Aqueous accessibility to the transmembrane regions of subunit c of the Escherichia coli F1F0 ATP synthase.
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Alkaliphilic Bacteria with Impact on Industrial Applications, Concepts of Early Life Forms, and Bioenergetics of ATP SynthesisA new type of proton coordination in an F(1)F(o)-ATP synthase rotor ringCryo-EM studies of the structure and dynamics of vacuolar-type ATPasesHigh-resolution structure of the rotor ring of a proton-dependent ATP synthaseSubnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthaseStructure of the c10 ring of the yeast mitochondrial ATP synthase in the open conformationA new type of Na(+)-driven ATP synthase membrane rotor with a two-carboxylate ion-coupling motifRealistic simulations of the coupling between the protomotive force and the mechanical rotation of the F0-ATPase.F1F0-ATP synthases of alkaliphilic bacteria: lessons from their adaptations.The ATP synthase a-subunit of extreme alkaliphiles is a distinct variant: mutations in the critical alkaliphile-specific residue Lys-180 and other residues that support alkaliphile oxidative phosphorylation.Structural study on the architecture of the bacterial ATP synthase Fo motor.Chemical reactivities of cysteine substitutions in subunit a of ATP synthase define residues gating H+ transport from each side of the membrane.Direct observation of stepped proteolipid ring rotation in E. coli F₀F₁-ATP synthase.Interacting cytoplasmic loops of subunits a and c of Escherichia coli F1F0 ATP synthase gate H+ transport to the cytoplasm.Understanding structure, function, and mutations in the mitochondrial ATP synthase.Promiscuous archaeal ATP synthase concurrently coupled to Na+ and H+ translocation.Obstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase.Structure and mechanism of the ATP synthase membrane motor inferred from quantitative integrative modeling.Residues in the polar loop of subunit c in Escherichia coli ATP synthase function in gating proton transport to the cytoplasm.Predicted Structures of the Proton-Bound Membrane-Embedded Rotor Rings of the Saccharomyces cerevisiae and Escherichia coli ATP Synthases.New mutations in the mycobacterial ATP synthase: new insights into the binding of the diarylquinoline TMC207 to the ATP synthase C-ring structure.Resolving the negative potential side (n-side) water-accessible proton pathway of F-type ATP synthase by molecular dynamics simulations.On the question of hydronium binding to ATP-synthase membrane rotorsBiophysical Characterization of a Thermoalkaliphilic Molecular Motor with a High Stepping Torque Gives Insight into Evolutionary ATP Synthase Adaptation.Analysis of an N-terminal deletion in subunit a of the Escherichia coli ATP synthase.
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Aqueous accessibility to the transmembrane regions of subunit c of the Escherichia coli F1F0 ATP synthase.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 19 June 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Aqueous accessibility to the t ...... richia coli F1F0 ATP synthase.
@en
Aqueous accessibility to the t ...... richia coli F1F0 ATP synthase.
@nl
type
label
Aqueous accessibility to the t ...... richia coli F1F0 ATP synthase.
@en
Aqueous accessibility to the t ...... richia coli F1F0 ATP synthase.
@nl
prefLabel
Aqueous accessibility to the t ...... richia coli F1F0 ATP synthase.
@en
Aqueous accessibility to the t ...... richia coli F1F0 ATP synthase.
@nl
P2860
P356
P1476
Aqueous accessibility to the t ...... richia coli F1F0 ATP synthase.
@en
P2093
P Ryan Steed
Robert H Fillingame
P2860
P304
23243-23250
P356
10.1074/JBC.M109.002501
P407
P577
2009-06-19T00:00:00Z