Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5156
pubmed:dateCreated
1994-5-3
pubmed:abstractText
An amino-terminal transactivation domain is required for Myc to function as a transcription factor controlling cell proliferation, differentiation, and apoptosis. A complementary DNA expression library was screened with a Myc fusion protein to identify proteins interacting with this domain, and a clone encoding the Rb-related p107 protein was isolated. The p107 protein was shown to associate with Myc in vivo and to suppress the activity of the Myc transactivation domain. However, mutant forms of Myc from Burkitt lymphoma cells, which contain sequence alterations in the transactivation domain, were resistant to p107-mediated suppression. Thus, disruption of a regulatory interaction between Myc and p107 may be important in tumorigenesis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Basic Helix-Loop-Helix Leucine..., http://linkedlifedata.com/resource/pubmed/chemical/Basic-Leucine Zipper Transcription..., http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Max protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Myc associated factor X, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myc, http://linkedlifedata.com/resource/pubmed/chemical/Rbl1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma-Like Protein p107, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
264
pubmed:geneSymbol
myc
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
251-4
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:8146655-3T3 Cells, pubmed-meshheading:8146655-Animals, pubmed-meshheading:8146655-Base Sequence, pubmed-meshheading:8146655-Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, pubmed-meshheading:8146655-Basic-Leucine Zipper Transcription Factors, pubmed-meshheading:8146655-DNA-Binding Proteins, pubmed-meshheading:8146655-Helix-Loop-Helix Motifs, pubmed-meshheading:8146655-Lymphoma, B-Cell, pubmed-meshheading:8146655-Mice, pubmed-meshheading:8146655-Molecular Sequence Data, pubmed-meshheading:8146655-Nuclear Proteins, pubmed-meshheading:8146655-Point Mutation, pubmed-meshheading:8146655-Proteins, pubmed-meshheading:8146655-Proto-Oncogene Proteins c-myc, pubmed-meshheading:8146655-Recombinant Fusion Proteins, pubmed-meshheading:8146655-Retinoblastoma-Like Protein p107, pubmed-meshheading:8146655-Suppression, Genetic, pubmed-meshheading:8146655-Transcription Factors, pubmed-meshheading:8146655-Transcriptional Activation, pubmed-meshheading:8146655-Transfection, pubmed-meshheading:8146655-Tumor Cells, Cultured
pubmed:year
1994
pubmed:articleTitle
Binding and suppression of the Myc transcriptional activation domain by p107.
pubmed:affiliation
Department of Pathology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't