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Davidson, F. F., Loewen, P. C., Khorana, H. G. (1994) Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state. Proceedings of the National Academy of Sciences, 91 (9) 4029-4033 doi:10.1073/pnas.91.9.4029

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Reference TypeJournal (article/letter/editorial)
TitleStructure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state.
JournalProceedings of the National Academy of Sciences
AuthorsDavidson, F. F.Author
Loewen, P. C.Author
Khorana, H. G.Author
Year1994 (April 26)Volume91
Issue9
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.91.9.4029Search in ResearchGate
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Mindat Ref. ID1554718Long-form Identifiermindat:1:5:1554718:3
GUID0
Full ReferenceDavidson, F. F., Loewen, P. C., Khorana, H. G. (1994) Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state. Proceedings of the National Academy of Sciences, 91 (9) 4029-4033 doi:10.1073/pnas.91.9.4029
Plain TextDavidson, F. F., Loewen, P. C., Khorana, H. G. (1994) Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state. Proceedings of the National Academy of Sciences, 91 (9) 4029-4033 doi:10.1073/pnas.91.9.4029
In(1994, April) Proceedings of the National Academy of Sciences Vol. 91 (9) Proceedings of the National Academy of Sciences

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Resek, J. F., Farrens, D., Khorana, H. G. (1994) Structure and function in rhodopsin: covalent crosslinking of the rhodopsin (metarhodopsin II)-transducin complex--the rhodopsin cytoplasmic face links to the transducin alpha subunit. Proceedings of the National Academy of Sciences, 91 (16) 7643-7647 doi:10.1073/pnas.91.16.7643
Sakamoto, T., Khorana, H. G. (1995) Structure and function in rhodopsin: the fate of opsin formed upon the decay of light-activated metarhodopsin II in vitro. Proceedings of the National Academy of Sciences, 92 (1) 249-253 doi:10.1073/pnas.92.1.249
Hwa, J., Reeves, P. J., Klein-Seetharaman, J., Davidson, F., Khorana, H. G. (1999) Structure and function in rhodopsin: Further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function. Proceedings of the National Academy of Sciences, 96 (5) 1932-1935 doi:10.1073/pnas.96.5.1932
Karnik, S. S., Sakmar, T. P., Chen, H. B., Khorana, H. G. (1988) Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin. Proceedings of the National Academy of Sciences, 85 (22) 8459-8463 doi:10.1073/pnas.85.22.8459
Mollaaghababa, R., Davidson, F. F., Kaiser, C., Khorana, H. G. (1996) Structure and function in rhodopsin: expression of functional mammalian opsin in Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences, 93 (21) 11482-11486 doi:10.1073/pnas.93.21.11482
Kaushal, S., Ridge, K. D., Khorana, H. G. (1994) Structure and function in rhodopsin: the role of asparagine-linked glycosylation. Proceedings of the National Academy of Sciences, 91 (9) 4024-4028 doi:10.1073/pnas.91.9.4024
Hwa, J., Klein-Seetharaman, J., Khorana, H. G. (2001) Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants. Proceedings of the National Academy of Sciences, 98 (9) 4872-4876 doi:10.1073/pnas.061632798
Niu, L., Kim, J.-M., Khorana, H. G. (2002) Structure and function in rhodopsin: Asymmetric reconstitution of rhodopsin in liposomes. Proceedings of the National Academy of Sciences, 99 (21) 13409-13412 doi:10.1073/pnas.212518899
Thurmond, R. L., Creuzenet, C., Reeves, P. J., Khorana, H. G. (1997) Structure and function in rhodopsin: Peptide sequences in the cytoplasmic loops of rhodopsin are intimately involved in interaction with rhodopsin kinase. Proceedings of the National Academy of Sciences, 94 (5) 1715-1720 doi:10.1073/pnas.94.5.1715
Kim, J.-M., Altenbach, C., Thurmond, R. L., Khorana, H. G., Hubbell, W. L. (1997) Structure and function in rhodopsin: Rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state. Proceedings of the National Academy of Sciences, 94 (26) 14273-14278 doi:10.1073/pnas.94.26.14273
Liu, X., Garriga, P., Khorana, H. G. (1996) Structure and function in rhodopsin: correct folding and misfolding in two point mutants in the intradiscal domain of rhodopsin identified in retinitis pigmentosa. Proceedings of the National Academy of Sciences, 93 (10) 4554-4559 doi:10.1073/pnas.93.10.4554
 
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