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Q27681454-18B564CB-F9FF-45AC-8A4A-92B7DC207D52
Q27681454-18B564CB-F9FF-45AC-8A4A-92B7DC207D52
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http://www.wikidata.org/entity/statement/Q27681454-18B564CB-F9FF-45AC-8A4A-92B7DC207D52
Structural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis Mechanism
P2860
Q27681454-18B564CB-F9FF-45AC-8A4A-92B7DC207D52
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27681454-18B564CB-F9FF-45AC-8A4A-92B7DC207D52
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wasDerivedFrom
b1a1de68ae9a452f895f2123369542c73434cca7
P2860
The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains