A2 Vertaisarvioitu katsausartikkeli tieteellisessä lehdessä
MYC PROTEIN - PARTNERS AND ANTAGONISTS
Tekijät: VASTRIK I, MAKELA TP, KOSKINEN PJ, KLEFSTROM J, ALITALO K
Kustantaja: BEGELL HOUSE INC
Julkaisuvuosi: 1994
Journal: Critical Review in Oncogenesis
Tietokannassa oleva lehden nimi: CRITICAL REVIEWS IN ONCOGENESIS
Lehden akronyymi: CRIT REV ONCOGENESIS
Vuosikerta: 5
Numero: 1
Aloitussivu: 59
Lopetussivu: 68
Sivujen määrä: 10
ISSN: 0893-9675
DOI: https://doi.org/10.1615/CritRevOncog.v5.i1.30
Tiivistelmä
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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