The ARF/p53 pathway

Current Opinion in Genetics and Development

Volumn 10, Issue 1, 2000, Pages 94-99

  Sherr, Charles J ^a   Weber, Jason D ^a  

^a ST JUDE CHILDREN S RESEARCH HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; PROTEIN P16; PROTEIN P53; RETINOBLASTOMA PROTEIN;

APOPTOSIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; REVIEW; STRESS; TUMOR SUPPRESSOR GENE;

ADP-RIBOSYLATION FACTORS; ANIMALS; CARRIER PROTEINS; CYCLIN-DEPENDENT KINASE INHIBITOR P16; CYCLIN-DEPENDENT KINASES; GENES, TUMOR SUPPRESSOR; HUMANS; MICE; NUCLEAR PROTEINS; ONCOGENES; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-MDM2; TUMOR SUPPRESSOR PROTEIN P53;

EID: 0033993563     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(99)00038-6     Document Type: Review

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39. ••] describe the injection of avian retroviral vectors into the brains of transgenic mice engineered to express an avian retroviral receptor. Different combinations of introduced genes, modeled from molecular genotyping of human gliomas, are shown to recapitulate this disease in mice. The ability of particular genes to collaborate in tumorigenesis and the biologic properties of the resulting tumors faithfully emulate cardinal features of human brain tumors.
40. ••].
41. ••].
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48. •] reinforce earlier findings [44,45] that Mdm2 may functionally interact with proteins other than p53, such as RB or E2F-1. p300, a known p53 co-activator, is shown to regulate Mdm2-mediated p53 turnover. Newly discovered p53 family members, such as p73, associate with Mdm2 but, surprisingly, they are not degraded as a consequence.
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