| pubmed-article:10375547 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10375547 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:10375547 | lifeskim:mentions | umls-concept:C0085536 | lld:lifeskim |
| pubmed-article:10375547 | lifeskim:mentions | umls-concept:C1823381 | lld:lifeskim |
| pubmed-article:10375547 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:10375547 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10375547 | lifeskim:mentions | umls-concept:C1547707 | lld:lifeskim |
| pubmed-article:10375547 | lifeskim:mentions | umls-concept:C0544726 | lld:lifeskim |
| pubmed-article:10375547 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:10375547 | pubmed:dateCreated | 1999-8-20 | lld:pubmed |
| pubmed-article:10375547 | pubmed:abstractText | Antigen-receptor signaling requires Src-family kinases to initiate tyrosine phosphorylation. CD45 dephosphorylates the inhibitory site in Src-family kinases before antigen-receptor engagement and thus serves to 'prime' the kinases. It has been unclear why CD45 does not also dephosphorylate 'activated' kinases or motifs within the cytoplasmic domains of antigen-receptors and thus prevent signal transduction. Recent reports raise the possibility that CD45 is excluded from engaged antigen-receptors by mechanisms that may include the formation of lipid microdomains. | lld:pubmed |
| pubmed-article:10375547 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10375547 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375547 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10375547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375547 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10375547 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10375547 | pubmed:issn | 0952-7915 | lld:pubmed |
| pubmed-article:10375547 | pubmed:author | pubmed-author:ThomasM LML | lld:pubmed |
| pubmed-article:10375547 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10375547 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:10375547 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10375547 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10375547 | pubmed:pagination | 270-6 | lld:pubmed |
| pubmed-article:10375547 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:10375547 | pubmed:meshHeading | pubmed-meshheading:10375547... | lld:pubmed |
| pubmed-article:10375547 | pubmed:meshHeading | pubmed-meshheading:10375547... | lld:pubmed |
| pubmed-article:10375547 | pubmed:meshHeading | pubmed-meshheading:10375547... | lld:pubmed |
| pubmed-article:10375547 | pubmed:meshHeading | pubmed-meshheading:10375547... | lld:pubmed |
| pubmed-article:10375547 | pubmed:meshHeading | pubmed-meshheading:10375547... | lld:pubmed |
| pubmed-article:10375547 | pubmed:meshHeading | pubmed-meshheading:10375547... | lld:pubmed |
| pubmed-article:10375547 | pubmed:meshHeading | pubmed-meshheading:10375547... | lld:pubmed |
| pubmed-article:10375547 | pubmed:meshHeading | pubmed-meshheading:10375547... | lld:pubmed |
| pubmed-article:10375547 | pubmed:meshHeading | pubmed-meshheading:10375547... | lld:pubmed |
| pubmed-article:10375547 | pubmed:meshHeading | pubmed-meshheading:10375547... | lld:pubmed |
| pubmed-article:10375547 | pubmed:meshHeading | pubmed-meshheading:10375547... | lld:pubmed |
| pubmed-article:10375547 | pubmed:meshHeading | pubmed-meshheading:10375547... | lld:pubmed |
| pubmed-article:10375547 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10375547 | pubmed:articleTitle | The regulation of antigen-receptor signaling by protein tyrosine phosphatases: a hole in the story. | lld:pubmed |
| pubmed-article:10375547 | pubmed:affiliation | Howard Hughes Medical Institute, Box 8118, Departments of Pathology andMolecular Microbiology, Washington University School of Medicine, St Louis, MO 63110, USA. mthomas@pathbox.wustl.edu | lld:pubmed |
| pubmed-article:10375547 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10375547 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:10375547 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10375547 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10375547 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10375547 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10375547 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10375547 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10375547 | lld:pubmed |
