| pubmed-article:17283041 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17283041 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:17283041 | lifeskim:mentions | umls-concept:C1155003 | lld:lifeskim |
| pubmed-article:17283041 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
| pubmed-article:17283041 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
| pubmed-article:17283041 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
| pubmed-article:17283041 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
| pubmed-article:17283041 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:17283041 | lifeskim:mentions | umls-concept:C2698651 | lld:lifeskim |
| pubmed-article:17283041 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:17283041 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:17283041 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:17283041 | lifeskim:mentions | umls-concept:C0599697 | lld:lifeskim |
| pubmed-article:17283041 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:17283041 | pubmed:dateCreated | 2007-3-30 | lld:pubmed |
| pubmed-article:17283041 | pubmed:abstractText | 3BP2 is a pleckstrin homology domain- and Src homology 2 (SH2) domain-containing adapter protein that is mutated in the rare human bone disorder cherubism and which has also been implicated in immunoreceptor signaling. However, a function for this protein has yet to be established. Here we show that mice lacking 3BP2 exhibited a perturbation in the peritoneal B1 and splenic marginal-zone B-cell compartments and diminished thymus-independent type 2 antigen response. 3BP2(-/-) B cells demonstrated a proliferation defect in response to antigen receptor cross-linking and a heightened sensitivity to B-cell receptor-induced death via a caspase-3-dependent apoptotic pathway. We show that 3BP2 binds via its SH2 domain to the CD19 signaling complex and is required for optimum Syk phosphorylation and calcium flux. | lld:pubmed |
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| pubmed-article:17283041 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17283041 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17283041 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17283041 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17283041 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17283041 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17283041 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17283041 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17283041 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:17283041 | pubmed:author | pubmed-author:ChenGraceG | lld:pubmed |
| pubmed-article:17283041 | pubmed:author | pubmed-author:TurnerMartinM | lld:pubmed |
| pubmed-article:17283041 | pubmed:author | pubmed-author:DimitriouIoan... | lld:pubmed |
| pubmed-article:17283041 | pubmed:author | pubmed-author:YehWen-ChenWC | lld:pubmed |
| pubmed-article:17283041 | pubmed:author | pubmed-author:RottapelRober... | lld:pubmed |
| pubmed-article:17283041 | pubmed:author | pubmed-author:IlangumaranSu... | lld:pubmed |
| pubmed-article:17283041 | pubmed:author | pubmed-author:La RoseJoseJ | lld:pubmed |
| pubmed-article:17283041 | pubmed:author | pubmed-author:DoodyGinaG | lld:pubmed |
| pubmed-article:17283041 | pubmed:author | pubmed-author:GommermanJenn... | lld:pubmed |
| pubmed-article:17283041 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17283041 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:17283041 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17283041 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17283041 | pubmed:pagination | 3109-22 | lld:pubmed |
| pubmed-article:17283041 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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