Dynamics of arrestin-rhodopsin interactions: arrestin and retinal release are directly linked events.
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Retinal remodeling in human retinitis pigmentosaCrystal structure of pre-activated arrestin p44Rhodopsin TM6 can interact with two separate and distinct sites on arrestin: evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin bindingPutative active states of a prototypic g-protein-coupled receptor from biased molecular dynamics.Arrestin can act as a regulator of rhodopsin photochemistry.Functional competence of a partially engaged GPCR-β-arrestin complexCore engagement with β-arrestin is dispensable for agonist-induced vasopressin receptor endocytosis and ERK activation.Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin.Arrestin-rhodopsin binding stoichiometry in isolated rod outer segment membranes depends on the percentage of activated receptors.G protein-coupled receptor rhodopsin.Rod outer segment retinol formation is independent of Abca4, arrestin, rhodopsin kinase, and rhodopsin palmitylationStructural insights into biased G protein-coupled receptor signaling revealed by fluorescence spectroscopy.Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsin.Visual rhodopsin sees the light: structure and mechanism of G protein signaling.Interphotoreceptor retinoid-binding protein is the physiologically relevant carrier that removes retinol from rod photoreceptor outer segments.Functional map of arrestin binding to phosphorylated opsin, with and without agonist.Rhodopsin kinase and arrestin binding control the decay of photoactivated rhodopsin and dark adaptation of mouse rods.Regulation of arrestin binding by rhodopsin phosphorylation level.Heterodimerization with Its splice variant blocks the ghrelin receptor 1a in a non-signaling conformation: a study with a purified heterodimer assembled into lipid discs.Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 bindingFormation of all-trans retinol after visual pigment bleaching in mouse photoreceptorsThe magnitude of the light-induced conformational change in different rhodopsins correlates with their ability to activate G proteins.Monomeric rhodopsin is the minimal functional unit required for arrestin binding.Inhibition of heterotrimeric G protein signaling by a small molecule acting on Galpha subunit.C-edge loops of arrestin function as a membrane anchorFluorescence spectroscopy of rhodopsins: insights and approaches.The cytoplasmic rhodopsin-protein interface: potential for drug discovery.Dynamics of arrestin-rhodopsin interactions: acidic phospholipids enable binding of arrestin to purified rhodopsin in detergent.SPECTRAL METHODS FOR STUDY OF THE G-PROTEIN-COUPLED RECEPTOR RHODOPSIN. I. VIBRATIONAL AND ELECTRONIC SPECTROSCOPY.Structural evidence for the role of polar core residue Arg175 in arrestin activation.High constitutive activity is an intrinsic feature of ghrelin receptor protein: a study with a functional monomeric GHS-R1a receptor reconstituted in lipid discs.The L49F mutation in alpha erythroid spectrin induces local disorder in the tetramer association region: Fluorescence and molecular dynamics studies of free and bound alpha spectrin.Influence of Arrestin on the Photodecay of Bovine Rhodopsin.The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin.Deactivation and proton transfer in light-induced metarhodopsin II/metarhodopsin III conversion: a time-resolved fourier transform infrared spectroscopic study.Rhodopsin deactivation is affected by mutations of Tyrl91.
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P2860
Dynamics of arrestin-rhodopsin interactions: arrestin and retinal release are directly linked events.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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name
Dynamics of arrestin-rhodopsin ...... se are directly linked events.
@en
Dynamics of arrestin-rhodopsin ...... se are directly linked events.
@nl
type
label
Dynamics of arrestin-rhodopsin ...... se are directly linked events.
@en
Dynamics of arrestin-rhodopsin ...... se are directly linked events.
@nl
prefLabel
Dynamics of arrestin-rhodopsin ...... se are directly linked events.
@en
Dynamics of arrestin-rhodopsin ...... se are directly linked events.
@nl
P2093
P2860
P356
P1476
Dynamics of arrestin-rhodopsin ...... se are directly linked events.
@en
P2093
David L Farrens
Martha E Sommer
W Clay Smith
P2860
P304
P356
10.1074/JBC.M411341200
P407
P577
2004-12-09T00:00:00Z