Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting

Molecular Biology of the Cell

Volumn 24, Issue 13, 2013, Pages 2076-2087

  Shiber, Ayala ^a   Breuer, William ^a   Brandeis, Michael ^a   Ravid, Tommer ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHAPERONE SIS1; CHAPERONE SSA1; CHAPERONE SSA2; DETERGENT; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; UBIQUITIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL FUNCTION; CELL INCLUSION; CELL TRANSFORMATION; CONJUGATION; CONTROLLED STUDY; FUNGAL STRAIN; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; SACCHAROMYCES CEREVISIAE; UBIQUITINATION; YEAST;

ADENOSINE TRIPHOSPHATASES; CYTOPLASM; GENE EXPRESSION REGULATION, FUNGAL; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; INCLUSION BODIES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STABILITY; PROTEOLYSIS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; UBIQUITIN;

EID: 84879625944     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E13-01-0010     Document Type: Article

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