Cdc34 self-association is facilitated by ubiquitin thiolester formation and is required for its catalytic activity

Molecular and Cellular Biology

Volumn 23, Issue 15, 2003, Pages 5388-5400

  Varelas, Xaralabos ^a   Ptak, Christopher ^a   Ellison, Michael J ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CDC34 PROTEIN; THIOESTER; UBIQUITIN; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CATALYST; CELL LYSATE; CONTROLLED STUDY; GENE MUTATION; IMMUNOPRECIPITATION; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; SACCHAROMYCES CEREVISIAE; SURFACE PROPERTY;

BINDING SITES; CATALYTIC DOMAIN; CROSS-LINKING REAGENTS; CYSTEINE; DNA MUTATIONAL ANALYSIS; ESTERS; IMMUNOBLOTTING; LIGASES; MODELS, BIOLOGICAL; MODELS, MOLECULAR; PLASMIDS; PRECIPITIN TESTS; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE; TEMPERATURE; UBIQUITIN; UBIQUITIN-PROTEIN LIGASE COMPLEXES;

BACTERIA (MICROORGANISMS); INSERTION SEQUENCES; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0042090923     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.15.5388-5400.2003     Document Type: Article

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