Specific domains of nucleolin interact with Hdm2 and antagonize Hdm2-mediated p53 ubiquitination

FEBS Journal

Volumn 279, Issue 3, 2012, Pages 370-383

  Bhatt, Purvi ^a   D'Avout, Claire ^a   Kane, Naomi S ^a   Borowiec, James A ^a   Saxena, Anjana ^b  

^a NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b CITY UNIVERSITY OF NEW YORK   (United States)

Author keywords

cancer therapy; MDM2; nucleolin; p53; ubiquitination

Indexed keywords

ARGININE; GLYCINE; NUCLEOLIN; PROTEIN MDM2; PROTEIN P53; UBIQUITIN PROTEIN LIGASE E3;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVITY; GENE SEQUENCE; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; NUCLEAR EXPORT SIGNAL; NUCLEAR LOCALIZATION SIGNAL; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; PROTEIN RNA BINDING; PROTEIN STABILITY; UBIQUITINATION;

BINDING SITES; HUMANS; NUCLEAR LOCALIZATION SIGNALS; PHOSPHOPROTEINS; PROTEIN BINDING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-MDM2; RNA-BINDING PROTEINS; TUMOR SUPPRESSOR PROTEIN P53; UBIQUITIN-PROTEIN LIGASES; UBIQUITINATION;

EID: 84856112991     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08430.x     Document Type: Article

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