Structure-function-rescue: The diverse nature of common p53 cancer mutants

Oncogene

Volumn 26, Issue 15, 2007, Pages 2226-2242

  Joerger, A C ^a   Fersht, A R ^a  

^a MEDICAL RESEARCH COUNCIL   (United Kingdom)

Author keywords

Cancer; Drug design; Mutation; p53; Structure

Indexed keywords

MUTANT PROTEIN; PROTEIN; PROTEIN P53; REGULATOR PROTEIN; TETRAMER; TUMOR SUPPRESSOR PROTEIN; ZINC;

AMINO ACID SUBSTITUTION; ANTIGEN BINDING; CANCER; CRYSTAL STRUCTURE; DNA SEQUENCE; DRUG DESIGN; DRUG TARGETING; GENE INACTIVATION; GENE MUTATION; HUMAN; MUTATIONAL ANALYSIS; NONHUMAN; PHENOTYPE; PHYSIOLOGY; PRIORITY JOURNAL; PROGNOSIS; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; REVIEW; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; SURFACE PROPERTY; TEMPERATURE SENSITIVITY; THERMOSTABILITY;

ANTINEOPLASTIC AGENTS; HUMANS; MUTATION; NEOPLASMS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; TUMOR SUPPRESSOR PROTEIN P53;

EID: 34047224955     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/sj.onc.1210291     Document Type: Review

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