A conserved c-terminal element in the yeast doa10 and human march6 ubiquitin ligases required for selective substrate degradation

Journal of Biological Chemistry

Volumn 291, Issue 23, 2016, Pages 12105-12118

  Zattas, Dimitrios ^a,c   Berk, Jason M ^a   Kreft, Stefan G ^a,b   Hochstrasser, Mark ^a  

^a YALE UNIVERSITY   (United States)

^b UNIVERSITY OF KONSTANZ   (Germany)

^c NEW YORK STRUCTURAL BIOLOGY CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL MEMBRANES; CYTOLOGY; DEGRADATION; ENZYMES; EPITOPES; GENES; SUBSTRATES; YEAST;

ASPARAGINE RESIDUE; ENDOPLASMIC RETICULUM; PROTEIN DEGRADATION; PROTEIN SUBSTRATE; SUBSTRATE DEGRADATION; SUBSTRATE DISCRIMINATION; TRANSMEMBRANE HELICES; UBIQUITIN LIGASES;

PROTEINS;

DOA10 PROTEIN; FUNGAL PROTEIN; MARCH6 PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; MARCH6 PROTEIN, HUMAN; MEMBRANE PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SSM4 PROTEIN, S CEREVISIAE; UBIQUITIN;

ARTICLE; AUTOREGULATION; C TERMINAL ELEMENT; CLUSTERED REGULARLY INTERSPACED SHORT PALINDROMIC REPEAT; CONTROLLED STUDY; GENE LOCUS; HUMAN; HUMAN CELL; MOLECULAR EVOLUTION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; RESIDUE ANALYSIS; UBIQUITINATION; AMINO ACID SEQUENCE; CONSERVED SEQUENCE; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION; ENZYME SPECIFICITY; FLUORESCENCE MICROSCOPY; GENETICS; HELA CELL LINE; IMMUNOBLOTTING; METABOLISM; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; CONSERVED SEQUENCE; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM-ASSOCIATED DEGRADATION; HELA CELLS; HUMANS; IMMUNOBLOTTING; MEMBRANE PROTEINS; MICROSCOPY, FLUORESCENCE; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; UBIQUITIN-PROTEIN LIGASES; UBIQUITINATION; UBIQUITINS;

EID: 84974588077     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M116.726877     Document Type: Article

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