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Volumn 21, Issue 6, 2002, Pages 867-877

MDMX stability is regulated by p53-induced caspase cleavage in NIH3T3 mouse fibroblasts

(7) Gentiletti, Francesca a Mancini, Francesca a D'Angelo, Marco a Sacchi, Ada a Pontecorvi, Alfredo a,b Jochemsen, Aart G c Moretti, Fabiola a,d

a REGINA ELENA NATIONAL CANCER INSTITUTE (Italy)

b CATHOLIC UNIVERSITY (Italy)

c LEIDEN UNIVERSITY MEDICAL CENTER (Netherlands)

d CNR (Italy)

Author keywords

Caspase cleavage; MDMX; p53; Proteolytic degradation

Indexed keywords

AMINO ACID; BINDING PROTEIN; CASPASE; DOXORUBICIN; MUTANT PROTEIN; PROTEIN MDM2; PROTEIN MDMX; PROTEIN P53; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL STRAIN 3T3; CELLULAR DISTRIBUTION; CONTROLLED STUDY; EMBRYO; ENZYME ACTIVITY; FIBROBLAST; IN VITRO STUDY; IN VIVO STUDY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN STABILITY; REGULATORY MECHANISM; SEQUENCE HOMOLOGY; TRANSACTIVATION;

3T3 CELLS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; CASPASES; CELL CYCLE; CONSENSUS SEQUENCE; CYSTEINE ENDOPEPTIDASES; CYSTEINE PROTEINASE INHIBITORS; DOXORUBICIN; DOXYCYCLINE; ENZYME INHIBITORS; ETHYLMALEIMIDE; FEEDBACK; GENES, P53; HALF-LIFE; HUMANS; MICE; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; NUCLEAR PROTEINS; PEPTIDE FRAGMENTS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN ISOFORMS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-MDM2; RECOMBINANT FUSION PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; TRANS-ACTIVATION (GENETICS); TRANSFECTION; TUMOR SUPPRESSOR PROTEIN P53; UBIQUITIN;

ANIMALIA;

EID: 85047699938 PISSN: 09509232 EISSN: None Source Type: Journal
DOI: 10.1038/sj.onc.1205137 Document Type: Article

Times cited : (35)

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