PML regulates p53 stability by sequestering Mdm2 to the nucleolus

Nature Cell Biology

Volumn 6, Issue 7, 2004, Pages 665-672

  Bernardi, Rosa ^a   Scaglioni, Pier Paolo ^a   Bergmann, Stephan ^a   Horn, Henning F ^b   Vousden, Karen H ^b   Pandolfi, Pier Paolo ^a  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^b BEATSON INSTITUTE FOR CANCER RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ARF PROTEIN; ATR PROTEIN; CELL DNA; NUCLEAR PROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN L 11; PROTEIN MDM2; PROTEIN P53; S PHASE KINASE ASSOCIATED PROTEIN; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG;

APOPTOSIS; ARTICLE; CANCER INHIBITION; CELLULAR DISTRIBUTION; CONTROLLED STUDY; DNA DAMAGE; HUMAN; HUMAN CELL; NUCLEAR LOCALIZATION SIGNAL; NUCLEOLUS; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; REGULATORY MECHANISM; TUMOR SUPPRESSOR GENE;

ACTIVE TRANSPORT, CELL NUCLEUS; ADP-RIBOSYLATION FACTOR 1; ANIMALS; CELL COMPARTMENTATION; CELL CYCLE PROTEINS; CELL LINE, TRANSFORMED; CELL NUCLEOLUS; CELLS, CULTURED; FIBROBLASTS; HUMANS; MICE; NEOPLASM PROTEINS; NIH 3T3 CELLS; NUCLEAR PROTEINS; PHOSPHORYLATION; PROTEIN TRANSPORT; PROTEIN-SERINE-THREONINE KINASES; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-MDM2; RIBOSOMAL PROTEINS; RNA STABILITY; TRANSCRIPTION FACTORS; TUMOR SUPPRESSOR PROTEIN P53; TUMOR SUPPRESSOR PROTEINS;

EID: 3242726103     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1147     Document Type: Article

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