Sequential Poly-ubiquitylation by Specialized Conjugating Enzymes Expands the Versatility of a Quality Control Ubiquitin Ligase

Molecular Cell

Volumn 63, Issue 5, 2016, Pages 827-839

  Weber, Annika ^a   Cohen, Itamar ^b   Popp, Oliver ^a   Dittmar, Gunnar ^a   Reiss, Yuval ^b   Sommer, Thomas ^a,c   Ravid, Tommer ^b   Jarosch, Ernst ^a  

^a MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^b HEBREW UNIVERSITY OF JERUSALEM   (Israel)

^c HUMBOLDT UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; UBIQUITIN PROTEIN LIGASE; LYSINE; POLYUBIQUITIN; PROTEASOME; SACCHAROMYCES CEREVISIAE PROTEIN; SSM4 PROTEIN, S CEREVISIAE; UBC6 PROTEIN, S CEREVISIAE; UBC7 PROTEIN, S CEREVISIAE; UBIQUITIN CONJUGATING ENZYME;

ARTICLE; BINDING SITE; CONJUGATION; CONTROLLED STUDY; ENZYME ACTIVITY; IN VITRO STUDY; MOLECULAR WEIGHT; QUALITY CONTROL; UBIQUITINATION; AMINO ACID SEQUENCE; ENZYME SPECIFICITY; GENE EXPRESSION REGULATION; GENETICS; HUMAN; HYDROXYLATION; METABOLISM; PROTEIN DEGRADATION; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; GENE EXPRESSION REGULATION, FUNGAL; HUMANS; HYDROXYLATION; LYSINE; POLYUBIQUITIN; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEOLYSIS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SIGNAL TRANSDUCTION; SUBSTRATE SPECIFICITY; UBIQUITIN-CONJUGATING ENZYMES; UBIQUITIN-PROTEIN LIGASES; UBIQUITINATION;

EID: 84992462623     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2016.07.020     Document Type: Article

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