The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin - Wikidata - awgldk - TriplyDB

The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin

The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin

http://www.wikidata.org/entity/Q24679774

about

PTPN14 is required for the density-dependent control of YAP1 Protein tyrosine phosphatase PTPN14 is a regulator of lymphatic function and choanal development in humans PTPN14 interacts with and negatively regulates the oncogenic function of YAP Large-scale structural analysis of the classical human protein tyrosine phosphatome Role of APC and DNA mismatch repair genes in the development of colorectal cancers.The Regulatory Role of KIBRA and PTPN14 in Hippo Signaling and Beyond YAP-Mediated Mechanotransduction in Skeletal Muscle Diverse Levels of Sequence Selectivity and Catalytic Efficiency of Protein-Tyrosine Phosphatases Differential induction of glioblastoma migration and growth by two forms of pleiotrophin Regulation of cadherin-mediated adhesion in morphogenesis The protein tyrosine phosphatase Pez regulates TGFbeta, epithelial-mesenchymal transition, and organ development Gene expression profiling of rat spermatogonia and Sertoli cells reveals signaling pathways from stem cells to niche and testicular cancer cells to surrounding stroma.PTPN14 forms a complex with Kibra and LATS1 proteins and negatively regulates the YAP oncogenic function The tyrosine phosphatase PTPN14 is a negative regulator of YAP activity.Sts-2 is a phosphatase that negatively regulates zeta-associated protein (ZAP)-70 and T cell receptor signaling pathways Three-step method for proliferation and differentiation of human embryonic stem cell (hESC)-derived male germ cells.Regulation of adherens junction dynamics by phosphorylation switches.A perspective on regulation of cell-cell adhesion and epithelial-mesenchymal transition: known and novel.YAP modifies cancer cell sensitivity to EGFR and survivin inhibitors and is negatively regulated by the non-receptor type protein tyrosine phosphatase 14.Automated time-lapse microscopy and high-resolution tracking of cell migration.Role of YAP and TAZ in pancreatic ductal adenocarcinoma and in stellate cells associated with cancer and chronic pancreatitis Mouse and human strategies identify PTPN14 as a modifier of angiogenesis and hereditary haemorrhagic telangiectasia.Protein tyrosine and serine-threonine phosphatases in the sea urchin, Strongylocentrotus purpuratus: identification and potential functions.Identification and functional characterization of p130Cas as a substrate of protein tyrosine phosphatase nonreceptor 14 Customized Array Comparative Genomic Hybridization Analysis of 25 Phosphatase-encoding Genes in Colorectal Cancer Tissues.Hippo gains weight: added insights and complexity to pathway control.Genetic alterations of protein tyrosine phosphatases in human cancers.A central role for cadherin signaling in cancer.The tyrosine phosphatase PTPN14 (Pez) inhibits metastasis by altering protein trafficking.Pathway-based identification of biomarkers for targeted therapeutics: personalized oncology with PI3K pathway inhibitors.The PTPN14 Tumor Suppressor Is a Degradation Target of Human Papillomavirus E7.Genetic variations in the Hippo signaling pathway and breast cancer risk in African American women in the AMBER Consortium.The PI3K-PTEN tug-of-war, oxidative stress and retinal degeneration.Distinct roles for N-Cadherin linked c-Src and fyn kinases in lens development.Modulation of N-cadherin junctions and their role as epicenters of differentiation-specific actin regulation in the developing lens High expression of PTPN21 in B-cell non-Hodgkin's gastric lymphoma, a positive mediator of STAT5 activity.A p53 Super-tumor Suppressor Reveals a Tumor Suppressive p53-Ptpn14-Yap Axis in Pancreatic Cancer.The impact of phosphatases on proliferative and survival signaling in cancer.

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The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin

http://www.wikidata.org/entity/Q24679774

description

2003 nî lūn-bûn

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2003 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի հունիսին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

The protein tyrosine phosphata ...... dephosphorylates beta-catenin

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The protein tyrosine phosphata ...... dephosphorylates beta-catenin

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The protein tyrosine phosphata ...... dephosphorylates beta-catenin

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type

label

The protein tyrosine phosphata ...... dephosphorylates beta-catenin

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The protein tyrosine phosphata ...... dephosphorylates beta-catenin

@en

The protein tyrosine phosphata ...... dephosphorylates beta-catenin

@nl

prefLabel

The protein tyrosine phosphata ...... dephosphorylates beta-catenin

@ast

The protein tyrosine phosphata ...... dephosphorylates beta-catenin

@en

The protein tyrosine phosphata ...... dephosphorylates beta-catenin

@nl

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P356

MBC.E02-09-0577

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Molecular Biology of the Cell

P1476

The protein tyrosine phosphata ...... dephosphorylates beta-catenin

@en

P2093

Carol Wadham

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

Jennifer R Gamble

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

Mathew A Vadas

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

Yeesim Khew-Goodall

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

P2860

Translocation of protein tyrosine phosphatase Pez/PTPD2/PTP36 to the nucleus is associated with induction of cell proliferation

Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex

Pez: a novel human cDNA encoding protein tyrosine phosphatase- and ezrin-like domains

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

Hepatocyte growth factor induces Wnt-independent nuclear translocation of beta-catenin after Met-beta-catenin dissociation in hepatocytes

The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane

Cadherins and tissue formation: integrating adhesion and signaling.

Cadherins and their connections: adhesion junctions have broader functions.

Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/beta-catenin complex in cells transformed with a temperature-sensitive v-SRC gene.

Cyclic changes in the organization of cell adhesions and the associated cytoskeleton, induced by stimulation of tyrosine phosphorylation in bovine aortic endothelial cells.

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2520-9

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scholarly article

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1237493

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10.1091/MBC.E02-09-0577

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6

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14

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12808048

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P932

194899

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