The C9 methyl group of retinal interacts with glycine-121 in rhodopsin.
about
Photoreceptor current and photoorientation in chlamydomonas mediated by 9-demethylchlamyrhodopsin.Mechanism of rhodopsin activation as examined with ring-constrained retinal analogs and the crystal structure of the ground state proteinHow a small change in retinal leads to G-protein activation: initial events suggested by molecular dynamics calculations.Structure and function of G protein-coupled receptors using NMR spectroscopy.Helix packing in polytopic membrane proteins: role of glycine in transmembrane helix association.Molecular dynamics investigation of primary photoinduced events in the activation of rhodopsin.Uncovering the triggers for GPCR activation using solid-state NMR spectroscopy.Cardiac GPCRs: GPCR signaling in healthy and failing hearts.Point mutations in a nucleoside transporter gene from Leishmania donovani confer drug resistance and alter substrate selectivity.Identification of a functionally critical GXXG motif and its relationship to the folate binding site of the proton-coupled folate transporter (PCFT-SLC46A1)Assays for inverse agonists in the visual systemRetinal orientation and interactions in rhodopsin reveal a two-stage trigger mechanism for activation.The 9-methyl group of retinal is essential for rapid Meta II decay and phototransduction quenching in red cones.Structural analysis and dynamics of retinal chromophore in dark and meta I states of rhodopsin from 2H NMR of aligned membranes.Amino acid conservation and interactions in rhodopsin: probing receptor activation by NMR spectroscopy.Insights into the activation mechanism of the visual receptor rhodopsin.Identification of a glycine motif required for packing in EmrE, a multidrug transporter from Escherichia coli.In vitro assays of rod and cone opsin activity: retinoid analogs as agonists and inverse agonistsDynamic structure of retinylidene ligand of rhodopsin probed by molecular simulationsProbing human red cone opsin activity with retinal analogues.Retinal Flip in Rhodopsin Activation?Light activation of rhodopsin: insights from molecular dynamics simulations guided by solid-state NMR distance restraints.Stress tensor analysis of the protein quake of photoactive yellow protein.Mutations at position 125 in transmembrane helix III of rhodopsin affect the structure and signalling of the receptor.Cold-adaptation mechanism of mutant enzymes of 3-isopropylmalate dehydrogenase from Thermus thermophilus.Critical role of transmembrane segment zinc binding in the structure and function of rhodopsin.G protein-coupled receptors. I. Diversity of receptor-ligand interactions.Structural models of the photointermediates in the rhodopsin photocascade, lumirhodopsin, metarhodopsin I, and metarhodopsin II.Signaling states of rhodopsin. Retinal provides a scaffold for activating proton transfer switches.
P2860
Q28362022-B9C74BAB-65D1-4B99-8A97-B9C9B6C1EE37Q28363502-6A2454BF-F80D-48C4-BE13-D6480A27EA44Q33763840-441F0443-2232-4082-8609-EF729499A32BQ34008693-2B1BC8F1-07AF-48E4-A003-7C2ED2B1AAA0Q34171355-6A6F6431-246E-41D4-A188-F26E4E6E2759Q34179328-8632D827-E457-40D3-BA90-B8A59D42C1C3Q35347156-29C2E30E-DEBF-43CD-B821-E407C7BC31E6Q35842857-0076A8B2-0A2B-442C-A9D6-096EA804AFC8Q35929550-A5CCD18E-C1D5-4B03-89CE-475805E8FA76Q36308965-E6EED953-1C7E-4F0D-BD09-685A3FB442FCQ36968966-6139C6D2-4313-4C95-ABF5-AFC0A2FF6B90Q37260861-74AC199F-7806-49D0-87EA-1C449DCF3972Q37280502-F54E690D-BA42-4066-AA23-6F87E6FF204BQ37584069-A0D2D0F0-9DD5-4284-B6A3-63952E0D5EABQ37662779-233A709E-E47F-4263-8FB0-65D162645DC7Q37995725-08F804F6-4C48-43FB-A497-218B6AFC85B5Q39259841-6CA0F436-35AE-4A46-B53B-148EB55E021FQ39863353-674D87CB-CD4E-4BDF-89E6-5EFE26E1F0F4Q41771911-446807F5-3FC2-416D-BB77-53562200086CQ41822910-4976A2B9-8EA6-4712-83B5-85DA5A7B4CE0Q42424796-887E8D3A-4147-4144-931F-8322284C4A6FQ42916146-A3E08387-F76A-430B-BB92-C260DA16CAFDQ43024175-2D8F32A7-118A-4286-AD7C-647D9D04E258Q43808606-916594A7-74A5-4794-852E-FA97A8EB22B1Q44040013-C686C6DA-5ADB-4957-B44A-9FE8533FB8B0Q44934620-C4935D74-DCD3-499D-BD00-262A1B0523BCQ47892279-97531ABE-0D2D-4883-B576-86F749CDB792Q48007631-6EE3C1E7-9FDA-4D7C-82E7-A5AC12082C07Q52972682-550CA1DE-3C14-4594-B252-47A165667274
P2860
The C9 methyl group of retinal interacts with glycine-121 in rhodopsin.
description
1997 nî lūn-bûn
@nan
1997 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
The C9 methyl group of retinal interacts with glycine-121 in rhodopsin.
@ast
The C9 methyl group of retinal interacts with glycine-121 in rhodopsin.
@en
type
label
The C9 methyl group of retinal interacts with glycine-121 in rhodopsin.
@ast
The C9 methyl group of retinal interacts with glycine-121 in rhodopsin.
@en
prefLabel
The C9 methyl group of retinal interacts with glycine-121 in rhodopsin.
@ast
The C9 methyl group of retinal interacts with glycine-121 in rhodopsin.
@en
P2093
P2860
P356
P1476
The C9 methyl group of retinal interacts with glycine-121 in rhodopsin
@en
P2093
P2860
P304
13442-13447
P356
10.1073/PNAS.94.25.13442
P407
P577
1997-12-01T00:00:00Z