(Q38356781)

2 September 2017

title

Nucleotide-dependent movement of the epsilon subunit between alpha and beta subunits in the Escherichia coli F1F0-type ATPase (English)

1 reference

2 September 2017

1 reference

Aggeler R

1

1 reference

2 September 2017

Capaldi RA

series ordinal

2

1 reference

2 September 2017

language of work or name

English

0 references

publication date

1 June 1996

1 reference

Journal of Biological Chemistry

2 September 2017

published in

1 reference

2 September 2017

volume

271

1 reference

2 September 2017

issue

23

1 reference

2 September 2017

page(s)

13888-13891

1 reference

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

2 September 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

Labeling of the ATP synthase of Escherichia coli from the head-group region of the lipid bilayer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

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.271.23.13888

Disulfide bond formation between the COOH-terminal domain of the beta subunits and the gamma and epsilon subunits of the Escherichia coli F1-ATPase. Structural implications and functional consequences.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

Zero-length crosslinking between subunits delta and I of the H(+)-translocating ATPase of chloroplasts

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

Coupling between catalytic sites and the proton channel in F1F0-type ATPases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

Conformational changes in the gamma and epsilon subunits are integral to the functioning of the Escherichia coli H(+)-pumping ATPase (ECF1F0).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

Components of the mitochondrial inner membrane. 3. Characterization of a seventh different subunit of beef heart cytochrome c oxidase. Similarities between the beef heart enzyme and that from other species

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

The stalk connecting the F1 and F0 domains of ATP synthase visualized by electron microscopy of unstained specimens

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

Ligand-dependent structural variations in Escherichia coli F1 ATPase revealed by cryoelectron microscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

Rapid and efficient site-specific mutagenesis without phenotypic selection

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

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.271.23.13888

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.271.23.13888

Asymmetry and structural changes in ECF1 examined by cryoelectronmicroscopy.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

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.271.23.13888

The proton-translocating ATPase of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

The structure of ATP synthase from chloroplasts. Conformational changes of CF1 studied by electron microscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

Cryoelectron microscopy of Escherichia coli F1 adenosinetriphosphatase decorated with monoclonal antibodies to individual subunits of the complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

Molecular architecture of Escherichia coli F1 adenosinetriphosphatase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

Inhibition of the adenosinetriphosphatase activity of Escherichia coli F1 by the water-soluble carbodiimide 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide is due to modification of several carboxyls in the beta subunit

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the .epsilon. subunit in the Escherichia coli adenosinetriphosphatase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.23.13888

21 January 2018

Identifiers

DOI

10.1074/JBC.271.23.13888

1 reference

release_gks2ib4nqfga5ej6jgfdeo6qai

2 September 2017

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/gks2ib4nqfga5ej6jgfdeo6qai

mapped directly with Wikidata item

24 November 2022

based on heuristic

1 reference