(19)74360-9CrossRefGoogle ScholarPubMed
Sung, C.-H., Schneider, B. G., Agarwal, N., Papermaster, D. S. & Nathans, J. (1991) Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa. Proceedings of the National Academy of Sciences USA 88: 8840–44. [aSPD]10.1073/pnas.88.19.8840CrossRefGoogle ScholarPubMed
Sutkowski, E. M., Tang, W., Broome, C. W., Robbins, J. D. & Seamon, K. B. (1994) Biochemistry 33: 12852–859. [MMR]10.1021/bi00209a017CrossRefGoogle Scholar
Takamatsu, K. & Uyemura, K. (1992) Identification of recoverin-like immunorcactivity in mouse brain. Brain Research 571:350–53. [KT]10.1016/0006-8993(92)90676-ZCrossRefGoogle ScholarPubMed
Tamura, T., Nakatani, K. & Yau, K.-W. (1991) Calcium feedback and sensitivity regulation in primate rods. Journal of General Physiology 98: 95–130. [aMDB]10.1085/jgp.98.1.95CrossRefGoogle ScholarPubMed
Tang, W. J. & Gilman, A. G. (1991) Type-specific regulation of adenylyl cyclase by G protein beta gamma subunits. Science 254: 1500–03. [TWA]10.1126/science.1962211CrossRefGoogle ScholarPubMed
Tang, W. J., Krupinski, J. & Gilman, A. G. (1991) Expression and characterization of calmodulin-activated (type I) adenylyl cyclase. Journal of Biological Chemistry 266: 8595–8603. [arZX, TWA, MMR]10.1016/S0021-9258(18)93016-4CrossRefGoogle Scholar
Taussig, R. T., Quarmby, L. R. & Gilman, A. G. (1993) Regulation of purified type I & type III adenylyl cyclases by C protein beta/gamma subunits. Journal of Biological Chemistry 268:9–12. [aZX]10.1016/S0021-9258(18)54106-5CrossRefGoogle Scholar
Thirkill, C. E., Tait, R. C., Tyler, N. K., Roth, A. M. & Keltner, J. L. (1992) The cancer-associated retinopathy antigen is a recoverin-like protein. Investigative Ophthalmology and Visual Science 33: 2768–72. [aJBH, JFM]Google ScholarPubMed
Tiberi, M. & Caron, M. G. (in press) Journal of Biolgical Chemistry. [MMR]Google Scholar
Ting, T. D. & Ho, Y.-K. (1991) Molecular mechanism of GTP hydrolysis by bovine transducin: Pre-steady-state kinetic analyses. Biochemistry 30: 8996–9007. [aMDB]10.1021/bi00101a013CrossRefGoogle ScholarPubMed
Toscano, W. A. Jr, Westcott, K. R., LaPorte, D. C. & Storm, D. R. (1979) Evidence for a dissociable protein subunit required for calmodulin stimulation of brain adenylate cyclase. Proceedings of the National Academy of Sciences USA 76: P5582–86. [aZX]10.1073/pnas.76.11.5582CrossRefGoogle ScholarPubMed
Tola, M. R., Xia, Z., Storm, D. R. & Schimerlik, M. I. (1990). Reconstitution of muscarinic receptor mediated inhibition of adenylyl cyclase. Molecular Pharmacology 37: 950–57. [aZX]Google Scholar
Toyoshima, C. & Unwin, N. (1990) Three-dimensional structure of the acetylcholine receptor by cryoelectron microscopy and helical image reconstruction. Journal of Cell Biology 111:2623–35. [aPAH]10.1083/jcb.111.6.2623CrossRefGoogle ScholarPubMed
Tranchina, D., Sneyd, J. & Cadenas, I. D. (1991) Light adaptation in turtle cones: Testing and analysis of a model for phototransduction. Biophysical Journal 60: 217–37. [aMDB]10.1016/S0006-3495(91)82045-8CrossRefGoogle Scholar
Travis, G. H. (1991) Name dropping. Nature 349: 24. [aSPD]10.1038/349024b0CrossRefGoogle ScholarPubMed
Travis, G. H., Brennan, M. B., Danielson, P. E., Kozak, C. A. & Sutcliffe, J. G. (1989) Identification of photoreceptor-specific mRNA encoded by the gene responsible for retinal degeneration slow (rds). Nature 338: 70–73. [MWK]10.1038/338070a0CrossRefGoogle Scholar
