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Q41662090-40F459D1-E0D5-473B-B5B0-14B59956A07E
Q41662090-40F459D1-E0D5-473B-B5B0-14B59956A07E
BestRank
Statement
http://www.wikidata.org/entity/statement/Q41662090-40F459D1-E0D5-473B-B5B0-14B59956A07E
Substrate binding by the yeast Hsp110 nucleotide exchange factor and molecular chaperone Sse1 is not obligate for its biological activities.
P2860
Q41662090-40F459D1-E0D5-473B-B5B0-14B59956A07E
BestRank
Statement
http://www.wikidata.org/entity/statement/Q41662090-40F459D1-E0D5-473B-B5B0-14B59956A07E
rank
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type
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Statement
wasDerivedFrom
6208237913ee2611d70257799b9435fc4f7121c6
P2860
Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates.