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The trapping of different conformations of the Escherichia coli F1 ATPase by disulfide bond formation. Effect on nucleotide binding affinities of the catalytic sites (Q71859967)

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scientific article published on 01 December 1996

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English	The trapping of different conformations of the Escherichia coli F1 ATPase by disulfide bond formation. Effect on nucleotide binding affinities of the catalytic sites	scientific article published on 01 December 1996

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8955091%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

The trapping of different conformations of the Escherichia coli F1 ATPase by disulfide bond formation. Effect on nucleotide binding affinities of the catalytic sites (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8955091%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

Escherichia coli

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G Grüber

1

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21 October 2019

R A Capaldi

2

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21 October 2019

publication date

1 December 1996

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21 October 2019

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Journal of Biological Chemistry

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21 October 2019

271

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21 October 2019

51

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21 October 2019

32623-32628

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21 October 2019

Molecular architecture of Escherichia coli F1 adenosinetriphosphatase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

Nucleotide-dependent and dicyclohexylcarbodiimide-sensitive conformational changes in the .epsilon. subunit of Escherichia coli ATP synthase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

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

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

Characterization of the interface between gamma and epsilon subunits of Escherichia coli F1-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

Arrangement of the epsilon subunit in the Escherichia coli ATP synthase from the reactivity of cysteine residues introduced at different positions in this subunit

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

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.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

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.271.51.32623

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

ATP hydrolysis by membrane-bound Escherichia coli F0F1 causes rotation of the gamma subunit relative to the beta subunits

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

Intersubunit rotation in active F-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

F1-ATPase in a spin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

Asymmetry of Escherichia coli F1-ATPase as a Function of the Interaction of α-β Subunit Pairs with the γ and ∊ Subunits

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

Differentiation of catalytic sites on Escherichia coli F1ATPase by laser photoactivated labeling with [3H]-2-Azido-ATP using the mutant beta Glu381Cys:epsilonSer108Cys to identify different beta subunits by their interactions with gamma and epsilon

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

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

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

Functional sites in F1-ATPases: location and interactions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.51.32623

21 January 2018

Catalytic properties of the Escherichia coli proton adenosinetriphosphatase: evidence that nucleotide bound at noncatalytic sites is not involved in regulation of oxidative phosphorylation

1 reference

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21 January 2018

Identifiers

10.1074/JBC.271.51.32623

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8955091%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8955091%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

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