Structural studies of p53 inactivation by DNA-contact mutations and its rescue by suppressor mutations via alternative protein-DNA interactions

Nucleic Acids Research

Volumn 41, Issue 18, 2013, Pages 8748-8759

  Eldar, Amir ^a   Rozenberg, Haim ^a   Diskin Posner, Yael ^a   Rohs, Remo ^b   Shakked, Zippora ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; PROTEIN P53;

ARTICLE; BASE PAIRING; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DNA PROTEIN COMPLEX; DNA STRUCTURE; HYDROGEN BOND; LOSS OF FUNCTION MUTATION; MOLECULAR STABILITY; PRIORITY JOURNAL; PROTEIN DNA INTERACTION; PROTEIN FUNCTION; STRUCTURE ANALYSIS; TUMOR SUPPRESSOR GENE;

CRYSTALLOGRAPHY, X-RAY; DNA; HUMANS; MODELS, MOLECULAR; MUTATION; NUCLEIC ACID CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SUPPRESSION, GENETIC; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84885907778     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt630     Document Type: Article

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