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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2003-10-2
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pubmed:abstractText |
MLL fusion proteins are leukemogenic, but their mechanism is unclear. Induced dimerization of a truncated MLL immortalizes bone marrow and imposes a reversible block on myeloid differentiation associated with upregulation of Hox a7, a9, and Meis1. Both dimerized MLL and exon-duplicated MLL are potent transcriptional activators, suggesting a link between dimerization and partial tandem duplication of DNA binding domains of MLL. Dimerized MLL binds with higher affinity than undimerized MLL to a CpG island within the Hox a9 locus. However, MLL-AF9 is not dimerized in vivo. The data support a model in which either MLL dimerization/exon duplication or fusion to a transcriptional activator results in Hox gene upregulation and ultimately transformation.
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pubmed:grant |
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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/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HOXA7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hoxa7 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/MLL protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mll protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Myeloid-Lymphoid Leukemia Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins, Fusion,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/myeloid ecotropic viral...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1535-6108
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
197-207
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:14522254-Animals,
pubmed-meshheading:14522254-Bone Marrow Cells,
pubmed-meshheading:14522254-Cell Survival,
pubmed-meshheading:14522254-Cell Transformation, Neoplastic,
pubmed-meshheading:14522254-Cells, Cultured,
pubmed-meshheading:14522254-Cricetinae,
pubmed-meshheading:14522254-Cricetulus,
pubmed-meshheading:14522254-DNA-Binding Proteins,
pubmed-meshheading:14522254-Dimerization,
pubmed-meshheading:14522254-Gene Expression Regulation, Leukemic,
pubmed-meshheading:14522254-Hematopoietic System,
pubmed-meshheading:14522254-Homeodomain Proteins,
pubmed-meshheading:14522254-Humans,
pubmed-meshheading:14522254-Mice,
pubmed-meshheading:14522254-Myeloid-Lymphoid Leukemia Protein,
pubmed-meshheading:14522254-Neoplasm Proteins,
pubmed-meshheading:14522254-Oncogene Proteins, Fusion,
pubmed-meshheading:14522254-Protein Binding,
pubmed-meshheading:14522254-Protein Structure, Tertiary,
pubmed-meshheading:14522254-Proto-Oncogenes,
pubmed-meshheading:14522254-Retroviridae,
pubmed-meshheading:14522254-Trans-Activators,
pubmed-meshheading:14522254-Transcription Factors
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pubmed:year |
2003
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pubmed:articleTitle |
Dimerization of MLL fusion proteins immortalizes hematopoietic cells.
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pubmed:affiliation |
Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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