Identification of substrates of human protein-tyrosine phosphatase PTPN22 - Wikidata - awgldk - TriplyDB

Identification of substrates of human protein-tyrosine phosphatase PTPN22

Identification of substrates of human protein-tyrosine phosphatase PTPN22

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Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases Identification of a variant form of tyrosine phosphatase LYP Insights 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 variants Substrate specificity of lymphoid-specific tyrosine phosphatase (Lyp) and identification of Src kinase-associated protein of 55 kDa homolog (SKAP-HOM) as a Lyp substrate Cutting edge: the PTPN22 allelic variant associated with autoimmunity impairs B cell signaling Investigation of protein-tyrosine phosphatase 1B function by quantitative proteomics Protein tyrosine phosphatase non-receptor type 22 modulates NOD2-induced cytokine release and autophagy Foxp3 occupancy and regulation of key target genes during T-cell stimulation Autoimmune-associated PTPN22 R620W variation reduces phosphorylation of lymphoid phosphatase on an inhibitory tyrosine residue The role for protein tyrosine phosphatase non-receptor type 22 in regulating intestinal homeostasis Phosphorylation-mediated regulation of GEFs for RhoA Cellular biochemistry methods for investigating protein tyrosine phosphatases pCAP-based peptide substrates: the new tool in the box of tyrosine phosphatase assays Thymus, innate immunity and autoimmune arthritis: interplay of gene and environment Studies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation A Potent and Selective Small-Molecule Inhibitor for the Lymphoid-Specific Tyrosine Phosphatase (LYP), a Target Associated with Autoimmune Diseases The role of PTPN22 risk variant in the development of autoimmunity: finding common ground between mouse and human Protein tyrosine phosphatase PTPN22 in human autoimmunity High basal activity of the PTPN22 gain-of-function variant blunts leukocyte responsiveness negatively affecting IL-10 production in ANCA vasculitis Biochemical and functional studies of lymphoid-specific tyrosine phosphatase (Lyp) variants S201F and R266W The 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 acids Lymphoid 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 pazopanib Why 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 processes ERK 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 inhibitors CD45, CD148, and Lyp/Pep: critical phosphatases regulating Src family kinase signaling networks in immune cells Regulation of lymphoid tyrosine phosphatase activity: inhibition of the catalytic domain by the proximal interdomain

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Identification of substrates of human protein-tyrosine phosphatase PTPN22

http://www.wikidata.org/entity/Q24303819

description

2006 nî lūn-bûn

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2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2006 թվականի ապրիլին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Identification of substrates of human protein-tyrosine phosphatase PTPN22

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Identification of substrates of human protein-tyrosine phosphatase PTPN22

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Identification of substrates of human protein-tyrosine phosphatase PTPN22

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Identification of substrates of human protein-tyrosine phosphatase PTPN22

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type

label

Identification of substrates of human protein-tyrosine phosphatase PTPN22

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Identification of substrates of human protein-tyrosine phosphatase PTPN22

@en

Identification of substrates of human protein-tyrosine phosphatase PTPN22

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Identification of substrates of human protein-tyrosine phosphatase PTPN22

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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

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Identification of substrates of human protein-tyrosine phosphatase PTPN22

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P1433

Journal of Biological Chemistry

P1476

Identification of substrates of human protein-tyrosine phosphatase PTPN22

@en

P2093

Anjali Katrekar

http://www.w3.org/2001/XMLSchema#string

Ashley M Smith

http://www.w3.org/2001/XMLSchema#string

Doug Jeffery

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James M Clark

http://www.w3.org/2001/XMLSchema#string

Jiansheng Wu

http://www.w3.org/2001/XMLSchema#string

Jie Tang

http://www.w3.org/2001/XMLSchema#string

Joseph Buggy

http://www.w3.org/2001/XMLSchema#string

Jun Sampang

http://www.w3.org/2001/XMLSchema#string

Kyle Mortara

http://www.w3.org/2001/XMLSchema#string

Lee A Honigberg

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P2860

Tyrosine 319 in the interdomain B of ZAP-70 is a binding site for the Src homology 2 domain of Lck

Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1

Subcellular localization of intracellular protein tyrosine phosphatases in T cells

LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation

Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases

Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1

Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation

The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of mitosis.

The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol.

Specific dephosphorylation of the Lck tyrosine protein kinase at Tyr-394 by the SHP-1 protein-tyrosine phosphatase

P304

11002-10

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scholarly article

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892202

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P356

10.1074/JBC.M600498200

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P433

16

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P478

281

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2006-04-21T00:00:00Z

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16461343

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P921

protein tyrosine phosphatase activity

Protein tyrosine phosphatase non-receptor type 22