(Q43015822)

12 November 2017

title

ATP synthase that lacks F0a-subunit: isolation, properties, and indication of F0b2-subunits as an anchor rail of a rotating c-ring (English)

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12 November 2017

Sakurako Ono

1

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12 November 2017

Nobuhito Sone

series ordinal

2

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12 November 2017

Masasuke Yoshida

series ordinal

3

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12 November 2017

Toshiharu Suzuki

series ordinal

4

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12 November 2017

language of work or name

English

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publication date

2 June 2004

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Journal of Biological Chemistry

12 November 2017

published in

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12 November 2017

volume

279

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12 November 2017

issue

32

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12 November 2017

page(s)

33409-33412

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The ATP synthase--a splendid molecular machine

12 November 2017

cites work

1 reference

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21 January 2018

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Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase

21 January 2018

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Mechanism of the F(1)F(0)-type ATP synthase, a biological rotary motor

21 January 2018

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Molecular architecture of the rotary motor in ATP synthase

21 January 2018

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Molecular architecture of the undecameric rotor of a bacterial Na+-ATP synthase

21 January 2018

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The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10.

21 January 2018

1 reference

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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

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Subunit organization of the stator part of the F0 complex from Escherichia coli ATP synthase

21 January 2018

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The second stalk of Escherichia coli ATP synthase

21 January 2018

1 reference

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F(0) of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring

21 January 2018

1 reference

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Interacting helical faces of subunits a and c in the F1Fo ATP synthase of Escherichia coli defined by disulfide cross-linking

21 January 2018

1 reference

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

21 January 2018

1 reference

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Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase

21 January 2018

1 reference

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Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(O) sector of Escherichia coli ATP synthase

21 January 2018

1 reference

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Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase

21 January 2018

1 reference

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Membrane topology of subunit a of the F1F0 ATP synthase as determined by labeling of unique cysteine residues

21 January 2018

1 reference

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Coupling proton movements to c-ring rotation in F(1)F(o) ATP synthase: aqueous access channels and helix rotations at the a-c interface

21 January 2018

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Mechanics of coupling proton movements to c-ring rotation in ATP synthase

21 January 2018

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Insights into the molecular mechanism of rotation in the Fo sector of ATP synthase

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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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

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Direct Interaction of Subunits a and b of the F0 Complex of Escherichia coli ATP Synthase by Forming an ab 2 Subcomplex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404993200

21 January 2018

Identifiers

DOI

10.1074/JBC.M404993200

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12 November 2017

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