Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins

Proceedings of the National Academy of Sciences of the United States of America

Volumn 110, Issue 15, 2013, Pages 5975-5980

  Gowda, Naveen Kumar Chandappa ^a   Kandasamy, Ganapathi ^b   Froehlich, Marceli S ^b   Jurgen Dohmen R ^b   Andréasson, Claes ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

^b UNIVERSITY OF COLOGNE   (Germany)

Author keywords

Hsp110; Proteasome; Triage; Ubiquitin ligase; Ubr1

Indexed keywords

CHAPERONE; FES1 PROTEIN; HEAT SHOCK PROTEIN 70; NUCLEOTIDE; PROTEASOME; UBIQUITIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CYTOSOL; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN INTERACTION; UBIQUITINATION;

CYTOSOL; HSP110 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MASS SPECTROMETRY; PLASMIDS; PROMOTER REGIONS, GENETIC; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN DENATURATION; PROTEIN FOLDING; QUALITY CONTROL; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TWO-HYBRID SYSTEM TECHNIQUES; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES; ULTRACENTRIFUGATION;

EID: 84876042495     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1216778110     Document Type: Article

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