pubmed-article:9570294 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9570294 | lifeskim:mentions | umls-concept:C0029016 | lld:lifeskim |
pubmed-article:9570294 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
pubmed-article:9570294 | lifeskim:mentions | umls-concept:C0033713 | lld:lifeskim |
pubmed-article:9570294 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
pubmed-article:9570294 | lifeskim:mentions | umls-concept:C1306673 | lld:lifeskim |
pubmed-article:9570294 | lifeskim:mentions | umls-concept:C0205099 | lld:lifeskim |
pubmed-article:9570294 | pubmed:issue | 2-3 | lld:pubmed |
pubmed-article:9570294 | pubmed:dateCreated | 1998-6-8 | lld:pubmed |
pubmed-article:9570294 | pubmed:abstractText | The c-cbl protooncogene was first identified as the cellular homologue of a viral oncogene v-cbl that induces pre-B lymphomas and myeloid leukemias in mice. Until recently, the biochemical basis for Cbl's transforming potential and its physiological role remained unclear. However, a convergence of biochemical studies in mammalian cells and genetic studies in C. elegans and Drosophila has now identified Cbl as a negative regulator of tyrosine kinase signaling. The N-terminal transforming region of Cbl (Cbl-N) and an adjacent RING finger domain are the elements most conserved during evolution. The Cbl-N region has now been shown to contain a novel phosphotyrosine-binding (PTB) domain that directly interacts with autophosphorylated tyrosine kinases via a D(N/D)XpY motif. A critical role of the PTB domain in Cbl function is demonstrated by the localization of a loss-of-function mutation in C. elegans Cbl homologue SLI-1 within this region. The corresponding mutation in human Cbl inactivates the PTB domain function and abrogates Cbl-mediated regulation of tyrosine kinase function. Recent studies have also identified a novel signaling pathway initiated by the interaction of mammalian Cbl proteins with the SH2 domains of Crk adaptor molecules, which results in Cbl's linkage with C3G, a guanine nucleotide exchange protein for Rap1 family of small G-proteins. Presently, Rap1 is thought to antagonize Ras function, although Rap1-specific targets have emerged recently. Thus, recent advances have firmly placed the little known protooncoprotein Cbl on the center stage of tyrosine kinase-mediated signal transduction. | lld:pubmed |
pubmed-article:9570294 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9570294 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9570294 | pubmed:language | eng | lld:pubmed |
pubmed-article:9570294 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9570294 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9570294 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9570294 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9570294 | pubmed:issn | 0893-9675 | lld:pubmed |
pubmed-article:9570294 | pubmed:author | pubmed-author:OtaSS | lld:pubmed |
pubmed-article:9570294 | pubmed:author | pubmed-author:RaoNN | lld:pubmed |
pubmed-article:9570294 | pubmed:author | pubmed-author:MiyakeSS | lld:pubmed |
pubmed-article:9570294 | pubmed:author | pubmed-author:BaniGG | lld:pubmed |
pubmed-article:9570294 | pubmed:author | pubmed-author:MEDAE MEM | lld:pubmed |
pubmed-article:9570294 | pubmed:author | pubmed-author:DouillardPP | lld:pubmed |
pubmed-article:9570294 | pubmed:author | pubmed-author:AndoniouC ECE | lld:pubmed |
pubmed-article:9570294 | pubmed:author | pubmed-author:LupherM LMLJr | lld:pubmed |
pubmed-article:9570294 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9570294 | pubmed:volume | 8 | lld:pubmed |
pubmed-article:9570294 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9570294 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9570294 | pubmed:pagination | 189-218 | lld:pubmed |
pubmed-article:9570294 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:9570294 | pubmed:meshHeading | pubmed-meshheading:9570294-... | lld:pubmed |
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pubmed-article:9570294 | pubmed:meshHeading | pubmed-meshheading:9570294-... | lld:pubmed |
pubmed-article:9570294 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9570294 | pubmed:articleTitle | The Cbl protooncogene product: from an enigmatic oncogene to center stage of signal transduction. | lld:pubmed |
pubmed-article:9570294 | pubmed:affiliation | Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA. | lld:pubmed |
pubmed-article:9570294 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9570294 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9570294 | pubmed:publicationType | Review | lld:pubmed |
pubmed-article:9570294 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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