Constant c10 ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking.
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Structure and flexibility of the C-ring in the electromotor of rotary F(0)F(1)-ATPase of pea chloroplastsRespiration and the F₁Fo-ATPase enhance survival under acidic conditions in Escherichia coliCryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase.F1F0-ATP synthases of alkaliphilic bacteria: lessons from their adaptations.Engineering rotor ring stoichiometries in the ATP synthase.Comparison of the H+/ATP ratios of the H+-ATP synthases from yeast and from chloroplast.Load-dependent destabilization of the γ-rotor shaft in FOF1 ATP synthase revealed by hydrogen/deuterium-exchange mass spectrometry.Single-molecule fluorescence resonance energy transfer techniques on rotary ATP synthases.Structural divergence of the rotary ATPases.Catalytic robustness and torque generation of the F1-ATPasePredicted Structures of the Proton-Bound Membrane-Embedded Rotor Rings of the Saccharomyces cerevisiae and Escherichia coli ATP Synthases.Membrane protein insertion and assembly by the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.Individual interactions of the b subunits within the stator of the Escherichia coli ATP synthaseSubunit δ is the key player for assembly of the H(+)-translocating unit of Escherichia coli F(O)F1 ATP synthase.Time-delayed in vivo assembly of subunit a into preformed Escherichia coli FoF1 ATP synthase.Biophysical Characterization of a Thermoalkaliphilic Molecular Motor with a High Stepping Torque Gives Insight into Evolutionary ATP Synthase Adaptation.Assembly of the Escherichia coli FoF1 ATP synthase involves distinct subcomplex formation.Refined method to study the posttranslational regulation of alternative oxidases from Arabidopsis thaliana in vitro.Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data.An exploration of how the thermodynamic efficiency of bioenergetic membrane systems varies with c-subunit stoichiometry of F₁F₀ ATP synthases.
P2860
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P2860
Constant c10 ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking.
description
2009 nî lūn-bûn
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2009年の論文
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
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name
Constant c10 ring stoichiometr ...... ase analyzed by cross-linking.
@en
Constant c10 ring stoichiometr ...... ase analyzed by cross-linking.
@nl
type
label
Constant c10 ring stoichiometr ...... ase analyzed by cross-linking.
@en
Constant c10 ring stoichiometr ...... ase analyzed by cross-linking.
@nl
prefLabel
Constant c10 ring stoichiometr ...... ase analyzed by cross-linking.
@en
Constant c10 ring stoichiometr ...... ase analyzed by cross-linking.
@nl
P2093
P2860
P356
P1476
Constant c10 ring stoichiometr ...... ase analyzed by cross-linking.
@en
P2093
Britta Ballhausen
Gabriele Deckers-Hebestreit
Karlheinz Altendorf
P2860
P304
P356
10.1128/JB.01390-08
P407
P577
2009-01-30T00:00:00Z