Travis, G. H., Sutcliffe, J. G. & Bok, D. (1991a) The retinal degeneration slow (rds) gene product is a photoreceptor disc membrane-associated glycoprotein. Neuron 6: 61–70. [aSPD, MWK]10.1016/0896-6273(91)90122-GCrossRefGoogle ScholarPubMed
Treisman, G., Bagley, S. & Gnegy, M. (1983) Calmodulin-sensitive and calmodulin-insensitive components of adenylate cyclase activity in rat striatum have differential responsiveness to guanyl nucleotides. Journal of Neurochemistry 41: 1398–1406. [MMR]10.1111/j.1471-4159.1983.tb00838.xCrossRefGoogle ScholarPubMed
Tsuboi, S. Matsumoto, H., Jackson, K. W., Tsujimoto, K., Williams, T. & Yamazaki, A. (1994a) Phosphorylation of an inhibitory subunit of cGMP phosphodiesterase in Rana catesbiana rod photoreceptors: 1. Characterization of the phosphorylation. Journal of Biological Chemistry 269: 15016–23. [aMDB]10.1016/S0021-9258(17)36568-7CrossRefGoogle Scholar
Tsuboi, S., Matsumoto, H. & Yamazaki, A. (1994) Phosphorylation of an inhibitory subunit of cGMP phosphodiesterase in Rana catesbiana rod photoreceptors: 2. A possible mechanism for the turnoff of cGMP phosphodiesterase without GTP hydrolysis. Journal of Biological Chemistry 269: 15024–29. [aMDB, AY]10.1016/S0021-9258(17)36569-9CrossRefGoogle Scholar
Tully, T., Preat, T., Boynton, S. C. & Del Vecchio, M. (in press). Genetic dissection of consolidated memory in Drosophila melanogaster. Cell. [EDR]Google Scholar
Tycko, R. & Smith, S. O. (1993) Symmetry principles in the design of pulse sequences for structural measurements in magic angle spinning nuclear magnetic resonance. Journal of Chemical Physics 98: 932– 43. [SOS]10.1063/1.465078CrossRefGoogle Scholar
Udovichenko, I. P., Cunnick, J., Gonzalez, K. & Takemoto, D. J. (1994) Functional effect of phosphorylation of the photoreceptor phosphodiesterase inhibitory subunit by protein kinase C. Journal of Biological Chemistry 269: 9850–56. [aMDB]10.1016/S0021-9258(17)36961-2CrossRefGoogle ScholarPubMed
Uhl, R., Wagner, R. & Ryba, N. (1990) Watching C proteins at work. Trends in Neuroscience 13:64–70. [aMDB]10.1016/0166-2236(90)90070-QCrossRefGoogle Scholar
Ulshafer, R. J., Garcia, C. A. & Hollyfield, J. G. (1980) Sensitivity of photoreceptors to elevated levels of cGMP in the human retina. Investigative Ophthamology and Visual Science 19: 1236–41. [aSPD]Google ScholarPubMed
Ulshafer, R. J., Sherry, D. M., Dawson, R. Jr, & Wallace, D. R. (1990) Excitatory amino acid involvement in retinal degeneration. Brain Research 531: 350–54. [MT]10.1016/0006-8993(90)90800-QCrossRefGoogle ScholarPubMed
Unger, V. M., Hargrave, P. A. & Schertler, G. F. X. (1995) Localization of the transmembrane helices in the three-dimensional structure of frog rhodopsin. Biophysics Journal 68: A330. [rPAH]Google Scholar
Unwin, P. N. T. & Zampighi, G. (1980) Structure of the junction between communicating cells. Nature 283: 545–49. [aPAH]10.1038/283545a0CrossRefGoogle ScholarPubMed
Vaithinathan, R., Berson, E. L. & Dryja, T. P. (1993) Further screening of the rhodopsin gene in patients with autosomal dominant retinitis pigmentosa. Investigative Ophthalmology and Visual Science 34:1149. [aSPD]Google Scholar
