Ubiquitin ligases: Structure, function, and regulation

Annual Review of Biochemistry

Volumn 86, Issue , 2017, Pages 129-157

  Zheng, Ning ^a   Shabek, Nitzan ^a  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

Author keywords

Agonist; Degron; Posttranslational modification; PTM; Ubiquitin ligase; Ubiquitination

Indexed keywords

PHYTOHORMONE; UBIQUITIN PROTEIN LIGASE E3; VIRAL PROTEIN; BACTERIAL PROTEIN; NEW DRUG; UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

CATALYSIS; ENZYME ACTIVATION; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN PROCESSING; REVIEW; SIGNAL TRANSDUCTION; UBIQUITINATION; ANIMAL; CHEMISTRY; CLASSIFICATION; ENZYME SPECIFICITY; EUKARYOTIC CELL; GENETICS; HOST PATHOGEN INTERACTION; HUMAN; METABOLISM; MICROBIOLOGY; MOLECULAR MODEL; PHOSPHORYLATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; SYNTHESIS; VIROLOGY;

ANIMALS; BACTERIAL PROTEINS; DRUGS, INVESTIGATIONAL; EUKARYOTIC CELLS; HOST-PATHOGEN INTERACTIONS; HUMANS; MODELS, MOLECULAR; PHOSPHORYLATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEOLYSIS; SUBSTRATE SPECIFICITY; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES; UBIQUITINATION; VIRAL PROTEINS;

EID: 85021691475     PISSN: 00664154     EISSN: 15454509     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-060815-014922     Document Type: Review

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