about
The remarkable transport mechanism of P-glycoprotein: a multidrug transporter.The rotary mechanism of the ATP synthase.Filming biomolecular processes by high-speed atomic force microscopyStructure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helicesThe metalloprotease encoded by ATP23 has a dual function in processing and assembly of subunit 6 of mitochondrial ATPase.Time-course proteome analysis reveals the dynamic response of Cryptococcus gattii cells to fluconazoleIntragenic and intergenic suppression of the Escherichia coli ATP synthase subunit a mutation of Gly-213 to Asn: functional interactions between residues in the proton transport siteTemperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of gamma-beta subunit interactions in the catalytic dwell.A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysisThe amino-terminal domain of the E subunit of vacuolar H(+)-ATPase (V-ATPase) interacts with the H subunit and is required for V-ATPase function.The mechanochemistry of V-ATPase proton pumpsAsymmetry in the F1-ATPase and its implications for the rotational cycle.Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase.The missing link between thermodynamics and structure in F1-ATPase.ATP synthesis driven by proton transport in F1F0-ATP synthase.A model for the cooperative free energy transduction and kinetics of ATP hydrolysis by F1-ATPase.Identification of the betaTP site in the x-ray structure of F1-ATPase as the high-affinity catalytic site.ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptidesMedicinal chemistry of ATP synthase: a potential drug target of dietary polyphenols and amphibian antimicrobial peptides.Biological Nanomotors with a Revolution, Linear, or Rotation Motion MechanismQuantitative determination of binding affinity of delta-subunit in Escherichia coli F1-ATPase: effects of mutation, Mg2+, and pH on Kd.Quantitative determination of direct binding of b subunit to F1 in Escherichia coli F1F0-ATP synthase.Does F1-ATPase have a catalytic site that preferentially binds MgADP?A thermo-physical analysis of the proton pump vacuolar-ATPase: the constructal approach.Transition state analysis of the coupling of drug transport to ATP hydrolysis by P-glycoprotein.Bi-site catalysis in F1-ATPase: does it exist?Identification of the F1-binding surface on the delta-subunit of ATP synthase.Mutations in the dimerization domain of the b subunit from the Escherichia coli ATP synthase. Deletions disrupt function but not enzyme assembly.Shrimp ATP synthase genes complement yeast null mutants for ATP hydrolysis but not synthesis activity.Analysis of sequence determinants of F1Fo-ATP synthase in the N-terminal region of alpha subunit for binding of delta subunit.High free energy of lipid/protein interaction in biological membranes.ATP synthase: the right size base model for nanomotors in nanomedicine.High-speed atomic force microscopy reveals rotary catalysis of rotorless F₁-ATPase.
P2860
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P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Rotational coupling in the F0F1 ATP synthase.
@ast
Rotational coupling in the F0F1 ATP synthase.
@en
type
label
Rotational coupling in the F0F1 ATP synthase.
@ast
Rotational coupling in the F0F1 ATP synthase.
@en
prefLabel
Rotational coupling in the F0F1 ATP synthase.
@ast
Rotational coupling in the F0F1 ATP synthase.
@en
P2093
P1476
Rotational coupling in the F0F1 ATP synthase.
@en
P2093
Ketchum CJ
Nakamoto RK
al-Shawi MK
P304
P356
10.1146/ANNUREV.BIOPHYS.28.1.205
P577
1999-01-01T00:00:00Z