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Q41832929-9C25DC4B-287E-4C03-B843-926D5F499D3B
Q41832929-9C25DC4B-287E-4C03-B843-926D5F499D3B
BestRank
Statement
http://www.wikidata.org/entity/statement/Q41832929-9C25DC4B-287E-4C03-B843-926D5F499D3B
Forces Driving Chaperone Action
P2860
Q41832929-9C25DC4B-287E-4C03-B843-926D5F499D3B
BestRank
Statement
http://www.wikidata.org/entity/statement/Q41832929-9C25DC4B-287E-4C03-B843-926D5F499D3B
rank
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wasDerivedFrom
1dc14db4ccda75910fdc0385afd4686a1da1694f
P2860
Substrate protein folds while it is bound to the ATP-independent chaperone Spy