(Q41699446)

7 October 2017

title

Structure of the vacuolar ATPase by electron microscopy (English)

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7 October 2017

S Wilkens

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7 October 2017

E Vasilyeva

series ordinal

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7 October 2017

M Forgac

series ordinal

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7 October 2017

language of work or name

English

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publication date

1 November 1999

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Journal of Biological Chemistry

7 October 2017

published in

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7 October 2017

volume

274

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7 October 2017

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7 October 2017

page(s)

31804-31810

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Structure, function and regulation of the vacuolar (H+)-ATPase

7 October 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

The vacuolar H+-ATPase: a universal proton pump of eukaryotes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

Evolution of the vacuolar H+-ATPase: implications for the origin of eukaryotes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

The evolution of H+-ATPases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

Subunit composition and ATP site labeling of the coated vesicle proton-translocating adenosinetriphosphatase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

A new generation of the IMAGIC image processing system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

Visualization of a peripheral stalk in V-type ATPase: evidence for the stator structure essential to rotational catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

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.274.45.31804

The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

Site-directed mutagenesis of the 100-kDa subunit (Vph1p) of the yeast vacuolar (H+)-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

The first putative transmembrane helix of the 16 kDa proteolipid lines a pore in the Vo sector of the vacuolar H(+)-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

Molecular characterization of the 50- and 57-kDa subunits of the bovine vacuolar proton pump

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

Structural changes in the gamma and epsilon subunits of the Escherichia coli F1F0-type ATPase during energy coupling

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

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

21 January 2018

1 reference

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ATP synthase: an electrochemical ransducer with rotatory mechanics

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

Rotation of the gamma subunit in F1-ATPase; evidence that ATP synthase is a rotary motor enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

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.274.45.31804

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.274.45.31804

Structure of the ATP synthase complex (ECF1F0) of Escherichia coli from cryoelectron microscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.45.31804

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.274.45.31804

21 January 2018

Identifiers

DOI

10.1074/JBC.274.45.31804

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7 October 2017

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