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Q46531306-1EA8D131-2C0D-4B6E-9E1B-AF99F76F2D0B
Q46531306-1EA8D131-2C0D-4B6E-9E1B-AF99F76F2D0B
BestRank
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http://www.wikidata.org/entity/statement/Q46531306-1EA8D131-2C0D-4B6E-9E1B-AF99F76F2D0B
Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.
P2860
Q46531306-1EA8D131-2C0D-4B6E-9E1B-AF99F76F2D0B
BestRank
Statement
http://www.wikidata.org/entity/statement/Q46531306-1EA8D131-2C0D-4B6E-9E1B-AF99F76F2D0B
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wasDerivedFrom
cc0308dbc504509130a3cfc130f8f4c3b589a533
P2860
Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation.