Associated Papers
Molecular Mechanisms Underlying the Spectral Shift in Zebrafish Cone Opsins.
Chi LA et al.
Biorxiv : the Preprint Server for Biology, 2024
Accurate Detection of Convergent Mutations in Large Protein Alignments With ConDor.
Morel M et al.
Genome Biology and Evolution, 2024
Rhodopsin gene polymorphism associated with divergent light environments in Atlantic cod.
Pampoulie C et al.
Behavior Genetics, 2015
Molecular Dynamics of Channelrhodopsin at the Early Stages of Channel Opening.
Takemoto M et al.
Plos One, 2015
Efficiencies of activation of transducin by cone and rod visual pigments.
Imamoto Y et al.
Biochemistry, 2013
Crystal structure of channelrhodopsin, a light-gated cation channel - all cations lead through the monomer.
Kato HE et al.
Biophysics (nagoya-shi, Japan), 2013
Complex patterns of divergence among green-sensitive (RH2a) African cichlid opsins revealed by Clade model analyses.
Weadick CJ et al.
Bmc Evolutionary Biology, 2012
Understanding rhodopsin mutations linked to the retinitis pigmentosa disease: a QM/MM and DFT/MRCI study.
Hernández-Rodríguez EW et al.
The Journal of Physical Chemistry. B, 2012
Effects of exogenous thyroid hormones on visual pigment composition in coho salmon (Oncorhynchus kisutch).
Temple SE et al.
The Journal of Experimental Biology, 2008
Molecular properties of rhodopsin and rod function.
Imai H et al.
The Journal of Biological Chemistry, 2007
The role of Glu181 in the photoactivation of rhodopsin.
Lüdeke S et al.
Journal of Molecular Biology, 2005
Amino acid residues responsible for the meta-III decay rates in rod and cone visual pigments.
Kuwayama S et al.
Biochemistry, 2005
The spectrum of human rhodopsin disease mutations through the lens of interspecific variation.
Briscoe AD et al.
Gene, 2004
Retinitis pigmentosa rhodopsin mutations L125R and A164V perturb critical interhelical interactions: new insights through compensatory mutations and crystal structure analysis.
Stojanovic A et al.
The Journal of Biological Chemistry, 2003
Conserved proline residue at position 189 in cone visual pigments as a determinant of molecular properties different from rhodopsins.
Kuwayama S et al.
Biochemistry, 2002
Development of stable cell lines expressing high levels of point mutants of human opsin for biochemical and biophysical studies.
Sullivan JM et al.
Methods in Enzymology, 2000
Spectroscopic evidence for interaction between transmembrane helices 3 and 5 in rhodopsin.
Beck M et al.
Biochemistry, 1998
Rhodopsin activation: effects on the metarhodopsin I-metarhodopsin II equilibrium of neutralization or introduction of charged amino acids within putative transmembrane segments.
Weitz CJ et al.
Biochemistry, 1993
Constitutive activation of opsin: influence of charge at position 134 and size at position 296.
Cohen GB et al.
Biochemistry, 1993
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
Determinants of visual pigment absorbance: identification of the retinylidene Schiff's base counterion in bovine rhodopsin.
Nathans J
Biochemistry, 1990
Effect of carboxyl mutations on functional properties of bovine rhodopsin.
DeCaluwé GL et al.
Biophysical Chemistry, 0