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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1999-3-1
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pubmed:abstractText |
The previously uncharacterized CDC24 homology domain of BCR, which is missing in the P185 BCR-ABL oncogene of Philadelphia chromosome (Ph1)-positive acute lymphocytic leukemia but is retained in P210 BCR-ABL of chronic myelogeneous leukemia, was found to bind to the xeroderma pigmentosum group B protein (XPB). The binding appeared to be required for XPB to be tyrosine-phosphorylated by BCR-ABL. The interaction not only reduced both the ATPase and the helicase activities of XPB purified in the baculovirus system but also impaired XPB-mediated cross-complementation of the repair deficiency in rodent UV-sensitive mutants of group 3. The persistent dysfunction of XPB may in part underlie genomic instability in blastic crisis.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-161695,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-1657398,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-1932738,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-2068108,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-2167179,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-2408149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-2499863,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-2581632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-2645949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-3103721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-7511595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-7565761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-7606740,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-7663514,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-7718873,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-7724587,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-8194528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-8196650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-8313895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-8408645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-8541551,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-8663064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-8663148,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-8791490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-8839830,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-9389724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9874796-9473236
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/CDC24 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fusion Proteins, bcr-abl,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/XPBC-ERCC-3 protein
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
96
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
203-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9874796-Adenosine Triphosphatases,
pubmed-meshheading:9874796-Animals,
pubmed-meshheading:9874796-Blast Crisis,
pubmed-meshheading:9874796-CHO Cells,
pubmed-meshheading:9874796-Cell Cycle Proteins,
pubmed-meshheading:9874796-Cricetinae,
pubmed-meshheading:9874796-DNA Helicases,
pubmed-meshheading:9874796-DNA-Binding Proteins,
pubmed-meshheading:9874796-Dose-Response Relationship, Radiation,
pubmed-meshheading:9874796-Fusion Proteins, bcr-abl,
pubmed-meshheading:9874796-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:9874796-Humans,
pubmed-meshheading:9874796-Leukemia, Myelogenous, Chronic, BCR-ABL Positive,
pubmed-meshheading:9874796-Protein Binding,
pubmed-meshheading:9874796-Proto-Oncogene Proteins,
pubmed-meshheading:9874796-Recombinant Proteins,
pubmed-meshheading:9874796-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9874796-Sequence Homology, Amino Acid,
pubmed-meshheading:9874796-Ultraviolet Rays
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pubmed:year |
1999
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pubmed:articleTitle |
The BCR-ABL oncoprotein potentially interacts with the xeroderma pigmentosum group B protein.
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pubmed:affiliation |
Department of Genetics, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan.
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pubmed:publicationType |
Journal Article
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