Highly coupled ATP synthesis by F1-ATPase single molecules (Q45270373)

11 December 2017

Highly coupled ATP synthesis by F1-ATPase single molecules (English)

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11 December 2017

Yannick Rondelez

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Shoji Takeuchi

object named as

Shoji Takeuchi

6

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author name string

Guillaume Tresset

2

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11 December 2017

Takako Nakashima

3

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11 December 2017

Yasuyuki Kato-Yamada

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11 December 2017

Hiroyuki Fujita

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11 December 2017

Hiroyuki Noji

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11 December 2017

language of work or name

English

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publication date

1 February 2005

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11 December 2017

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11 December 2017

433

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7027

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11 December 2017

773-777

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https://scigraph.springernature.com/pub.10.1038/nature03277

11 December 2017

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cites work

The ATP synthase--a splendid molecular machine

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

The molecular mechanism of ATP synthesis by F1F0-ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

ATP synthase--a marvellous rotary engine of the cell.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Structural model of F1-ATPase and the implications for rotary catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Direct observation of the rotation of F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Direct observation of the rotation of epsilon subunit in F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Subunit rotation in Escherichia coli FoF1-ATP synthase during oxidative phosphorylation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Mechanically driven ATP synthesis by F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Pause and rotation of F(1)-ATPase during catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Activation of pausing F1 motor by external force

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Microfabricated arrays of femtoliter chambers allow single molecule enzymology.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Inhibitory properties of endogenous subunit ϵ in the Escherichia coli F1 ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Epsilon subunit of Escherichia coli F1-ATPase: effects on affinity for aurovertin and inhibition of product release in unisite ATP hydrolysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Thermophilic F1-ATPase is activated without dissociation of an endogenous inhibitor, epsilon subunit.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

The C-terminal domain of the epsilon subunit of the chloroplast ATP synthase is not required for ATP synthesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Large conformational changes of the epsilon subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

F0F1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of epsilon subunit in response to proton motive force and ADP/ATP balance

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Rotor/Stator interactions of the epsilon subunit in Escherichia coli ATP synthase and implications for enzyme regulation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Purine but not pyrimidine nucleotides support rotation of F(1)-ATPase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Poly(dimethylsiloxane) as a material for fabricating microfluidic devices

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Monolithic microfabricated valves and pumps by multilayer soft lithography

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Expression of the wild-type and the Cys-/Trp-less alpha 3 beta 3 gamma complex of thermophilic F1-ATPase in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

Single-molecule imaging of rotation of F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE03277

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NATURE03277

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Dimensions Publication ID

11 December 2017

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