| pubmed-article:10933394 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10933394 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:10933394 | lifeskim:mentions | umls-concept:C0004561 | lld:lifeskim |
| pubmed-article:10933394 | lifeskim:mentions | umls-concept:C0033681 | lld:lifeskim |
| pubmed-article:10933394 | lifeskim:mentions | umls-concept:C1413206 | lld:lifeskim |
| pubmed-article:10933394 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10933394 | lifeskim:mentions | umls-concept:C1521871 | lld:lifeskim |
| pubmed-article:10933394 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:10933394 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10933394 | pubmed:dateCreated | 2000-8-22 | lld:pubmed |
| pubmed-article:10933394 | pubmed:abstractText | CD19 regulates constitutive and antigen receptor-induced signaling thresholds in B lymphocytes through its unique cytoplasmic domain. Herein, we demonstrate a novel molecular mechanism where interactions between CD19 and Lyn amplify basal and antigen receptor-induced Src family kinase activation. Lyn expression was required for CD19 tyrosine phosphorylation in primary B cells. Experiments with purified proteins demonstrated that CD19-Y513 was Lyn's initial phosphorylation and binding site. This led to processive phosphorylation of CD19-Y482, which recruited a second Lyn molecule, allowing for transphosphorylation and amplification of Lyn activation. In vivo, CD19 deficiency impaired, and CD19 overexpression enhanced, Lyn kinase activity. Thus, CD19 functions as a specialized adapter protein for the amplification of Src family kinases that is crucial for intrinsic and antigen receptor-induced signal transduction. | lld:pubmed |
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| pubmed-article:10933394 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10933394 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10933394 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10933394 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10933394 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10933394 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10933394 | pubmed:issn | 1074-7613 | lld:pubmed |
| pubmed-article:10933394 | pubmed:author | pubmed-author:FujimotoMM | lld:pubmed |
| pubmed-article:10933394 | pubmed:author | pubmed-author:FujimotoYY | lld:pubmed |
| pubmed-article:10933394 | pubmed:author | pubmed-author:DeFrancoA LAL | lld:pubmed |
| pubmed-article:10933394 | pubmed:author | pubmed-author:TedderT FTF | lld:pubmed |
| pubmed-article:10933394 | pubmed:author | pubmed-author:LowellC ACA | lld:pubmed |
| pubmed-article:10933394 | pubmed:author | pubmed-author:JansenP JPJ | lld:pubmed |
| pubmed-article:10933394 | pubmed:author | pubmed-author:PoeJ CJC | lld:pubmed |
| pubmed-article:10933394 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10933394 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:10933394 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10933394 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10933394 | pubmed:pagination | 47-57 | lld:pubmed |
| pubmed-article:10933394 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:10933394 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10933394 | pubmed:articleTitle | CD19 regulates Src family protein tyrosine kinase activation in B lymphocytes through processive amplification. | lld:pubmed |
| pubmed-article:10933394 | pubmed:affiliation | Department of Immunology, Duke University Medical Center, Durham, North Carolina 27710, USA. | lld:pubmed |
| pubmed-article:10933394 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10933394 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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