| http://purl.uniprot.org/citations/9813138 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9813138 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9813138 | http://www.w3.org/2000/01/rdf-schema#comment | "CTLA-4 and CD28 are differentially expressed on T-cells. They bind to a common ligand B71/2 (CD80/86), however with different avidities. Unlike CD28 which augments the T-cell response, CTLA-4 operates predominately as a negative regulator of T-cell proliferation. The mechanism by which CTLA-4 can generate these intracellular signals is unclear. Little is known regarding the identity of the protein-tyrosine kinase(s) responsible for CTLA-4 phosphorylation and thus creating conditions for the reported binding to PI 3-kinase and the protein tyrosine phosphatase SHP-2. In this study, we demonstrate that Rlk (resting lymphocyte kinase) is capable of phosphorylating CTLA-4 at the YVKM motif. Consistent with this finding, Rlk is capable of providing conditions for the binding of the SH2 domains of PI 3-kinase to the receptor. CTLA-4 is therefore the first known substrate for Rlk suggesting the possibility that this kinase may participate in CTLA-4 function."xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.org/dc/terms/identifier | "doi:10.1006/bbrc.1998.9559"xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.org/dc/terms/identifier | "doi:10.1006/bbrc.1998.9559"xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/author | "Schwartzberg P.L."xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/author | "Schwartzberg P.L."xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/author | "Schneider H."xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/author | "Schneider H."xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/author | "Rudd C.E."xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/author | "Rudd C.E."xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/pages | "14-19"xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/pages | "14-19"xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/title | "Resting lymphocyte kinase (Rlk/Txk) phosphorylates the YVKM motif and regulates PI 3-kinase binding to T-cell antigen CTLA-4."xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/title | "Resting lymphocyte kinase (Rlk/Txk) phosphorylates the YVKM motif and regulates PI 3-kinase binding to T-cell antigen CTLA-4."xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/volume | "252"xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://purl.uniprot.org/core/volume | "252"xsd:string |
| http://purl.uniprot.org/citations/9813138 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9813138 |
| http://purl.uniprot.org/citations/9813138 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9813138 |
| http://purl.uniprot.org/citations/9813138 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9813138 |
| http://purl.uniprot.org/citations/9813138 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9813138 |