| http://purl.uniprot.org/citations/9418872 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9418872 | http://www.w3.org/2000/01/rdf-schema#comment | "We have recently shown that protein tyrosine phosphatase 1B (PTP1B) associates with the docking protein p130Cas in 3Y1 rat fibroblasts. This interaction is mediated by a proline-rich sequence on PTP1B and the SH3 domain on p130Cas. Expression of wild-type PTP1B (WT-PTP1B), but not a catalytically competent, proline-to-alanine point mutant that cannot bind p130Cas (PA-PTP1B), causes substantial tyrosine dephosphorylation of p130Cas (F. Liu, D. E. Hill, and J. Chernoff, J. Biol. Chem. 271:31290-31295, 1996). Here we demonstrate that WT-, but not PA-PTP1B, inhibits transformation of rat 3Y1 fibroblasts by v-crk, -src, and -ras, but not by v-raf. These effects on transformation correlate with the phosphorylation status of p130Cas and two proteins that are associated with p130Cas, Paxillin and Fak. Expression of WT-PTP1B reduces formation of p130Cas-Crk complexes and inhibits mitogen-activated protein kinase activation by Src and Crk. These data show that transformation suppression by PTP1B requires a functional SH3 ligand and suggest that p130Cas may represent an important physiological target of PTP1B in cells."xsd:string |
| http://purl.uniprot.org/citations/9418872 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.18.1.250"xsd:string |
| http://purl.uniprot.org/citations/9418872 | http://purl.uniprot.org/core/author | "Liu F."xsd:string |
| http://purl.uniprot.org/citations/9418872 | http://purl.uniprot.org/core/author | "Chernoff J."xsd:string |
| http://purl.uniprot.org/citations/9418872 | http://purl.uniprot.org/core/author | "Sells M.A."xsd:string |
| http://purl.uniprot.org/citations/9418872 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9418872 | http://purl.uniprot.org/core/name | "Mol Cell Biol"xsd:string |
| http://purl.uniprot.org/citations/9418872 | http://purl.uniprot.org/core/pages | "250-259"xsd:string |
| http://purl.uniprot.org/citations/9418872 | http://purl.uniprot.org/core/title | "Transformation suppression by protein tyrosine phosphatase 1B requires a functional SH3 ligand."xsd:string |
| http://purl.uniprot.org/citations/9418872 | http://purl.uniprot.org/core/volume | "18"xsd:string |
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| http://purl.uniprot.org/uniprot/#_A0A0J9YTZ8-mappedCitation-9418872 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/9418872 |
| http://purl.uniprot.org/uniprot/#_A0A0J9YV30-mappedCitation-9418872 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/9418872 |
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| http://purl.uniprot.org/uniprot/#_A0A1D5RMM8-mappedCitation-9418872 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/9418872 |
| http://purl.uniprot.org/uniprot/#_P56945-mappedCitation-9418872 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/9418872 |
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| http://purl.uniprot.org/uniprot/#_A0A2I3BPK4-mappedCitation-9418872 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/9418872 |
| http://purl.uniprot.org/uniprot/#_A0A2I3BQ85-mappedCitation-9418872 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/9418872 |
| http://purl.uniprot.org/uniprot/#_A0A2I3BR46-mappedCitation-9418872 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/9418872 |
| http://purl.uniprot.org/uniprot/#_A0A2I3BRG7-mappedCitation-9418872 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/9418872 |
| http://purl.uniprot.org/uniprot/#_F8VQ28-mappedCitation-9418872 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/9418872 |
| http://purl.uniprot.org/uniprot/#_P18031-mappedCitation-9418872 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/9418872 |