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Q46986565-574B050C-D2D0-40B2-9FF0-1585F20E8B71
Q46986565-574B050C-D2D0-40B2-9FF0-1585F20E8B71
BestRank
Statement
http://www.wikidata.org/entity/statement/Q46986565-574B050C-D2D0-40B2-9FF0-1585F20E8B71
Mitochondrial ATP synthase. Crystal structure of the catalytic F1 unit in a vanadate-induced transition-like state and implications for mechanism.
P2860
Q46986565-574B050C-D2D0-40B2-9FF0-1585F20E8B71
BestRank
Statement
http://www.wikidata.org/entity/statement/Q46986565-574B050C-D2D0-40B2-9FF0-1585F20E8B71
rank
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type
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Statement
wasDerivedFrom
c6e6d67b0af5a9bbca32af2440f1f5c1b2e3af4b
P2860
Kinetic mechanism of mitochondrial adenosine triphosphatase. Inhibition by azide and activation by sulphite.