Associated Papers
Structure of human green cone opsin yields insights into mechanisms underlying the rapid decay of its active, signaling state.
Yao W et al.
Proceedings of the National Academy of Sciences of the United States of America, 2025
41329744 (PubMed )
Supplement: pnas.2516318122.sapp.pdf
Role of the retinal hydrogen bond network in rhodopsin Schiff base stability and hydrolysis.
Janz JM et al.
The Journal of Biological Chemistry, 2004
The spectrum of human rhodopsin disease mutations through the lens of interspecific variation.
Briscoe AD et al.
Gene, 2004
Point mutations in bovine opsin can be classified in four groups with respect to their effect on the biosynthetic pathway of opsin.
DeCaluwé GL et al.
The Biochemical Journal, 1996
Molecular Architecture of G Protein-Coupled Receptors.
van Rhee AM et al.
Drug Development Research, 1996
Light-stable rhodopsin. II. An opsin mutant (TRP-265----Phe) and a retinal analog with a nonisomerizable 11-cis configuration form a photostable chromophore.
Ridge KD et al.
The Journal of Biological Chemistry, 1992
Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin.
Nakayama TA et al.
The Journal of Biological Chemistry, 1991
Structural coupling of 11-cis-7-methyl-retinal and amino acids at the ligand binding pocket of rhodopsin.
Aguilà M et al.
Photochemistry and Photobiology, 0
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