Regulation of the E3 ubiquitin ligase activity of MDM2 by an N-terminal pseudo-substrate motif

Journal of Chemical Biology

Volumn 2, Issue 3, 2009, Pages 113-129

  Worrall, Erin G ^a   Wawrzynow, Bartosz ^a   Worrall, Liam ^a,b   Walkinshaw, Malcolm ^a   Ball, Kathryn L ^a   Hupp, Ted R ^a  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

Allostery; Kinase; MDM2; P53; Ubiquitination

Indexed keywords

ARGININE; ASPARTIC ACID; LYSINE; PROTEASOME; PROTEIN MDM2; PROTEIN MDMX; PROTEIN P53; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3;

ARTICLE; CATALYSIS; CODON; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME REGULATION; FEEDBACK SYSTEM; GENE MUTATION; HUMAN; HUMAN CELL; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMOSTABILITY; UBIQUITINATION;

EID: 68949161579     PISSN: 18646158     EISSN: 18646166     Source Type: Journal    
DOI: 10.1007/s12154-009-0019-5     Document Type: Article

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