(Q73643345)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10753949%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

title

Mutations in single hairpin units of genetically fused subunit c provide support for a rotary catalytic mechanism in F(0)F(1) ATP synthase (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10753949%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

author name string

P C Jones

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10753949%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

J Hermolin

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10753949%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

R H Fillingame

series ordinal

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10753949%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

language of work or name

English

0 references

publication date

1 April 2000

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10753949%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

5 November 2019

published in

1 reference

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5 November 2019

volume

275

1 reference

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5 November 2019

issue

15

1 reference

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5 November 2019

page(s)

11355-11360

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10753949%20AND%20SRC:MED&resulttype=core&format=json

Subunit organization and structure in the F0 sector of Escherichia coli F1F0 ATP synthase

5 November 2019

cites work

1 reference

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Genetic fusions of subunit c in the F0 sector of H+-transporting ATP synthase. Functional dimers and trimers and determination of stoichiometry by cross-linking analysis

21 January 2018

1 reference

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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.275.15.11355

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Intersubunit rotation in active F-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Direct observation of the rotation of F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

The ATP synthase--a splendid molecular machine

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Rotational coupling in the F0F1 ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

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.275.15.11355

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.275.15.11355

Direct observation of the rotation of epsilon subunit in F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Rotation of the epsilon subunit during catalysis by Escherichia coli FOF1-ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

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.275.15.11355

Subunits coupling H+ transport and ATP synthesis in the Escherichia coli ATP synthase. Cys-Cys cross-linking of F1 subunit epsilon to the polar loop of F0 subunit c.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Defining the domain of binding of F1 subunit epsilon with the polar loop of F0 subunit c in the Escherichia coli ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Molecular imaging of Escherichia coli F0F1-ATPase in reconstituted membranes using atomic force microscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Topographical structure of membrane-bound Escherichia coli F1F0 ATP synthase in aqueous buffer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Arrangement of the multicopy H+-translocating subunit c in the membrane sector of the Escherichia coli F1F0 ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

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

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Structure of the subunit c oligomer in the F1Fo ATP synthase: model derived from solution structure of the monomer and cross-linking in the native enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Molecular architecture of the rotary motor in ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

ATP synthase: a tentative structural model

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Energy transduction in ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

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.275.15.11355

Gene duplication as a means for altering H+/ATP ratios during the evolution of FoF1 ATPases and synthases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

The UNC operon nucleotide sequence, regulation and structure of ATP-synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Organization of the F0 sector of Escherichia coli H+-ATPase: the polar loop region of subunit c extends from the cytoplasmic face of the membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Activation of Escherichia coli F1-ATPase by lauryldimethylamine oxide and ethylene glycol: relationship of ATPase activity to the interaction of the epsilon and beta subunits.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

A mutation in the Escherichia coli F0F1-ATP synthase rotor, gammaE208K, perturbs conformational coupling between transport and catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Interactions between the F1 and F0 parts in the Escherichia coli ATP synthase. Associations involving the loop region of C subunits.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

The gammaepsilon-c subunit interface in the ATP synthase of Escherichia coli. cross-linking of the epsilon subunit to the c subunit ring does not impair enzyme function, that of gamma to c subunits leads to uncoupling

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

On the role of Arg-210 and Glu-219 of subunit a in proton translocation by the Escherichia coli F0F1-ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Reconstitution of the Fo complex of Escherichia coli ATP synthase from isolated subunits. Varying the number of essential carboxylates by co-incorporation of wild-type and mutant subunit c after purification in organic solvent.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

Structural changes linked to proton translocation by subunit c of the ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.15.11355

21 January 2018

Identifiers

DOI

10.1074/JBC.275.15.11355

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10753949%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

1 reference