van der Steen, R., Groesbeek, M., van Amsterdam, L. J. P., Lugtenburg, J., van Oostrum, J. & de Grip, W. J. (1989) All E–10,20-methanoretinylopsin, light-stable rhodopsin. Synthesis and spectroscopy of all E–10,20-methano- and all-E-retinoyl fluoride and their reaction with bovine opsin. Recueil des Travauz Chimiques des Pays-Bos 108:20–27. [aPAH]10.1002/recl.19891080105CrossRefGoogle Scholar
Van Nie, R., Ivanyi, D. & Demant, P. 91978) A new H-2 linked mutation, rds, causing retinal degeneration in the mouse. Tissue Antigens 12: 106–8. [MWK]Google Scholar
van Soest, S., van den Bora, L. I., Gal, A., Farrar, G. J., Bleeker, Wagemakers L. M., Westerveld, A., Humphries, P., Sandkuijl, L. A. & Bergen, A. A. B. (1994) Assignment of a gene for autosomal dominant recessive retinitis pigmentosa (RP12) to chromosome lq31-q32.1 in an inbred and genetically heterogeneous disease population. Genomics 22: 499–504. [aSPD, AB]10.1006/geno.1994.1422CrossRefGoogle Scholar
Vanderkooi, G. (1974) Organisation of proteins in membranes with special reference to the cytochrome oxidase system. Biochimica et Biophysica Acta 344: 307–45. [aPAH]10.1016/0304-4157(74)90011-2CrossRefGoogle Scholar
Villacres, E. C., Xia, Z., Bookbinder, L. H., Edelhoff, S., Adler, D. A., Disteche, C. M. & Storm, D. R. (1993) Cloning, chromosomal mapping, and expression of human fetal brain type I adenylyl cyclase. Genomics 16: 473–78. [aZX]10.1006/geno.1993.1213CrossRefGoogle ScholarPubMed
Vuong, T. M. & Chabre, M. (1990) Subsecond deactivation of transducin by endogenous GTP hydrolysis. Nature 346: 71–74. [aMDB]10.1038/346071a0CrossRefGoogle ScholarPubMed
Vuong, T. M. & Chabre, M. (1991) Deactivation kinetics of the transduction cascade of vision. Proceedings of the National Academy of Sciences USA 88: 9813–17. [aMDB]10.1073/pnas.88.21.9813CrossRefGoogle Scholar
Vuong, R. M., Chabre, M. & Stryer, L. (1984) Millisecond activation of transducin in the cyclic nucleotide cascade of vision. Nature 311:659–61. [aMDB]10.1038/311659a0CrossRefGoogle Scholar
Wagner, R., Ryba, N. & Uhl, R. (1988) Sub-second turnover of transducin GTPase in bovine rod outer segments. FEBS Letters 234:44–48. [aMDB]10.1016/0014-5793(88)81299-7CrossRefGoogle ScholarPubMed
Wagner, R., Ryba, N. & Uhl, R. (1989) Calcium regulates the rate of rhodopsin disactivation and the primary amplification step in visual transduction. FEBS Letters 242:249–54. [aMDB]10.1016/0014-5793(89)80479-XCrossRefGoogle ScholarPubMed
Wahlsten, D. (1991) Sample size to detect a planned contrast and a one degree-of-freedom interaction effect. Psychological Bulletin 110:587–95. [DW]10.1037/0033-2909.110.3.587CrossRefGoogle Scholar
Walsh, M. P., Valentine, K. A., Ngai, P. K., Carruthers, C. A. & Hollenberg, M. D. (1984) Ca2+-dependent hydrophobic-interaction chromatography: Isolation of a novel Ca2+-binding protein and protein kinase C from bovine brain. Biochemistry Journal 224:117–27. [KT]10.1042/bj2240117CrossRefGoogle ScholarPubMed
Wang, N. & Rasenick, M. M. (1991) Tubulin-G protein interactions involve microtubule polymerization domains. Biochemistry 30: 10957– 65. [MMR]10.1021/bi00109a021CrossRefGoogle ScholarPubMed
Wang, N., Yan, K. & Rasenick, M. M. (1990) Tubulin binds specifically to the signal-transducing proteins, Csa and Gial. Journal of Biological Chemistry 265: 1239–42. [MMR]10.1016/S0021-9258(19)40002-1CrossRefGoogle Scholar
Watanabe, S. I. & Murakami, M. (1991) Similar properties of the cGMPactivated channels between cones and rods in the carp retina. Visual Neuroscience 6:563–68. [aRSM]10.1017/S0952523800002546CrossRefGoogle ScholarPubMed
