Identification of substrates of human protein-tyrosine phosphatase PTPN22
about
Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseasesIdentification of a variant form of tyrosine phosphatase LYPInsights into the suppressor of T-cell receptor (TCR) signaling-1 (Sts-1)-mediated regulation of TCR signaling through the use of novel substrate-trapping Sts-1 phosphatase variantsSubstrate specificity of lymphoid-specific tyrosine phosphatase (Lyp) and identification of Src kinase-associated protein of 55 kDa homolog (SKAP-HOM) as a Lyp substrateCutting edge: the PTPN22 allelic variant associated with autoimmunity impairs B cell signalingInvestigation of protein-tyrosine phosphatase 1B function by quantitative proteomicsProtein tyrosine phosphatase non-receptor type 22 modulates NOD2-induced cytokine release and autophagyFoxp3 occupancy and regulation of key target genes during T-cell stimulationAutoimmune-associated PTPN22 R620W variation reduces phosphorylation of lymphoid phosphatase on an inhibitory tyrosine residueThe role for protein tyrosine phosphatase non-receptor type 22 in regulating intestinal homeostasisPhosphorylation-mediated regulation of GEFs for RhoACellular biochemistry methods for investigating protein tyrosine phosphatasespCAP-based peptide substrates: the new tool in the box of tyrosine phosphatase assaysThymus, innate immunity and autoimmune arthritis: interplay of gene and environmentStudies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradationA 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 humanProtein tyrosine phosphatase PTPN22 in human autoimmunityHigh basal activity of the PTPN22 gain-of-function variant blunts leukocyte responsiveness negatively affecting IL-10 production in ANCA vasculitisBiochemical and functional studies of lymphoid-specific tyrosine phosphatase (Lyp) variants S201F and R266WThe autoimmunity risk variant LYP-W620 cooperates with CSK in the regulation of TCR signaling.Distinct functional and conformational states of the human lymphoid tyrosine phosphatase catalytic domain can be targeted by choice of the inhibitor chemotype.Discovery of a novel series of inhibitors of lymphoid tyrosine phosphatase with activity in human T cells.PTPN22 -1123G > C polymorphism is associated with susceptibility to primary immune thrombocytopenia in Chinese population.Identifying potent, selective protein tyrosine phosphatase inhibitors from a library of Au(I) complexes.The autoimmune-predisposing variant of lymphoid tyrosine phosphatase favors T helper 1 responses.ERK-dependent T cell receptor threshold calibration in rheumatoid arthritis.Association of the protein tyrosine phosphatase non-receptor 22 polymorphism (PTPN22) with endometriosis: a meta-analysis.The PTPN22 locus and rheumatoid arthritis: no evidence for an effect on risk independent of Arg620Trp.Inhibition of lymphoid tyrosine phosphatase by benzofuran salicylic acidsLymphoid tyrosine phosphatase and autoimmunity: human genetics rediscovers tyrosine phosphatases.Covalent inhibition of the lymphoid tyrosine phosphatase.Lyn kinase and ZAP70 are substrates of PTPROt in B-cells: Lyn inactivation by PTPROt sensitizes leukemia cells to VEGF-R inhibitor pazopanibWhy is PTPN22 a good candidate susceptibility gene for autoimmune disease?PTPN22.6, a dominant negative isoform of PTPN22 and potential biomarker of rheumatoid arthritis.Global analysis of Cdc14 phosphatase reveals diverse roles in mitotic processesERK positive feedback regulates a widespread network of tyrosine phosphorylation sites across canonical T cell signaling and actin cytoskeletal proteins in Jurkat T cells.Substrate selection influences molecular recognition in a screen for lymphoid tyrosine phosphatase inhibitorsCD45, CD148, and Lyp/Pep: critical phosphatases regulating Src family kinase signaling networks in immune cellsRegulation of lymphoid tyrosine phosphatase activity: inhibition of the catalytic domain by the proximal interdomain
P2860
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P2860
Identification of substrates of human protein-tyrosine phosphatase PTPN22
description
2006 nî lūn-bûn
@nan
2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Identification of substrates of human protein-tyrosine phosphatase PTPN22
@ast
Identification of substrates of human protein-tyrosine phosphatase PTPN22
@en
Identification of substrates of human protein-tyrosine phosphatase PTPN22
@en-gb
Identification of substrates of human protein-tyrosine phosphatase PTPN22
@nl
type
label
Identification of substrates of human protein-tyrosine phosphatase PTPN22
@ast
Identification of substrates of human protein-tyrosine phosphatase PTPN22
@en
Identification of substrates of human protein-tyrosine phosphatase PTPN22
@en-gb
Identification of substrates of human protein-tyrosine phosphatase PTPN22
@nl
prefLabel
Identification of substrates of human protein-tyrosine phosphatase PTPN22
@ast
Identification of substrates of human protein-tyrosine phosphatase PTPN22
@en
Identification of substrates of human protein-tyrosine phosphatase PTPN22
@en-gb
Identification of substrates of human protein-tyrosine phosphatase PTPN22
@nl
P2093
P2860
P3181
P356
P1476
Identification of substrates of human protein-tyrosine phosphatase PTPN22
@en
P2093
Anjali Katrekar
Ashley M Smith
Doug Jeffery
James M Clark
Jiansheng Wu
Joseph Buggy
Jun Sampang
Kyle Mortara
Lee A Honigberg
P2860
P304
P3181
P356
10.1074/JBC.M600498200
P407
P577
2006-04-21T00:00:00Z