| pubmed-article:7512728 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7512728 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
| pubmed-article:7512728 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:7512728 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:7512728 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:7512728 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:7512728 | lifeskim:mentions | umls-concept:C1332709 | lld:lifeskim |
| pubmed-article:7512728 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:7512728 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:7512728 | pubmed:dateCreated | 1994-5-16 | lld:pubmed |
| pubmed-article:7512728 | pubmed:abstractText | CD28 is a costimulatory receptor that can provide the second signal necessary for T-cell activation and function in response to stimulation through the T-cell antigen receptor/CD3 complex. We found that a distinct array of proteins was phosphorylated on tyrosine following stimulation with anti-CD28 monoclonal antibody, as detected by immune-complex kinase assays. Anti-CD28 stimulation of in vitro kinase activity was detergent-dependent, occurring in immune complexes prepared with Brij 96 but not Nonidet P-40. Pretreatment of cells with low concentrations of phorbol ester increased the activation-independent phosphorylation of proteins in CD28 immune complexes. Reimmunoprecipitation studies indicated that the cytoplasmic protein-tyrosine kinases Lck and Fyn were associated with CD28. CD28 itself was phosphorylated both in vitro and in vivo in an activation-dependent manner, as detected by nonreducing/reducing SDS/PAGE analyses. The activation-stimulated phosphorylation of CD28 may play a key role in signaling through this receptor. | lld:pubmed |
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| pubmed-article:7512728 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7512728 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7512728 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7512728 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:7512728 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:7512728 | pubmed:author | pubmed-author:BiererB EBE | lld:pubmed |
| pubmed-article:7512728 | pubmed:author | pubmed-author:HutchcroftJ... | lld:pubmed |
| pubmed-article:7512728 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7512728 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:7512728 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:7512728 | pubmed:geneSymbol | lyn | lld:pubmed |
| pubmed-article:7512728 | pubmed:geneSymbol | fyn | lld:pubmed |
| pubmed-article:7512728 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7512728 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7512728 | pubmed:pagination | 3260-4 | lld:pubmed |
| pubmed-article:7512728 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:7512728 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7512728 | pubmed:articleTitle | Activation-dependent phosphorylation of the T-lymphocyte surface receptor CD28 and associated proteins. | lld:pubmed |
| pubmed-article:7512728 | pubmed:affiliation | Division of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA 02115. | lld:pubmed |
| pubmed-article:7512728 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7512728 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7512728 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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