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Wolfgang Junge et al.
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Variations of Subunit ε of the Mycobacterium tuberculosis F1Fo ATP Synthase and a Novel Model for Mechanism of Action of the Tuberculosis Drug TMC207
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Novel Antibiotics Targeting Respiratory ATP Synthesis in Gram-Positive Pathogenic Bacteria
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Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an autoinhibited conformation
Gino Cingolani et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2011)
ATP synthase in slow- and fast-growing mycobacteria is active in ATP synthesis and blocked in ATP hydrolysis direction
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Single Molecule Behavior of Inhibited and Active States of Escherichia coli ATP Synthase F1 Rotation
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Salmonella enterica serovar Typhimurium mutants completely lacking the F0F1 ATPase are novel live attenuated vaccine strains
H. Northen et al.
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Effect of ε subunit on the rotation of thermophilic Bacillus F1-ATPase
Masato Tsumuraya et al.
FEBS LETTERS (2009)
The Role of the βDELSEED-loop of ATP Synthase
Nelli Mnatsakanyan et al.
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Mechanism of Inhibition by C-terminal α-Helices of the ε Subunit of Escherichia coli FoF1-ATP Synthase
Ryota Iino et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2009)
Unique rotary ATP synthase and its biological diversity
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A complete collection of single-gene deletion mutants of Acinetobacter baylyi ADP1
Veronique de Berardinis et al.
MOLECULAR SYSTEMS BIOLOGY (2008)
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
Hiromasa Yagi et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2007)
The regulator of the F1 motor:: inhibition of rotation of cyanobacterial F1-ATPase by the ε subunit
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Alterations of cellular physiology in Escherichia coli in response to oxidative phosphorylation impaired by defective F1-ATPase
Sakiko Noda et al.
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The role of subunit epsilon in the catalysis and regulation of FOF1-ATP synthase
Boris A. Feniouk et al.
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Probing conformations of the β subunit of F0F1-ATP synthase in catalysis
T Masaike et al.
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An ordered, nonredundant library of Pseudomonas aeruginosa strain PA14 transposon insertion mutants
NT Liberati et al.
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The role of the ∈ subunit in the Escherichia coli ATP synthase -: The C-terminal domain is required for efficient energy coupling
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Inhibition of ATP hydrolysis by thermoalkaliphilic F1Fo-ATP synthase is controlled by the C terminus of the epsilon subunit
Stefanie Keis et al.
JOURNAL OF BACTERIOLOGY (2006)
Regulation of the F0F1-ATP synthase:: The conformation of subunit ε might be determined by directionality of subunit γ rotation
BA Feniouk et al.
FEBS LETTERS (2005)
Activation of pausing F1 motor by external force
Y Hirono-Hara et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2005)
A diarylquinoline drug active on the ATP synthase of Mycobacterium tuberculosis
K Andries et al.
SCIENCE (2005)
The Escherichia coli F1F0 ATP synthase displays biphasic synthesis kinetics
JJ Tomashek et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
UCSF chimera - A visualization system for exploratory research and analysis
EF Pettersen et al.
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
T Suzuki et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
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
DJ Cipriano et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
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.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2001)
Identification of loci essential for the growth of Helicobacter pylori under acidic conditions
JJE Bijlsma et al.
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The activity of the ATP synthase from Escherichia coli is regulated by the transmembrane proton motive force
S Fischer et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2000)
The introduction of Escherichia coli and biochemical genetics to the study of oxidative phosphorylation
F Gibson
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