A structure-based model for the synthesis and hydrolysis of ATP by F1-ATPase (Q28278202)

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English	A structure-based model for the synthesis and hydrolysis of ATP by F1-ATPase	scientific article

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A structure-based model for the synthesis and hydrolysis of ATP by F1-ATPase (English)

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3

Martin Karplus

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author name string

Yi Qin Gao

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1

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Wei Yang

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2

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language of work or name

English

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publication date

21 October 2005

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published in

Cell

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volume

123

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issue

2

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page(s)

195-205

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cites work

F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps

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The Escherichia coli FOF1 gammaM23K uncoupling mutant has a higher K0.5 for Pi. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway

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Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase

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The structure of bovine F1-ATPase inhibited by ADP and beryllium fluoride

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Molecular mechanisms of rotational catalysis in the F(0)F(1) ATP synthase

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Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride

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Free energy simulations: use of reverse cumulative averaging to determine the equilibrated region and the time required for convergence

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Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis

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ATP hydrolysis in the betaTP and betaDP catalytic sites of F1-ATPase

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The cell as a collection of protein machines: preparing the next generation of molecular biologists

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A dynamic analysis of the rotation mechanism for conformational change in F(1)-ATPase

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Structural changes linked to proton translocation by subunit c of the ATP synthase

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The missing link between thermodynamics and structure in F1-ATPase

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A model for the cooperative free energy transduction and kinetics of ATP hydrolysis by F 1 -ATPase

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Direct observation of the rotation of F1-ATPase

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Free energy simulations come of age: protein-ligand recognition

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Rotation of F1-ATPase: how an ATP-driven molecular machine may work

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

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Catalytic mechanism of F1-ATPase

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Mutagenesis of residue betaArg-246 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F1-ATPase

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Elastic energy storage in beta-sheets with application to F1-ATPase

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Mechanically driven ATP synthesis by F1-ATPase

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The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution

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The molecular mechanism of ATP synthesis by F1F0-ATP synthase

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A normal mode analysis of structural plasticity in the biomolecular motor F(1)-ATPase

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The unbinding of ATP from F1-ATPase

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Energy Interconversion by the Ca2+-Dependent ATPase of the Sarcoplasmic Reticulum

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Interactions among γR268, γQ269, and the β Subunit Catch Loop of Escherichia coli F1-ATPase Are Important for Catalytic Activity

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Conformational change of H+-ATPase beta monomer revealed on segmental isotope labeling NMR spectroscopy

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Importance of F1-ATPase residue alpha-Arg-376 for catalytic transition state stabilization

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The binding change mechanism for ATP synthase--some probabilities and possibilities

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Biomolecular motors: the F1-ATPase paradigm

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Energy transduction in the F1 motor of ATP synthase

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Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP

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The ATP synthase--a splendid molecular machine

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Proton-powered subunit rotation in single membrane-bound F0F1-ATP synthase.

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.CELL.2005.10.001

A structure-based model for the synthesis and hydrolysis of ATP by F1-ATPase (Q28278202)

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A structure-based model for the synthesis and hydrolysis of ATP by F1-ATPase (Q28278202)

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