Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation
about
Structure-guided studies of the SHP-1/JAK1 interaction provide new insights into phosphatase catalytic domain substrate recognitionSHP family protein tyrosine phosphatases adopt canonical active-site conformations in the apo and phosphate-bound statesStructural, Functional, and Clinical Characterization of a Novel PTPN11 Mutation Cluster Underlying Noonan SyndromeStructure-based reassessment of the caveolin signaling model: do caveolae regulate signaling through caveolin-protein interactions?Structural interrogation of phosphoproteome identified by mass spectrometry reveals allowed and disallowed regions of phosphoconformation.Src-homology protein tyrosine phosphatase-1 agonist, SC-43, reduces liver fibrosis.SHP-1 is a target of regorafenib in colorectal cancer.Downregulation of signal transducer and activator of transcription 3 by sorafenib: a novel mechanism for hepatocellular carcinoma therapy.Phosphotyrosine recognition domains: the typical, the atypical and the versatile.Fibroblast growth factor receptor like-1 (FGFRL1) interacts with SHP-1 phosphatase at insulin secretory granules and induces beta-cell ERK1/2 protein activation.Disrupting VEGF-A paracrine and autocrine loops by targeting SHP-1 suppresses triple negative breast cancer metastasis.Novel sorafenib analogues induce apoptosis through SHP-1 dependent STAT3 inactivation in human breast cancer cells.Biophysical assay for tethered signaling reactions reveals tether-controlled activity for the phosphatase SHP-1.Discovery of novel Src homology region 2 domain-containing phosphatase 1 agonists from sorafenib for the treatment of hepatocellular carcinoma.Shp1 function in myeloid cells.Regulation of Nephrin Phosphorylation in Diabetes and Chronic Kidney Injury.Sorafenib analogue SC-60 induces apoptosis through the SHP-1/STAT3 pathway and enhances docetaxel cytotoxicity in triple-negative breast cancer cells.Targeting SHP-1-STAT3 signaling: A promising therapeutic approach for the treatment of cholangiocarcinoma.Superresolution microscopy reveals nanometer-scale reorganization of inhibitory natural killer cell receptors upon activation of NKG2D.Actin retrograde flow controls natural killer cell response by regulating the conformation state of SHP-1.Structural reorganization of SHP2 by oncogenic mutations and implications for oncoprotein resistance to allosteric inhibitionMechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2Protein Tyrosine Phosphatases as Potential Regulators of STAT3 Signaling
P2860
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P2860
Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation
description
2011 nî lūn-bûn
@nan
2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation
@ast
Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation
@en
Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation
@nl
type
label
Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation
@ast
Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation
@en
Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation
@nl
prefLabel
Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation
@ast
Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation
@en
Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation
@nl
P2093
P2860
P921
P3181
P356
P1476
Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation
@en
P2093
Chandrasekhar Komma
G Wayne Zhou
Henry D Bellamy
Zhizhuang Joe Zhao
P2860
P304
P3181
P356
10.1002/JCB.23125
P577
2011-08-01T00:00:00Z