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rdf:type |
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lifeskim:mentions |
umls-concept:C0000744,
umls-concept:C0029016,
umls-concept:C0080279,
umls-concept:C0162326,
umls-concept:C0205224,
umls-concept:C0220905,
umls-concept:C0812385,
umls-concept:C1145667,
umls-concept:C1412097,
umls-concept:C1510411,
umls-concept:C1514562,
umls-concept:C1826328,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1977882,
umls-concept:C2266681
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pubmed:issue |
1
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pubmed:dateCreated |
1991-8-21
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pubmed:abstractText |
BCR-ABL is a chimeric oncogene implicated in the pathogenesis of Philadelphia chromosome-positive human leukemias. BCR first exon sequences specifically activate the tyrosine kinase and transforming potential of BCR-ABL. We have tested the hypothesis that activation of BCR-ABL may involve direct interaction between BCR sequences and the tyrosine kinase regulatory domains of ABL. Full-length c-BCR as well as BCR sequences retained in BCR-ABL bind specifically to the SH2 domain of ABL. The binding domain has been localized within the first exon of BCR and consists of at least two SH2-binding sites. This domain is essential for BCR-ABL-mediated transformation. Phosphoserine/phosphothreonine but not phosphotyrosine residues on BCR are required for interaction with the ABL SH2 domain. These findings extend the range of potential SH2-protein interactions in growth control pathways and suggest a function for SH2 domains in the activation of the BCR-ABL oncogene as well as a role for BCR in cellular signaling pathways.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
161-71
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1712671-Amino Acid Sequence,
pubmed-meshheading:1712671-Animals,
pubmed-meshheading:1712671-Binding Sites,
pubmed-meshheading:1712671-Cell Line,
pubmed-meshheading:1712671-Cell Transformation, Neoplastic,
pubmed-meshheading:1712671-Exons,
pubmed-meshheading:1712671-Fusion Proteins, bcr-abl,
pubmed-meshheading:1712671-Genes, abl,
pubmed-meshheading:1712671-Genetic Variation,
pubmed-meshheading:1712671-Humans,
pubmed-meshheading:1712671-Insects,
pubmed-meshheading:1712671-Molecular Sequence Data,
pubmed-meshheading:1712671-Oncogene Proteins,
pubmed-meshheading:1712671-Oncogenes,
pubmed-meshheading:1712671-Phosphotyrosine,
pubmed-meshheading:1712671-Plasmids,
pubmed-meshheading:1712671-Protein Biosynthesis,
pubmed-meshheading:1712671-Protein-Tyrosine Kinases,
pubmed-meshheading:1712671-Proto-Oncogene Proteins,
pubmed-meshheading:1712671-Proto-Oncogene Proteins c-bcr,
pubmed-meshheading:1712671-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:1712671-Transcription, Genetic,
pubmed-meshheading:1712671-Transfection,
pubmed-meshheading:1712671-Tyrosine
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pubmed:year |
1991
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pubmed:articleTitle |
BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner.
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pubmed:affiliation |
Department of Microbiology and Molecular Genetics, University of California, Los Angeles 90024-1570.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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