Watson, J. B., Battenberg, E. F., Wong, K. K., Bloom, F. E. & Sutcliffe, J. G. (1990) Subtractive cDNA cloning of RC3, a rodent cortex-enriched mRNA encoding a novel 78 residue protein. Journal of Neuroscience Research 26:397–408. [EDR]10.1002/jnr.490260402CrossRefGoogle ScholarPubMed
Watson, J. B., Sutcliffe, J. G. & Fisher, R. S. (1992) Localization of the protein kinase C phosphorylation/calmodulin binding substrate RC3 in dendritic spines of neostriatal neurons. Proceedings of the National Academy of Sciences USA 89: 8581–85. [EDR]10.1073/pnas.89.18.8581CrossRefGoogle Scholar
Wayman, G. A., Impey, S., Wu, Z., Kinsvogel, W., Prichard, L. & Storm, D. R. (1994) Synergistic activation of the type I adenylyl cyclase by Ca2+ and Gs coupled receptors in vivo. Journal of Biological Chemistry 269: 25400–5. [arZX, TWA, MMR]10.1016/S0021-9258(18)47263-8CrossRefGoogle ScholarPubMed
Weber, B. H. F., Vogt, G., Pruett, R. C., Stöhr, H. & Felbor, U. (1994) Mutations in the tissue inhibitor of metalloproteinases-3 (TIMP3) in patients with Sorby's fundus dystrophy. Nature Genetics 8: 352–55. [rSPD]10.1038/ng1294-352CrossRefGoogle Scholar
Wehner, R., Marsh, A. C. & Wehner, S. (1992) Desert ants on a thermal tightrope. Nature 357: 586–87. [aPAH]10.1038/357586a0CrossRefGoogle Scholar
Weitz, C. J. & Nathans, J. (1992) Histidine residues regulate the transition of photoexcited rhodopsin to its active conformation, metarhodopsin II. Neuron 8:465–72. [aSPD]10.1016/0896-6273(92)90274-HCrossRefGoogle ScholarPubMed
Weitz, C. J., Went, L. N. & Nathans, J. (1992a) Human tritanopia associated with a third amino acid substitution in the blue-sensitive visual pigment. American Journal of Human Genetics 51:444–46. [aSPD]Google ScholarPubMed
Weleber, R. G., Carr, R. E., Murphey, W. H., Sheffield, V. & Stone, E. M. (1993) Phenotypic variation including retinitis pigmentosa, pattern dystrophy and fundus flavimaculatis in a single family with a deletion of codon 153 or 154 of the pheripherin/RDS gene. Archives of Ophthalmology 111: 1531–42. [AB, aSPD]10.1001/archopht.1993.01090110097033CrossRefGoogle Scholar
Well, D., Blanchard, S., Kaplan, J., Guilford, P., Gibson, F., Walsh, J., Mburu, P., Varela, A., Levillers, J., Weston, M. D., Kelly, P. M., Kimberling, W. J., Wagenaar, M., Levi-Acobas, F., Larget-Piet, D., Munnich, A., Steel, K. P., Brown, S. D. M. & Petit, C. (1995) Defective mysin VIIA gene responsible for Usher syndrome type IB. Nature 374:60–61. [rSPD]10.1038/374060a0CrossRefGoogle Scholar
Wells, J., Wroblewski, J., Keen, J., Inglehearn, C., Jubb, C., Eckstein, A., Jay, M., Arden, G., Bhattacharya, S., Fitzke, F. & Bird, A. (1993) Mutations in the human retinal degeneration slow (rds) gene can cause either retinitis pigmentosa or macular dystrophy. Nature Genetics 3: 213–18. [aSPD]10.1038/ng0393-213CrossRefGoogle ScholarPubMed
Welte, W. & Wacker, T. (1991). Protein-detergent micellar solutions for the crystallization of membrane proteins: Some general approaches and experiences with the crystallization of pigment-protein complexes from purple bacteria. In: Crystallization of membrane proteins, ed. Michel, H.. CRC Press. [aPAH]Google Scholar
Westcott, K. R., LaPorte, D. C. & Storm, D. R. (1979) Resolution of adenylyl cyclase sensitive and insensitive to Ca2+ and CDR by CDR-sepharose affinity chromatography. Proceedings of the National Academy of Sciences USA 76: 204–28. [WH, aZX]10.1073/pnas.76.1.204CrossRefGoogle ScholarPubMed
