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Arrestins: ubiquitous regulators of cellular signaling pathwaysThe structural basis of arrestin-mediated regulation of G-protein-coupled receptorsAnalyzing the roles of multi-functional proteins in cells: The case of arrestins and GRKsStructure of an Arrestin2-Clathrin Complex Reveals a Novel Clathrin Binding Domain That Modulates Receptor TraffickingCrystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual Subtypeskurtz, a novel nonvisual arrestin, is an essential neural gene in Drosophila.Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins.Identification of arrestin-3-specific residues necessary for JNK3 kinase activationReduced expression of G protein-coupled receptor kinases in schizophrenia but not in schizoaffective disorderG Protein-coupled Receptor Kinases of the GRK4 Protein Subfamily Phosphorylate Inactive G Protein-coupled Receptors (GPCRs).Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors.Silent scaffolds: inhibition OF c-Jun N-terminal kinase 3 activity in cell by dominant-negative arrestin-3 mutantManipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestinsDistinct loops in arrestin differentially regulate ligand binding within the GPCR opsin.Characterization of a truncated form of arrestin isolated from bovine rod outer segments.A Drosophila nonvisual arrestin is required for the maintenance of olfactory sensitivity.Arrestins and two receptor kinases are upregulated in Parkinson's disease with dementia.Cone arrestin binding to JNK3 and Mdm2: conformational preference and localization of interaction sitesVisual and both non-visual arrestins in their "inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm.Rich tapestry of G protein-coupled receptor signaling and regulatory mechanisms.Arrestin-3 binds c-Jun N-terminal kinase 1 (JNK1) and JNK2 and facilitates the activation of these ubiquitous JNK isoforms in cells via scaffolding.Negative impact of β-arrestin-1 on post-myocardial infarction heart failure via cardiac and adrenal-dependent neurohormonal mechanisms.C-edge loops of arrestin function as a membrane anchorCustom-designed proteins as novel therapeutic tools? The case of arrestins.Getting in touch with the clathrin terminal domain.Structural determinants of arrestin functionsβ-arrestins and G protein-coupled receptor trafficking.Peptide mini-scaffold facilitates JNK3 activation in cellsBiased agonism: An emerging paradigm in GPCR drug discovery.Mutations in arrestin-3 differentially affect binding to neuropeptide Y receptor subtypesStructure and functions of arrestins.Site-specific cleavage of G protein-coupled receptor-engaged beta-arrestin. Influence of the AT1 receptor conformation on scissile site selection.Regulatory mechanisms that modulate signalling by G-protein-coupled receptors.Arrestin-3 binds the MAP kinase JNK3α2 via multiple sites on both domains.Arrestin-dependent activation of JNK family kinasesDifferential manipulation of arrestin-3 binding to basal and agonist-activated G protein-coupled receptors.Topographic study of arrestin using differential chemical modifications and hydrogen/deuterium exchange.Trout red blood cell arrestin (TRCarr), a novel member of the arrestin family: cloning, immunoprecipitation and expression of recombinant TRCarr.How does arrestin assemble MAPKs into a signaling complex?ADRB2:Catecholamine binds ARRB1; ARRB2
P2860
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P2860
description
1993 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1993
@ast
im Juli 1993 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1993/07/25)
@sk
vědecký článek publikovaný v roce 1993
@cs
wetenschappelijk artikel (gepubliceerd op 1993/07/25)
@nl
наукова стаття, опублікована в липні 1993
@uk
name
Polypeptide variants of beta-arrestin and arrestin3
@ast
Polypeptide variants of beta-arrestin and arrestin3
@en
Polypeptide variants of beta-arrestin and arrestin3
@nl
type
label
Polypeptide variants of beta-arrestin and arrestin3
@ast
Polypeptide variants of beta-arrestin and arrestin3
@en
Polypeptide variants of beta-arrestin and arrestin3
@nl
prefLabel
Polypeptide variants of beta-arrestin and arrestin3
@ast
Polypeptide variants of beta-arrestin and arrestin3
@en
Polypeptide variants of beta-arrestin and arrestin3
@nl
P2093
P1476
Polypeptide variants of beta-arrestin and arrestin3
@en
P2093
C. Sanders
J. L. Benovic
L. A. Donoso
P. Goldsmith
R. C. Bodine
R. Sterne-Marr
V. V. Gurevich
P304
15640–15648
P407
P577
1993-07-25T00:00:00Z