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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 (Q54613743)

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English	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	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7721834

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 (English)

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7721834

Escherichia coli

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author name string

Aggeler R

1

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7721834

Haughton MA

2

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7721834

Capaldi RA

3

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7721834

publication date

1 April 1995

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PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7721834

language of work or name

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Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7721834

270

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PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7721834

16

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7721834

9185-9191

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7721834

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

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Monoclonal antibody modification of the ATPase activity of Escherichia coli F1 ATPase

1 reference

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21 January 2018

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

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Effect of disulfide cross-linking between alpha and delta subunits on the properties of the F1 adenosine triphosphatase of Escherichia coli

1 reference

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21 January 2018

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

1 reference

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21 January 2018

The number of functional catalytic sites on F1-ATPases and the effects of quaternary structural asymmetry on their properties

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Epsilon subunit of Escherichia coli F1-ATPase: effects on affinity for aurovertin and inhibition of product release in unisite ATP hydrolysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.16.9185

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.16.9185

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.16.9185

21 January 2018

Rapid and efficient site-specific mutagenesis without phenotypic selection

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.16.9185

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.16.9185

21 January 2018

Structure-function relationships of domains of the delta subunit in Escherichia coli adenosine triphosphatase

1 reference

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21 January 2018

Column centrifugation generates an intersubunit disulfide bridge in Escherichia coli F1-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.16.9185

21 January 2018

ATP binding causes a conformational change in the gamma subunit of the Escherichia coli F1ATPase which is reversed on bond cleavage

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.16.9185

21 January 2018

Asymmetry and structural changes in ECF1 examined by cryoelectronmicroscopy

1 reference

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21 January 2018

A cryoelectron microscopy study of the interaction of the Escherichia coli F1-ATPase with subunit b dimer

1 reference

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21 January 2018

The proton-translocating ATPase of Escherichia coli

1 reference

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21 January 2018

Removal of the epsilon subunit from Escherichia coli F1-ATPase using monoclonal anti-epsilon antibody affinity chromatography

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.16.9185

21 January 2018

Molecular architecture of Escherichia coli F1 adenosinetriphosphatase

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Structural asymmetry of the F1 of Escherichiacoli as indicated by reaction with dicyclohexylcarbodiimide

1 reference

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21 January 2018

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

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Identifiers

10.1074/JBC.270.16.9185

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7721834

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7721834

ResearchGate publication ID

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