Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90

Proceedings of the National Academy of Sciences of the United States of America

Volumn 93, Issue 16, 1996, Pages 8379-8383

  Blagosklonny, Mikhail V ^a,b   Toretsky, Jeffrey ^a   Bohen, Sean ^a,c   Neckers, Len ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

chaperone; conformational recognition; geldanamycin; mutated p53

Indexed keywords

CHAPERONE; GELDANAMYCIN; HEAT SHOCK PROTEIN; MUTANT PROTEIN; PROTEIN P53;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SYNTHESIS; RABBIT; RETICULOCYTE LYSATE; TRANSLATION REGULATION; WHEAT GERM;

ANIMALS; BENZOQUINONES; CELL-FREE SYSTEM; GENES, P53; HSP90 HEAT-SHOCK PROTEINS; LACTAMS, MACROCYCLIC; MOLECULAR CHAPERONES; POINT MUTATION; PRECIPITIN TESTS; PROTEIN BIOSYNTHESIS; PROTEIN CONFORMATION; PROTEIN FOLDING; QUINONES; RABBITS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; TRITICUM; TUMOR SUPPRESSOR PROTEIN P53;

ANIMALIA; ORYCTOLAGUS CUNICULUS; TRITICUM AESTIVUM;

EID: 0029737509     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.16.8379     Document Type: Article

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