| pubmed-article:10928987 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10928987 | lifeskim:mentions | umls-concept:C0030705 | lld:lifeskim |
| pubmed-article:10928987 | lifeskim:mentions | umls-concept:C0023473 | lld:lifeskim |
| pubmed-article:10928987 | lifeskim:mentions | umls-concept:C0368761 | lld:lifeskim |
| pubmed-article:10928987 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:10928987 | lifeskim:mentions | umls-concept:C0282535 | lld:lifeskim |
| pubmed-article:10928987 | lifeskim:mentions | umls-concept:C1552913 | lld:lifeskim |
| pubmed-article:10928987 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
| pubmed-article:10928987 | lifeskim:mentions | umls-concept:C1514485 | lld:lifeskim |
| pubmed-article:10928987 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:10928987 | pubmed:dateCreated | 2000-8-25 | lld:pubmed |
| pubmed-article:10928987 | pubmed:abstractText | Bcr-Abl contributes prominently to the development of most chronic myeloid leukemias (CMLs). Prior work has identified the adapter protein CRKL as a major substrate of the Bcr-Abl tyrosine kinase. CRKL can also bind via its first SH3 domain [SH3(1)] to specific sequences in Bcr-Abl. Cell-penetrating peptides were developed that bind with high affinity and selectivity to the SH3(1) domain of CRKL. They disrupt Bcr-Abl-CRKL complexes and strongly reduce the proliferation of primary CML blast cells and cell lines established from Bcr-Abl-positive patients. Activation-specific antibodies against phosphorylated MAP kinase (MAPK) showed that MAPK activity is down-regulated in blast cells treated with the CRKLSH3(1) blocker peptides. We conclude that the Bcr-Abl-CRKL complexes are largely dependent on the CRKLSH3(1) domain, that the central mitogenic cascade is down-regulated as a consequence of the disruption of CRKLSH3(1) interactions, and that CRKL therefore contributes to the proliferation of CML blast cells. | lld:pubmed |
| pubmed-article:10928987 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10928987 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10928987 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10928987 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10928987 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10928987 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10928987 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10928987 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10928987 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10928987 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10928987 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10928987 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10928987 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10928987 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10928987 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10928987 | pubmed:issn | 0892-6638 | lld:pubmed |
| pubmed-article:10928987 | pubmed:author | pubmed-author:LipJJ | lld:pubmed |
| pubmed-article:10928987 | pubmed:author | pubmed-author:EulitzMM | lld:pubmed |
| pubmed-article:10928987 | pubmed:author | pubmed-author:ArlinghausR... | lld:pubmed |
| pubmed-article:10928987 | pubmed:author | pubmed-author:TalpazMM | lld:pubmed |
| pubmed-article:10928987 | pubmed:author | pubmed-author:SchulzAA | lld:pubmed |
| pubmed-article:10928987 | pubmed:author | pubmed-author:EstrovZZ | lld:pubmed |
| pubmed-article:10928987 | pubmed:author | pubmed-author:FellerS MSM | lld:pubmed |
| pubmed-article:10928987 | pubmed:author | pubmed-author:AdermannKK | lld:pubmed |
| pubmed-article:10928987 | pubmed:author | pubmed-author:KardinalCC | lld:pubmed |
| pubmed-article:10928987 | pubmed:author | pubmed-author:PosernGG | lld:pubmed |
| pubmed-article:10928987 | pubmed:author | pubmed-author:KonkolBB | lld:pubmed |
| pubmed-article:10928987 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10928987 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:10928987 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10928987 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10928987 | pubmed:pagination | 1529-38 | lld:pubmed |
| pubmed-article:10928987 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10928987 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10928987 | pubmed:articleTitle | Cell-penetrating SH3 domain blocker peptides inhibit proliferation of primary blast cells from CML patients. | lld:pubmed |
| pubmed-article:10928987 | pubmed:affiliation | Laboratory of Molecular Oncology, MSZ, Universität Würzburg, Germany. | lld:pubmed |
| pubmed-article:10928987 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10928987 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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