The E3 ubiquitin ligase UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates

Journal of Biological Chemistry

Volumn 288, Issue 48, 2013, Pages 34575-34587

  Chu, Bernard W ^a   Kovary, Kyle M ^a   Guillaume, Johan ^a   Chen, Ling Chun ^a   Teruel, Mary N ^a   Wandless, Thomas J ^a  

^a STANFORD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR PROTEINS; HIGH AFFINITY LIGANDS; PARTIAL PROTEOLYSIS; POLYUBIQUITINATION; PROTEIN AGGREGATES; PROTEIN DEGRADATION; PROTEIN FRAGMENTS; PROTEIN SYNTHESIS;

AMINO ACIDS; PROTEINS; PROTEOLYSIS;

SUBSTRATES;

PROTEASOME; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN PROTEIN LIGASE E3C; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; ENZYME DEGRADATION; ENZYME SPECIFICITY; FLOW CYTOMETRY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; HUMAN CELL; IMMUNOBLOTTING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PROCESSING; RNA INTERFERENCE; UBIQUITINATION;

EID: 84889072454     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.499350     Document Type: Article

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