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rdf:type |
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lifeskim:mentions |
umls-concept:C0029016,
umls-concept:C0040715,
umls-concept:C0380093,
umls-concept:C0599718,
umls-concept:C0599813,
umls-concept:C0599893,
umls-concept:C0682323,
umls-concept:C0919528,
umls-concept:C1145667,
umls-concept:C1334343,
umls-concept:C1334516,
umls-concept:C1522702
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pubmed:issue |
1-3
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pubmed:dateCreated |
2002-6-17
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pubmed:abstractText |
The LIM only protein Lmo2 plays an important role in hematopoiesis and leukemogenesis. Lmo2 acts as a bridging molecule between components of hematopoietic gene regulatory protein complexes. We used the yeast two-hybrid system to identify novel Lmo2 interacting proteins and found that the AF6 protein binds to Lmo2. AF6 is a recurrent fusion partner of MLL, the human homolog of Drosophila trithorax chromatin remodeling protein that is involved in childhood leukemia and mixed lineage leukemia. Our data support the notion that recurrent fusion partners of chimeric MLL proteins recruit hematopoietic gene regulatory complexes.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Kinesin,
http://linkedlifedata.com/resource/pubmed/chemical/LIM Domain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/LMO2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MLL protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MLLT4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myeloid-Lymphoid Leukemia Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/canoe protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
521
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
36-8
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:12067721-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:12067721-Animals,
pubmed-meshheading:12067721-Cell Line,
pubmed-meshheading:12067721-DNA-Binding Proteins,
pubmed-meshheading:12067721-Drosophila Proteins,
pubmed-meshheading:12067721-Humans,
pubmed-meshheading:12067721-Jurkat Cells,
pubmed-meshheading:12067721-Kinesin,
pubmed-meshheading:12067721-LIM Domain Proteins,
pubmed-meshheading:12067721-Metalloproteins,
pubmed-meshheading:12067721-Myeloid-Lymphoid Leukemia Protein,
pubmed-meshheading:12067721-Myosins,
pubmed-meshheading:12067721-Proto-Oncogene Proteins,
pubmed-meshheading:12067721-Proto-Oncogenes,
pubmed-meshheading:12067721-Quail,
pubmed-meshheading:12067721-Recombinant Fusion Proteins,
pubmed-meshheading:12067721-Transcription Factors
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pubmed:year |
2002
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pubmed:articleTitle |
The LIM domain protein Lmo2 binds to AF6, a translocation partner of the MLL oncogene.
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pubmed:affiliation |
Max-Delbrueck-Center for Molecular Medicine, Robert-Roessle-Str. 10, 13122 Berlin, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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