Weyand, I., Godde, M., Frings, S., Weiner, J., Müller, , Altenhofen, W., Hatt, H. & Kaupp, U. B. (1994) Cloning and functional expression of a cyclicnucleotide-gated channel from mammalian sperm. Nature 368: 859–63. [rRSM]10.1038/368859a0CrossRefGoogle Scholar
Whelan, J. P. & McGinnis, J. F. (1988) Light-dependent subcellular movement of photoreceptor proteins. Journal of Neuroscience Research 20: 263–70. [JFM]10.1002/jnr.490200216CrossRefGoogle ScholarPubMed
Wilden, U., Hall, S. W. & Kuhn, H. (1986) Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48 KDa protein of rod outer segments. Proceedings of the National Academy of Sciences USA 83:1174–78. [aMDB]10.1073/pnas.83.5.1174CrossRefGoogle ScholarPubMed
Wilden, U. & Kuhn, H. (1982) Light-dependent phosphorylation of rhodopsin: Number of phosphorylation sites. Biochemistry 21: 3014–22. [aMDB]10.1021/bi00541a032CrossRefGoogle ScholarPubMed
Williams, D. S., Linberg, K. A., Vaughan, D. K., Fariss, R. N. & Fisher, S. K. (1988) Disruption of microfilament organization and deregulation of disk membrane morphogenesis by cytochalasin D in rod and cone photoreceptors. Journal of Comparative Neurology 272:161–76. [aMDB]10.1002/cne.902720202CrossRefGoogle ScholarPubMed
Wohlfart, P., Haase, H., Molday, R. S. & Cook, N. J. (1992) Antibodies against synthetic peptides used to determine the topology and site of glycosylation of the cGMP-gated channel from bovine rod photoreceptors. Journal of Biological Chemistry 267:644–48. [aRSM]10.1016/S0021-9258(18)48542-0CrossRefGoogle ScholarPubMed
Wohlfart, P., Muller, H. & Cook, N. J. (1989) Lectin binding and enzymatic deglycosylation of cGMP-gated channel from bovine rod photoreceptors. Journal of Biological Chemistry 264:20934–39. [aRSM]10.1016/S0021-9258(19)30026-2CrossRefGoogle ScholarPubMed
Wong, S. & Molday, R. S. (1986) A spectrin-like protein in retinal rod outer segments. Biochemistry 25: 6294–6300. [aRSM]10.1021/bi00368a069CrossRefGoogle ScholarPubMed
Wu, S. M., Qiao, X., Noebels, J. L. & Yang, X. L.: Localization and modulatory actions of zinc in vertebrate retina. Vision Research 33:2611–16. [MT]10.1016/0042-6989(93)90219-MCrossRefGoogle Scholar
Wu, Z., Thomas, S. A., Xia, Z., Willacres, E. C., Palmiter, R. D. & Storm, D. R. (in press) Deficient spatial memory and altered LTP in type 1 adenylyl cyclase mutant mice. Proceedings of the National Academy of Sciences 92: 220–4. [arZX]10.1073/pnas.92.1.220CrossRefGoogle Scholar
Wu, Z., Wong, S. T. & Storm, D. R. (1993) Modification of the calcium and calmodulin sensitivity of the type I adenylyl cyclase by mutagenesis of its calmodulin binding domain. Journal of Biological Chemistry 268:23766–68. [aZX]10.1016/S0021-9258(20)80447-5CrossRefGoogle ScholarPubMed
Xia, Z., Choi, E. J., Wang, F., Blazynski, C., & Storm, D. R. (1993) The type I calmodulin sensitive adenylyl cyclase is neural specific. Journal of Neurochemistry 60: 305–11. [aZX]10.1111/j.1471-4159.1993.tb05852.xCrossRefGoogle ScholarPubMed
Xia, Z., Choi, E. J., Wang, F. & Storm, D. R. (1992) The type III calcium/calmodulin-sensitive adenylyl cyclase is not specific to olfactory sensory neurons. Neuroscience Letters 144:169–73. [aZX]10.1016/0304-3940(92)90742-PCrossRefGoogle Scholar
