PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
about
Confirmation of the genetic association of CTLA4 and PTPN22 with ANCA-associated vasculitisT cell protein tyrosine phosphatase attenuates T cell signaling to maintain tolerance in miceStructure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseasesIdentification of substrates of human protein-tyrosine phosphatase PTPN22The autoimmunity-associated gene PTPN22 potentiates toll-like receptor-driven, type 1 interferon-dependent immunityProtein tyrosine phosphatase non-receptor type 22 modulates NOD2-induced cytokine release and autophagyAutoimmune-associated PTPN22 R620W variation reduces phosphorylation of lymphoid phosphatase on an inhibitory tyrosine residueA biosynthetic pathway for anandamideThe role for protein tyrosine phosphatase non-receptor type 22 in regulating intestinal homeostasisA functional framework for interpretation of genetic associations in T1DA Potent and Selective Small-Molecule Inhibitor for the Lymphoid-Specific Tyrosine Phosphatase (LYP), a Target Associated with Autoimmune DiseasesThe role of PTPN22 risk variant in the development of autoimmunity: finding common ground between mouse and humanRecent advances in the genetics of autoimmune diseasePathways to gene identification in rheumatoid arthritis: PTPN22 and beyondProtein tyrosine phosphatase PTPN22 in human autoimmunityDifferential association of the PTPN22 coding variant with autoimmune diseases in a Dutch populationA missense single-nucleotide polymorphism in a gene encoding a protein tyrosine phosphatase (PTPN22) is associated with rheumatoid arthritis.Genetic association of the R620W polymorphism of protein tyrosine phosphatase PTPN22 with human SLE.Autoimmune-associated lymphoid tyrosine phosphatase is a gain-of-function variantPTPN22 1858C>T (R620W) functional polymorphism and human longevityProtein tyrosine phosphatases and the immune responseThe protein tyrosine phosphatase PTPN4/PTP-MEG1, an enzyme capable of dephosphorylating the TCR ITAMs and regulating NF-kappaB, is dispensable for T cell development and/or T cell effector functionsThe phosphatase JKAP/DUSP22 inhibits T-cell receptor signalling and autoimmunity by inactivating LckThe autoimmunity risk variant LYP-W620 cooperates with CSK in the regulation of TCR signaling.The PTPN22 R620W polymorphism associates with RF positive rheumatoid arthritis in a dose-dependent manner but not with HLA-SE status.Discovery of a novel series of inhibitors of lymphoid tyrosine phosphatase with activity in human T cells.The FERM and PDZ domain-containing protein tyrosine phosphatases, PTPN4 and PTPN3, are both dispensable for T cell receptor signal transduction.Meta-analysis reveals an association of PTPN22 C1858T with autoimmune diseases, which depends on the localization of the affected tissue.Autoimmunity-associated protein tyrosine phosphatase PEP negatively regulates IFN-α receptor signalingCharacterization of protein tyrosine phosphatase H1 knockout mice in animal models of local and systemic inflammationLymphoid tyrosine phosphatase and autoimmunity: human genetics rediscovers tyrosine phosphatases.Analysis of families in the multiple autoimmune disease genetics consortium (MADGC) collection: the PTPN22 620W allele associates with multiple autoimmune phenotypes.Fine-tuning T cell receptor signaling to control T cell developmentWhy is PTPN22 a good candidate susceptibility gene for autoimmune disease?PTPN22.6, a dominant negative isoform of PTPN22 and potential biomarker of rheumatoid arthritis.Use of nonobese diabetic mice to understand human type 1 diabetesPTPN22 genetic variation: evidence for multiple variants associated with rheumatoid arthritisProtein tyrosine phosphatases as potential therapeutic targets.Association of functional variants of PTPN22 and tp53 in psoriatic arthritis: a case-control study.PTPN22 polymorphism and anti-cyclic citrullinated peptide antibodies in combination strongly predicts future onset of rheumatoid arthritis and has a specificity of 100% for the disease.
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P2860
PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
description
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Science
@fr
artículu científicu espublizáu en 2004
@ast
im Januar 2004 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2004/01/30)
@sk
vědecký článek publikovaný v roce 2004
@cs
wetenschappelijk artikel (gepubliceerd op 2004/01/30)
@nl
наукова стаття, опублікована в січні 2004
@uk
name
PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
@ast
PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
@en
PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
@nl
type
label
PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
@ast
PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
@en
PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
@nl
prefLabel
PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
@ast
PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
@en
PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
@nl
P2093
P3181
P356
P1433
P1476
PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
@en
P2093
Andrew C. Chan
Flavius Martin
Guangming Huang
Kiminori Hasegawa
P304
P3181
P356
10.1126/SCIENCE.1092138
P407
P50
P577
2004-01-30T00:00:00Z