Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates

Journal of Biological Chemistry

Volumn 288, Issue 29, 2013, Pages 21399-21411

  Mattoo, Rayees U H ^a   Sharma, Sandeep K ^a,b   Priya, Smriti ^a   Finka, Andrija ^a   Goloubinoff, Pierre ^a  

^a UNIVERSITY OF LAUSANNE   (Switzerland)

^b UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSOLIC; DEGENERATIVE DISEASE; MISFOLDING; NUCLEOTIDE-EXCHANGE FACTOR; PROTEIN AGGREGATES;

POLYPEPTIDES; PROTEINS;

AGGREGATES;

ADENOSINE TRIPHOSPHATE; CHAPERONE; HEAT SHOCK PROTEIN 110; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; POLYPEPTIDE;

ARTICLE; BINDING AFFINITY; CATALYSIS; ENZYME RELEASE; HUMAN; HYDROLYSIS; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; RESTRICTION SITE;

ATPASES; HEAT SHOCK PROTEIN; MOLECULAR CHAPERONE; PROTEIN AGGREGATION; PROTEIN MISFOLDING;

ADENOSINE TRIPHOSPHATE; BIOCATALYSIS; ENZYME STABILITY; HSP110 HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HUMANS; HYDROLYSIS; LUCIFERASES; MODELS, BIOLOGICAL; PEPTIDES; PROTEIN BINDING; PROTEIN REFOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN UNFOLDING; SOLUBILITY; SUBSTRATE SPECIFICITY; TEMPERATURE; TRYPSIN;

EID: 84880515581     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.479253     Document Type: Article

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