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Q26766168-D8B11D11-3EFF-458D-BC9E-B9E93EDB34D4
Q26766168-D8B11D11-3EFF-458D-BC9E-B9E93EDB34D4
BestRank
Statement
http://www.wikidata.org/entity/statement/Q26766168-D8B11D11-3EFF-458D-BC9E-B9E93EDB34D4
Molecular chaperones: guardians of the proteome in normal and disease states
P2860
Q26766168-D8B11D11-3EFF-458D-BC9E-B9E93EDB34D4
BestRank
Statement
http://www.wikidata.org/entity/statement/Q26766168-D8B11D11-3EFF-458D-BC9E-B9E93EDB34D4
rank
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wasDerivedFrom
261b3bbbd450ac9d0e380d83b69a5e5fb1a8e639
P2860
Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity.