awgldk
/
wikidata
/
Login
Register
TriplyDB
Wikidata
Browser
Triples
Insights
Schema
BETA
Class frequency
Class hierarchy
SPARQL
Graphs
1
Q39254884-5487CEF2-78DF-417D-B486-5E922153A208
Q39254884-5487CEF2-78DF-417D-B486-5E922153A208
BestRank
Statement
http://www.wikidata.org/entity/statement/Q39254884-5487CEF2-78DF-417D-B486-5E922153A208
Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM.
P2860
Q39254884-5487CEF2-78DF-417D-B486-5E922153A208
BestRank
Statement
http://www.wikidata.org/entity/statement/Q39254884-5487CEF2-78DF-417D-B486-5E922153A208
rank
NormalRank
type
BestRank
Statement
wasDerivedFrom
2399937a4476f4f1ea845cc46aa770acb5fc0b80
P2860
Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis.