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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2-3
|
pubmed:dateCreated |
1992-1-24
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pubmed:abstractText |
Genetic alterations of the c-myc locus in various malignancies and the ability of c-myc to transform cultured cells and induce tumors in transgenic animals attest to its central role in many neoplasms. By dissecting the c-Myc protein, a number of critical functional domains of c-Myc have been identified and characterized; these findings suggest a model for c-Myc function and intracellular activity (Fig. 4). c-Myc is synthesized in the cytoplasm and undergoes oligomerization another protein such as Max. Its nuclear localization signal allows c-Myc to be targeted to and retained in the nucleus, where the protein seeks out and binds to specific DNA sites, perhaps facilitated by c-Myc's ability to bind non-specifically to DNA. Once bound to specific DNA sequences, c-Myc then activates or inhibits transcription of a number of target genes, with consequent alterations in cell growth and differentiation. Continued studies of c-Myc and its partner Max should further elucidate the mechanisms by which c-Myc can contribute both to the regulation of normal cell growth and the alteration in that regulation in neoplasia.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
|
pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
10
|
pubmed:volume |
1072
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
103-13
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1751543-Amino Acid Sequence,
pubmed-meshheading:1751543-Animals,
pubmed-meshheading:1751543-Cell Differentiation,
pubmed-meshheading:1751543-Cell Nucleus,
pubmed-meshheading:1751543-Cell Transformation, Neoplastic,
pubmed-meshheading:1751543-DNA-Binding Proteins,
pubmed-meshheading:1751543-Humans,
pubmed-meshheading:1751543-Leucine Zippers,
pubmed-meshheading:1751543-Molecular Sequence Data,
pubmed-meshheading:1751543-Protein Conformation,
pubmed-meshheading:1751543-Protein Processing, Post-Translational,
pubmed-meshheading:1751543-Proto-Oncogene Proteins c-myc,
pubmed-meshheading:1751543-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1751543-Transcription, Genetic
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pubmed:year |
1991
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pubmed:articleTitle |
c-myc oncoprotein function.
|
pubmed:affiliation |
Department of Medicine, Johns Hopkins Oncology Center, Johns Hopkins University School of Medicine, Baltimore, MD.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
|