(Q32050424)

5 July 2017

Direct observation of the rotation of epsilon subunit in F1-ATPase (English)

1 reference

5 July 2017

Kato-Yamada Y

1

1 reference

5 July 2017

Noji H

2

1 reference

5 July 2017

Yasuda R

3

1 reference

5 July 2017

Kinosita K Jr

4

1 reference

5 July 2017

Yoshida M

5

1 reference

5 July 2017

language of work or name

English

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publication date

1 July 1998

1 reference

Journal of Biological Chemistry

5 July 2017

1 reference

5 July 2017

273

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5 July 2017

19375-19377

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5 July 2017

31

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ATP synthase (H+-ATPase): results by combined biochemical and molecular biological approaches

5 July 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

The ATP synthase--a splendid molecular machine

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

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/10.1074%2FJBC.273.31.19375

Structural asymmetry of F1-ATPase caused by the gamma subunit generates a high affinity nucleotide binding site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

ATP hydrolysis by membrane-bound Escherichia coli F0F1 causes rotation of the gamma subunit relative to the beta subunits

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

Direct observation of the rotation of F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

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/10.1074%2FJBC.273.31.19375

Purification of membrane attachment and inhibitory subunits of the proton translocating adenosine triphosphatase from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

The regulatory functions of the gamma and epsilon subunits from chloroplast CF1 are transferred to the core complex, alpha3beta3, from thermophilic bacterial F1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

Epsilon-binding regions of the gamma subunit of Escherichia coli ATP synthase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

Rotation of a gamma-epsilon subunit domain in the Escherichia coli F1F0-ATP synthase complex. The gamma-epsilon subunits are essentially randomly distributed relative to the alpha3beta3delta domain in the intact complex.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

Arrangement of the epsilon subunit in the Escherichia coli ATP synthase from the reactivity of cysteine residues introduced at different positions in this subunit.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

The force exerted by a single kinesin molecule against a viscous load

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

Introduction of reactive cysteine residues in the epsilon subunit of Escherichia coli F1 ATPase, modification of these sites with tetrafluorophenyl azide-maleimides, and examination of changes in the binding of the epsilon subunit when different nuc

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

The stalk region of the Escherichia coli ATP synthase. Tyrosine 205 of the gamma subunit is in the interface between the F1 and F0 parts and can interact with both the epsilon and c oligomer.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

Intersubunit rotation in active F-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

Characterization of the interface between gamma and epsilon subunits of Escherichia coli F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

Cross-linking of chloroplast F0F1-ATPase subunit epsilon to gamma without effect on activity. Epsilon and gamma are parts of the rotor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.31.19375

21 January 2018

Identifiers

DOI

10.1074/JBC.273.31.19375

1 reference

5 July 2017

1 reference