相关参考文献
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Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotation
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Temperature-sensitive reaction intermediate of F-1-ATPase
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F1-ATPase rotates by an asymmetric, sequential mechanism using all three catalytic subunits
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Coupling of rotation and catalysis in F1-ATPase revealed by single-molecule imaging and manipulation
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The role of subunit epsilon in the catalysis and regulation of FOF1-ATP synthase
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Probing conformations of the β subunit of F0F1-ATP synthase in catalysis
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Stochastic high-speed rotation of Escherichia coli ATP synthase F1 sector -: The ε subunit-sensitive rotation
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Real-time monitoring of conformational dynamics of the ε subunit in F1-ATPase
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Chemomechanical coupling in single-molecule F-type ATP synthase
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Movements of the ε-subunit during catalysis and activation in single membrane-bound H+-ATP synthase
B Zimmermann et al.
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Activation of pausing F1 motor by external force
Y Hirono-Hara et al.
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Highly coupled ATP synthesis by F1-ATPase single molecules
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Rotor/stator interactions of the ε subunit in Escherichia coli ATP synthase and implications for enzyme regulation
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Catalysis and rotation of F1 motor:: Cleavage of ATP at the catalytic site occurs in 1 ms before 40° substep rotation
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F0F1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of ε subunit in response to proton motive force and ADP/ATP balance
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H+/ATP ratio of proton transport-coupled ATP synthesis and hydrolysis catalysed by CF0F1-liposomes
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The molecular mechanism of ATP synthesis by F1F0-ATP synthase
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Mechanism of the F1F0-type ATP synthase, a biological rotary motor
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The conformation of the ε- and γ-subunits within the Escherichia coli F1 ATPase
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ATP synthase - A marvellous rotary engine of the cell
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Large conformational changes of the ε subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme
SP Tsunoda et al.
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The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10
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Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase
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Movement of the helical domain of the ε subunit is required for the activation of thermophilic F1-ATPase
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What is the role of ε in the Escherichia coli ATP synthase?
SB Vik
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