about
Arrestins: ubiquitous regulators of cellular signaling pathwaysCrystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual SubtypesInsights into congenital stationary night blindness based on the structure of G90D rhodopsinArrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domainKinetics of rhodopsin deactivation and its role in regulating recovery and reproducibility of rod photoresponseA dopamine D2 receptor mutant capable of G protein-mediated signaling but deficient in arrestin bindingBeta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptorConformational differences between arrestin2 and pre-activated mutants as revealed by hydrogen exchange mass spectrometry.Non-visual arrestins are constitutively associated with the centrosome and regulate centrosome function.Identification of receptor binding-induced conformational changes in non-visual arrestins.The effect of arrestin conformation on the recruitment of c-Raf1, MEK1, and ERK1/2 activationFunctional comparisons of visual arrestins in rod photoreceptors of transgenic miceIdentification of phosphorylation sites in the COOH-terminal tail of the μ-opioid receptorMonomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 bindingIdentification of key factors that reduce the variability of the single photon responseDevelopment of an MRI biomarker sensitive to tetrameric visual arrestin 1 and its reduction via light-evoked translocation in vivo.Identification of arrestin-3-specific residues necessary for JNK3 kinase activationA single mutation in arrestin-2 prevents ERK1/2 activation by reducing c-Raf1 binding.G protein-coupled receptor kinases: more than just kinases and not only for GPCRsC-terminal threonines and serines play distinct roles in the desensitization of rhodopsin, a G protein-coupled receptorGPCR structure, function, drug discovery and crystallography: report from Academia-Industry International Conference (UK Royal Society) Chicheley Hall, 1-2 September 2014.The origin and evolution of G protein-coupled receptor kinases.Quantitative Signaling and Structure-Activity Analyses Demonstrate Functional Selectivity at the Nociceptin/Orphanin FQ Opioid Receptor.Silent scaffolds: inhibition OF c-Jun N-terminal kinase 3 activity in cell by dominant-negative arrestin-3 mutantßarrestin1-biased agonism at human δ-opioid receptor by peptidic and alkaloid ligands.Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestinsConformation of receptor-bound visual arrestin.Ligand directed signaling differences between rodent and human κ-opioid receptors.Diffusion of the second messengers in the cytoplasm acts as a variability suppressor of the single photon response in vertebrate phototransduction.Critical role of the central 139-loop in stability and binding selectivity of arrestin-1.Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 bindingOverexpression of rhodopsin alters the structure and photoresponse of rod photoreceptors.Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions.Direct binding of visual arrestin to microtubules determines the differential subcellular localization of its splice variants in rod photoreceptors.Mutations in arrestin-3 differentially affect binding to neuropeptide Y receptor subtypesAn intracellular loop 2 amino acid residue determines differential binding of arrestin to the dopamine D2 and D3 receptors.Arrestin mobilizes signaling proteins to the cytoskeleton and redirects their activity.A model for the solution structure of the rod arrestin tetramer.Partial phosphorylation of the N-formyl peptide receptor inhibits G protein association independent of arrestin binding.Arrestin binding to the M(2) muscarinic acetylcholine receptor is precluded by an inhibitory element in the third intracellular loop of the receptor.
P50
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P50
description
hulumtues
@sq
pharmacologist
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ricercatore
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wetenschapper
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հետազոտող
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name
Vsevolod V. Gurevich
@ast
Vsevolod V. Gurevich
@en
Vsevolod V. Gurevich
@es
Vsevolod V. Gurevich
@nl
Vsevolod V. Gurevich
@sl
type
label
Vsevolod V. Gurevich
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Vsevolod V. Gurevich
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Vsevolod V. Gurevich
@es
Vsevolod V. Gurevich
@nl
Vsevolod V. Gurevich
@sl
altLabel
Seva Gurevich
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prefLabel
Vsevolod V. Gurevich
@ast
Vsevolod V. Gurevich
@en
Vsevolod V. Gurevich
@es
Vsevolod V. Gurevich
@nl
Vsevolod V. Gurevich
@sl
P214
P244
P1053
A-3236-2008
P106
P1153
24294144900
P21
P214
P244
nb2014003571
P31
P3829
P496
0000-0002-3950-5351
P734
P735
P7859
lccn-nb2014003571