| pubmed-article:10072516 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10072516 | lifeskim:mentions | umls-concept:C1155003 | lld:lifeskim |
| pubmed-article:10072516 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10072516 | lifeskim:mentions | umls-concept:C0033681 | lld:lifeskim |
| pubmed-article:10072516 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
| pubmed-article:10072516 | lifeskim:mentions | umls-concept:C1274040 | lld:lifeskim |
| pubmed-article:10072516 | lifeskim:mentions | umls-concept:C0205217 | lld:lifeskim |
| pubmed-article:10072516 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:10072516 | lifeskim:mentions | umls-concept:C1150423 | lld:lifeskim |
| pubmed-article:10072516 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:10072516 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:10072516 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:10072516 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:10072516 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:10072516 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:10072516 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:10072516 | pubmed:dateCreated | 1999-4-14 | lld:pubmed |
| pubmed-article:10072516 | pubmed:abstractText | The Src-homology domain 2 (SH2)-containing cytoplasmic tyrosine phosphatase, SHP-1 (SH2-containing protein tyrosine phosphatase-1), interacts with several B cell surface and intracellular signal transduction molecules through its SH2 domains. Mice with the motheaten and viable motheaten mutations are deficient in SHP-1 and lack most mature B cells. To define the role of SHP-1 in mature B cells, we expressed phosphatase-inactive SHP-1 (C453S) in a mature B cell lymphoma line. SHP-1 (C453S) retains the ability to bind to both substrates and appropriate tyrosine-phosphorylated proteins and therefore can compete with the endogenous wild-type enzyme. We found that B cells expressing SHP-1 (C453S) demonstrated enhanced and prolonged tyrosine phosphorylation of proteins with molecular masses of 110, 70, and 55-60 kDa after stimulation with anti-mouse IgG. The tyrosine kinase Syk was hyperphosphorylated and hyperactive in B cells expressing SHP-1 (C453S). SHP-1 and Syk were coimmunoprecipitated from wild-type K46 cells, K46 SHP-1 (C453S) cells, and splenic B cells, and SHP-1 dephosphorylated Syk. Cells expressing SHP-1 (C453S) showed increased Ca2+ mobilization, extracellular signal-regulated kinase activation, and homotypic adhesion after B cell Ag receptor engagement. Thus, SHP-1 regulates multiple early and late events in B lymphocyte activation. | lld:pubmed |
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| pubmed-article:10072516 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10072516 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10072516 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:10072516 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10072516 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10072516 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10072516 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10072516 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:10072516 | pubmed:author | pubmed-author:WongJJ | lld:pubmed |
| pubmed-article:10072516 | pubmed:author | pubmed-author:ThomasM LML | lld:pubmed |
| pubmed-article:10072516 | pubmed:author | pubmed-author:HOPFH CHC | lld:pubmed |
| pubmed-article:10072516 | pubmed:author | pubmed-author:HoY NYN | lld:pubmed |
| pubmed-article:10072516 | pubmed:author | pubmed-author:SotoCC | lld:pubmed |
| pubmed-article:10072516 | pubmed:author | pubmed-author:DustinL BLB | lld:pubmed |
| pubmed-article:10072516 | pubmed:author | pubmed-author:PlasD RDR | lld:pubmed |
| pubmed-article:10072516 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10072516 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:10072516 | pubmed:volume | 162 | lld:pubmed |
| pubmed-article:10072516 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10072516 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10072516 | pubmed:pagination | 2717-24 | lld:pubmed |
| pubmed-article:10072516 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:10072516 | pubmed:meshHeading | pubmed-meshheading:10072516... | lld:pubmed |
| pubmed-article:10072516 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10072516 | pubmed:articleTitle | Expression of dominant-negative src-homology domain 2-containing protein tyrosine phosphatase-1 results in increased Syk tyrosine kinase activity and B cell activation. | lld:pubmed |
| pubmed-article:10072516 | pubmed:affiliation | Departments ofPathology and Molecular Microbiology and Medicine, Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, MO 63110, USA. | lld:pubmed |
| pubmed-article:10072516 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10072516 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10072516 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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