USP14 deubiquitinates proteasome-bound substrates that are ubiquitinated at multiple sites

Nature

Volumn 532, Issue 7599, 2016, Pages 398-401

  Lee, Byung Hoon ^a   Lu, Ying ^a   Prado, Miguel A ^a   Shi, Yuan ^a,c   Tian, Geng ^a   Sun, Shuangwu ^a,b   Elsasser, Suzanne ^a   Gygi, Steven P ^a   King, Randall W ^a   Finley, Daniel ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b ZHEJIANG UNIVERSITY   (China)

^c University of Los Angeles   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN B; PROTEASOME; UBIQUITIN; UNCLASSIFIED DRUG; USP14 PROTEIN; UBIQUITIN THIOLESTERASE; USP14 PROTEIN, HUMAN;

BIOCHEMISTRY; CHEMICAL BINDING; ENZYME ACTIVITY; PHYSIOLOGICAL RESPONSE; PROTEIN; YEAST;

ARTICLE; ENZYME ACTIVE SITE; HUMAN; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; UBIQUITINATION; BIOCATALYSIS; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; KINETICS; METABOLISM; MOLECULAR MODEL; YEAST;

BIOCATALYSIS; CYCLIN B; HUMANS; KINETICS; MODELS, MOLECULAR; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEOLYSIS; SUBSTRATE SPECIFICITY; UBIQUITIN; UBIQUITIN THIOLESTERASE; UBIQUITINATION; YEASTS;

EID: 84964453431     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature17433     Document Type: Article

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