Xia, Z., Refsdal, C. D., Merchant, K. M., Dorsa, D. M. & Storm, D. R. (1991) Distinct patterns for the distribution of mRNA for the calmodulinsensitive adenylyl cyclase in rat brain: Expression in areas associated with learning and memory. Neuron 6: 431–43. [aZX]10.1016/0896-6273(91)90251-TCrossRefGoogle Scholar
Yamagata, K., Goto, K., Kuo, C.-H., Kondo, H. & Miki, N. (1990) Visinin: A novel calcium binding protein expressed in retinal cone cells. Neuron 2:469–76. [aJBH, KT]10.1016/0896-6273(90)90059-OCrossRefGoogle Scholar
Yamazaki, A., Hayashi, F., Tatsumi, M., Bitenski, M. W. & George, J. S. (1990) Interaction between the subunits of transducin and cyclic GMP phosphodiesterase in Rana catesbiana rod photoreceptors. Journal of Biological Chemistry 265: 11539–48. [aMDB, AY]10.1016/S0021-9258(19)38431-5CrossRefGoogle ScholarPubMed
Yamazaki, A., Yamazaki, M., Tsuboi, S., Kishigami, A., Umbarger, K. O., Hutson, L. D., Madland, W. T. & Hayashi, F. (1993) Regulation of G protein function by an effector in GTP-dependent signal transduction. An inhibitory subunit of cGMP phosphodiesterase inhibits GTP hydrolysis by transducin in vertebrate rod photoreceptors. Journal of Biological Chemistry 268:8899–8907. [rMDB]10.1016/S0021-9258(18)52958-6CrossRefGoogle ScholarPubMed
Yarfitz, S. & Hurley, J. B. (1994) Transduction mechanisms of vertebrate and invertebrate photoreceptors. Journal of Biological Chemistry 269: 14329–32. [aMDB]10.1016/S0021-9258(17)36620-6CrossRefGoogle ScholarPubMed
Yau, K.-W. (1994) Phototransduction mechanism in retinal rods and cones: The Friedenwald lecture. Investigative Ophthalmology and Visual Science 35: 9–32. [aMDB]Google ScholarPubMed
Yau, K.-W. & Baylor, D. A. (1989) Cyclic GMP-activated conductance of retinal photoreceptor cells. Annual Review of Neuroscience 12:289–327. [arMDB, aRSM, LWH, RLH]10.1146/annurev.ne.12.030189.001445CrossRefGoogle ScholarPubMed
Yau, K.-W & Nakatani, K. (1984a) Electrogenic Na-Ca exchange in retinal rod outer segment. Nature 311:661–63. [aRSM]10.1038/311661a0CrossRefGoogle ScholarPubMed
Yau, K.-W & Nakatani, K.(1984b) Cation selectivity of light-sensitive conductance in retinal rods. Nature 309:352–54. [aRSM]10.1038/309352a0CrossRefGoogle ScholarPubMed
Yau, K.-W & Nakatani, K.(1985a) Light-suppressible, cyclic GMP-sensitive conductance in the plasma membrane of a truncated rod outer segment. Nature 317: 252–55. [aRSM]10.1038/317252a0CrossRefGoogle ScholarPubMed
Yau, K.-W & Nakatani, K. (1985b) Light-induced reduction of cytoplasmic free calcium in retinal rod outer segment. Nature 313: 579–82. [aRSM]10.1038/313579a0CrossRefGoogle ScholarPubMed
Yeager, R. E., Heideman, W., Rosenberg, G. B. & Storm, D. R. (1985) Purification of the calmodulin-sensitive sensitive adenylyl cyclase from bovine brain. Biochemistry 24:3776–83. [aZX]10.1021/bi00335a054CrossRefGoogle Scholar
Yellen, G., Jurman, M. E., Abramson, T. & MacKinnon, R. (1991) Mutations affecting internal TEA blockage identify the probable pore-forming region of K+ channels. Science 251:939–42. [aRSM]10.1126/science.2000494CrossRefGoogle Scholar
Yool, A. J. & Schwartz, T. L. (1991) Alteration of ionic selectivity of a K+ channel by mutation of the H5 region. Nature 349:700–4.[aRSM]10.1038/349700a0CrossRefGoogle Scholar
