(Q43022492)

12 November 2017

Stiffness of γ subunit of F(1)-ATPase (English)

1 reference

12 November 2017

Daichi Okuno

1

1 reference

PubMed ID

20549499

12 November 2017

Ryota Iino

series ordinal

2

1 reference

PubMed ID

20549499

12 November 2017

Hiroyuki Noji

series ordinal

3

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12 November 2017

13 June 2010

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European Biophysics Journal

12 November 2017

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12 November 2017

39

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12 November 2017

12

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12 November 2017

1589-1596

1 reference

https://scigraph.springernature.com/pub.10.1007/s00249-010-0616-9

12 November 2017

0 references

cites work

Torque generation and elastic power transmission in the rotary F(O)F(1)-ATPase.

1 reference

12 December 2020

Temperature-sensitive reaction intermediate of F1-ATPase.

1 reference

12 December 2020

The ionic track in the F1-ATPase from the thermophilic Bacillus PS3.

1 reference

12 December 2020

Catalysis and rotation of F1 motor: cleavage of ATP at the catalytic site occurs in 1 ms before 40 degree substep rotation

1 reference

12 December 2020

Single-molecule study on the temperature-sensitive reaction of F1-ATPase with a hybrid F1 carrying a single beta(E190D).

1 reference

12 December 2020

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

1 reference

12 December 2020

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

1 reference

12 December 2020

Unique rotary ATP synthase and its biological diversity

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12 December 2020

Thermophilic ATP synthase has a decamer c-ring: indication of noninteger 10:3 H+/ATP ratio and permissive elastic coupling

1 reference

12 December 2020

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

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12 December 2020

Highly coupled ATP synthesis by F1-ATPase single molecules

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12 December 2020

Kinetic modeling of rotary CF0F1-ATP synthase: storage of elastic energy during energy transduction

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12 December 2020

Simple dark-field microscopy with nanometer spatial precision and microsecond temporal resolution.

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12 December 2020

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

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12 December 2020

Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotation

1 reference

12 December 2020

36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase

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12 December 2020

Domain compliance and elastic power transmission in rotary F(O)F(1)-ATPase

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12 December 2020

Activation of pausing F1 motor by external force

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12 December 2020

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

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12 December 2020

Direct observation of the rotation of F1-ATPase

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12 December 2020

Acceleration of the ATP-binding rate of F1-ATPase by forcible forward rotation

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12 December 2020

Coupling of rotation and catalysis in F(1)-ATPase revealed by single-molecule imaging and manipulation.

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12 December 2020

Reverse engineering a protein: the mechanochemistry of ATP synthase

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12 December 2020

Axle-less F1-ATPase rotates in the correct direction

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12 December 2020

F1-ATPase rotates by an asymmetric, sequential mechanism using all three catalytic subunits

1 reference

12 December 2020

10.1007/S00249-010-0616-9

Identifiers

DOI

1 reference

12 November 2017

1 reference

PubMed ID

20549499