| pubmed-article:8663064 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8663064 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
| pubmed-article:8663064 | lifeskim:mentions | umls-concept:C0017837 | lld:lifeskim |
| pubmed-article:8663064 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8663064 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8663064 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8663064 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8663064 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:8663064 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:8663064 | pubmed:dateCreated | 1996-8-20 | lld:pubmed |
| pubmed-article:8663064 | pubmed:abstractText | Bcr-Abl oncoproteins are responsible for the pathogenesis of human leukemias with a reciprocal chromosome translocation t(9;22). The amino-terminal Bcr sequence has a potential to form a homotetramer (tetramer domain), and destructions of the tetramer domain cause a complete loss of biological activities in Bcr-Abl. Here we show that Bcr-Abl in which the tetramer domain is replaced with glutathione S-transferase (GST) with a dimerizing ability (GST/Bcr-Abl-(Delta1-160)) can no longer induce an interleukin-3 (IL-3) independence in Ba/F3 cells or transform mouse bone marrow cells but still retains by 30-40% the ability to transform Rat1 cells. Compared with the wild type Bcr-Abl, autophosphorylation of GST/Bcr-Abl-(Delta1-160) in vivo was reduced by more than 50%. The Grb-2 binding to GST/Bcr-Abl-(Delta1-160) was 50% reduced in Rat1 cells and undetectable in Ba/F3 cells. In Rat1 cells expressing GST/Bcr-Abl-(Delta1-160), phosphotyrosine contents of p62 and Shc were 70% decreased. | lld:pubmed |
| pubmed-article:8663064 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8663064 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8663064 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8663064 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8663064 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8663064 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8663064 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8663064 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8663064 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8663064 | pubmed:author | pubmed-author:ShibuyaMM | lld:pubmed |
| pubmed-article:8663064 | pubmed:author | pubmed-author:WitteO NON | lld:pubmed |
| pubmed-article:8663064 | pubmed:author | pubmed-author:MaraMM | lld:pubmed |
| pubmed-article:8663064 | pubmed:author | pubmed-author:AfarD EDE | lld:pubmed |
| pubmed-article:8663064 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8663064 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:8663064 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:8663064 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8663064 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8663064 | pubmed:pagination | 15353-7 | lld:pubmed |
| pubmed-article:8663064 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:8663064 | pubmed:meshHeading | pubmed-meshheading:8663064-... | lld:pubmed |
| pubmed-article:8663064 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8663064 | pubmed:articleTitle | The dimerization property of glutathione S-transferase partially reactivates Bcr-Abl lacking the oligomerization domain. | lld:pubmed |
| pubmed-article:8663064 | pubmed:affiliation | Department of Genetics, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108, Japan. | lld:pubmed |
| pubmed-article:8663064 | pubmed:publicationType | Journal Article | lld:pubmed |
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