Ufd2p synthesizes branched ubiquitin chains to promote the degradation of substrates modified with atypical chains

Nature Communications

Volumn 8, Issue , 2017, Pages

  Liu, Chao ^a   Liu, Weixiao ^a   Ye, Yihong ^b   Li, Wei ^a  

^a INSTITUTE OF ZOOLOGY   (China)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

OLEIC ACID; PROTEASOME; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UFD2P PROTEIN; UNCLASSIFIED DRUG; LYSINE; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE PROTEIN; UBIQUITIN CONJUGATING ENZYME; UFD2 PROTEIN, S CEREVISIAE;

CATALYSIS; CHEMICAL ALTERATION; DEGRADATION; ENZYME ACTIVITY; PROTEIN; SUBSTRATE; YEAST;

AMINO TERMINAL SEQUENCE; ARTICLE; ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION; ENZYME MECHANISM; NONHUMAN; PH; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; PROTEIN SYNTHESIS; SACCHAROMYCES CEREVISIAE; UBIQUITINATION; BIOSYNTHESIS; METABOLISM; PHYSIOLOGY;

SACCHAROMYCES CEREVISIAE;

LYSINE; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BINDING; PROTEOLYSIS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; UBIQUITIN; UBIQUITIN-CONJUGATING ENZYMES; UBIQUITINATION;

EID: 85011659378     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms14274     Document Type: Article

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