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
The Role of Individual Residues in the N-Terminus of Arrestin-1 in Rhodopsin Binding.
Vishnivetskiy SA et al.
International Journal of Molecular Sciences, 2025
Long-term vitamin A supplementation in a preclinical mouse model for RhoD190N-associated retinitis pigmentosa.
Cui X et al.
Human Molecular Genetics, 2022
New insights into the molecular mechanism of rhodopsin retinitis pigmentosa from the biochemical and functional characterization of G90V, Y102H and I307N mutations.
Herrera-Hernández MG et al.
Cellular and Molecular Life Sciences : Cmls, 2022
Light Dynamics of the Retinal-Disease-Relevant G90D Bovine Rhodopsin Mutant.
Kubatova N et al.
Angewandte Chemie (international Ed. in English), 2020
Schizorhodopsins: A family of rhodopsins from Asgard archaea that function as light-driven inward H+ pumps.
Inoue K et al.
Science Advances, 2020
Residues and residue pairs of evolutionary importance differentially direct signaling bias of D2 dopamine receptors.
Terrón-Díaz ME et al.
The Journal of Biological Chemistry, 2019
Screening of Chemical Libraries Using a Yeast Model of Retinal Disease.
Scott BM et al.
Slas Discovery : Advancing Life Sciences R & D, 2019
Molecular assembly of rhodopsin with G protein-coupled receptor kinases.
He Y et al.
Cell Research, 2017
Structure and dynamics of a constitutively active neurotensin receptor.
Krumm BE et al.
Scientific Reports, 2016
The mutation p.E113K in the Schiff base counterion of rhodopsin is associated with two distinct retinal phenotypes within the same family.
Reiff C et al.
Scientific Reports, 2016
Relocating the Active-Site Lysine in Rhodopsin: 2. Evolutionary Intermediates.
Devine EL et al.
Biochemistry, 2016
A structural snapshot of the rhodopsin-arrestin complex.
Kang Y et al.
The Febs Journal, 2016
Analysis of Conserved Glutamate and Aspartate Residues in Drosophila Rhodopsin 1 and Their Influence on Spectral Tuning.
Zheng L et al.
The Journal of Biological Chemistry, 2015
Crystallization scale preparation of a stable GPCR signaling complex between constitutively active rhodopsin and G-protein.
Maeda S et al.
Plos One, 2014
Spectral tuning of ultraviolet cone pigments: an interhelical lock mechanism.
Sekharan S et al.
Journal of the American Chemical Society, 2013
Insights into congenital stationary night blindness based on the structure of G90D rhodopsin.
Singhal A et al.
Embo Reports, 2013
Rapid release of retinal from a cone visual pigment following photoactivation.
Chen MH et al.
Biochemistry, 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
Site-directed mutations and the polymorphic variant Ala160Thr in the human thromboxane receptor uncover a structural role for transmembrane helix 4.
Chakraborty R et al.
Plos One, 2012
The structural basis of agonist-induced activation in constitutively active rhodopsin.
Standfuss J et al.
Nature, 2011
Structural impact of the E113Q counterion mutation on the activation and deactivation pathways of the G protein-coupled receptor rhodopsin.
Standfuss J et al.
Journal of Molecular Biology, 2008
G protein-coupled receptors disrupted in human genetic disease.
Thompson MD et al.
Methods in Molecular Biology (clifton, N.j.), 2008
Engineering a "steric doorstop" in rhodopsin: converting an inverse agonist to an agonist.
McKee TD et al.
Biochemistry, 2007
Comparison of the retinitis pigmentosa mutations in rhodopsin with a functional map of the C5a receptor.
Hagemann IS et al.
Vision Research, 2006
Vertebrate opsins belonging to different classes vary in constitutively active properties resulting from salt-bridge mutations.
Nickle B et al.
Biochemistry, 2006
Role of the retinal hydrogen bond network in rhodopsin Schiff base stability and hydrolysis.
Janz JM et al.
The Journal of Biological Chemistry, 2004
Structural origins of constitutive activation in rhodopsin: Role of the K296/E113 salt bridge.
Kim JM et al.
Proceedings of the National Academy of Sciences of the United States of America, 2004
Assessing structural elements that influence Schiff base stability: mutants E113Q and D190N destabilize rhodopsin through different mechanisms.
Janz JM et al.
Vision Research, 2003
Opsin activation as a cause of congenital night blindness.
Jin S et al.
Nature Neuroscience, 2003
Slow binding of retinal to rhodopsin mutants G90D and T94D.
Gross AK et al.
Biochemistry, 2003
Characterization of rhodopsin congenital night blindness mutant T94I.
Gross AK et al.
Biochemistry, 2003
Unusual thermal and conformational properties of the rhodopsin congenital night blindness mutant Thr-94 --> Ile.
Ramon E et al.
The Journal of Biological Chemistry, 2003
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
Constitutive activation of opsin by mutation of methionine 257 on transmembrane helix 6.
Han M et al.
Biochemistry, 1998
Rhodopsin arginine-135 mutants are phosphorylated by rhodopsin kinase and bind arrestin in the absence of 11-cis-retinal.
Shi W et al.
Biochemistry, 1998
Partial agonist activity of 11-cis-retinal in rhodopsin mutants.
Han M et al.
The Journal of Biological Chemistry, 1997
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
Characterization of the mutant visual pigment responsible for congenital night blindness: a biochemical and Fourier-transform infrared spectroscopy study.
Zvyaga TA et al.
Biochemistry, 1996
Constitutive activation of opsin: interaction of mutants with rhodopsin kinase and arrestin.
Rim J et al.
Biochemistry, 1995
Active site-directed inactivation of constitutively active mutants of rhodopsin.
Govardhan CP et al.
The Journal of Biological Chemistry, 1994
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
Changing the location of the Schiff base counterion in rhodopsin.
Zhukovsky EA et al.
Biochemistry, 1992
Histidine residues regulate the transition of photoexcited rhodopsin to its active conformation, metarhodopsin II.
Weitz CJ et al.
Neuron, 1992
Determinants of visual pigment absorbance: identification of the retinylidene Schiff's base counterion in bovine rhodopsin.
Nathans J
Biochemistry, 1990