Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase
about
Protein tyrosine phosphatase alpha (PTPalpha) and contactin form a novel neuronal receptor complex linked to the intracellular tyrosine kinase fynA phosphotyrosine displacement mechanism for activation of Src by PTPalphaIdentification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell linesMitotic activation of protein-tyrosine phosphatase alpha and regulation of its Src-mediated transforming activity by its sites of protein kinase C phosphorylationTyrosine phosphorylation of CD45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphatasePhosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivoSrc kinase associates with a member of a distinct subfamily of protein-tyrosine phosphatases containing an ezrin-like domainThe SPOT technique as a tool for studying protein tyrosine phosphatase substrate specificitiesActivation of Src and transformation by an RPTPĪ± splice mutant found in human tumoursPhysical and functional interactions between receptor-like protein-tyrosine phosphatase alpha and p59fynCloning and characterization of islet cell antigen-related protein-tyrosine phosphatase (PTP), a novel receptor-like PTP and autoantigen in insulin-dependent diabetesDeciphering the cross talk between hnRNP K and c-Src: the c-Src activation domain in hnRNP K is distinct from a second interaction siteIncrease in receptor-like protein tyrosine phosphatase activity and expression level on density-dependent growth arrest of endothelial cellsMolecular cloning and characterization of PTP pi, a novel receptor-like protein-tyrosine phosphataseReceptor protein tyrosine phosphatase alpha participates in the m1 muscarinic acetylcholine receptor-dependent regulation of Kv1.2 channel activityReceptor protein tyrosine phosphatase alpha activates pp60c-src and is involved in neuronal differentiationCloning and characterization of R-PTP-kappa, a new member of the receptor protein tyrosine phosphatase family with a proteolytically cleaved cellular adhesion molecule-like extracellular regionReceptor tyrosine phosphatase R-PTP-kappa mediates homophilic bindingOverexpressed Csk tyrosine kinase is localized in focal adhesions, causes reorganization of alpha v beta 5 integrin, and interferes with HeLa cell spreadingThe effect of overexpression of the protein tyrosine phosphatase PTPMEG on cell growth and on colony formation in soft agar in COS-7 cellsLIME: a new membrane Raft-associated adaptor protein involved in CD4 and CD8 coreceptor signalingHomophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregationDimerization of receptor protein-tyrosine phosphatase alpha in living cellsProtein-tyrosine Phosphatase and Kinase Specificity in Regulation of SRC and Breast Tumor KinaseCharacterization of a prostate-specific tyrosine phosphatase by mutagenesis and expression in human prostate cancer cellsMultiple interactions between receptor protein-tyrosine phosphatase (RPTP) alpha and membrane-distal protein-tyrosine phosphatase domains of various RPTPsMeeting at mitosis: cell cycle-specific regulation of c-Src by RPTPalphaKinetic analysis of two closely related receptor-like protein-tyrosine-phosphatases, PTP alpha and PTP epsilonRegulation of SRC family kinases in human cancersSrc kinase activity is regulated by the SHP-1 protein-tyrosine phosphataseProtein-tyrosine phosphatase alpha regulates Src family kinases and alters cell-substratum adhesionRegulation of cell adhesion by protein-tyrosine phosphatases. I. Cell-matrix adhesionRPTP delta and the novel protein tyrosine phosphatase RPTP psi are expressed in restricted regions of the developing central nervous systemProtein tyrosine phosphatases and the immune responseTwo mechanisms activate PTPalpha during mitosisDimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alphaSpatiotemporal regulation of Src and its substrates at invadosomesA RNA interference screen identifies the protein phosphatase 2A subunit PR55gamma as a stress-sensitive inhibitor of c-SRCThe receptor-like protein-tyrosine phosphatase, RPTP alpha, is phosphorylated by protein kinase C on two serines close to the inner face of the plasma membranePRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
P2860
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P2860
Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase
description
1992 Õ©ÕøÖÕ”ÕÆÕ”Õ¶Õ« ÕÕ„ÕŗÕæÕ„Õ“Õ¢Õ„ÖÕ«Õ¶ Õ°ÖÕ”ÕæÕ”ÖÕ”ÕÆÕøÖÕ”Õ® Õ£Õ«ÕæÕ”ÕÆÕ”Õ¶ ÕµÖ
Õ¤ÕøÖÕ”Õ®
@hyw
1992 Õ©Õ¾Õ”ÕÆÕ”Õ¶Õ« Õ½Õ„ÕŗÕæÕ„Õ“Õ¢Õ„ÖÕ«Õ¶ Õ°ÖÕ”ÕæÕ”ÖÕ”ÕÆÕ¾Õ”Õ® Õ£Õ«ÕæÕ”ÕÆÕ”Õ¶ Õ°ÕøÕ¤Õ¾Õ”Õ®
@hy
article publiƩ dans la revue scientifique Nature
@fr
artĆculu cientĆficu espublizĆ”u en 1992
@ast
scientific article (publication date: 24 September 1992)
@en
vedeckĆ½ ÄlĆ”nok (publikovanĆ½ 1992/09/24)
@sk
vÄdeckĆ½ ÄlĆ”nek publikovanĆ½ v roce 1992
@cs
wetenschappelijk artikel (gepubliceerd op 1992/09/24)
@nl
Š½Š°ŃŠŗŠ¾Š²Š° ŃŃŠ°ŃŃŃ, Š¾ŠæŃŠ±Š»ŃŠŗŠ¾Š²Š°Š½Š° Ń Š²ŠµŃŠµŃŠ½Ń 1992
@uk
Ł
ŁŲ§ŁŲ© Ų¹ŁŁ
ŁŲ© (ŁŲ“Ų±ŲŖ ŁŁ 24-9-1992)
@ar
name
Cell transformation and activa ...... a protein tyrosine phosphatase
@ast
Cell transformation and activa ...... a protein tyrosine phosphatase
@en
Cell transformation and activa ...... a protein tyrosine phosphatase
@nl
type
label
Cell transformation and activa ...... a protein tyrosine phosphatase
@ast
Cell transformation and activa ...... a protein tyrosine phosphatase
@en
Cell transformation and activa ...... a protein tyrosine phosphatase
@nl
prefLabel
Cell transformation and activa ...... a protein tyrosine phosphatase
@ast
Cell transformation and activa ...... a protein tyrosine phosphatase
@en
Cell transformation and activa ...... a protein tyrosine phosphatase
@nl
P2093
P356
P1433
P1476
Cell transformation and activa ...... a protein tyrosine phosphatase
@en
P2093
P2888
P356
10.1038/359336A0
P407
P577
1992-09-24T00:00:00Z
P6179
1047300617