Agonist-independent interactions between beta-arrestins and mutant vasopressin type II receptors associated with nephrogenic syndrome of inappropriate antidiuresis.
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The chemokine receptor CCR1 is constitutively active, which leads to G protein-independent, β-arrestin-mediated internalizationFluorescence correlation spectroscopy, combined with bimolecular fluorescence complementation, reveals the effects of β-arrestin complexes and endocytic targeting on the membrane mobility of neuropeptide Y receptorsThe constitutively active V2 receptor mutants conferring NSIAD are weakly sensitive to agonist and antagonist regulation.Altered agonist sensitivity of a mutant v2 receptor suggests a novel therapeutic strategy for nephrogenic diabetes insipidus.Using nanoBRET and CRISPR/Cas9 to monitor proximity to a genome-edited protein in real-time.Functional characterization of vasopressin type 2 receptor substitutions (R137H/C/L) leading to nephrogenic diabetes insipidus and nephrogenic syndrome of inappropriate antidiuresis: implications for treatments.Application of G protein-coupled receptor-heteromer identification technology to monitor β-arrestin recruitment to G protein-coupled receptor heteromersSignalling profiles of H3 relaxin, H2 relaxin and R3(BΔ23-27)R/I5 acting at the relaxin family peptide receptor 3 (RXFP3)Identification and profiling of novel α1A-adrenoceptor-CXC chemokine receptor 2 heteromer.Enhanced BRET Technology for the Monitoring of Agonist-Induced and Agonist-Independent Interactions between GPCRs and β-ArrestinsSignaling Modification by GPCR Heteromer and Its Implication on X-Linked Nephrogenic Diabetes Insipidus.Identification and characterization of an activating F229V substitution in the V2 vasopressin receptor in an infant with NSIAD.Therapeutic potential of β-arrestin- and G protein-biased agonists.The bile acid receptor TGR5 does not interact with β-arrestins or traffic to endosomes but transmits sustained signals from plasma membrane rafts.Mutations of Vasopressin Receptor 2 Including Novel L312S Have Differential Effects on Trafficking.Biophysical Detection of Diversity and Bias in GPCR Function.V2 vasopressin receptor (V2R) mutations in partial nephrogenic diabetes insipidus highlight protean agonism of V2R antagonists.Characterization of three vasopressin receptor 2 variants: an apparent polymorphism (V266A) and two loss-of-function mutations (R181C and M311V)Investigation of interactions between TLR2, MyD88 and TIRAP by bioluminescence resonance energy transfer is hampered by artefacts of protein overexpression
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P2860
Agonist-independent interactions between beta-arrestins and mutant vasopressin type II receptors associated with nephrogenic syndrome of inappropriate antidiuresis.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 29 January 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Agonist-independent interactio ...... of inappropriate antidiuresis.
@en
Agonist-independent interactio ...... of inappropriate antidiuresis.
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type
label
Agonist-independent interactio ...... of inappropriate antidiuresis.
@en
Agonist-independent interactio ...... of inappropriate antidiuresis.
@nl
prefLabel
Agonist-independent interactio ...... of inappropriate antidiuresis.
@en
Agonist-independent interactio ...... of inappropriate antidiuresis.
@nl
P2093
P2860
P50
P356
P1476
Agonist-independent interactio ...... of inappropriate antidiuresis
@en
P2093
Heng B See
Karin A Eidne
Kevin D G Pfleger
P2860
P304
P356
10.1210/ME.2008-0321
P577
2009-01-29T00:00:00Z