Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization

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

Volumn 96, Issue 7, 1999, Pages 3595-3599

  Mateu, Mauricio G ^a,b   Fersht, Alan R ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSIDAD AUTÓNOMA DE MADRID   (Spain)

Author keywords

Negative dominance; p51; p73; Protein engineering; Stability

Indexed keywords

PROTEIN P53; TETRAMER;

ARTICLE; GENE EXPRESSION; GENE MUTATION; GENE SEQUENCE; GENE STRUCTURE; GENETIC ENGINEERING; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; STOICHIOMETRY; THERMOSTABILITY;

ANIMALS; CLONING, MOLECULAR; EVOLUTION, MOLECULAR; GUANIDINE; HUMANS; MACROMOLECULAR SUBSTANCES; MAMMALS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; TUMOR SUPPRESSOR PROTEIN P53;

GALLUS GALLUS; INVERTEBRATA; VERTEBRATA;

EID: 0033616825     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.96.7.3595     Document Type: Article

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