(Q38308651)

2 September 2017

title

Second stalk of ATP synthase. Cross-linking of gamma subunit in F1 to truncated Fob subunit prevents ATP hydrolysis (English)

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2 September 2017

Suzuki T

1

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2 September 2017

Suzuki J

2

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2 September 2017

Mitome N

3

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2 September 2017

Ueno H

4

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2 September 2017

Yoshida M

5

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2 September 2017

language of work or name

English

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publication date

1 December 2000

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Journal of Biological Chemistry

2 September 2017

published in

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2 September 2017

volume

275

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2 September 2017

issue

48

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2 September 2017

page(s)

37902-37906

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The ATP synthase--a splendid molecular machine

2 September 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.M007075200

Direct observation of the rotation of F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

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.M007075200

The rotary binding change mechanism of ATP synthases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Electron microscopic evidence of two stalks linking the F1 and F0 parts of the Escherichia coli ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Catalytic mechanism of F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Cross-linking of engineered subunit delta to (alphabeta)3 in chloroplast F-ATPase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Cross-linking of the delta subunit to one of the three alpha subunits has no effect on functioning, as expected if delta is a part of the stator that links the F1 and F0 parts of the Escherichia coli ATP synthase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Localization of the delta subunit in the Escherichia coli F(1)F(0)-ATPsynthase by immuno electron microscopy: the delta subunit binds on top of the F(1).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

The b and delta subunits of the Escherichia coli ATP synthase interact via residues in their C-terminal regions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

The second stalk composed of the b- and delta-subunits connects F0 to F1 via an alpha-subunit in the Escherichia coli ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

The second stalk of Escherichia coli ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Rapid and efficient site-specific mutagenesis without phenotypic selection

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Sequence and over-expression of subunits of adenosine triphosphate synthase in thermophilic bacterium PS3.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Catalytic activity of the alpha3beta3gamma complex of F1-ATPase without noncatalytic nucleotide binding site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Unisite catalysis without rotation of the gamma-epsilon domain in Escherichia coli F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

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.M007075200

Direct indication for the existence of a double stalk in CF 0 F 1 1 1Edited by J. Karn

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Transient accumulation of elastic energy in proton translocating ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

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.M007075200

Direct visualisation of conformational changes in EF(0)F(1) by electron microscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

The subunit delta-subunit b domain of the Escherichia coli F1F0 ATPase. The B subunits interact with F1 as a dimer and through the delta subunit

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Characterization of a b2delta complex from Escherichia coli ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Disulfide linkage of the b and delta subunits does not affect the function of the Escherichia coli ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

The dimerization domain of the b subunit of the Escherichia coli F(1)F(0)-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Deletions in the second stalk of F1F0-ATP synthase in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Lengthening the second stalk of F(1)F(0) ATP synthase in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

Interconversion of high and low adenosinetriphosphatase activity forms of Escherichia coli F1 by the detergent lauryldimethylamine oxide

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M007075200

21 January 2018

Identifiers

DOI

10.1074/JBC.M007075200

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2 September 2017

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