The gamma subunit in the Escherichia coli ATP synthase complex (ECF1F0) extends through the stalk and contacts the c subunits of the F0 part (Q71940795)

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scientific article published on 01 July 1995

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English	The gamma subunit in the Escherichia coli ATP synthase complex (ECF1F0) extends through the stalk and contacts the c subunits of the F0 part	scientific article published on 01 July 1995

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22 October 2019

The gamma subunit in the Escherichia coli ATP synthase complex (ECF1F0) extends through the stalk and contacts the c subunits of the F0 part (English)

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22 October 2019

Escherichia coli

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2

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22 October 2019

author name string

Watts SD

1

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22 October 2019

Fillingame RH

3

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22 October 2019

Capaldi RA

4

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publication date

1 July 1995

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22 October 2019

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4

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22 October 2019

368

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22 October 2019

2

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22 October 2019

235-238

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22 October 2019

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

1 reference

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The proton-translocating ATPase of Escherichia coli

1 reference

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

1 reference

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Molecular architecture of Escherichia coli F1 adenosinetriphosphatase

1 reference

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

1 reference

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

1 reference

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

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H+ transport and coupling by the F0 sector of the ATP synthase: insights into the molecular mechanism of function

1 reference

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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.

1 reference

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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

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Activation and inhibition of the Escherichia coli F1-ATPase by monoclonal antibodies which recognize the epsilon subunit

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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

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

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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

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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

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Structure-function relationships of the Escherichia coli ATP synthase probed by trypsin digestion.

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21 January 2018

Identification of Amino-Acid Substitutions in the Proteolipid Subunit of the ATP Synthase from Dicyclohexylcarbodiimide-Resistant Mutants of Escherichia coli

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21 January 2018

The atp operon: nucleotide sequence of the genes for the γ, β, and ε subunits of Escherichia coli ATP synthase

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Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase

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Identifiers

10.1016/0014-5793(95)00658-V

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7628612%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7628612%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

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