The interplay of Hrd3 and the molecular chaperone system ensures efficient degradation of malfolded secretory proteins

Molecular Biology of the Cell

Volumn 26, Issue 2, 2015, Pages 185-194

  Mehnert, Martin ^a,b   Sommermeyer, Franziska ^a,d   Berger, Maren ^a   Lakshmipathy, Sathish Kumar ^a   Gauss, Robert ^b   Aebi, Markus ^b   Jarosch, Ernst ^a   Sommer, Thomas ^a,c  

^a MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^b ETH ZURICH   (Switzerland)

^c HUMBOLDT UNIVERSITY   (Germany)

^d Fred Hutchinson Cancer Research Center   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE DEGRADATION LIGASE; LIGASE; MEMBRANE PROTEIN; PROTEIN DER1; PROTEIN HRD3; PROTEIN HRD3KR; PROTEIN KAR2; PROTEIN SCJ1; UNCLASSIFIED DRUG; DER1 PROTEIN, S CEREVISIAE; FUNGAL PROTEIN; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HRD3 PROTEIN, S CEREVISIAE; KAR2 PROTEIN, YEAST; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE PROTEIN; SCJ1 PROTEIN, S CEREVISIAE;

ARTICLE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION; GENE DELETION; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE; CHEMICAL STRUCTURE; CHEMISTRY; ENDOPLASMIC RETICULUM; GENETICS; IMMUNOBLOTTING; METABOLISM; MUTATION; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE; UNFOLDED PROTEIN RESPONSE;

ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM-ASSOCIATED DEGRADATION; FUNGAL PROTEINS; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; IMMUNOBLOTTING; MEMBRANE GLYCOPROTEINS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MUTATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; UNFOLDED PROTEIN RESPONSE;

EID: 84920984442     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E14-07-1202     Document Type: Article

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