Yoshida, T., Willardson, B. M., Wilkins, J. F., Jensen, G. J., Thornton, B. D. & Bitensky, M. W. (1994) The phosphorylation state of phosducin determines its ability to block transducin subunit interactions and inhibit transducin binding to activated rhodopsin. Journal of Biological Chemistry 269: 24050–57. [BMW]10.1016/S0021-9258(19)51046-8CrossRefGoogle ScholarPubMed
Yoshikami, S., George, J. S. & Hagins, W. A. (1980) Light-induced calcium fluxes from outer segment layer of vertebrate retinas. Nature 287:395–98. [TGW]10.1038/286395a0CrossRefGoogle Scholar
Yoshimura, M. & Cooper, D. M. (1992) Cloning and expression of a Ca2+ inhibitable adenylyl cyclase from NCB-20 cells. Proceedings of National Academy of Sciences USA 89: 6716–20. [aZX]10.1073/pnas.89.15.6716CrossRefGoogle ScholarPubMed
Younger, J. P., McCarthy, S. T. & Owen, W. G. (1992) Modulation of cytosolic free calcium and changes in sensitivity and circulating current occur over the same range of steady-state adapting lights in rod photoreceptors. Incostigatice Ophthalmology and Visual Science 33: 1104. [aMDB]Google Scholar
Yovell, Y. & Abrams, T. W. (1992) Temporal asymmetry in activation of Aplysia adenylyl cyclase may explain properties of conditioning. Proceedings of the National Academy of Sciences USA 89: 6526–30. [TWA]10.1073/pnas.89.14.6526CrossRefGoogle Scholar
Yovell, Y., Kandel, E. R., Dudai, Y. & Abrams, T. W. (1992) A quantitative study of the Ca2+/calmodulin sensitivity of adenylyl cyclase in Aplysia, Drosophila, and rat. Journal of Ncurochemistry 59: 1736–44. [aZX]10.1111/j.1471-4159.1992.tb11005.xCrossRefGoogle ScholarPubMed
Yurkova, E. V., Demin, V. V. & Abdulaev, N. G. (1990) Crystallization of membrane proteins: Bovine rhodopsin. Biotnedical Science 1: 585–90. [aPAH]Google ScholarPubMed
Zankel, T., Ok, H., Johnson, R., Chang, C. W., Sekiya, N., Naoki, H., Yoshihara, K. & Nakanishi, K. (1990) Bovine rhodopsin with 11-cis-locked retinal chromophore neither activates rhodopsin kinase nor undergoes conformational change upon irradiation. Journal of the American Chemical Society 112: 5387–88. [aPAH]10.1021/ja00169a077CrossRefGoogle Scholar
Zhong, Y. & Wu, C. F. (1991) Altered synaptic plasticity in Drosophila memory mutants with a defective cyclic AMP cascade. Science 251:198–201. [aZX]10.1126/science.1670967CrossRefGoogle ScholarPubMed
Zhukovsky, E. A. & Oprian, D. D. (1989) Effect of carboxylic acid side chains on the absorption maximum of visual pigments. Science 245:928–30. [aPAH]10.1126/science.2573154CrossRefGoogle Scholar
Zimmerman, A. L. & Baylor, D. A. (1986) Cyclic GMP-sensitive conductance of retinal rods consists of aqueous pores. Nature 321:70–72. [aRSM]10.1038/321070a0CrossRefGoogle ScholarPubMed
Zimmmerman, A. L., Yamanaka, G., Eckstein, F., Baylor, D. A., & Stryer, L. (1985) Interaction of hydrolysis-resistant analogs of cyclic GMP with the phosphodiesterase and light-sensitive channel of retinal rod outer segments. Proceedings of the National Academy of Sciences USA 82:8813–17. [aRSM]10.1073/pnas.82.24.8813CrossRefGoogle Scholar
Zong-Yi, L., Jacobson, S. G. & Milam, S. G. (1994) Autosomal dominant retinitis pigmentosa caused by the threonine-17-methionine rhodopsin mutation: Retinal histopathology and immunochemistry. Experimental Eye Research 58:397–408. [AB]Google Scholar
Zozulya, S. & Stryer, L. (1992) Calcium-myristoyl protein switch. Proceedings of the National Academy of Sciences USA 89:11569–73. [aJBH, SK]10.1073/pnas.89.23.11569CrossRefGoogle ScholarPubMed