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Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an autoinhibited conformation
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Salmonella enterica serovar Typhimurium mutants completely lacking the F0F1 ATPase are novel live attenuated vaccine strains
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Effect of ε subunit on the rotation of thermophilic Bacillus F1-ATPase
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FEBS LETTERS (2009)
The Role of the βDELSEED-loop of ATP Synthase
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Mechanism of Inhibition by C-terminal α-Helices of the ε Subunit of Escherichia coli FoF1-ATP Synthase
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A complete collection of single-gene deletion mutants of Acinetobacter baylyi ADP1
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ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas
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The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase
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Structures of the thermophilic F1-ATPase ε subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1
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The regulator of the F1 motor:: inhibition of rotation of cyanobacterial F1-ATPase by the ε subunit
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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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Inhibition of ATP hydrolysis by thermoalkaliphilic F1Fo-ATP synthase is controlled by the C terminus of the epsilon subunit
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Activation of pausing F1 motor by external force
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A diarylquinoline drug active on the ATP synthase of Mycobacterium tuberculosis
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The Escherichia coli F1F0 ATP synthase displays biphasic synthesis kinetics
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JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
UCSF chimera - A visualization system for exploratory research and analysis
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JOURNAL OF COMPUTATIONAL CHEMISTRY (2004)
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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Genetic fusions of globular proteins to the ε subunit of the Escherichia coli ATP synthase -: Implications for in vivo rotational catalysis and ε subunit function
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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
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Identification of loci essential for the growth of Helicobacter pylori under acidic conditions
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The activity of the ATP synthase from Escherichia coli is regulated by the transmembrane proton motive force
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