Refereed review article in scientific journal (A2)
MYC PROTEIN - PARTNERS AND ANTAGONISTS
List of Authors: VASTRIK I, MAKELA TP, KOSKINEN PJ, KLEFSTROM J, ALITALO K
Publisher: BEGELL HOUSE INC
Publication year: 1994
Journal: Critical Review in Oncogenesis
Journal name in source: CRITICAL REVIEWS IN ONCOGENESIS
Journal acronym: CRIT REV ONCOGENESIS
Volume number: 5
Issue number: 1
Start page: 59
End page: 68
Number of pages: 10
ISSN: 0893-9675
DOI: http://dx.doi.org/10.1615/CritRevOncog.v5.i1.30
Abstract
One of the first oncogenes identified from human tumors was c-myc, which is frequently activated in Burkitt's lymphomas due to chromosomal translocations. Subsequently, members of the myc oncogene family were found to be amplified in neuroblastoma and small-cell lung cancer. In normal cells, Myc activity has been shown to be both necessary and sufficient for resting cells to enter the cell cycle. Interestingly, it appears that Myc not only drives the cell cycle, but also induces cell death by apoptosis in certain situations. Myc contains a transcriptional activation domain and a basic helix-loop-helix-leucine zipper DNA-binding and dimerization domain. As a heterodimer with a structurally related protein, Max, Myc can bind DNA in a sequence-specific manner. These results suggest that the Myc/Max heterodimer functions as a transcriptional activator of genes that are critical for the regulation of cell growth.
One of the first oncogenes identified from human tumors was c-myc, which is frequently activated in Burkitt's lymphomas due to chromosomal translocations. Subsequently, members of the myc oncogene family were found to be amplified in neuroblastoma and small-cell lung cancer. In normal cells, Myc activity has been shown to be both necessary and sufficient for resting cells to enter the cell cycle. Interestingly, it appears that Myc not only drives the cell cycle, but also induces cell death by apoptosis in certain situations. Myc contains a transcriptional activation domain and a basic helix-loop-helix-leucine zipper DNA-binding and dimerization domain. As a heterodimer with a structurally related protein, Max, Myc can bind DNA in a sequence-specific manner. These results suggest that the Myc/Max heterodimer functions as a transcriptional activator of genes that are critical for the regulation of cell growth.
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