Point mutations confer loss of ATP-induced human P2X(7) receptor function
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Protein kinase C regulation of P2X3 receptors is unlikely to involve direct receptor phosphorylationExploring the ATP-binding site of P2X receptorsInsights into the Molecular Mechanisms Underlying Mammalian P2X7 Receptor Functions and Contributions in Diseases, Revealed by Structural Modeling and Single Nucleotide PolymorphismsSpecific detection of non-functional human P2X(7) receptors in HEK293 cells and B-lymphocytesATP-induced autophagy is associated with rapid killing of intracellular mycobacteria within human monocytes/macrophagesNon-synonymous single nucleotide polymorphisms in the P2X receptor genes: association with diseases, impact on receptor functions and potential use as diagnosis biomarkersThe hyposensitive N187D P2X7 mutant promotes malignant progression in nude mice.cAMP potentiates ATP-evoked calcium signaling in human parotid acinar cells.Chelerythrine and other benzophenanthridine alkaloids block the human P2X7 receptor.Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors.P2X(7) receptor: Death or life?Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Identification and characterization of a novel variant of the human P2X(7) receptor resulting in gain of function.Participation of the Lys313-Ile333 sequence of the purinergic P2X4 receptor in agonist binding and transduction of signals to the channel gate.P2X7 receptor activates extracellular signal-regulated kinases ERK1 and ERK2 independently of Ca2+ influxP2X7 receptor cell surface expression and cytolytic pore formation are regulated by a distal C-terminal region.A rare P2X7 variant Arg307Gln with absent pore formation function protects against neuroinflammation in multiple sclerosis.Regulation of activity of P2X7 receptor by its splice variants in cultured mouse astrocytes.Residues 155 and 348 contribute to the determination of P2X7 receptor function via distinct mechanisms revealed by single-nucleotide polymorphisms.Activation of the P2X7 ion channel by soluble and covalently bound ligands.
P2860
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P2860
Point mutations confer loss of ATP-induced human P2X(7) receptor function
description
2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2002
@ast
im Februar 2002 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: 13 February 2002)
@en
vedecký článok (publikovaný 2002/02/13)
@sk
vědecký článek publikovaný v roce 2002
@cs
wetenschappelijk artikel (gepubliceerd op 2002/02/13)
@nl
наукова стаття, опублікована в лютому 2002
@uk
مقالة علمية (نشرت في 13-2-2002)
@ar
name
Point mutations confer loss of ATP-induced human P2X(7) receptor function
@ast
Point mutations confer loss of ATP-induced human P2X(7) receptor function
@en
Point mutations confer loss of ATP-induced human P2X(7) receptor function
@nl
type
label
Point mutations confer loss of ATP-induced human P2X(7) receptor function
@ast
Point mutations confer loss of ATP-induced human P2X(7) receptor function
@en
Point mutations confer loss of ATP-induced human P2X(7) receptor function
@nl
prefLabel
Point mutations confer loss of ATP-induced human P2X(7) receptor function
@ast
Point mutations confer loss of ATP-induced human P2X(7) receptor function
@en
Point mutations confer loss of ATP-induced human P2X(7) receptor function
@nl
P2093
P2860
P1433
P1476
Point mutations confer loss of ATP-induced human P2X(7) receptor function
@en
P2093
D A Williams
J A Barden
R A Worthington
P2860
P356
10.1016/S0014-5793(01)03311-7
P407
P50
P577
2002-02-01T00:00:00Z