Isolated epsilon subunit of thermophilic F1-ATPase binds ATP. (Q43033766)

12 November 2017

title

Isolated epsilon subunit of thermophilic F1-ATPase binds ATP. (English)

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12 November 2017

Yasuyuki Kato-Yamada

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12 November 2017

Masasuke Yoshida

series ordinal

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12 November 2017

language of work or name

English

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publication date

1 July 2003

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Journal of Biological Chemistry

12 November 2017

published in

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12 November 2017

volume

278

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12 November 2017

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12 November 2017

page(s)

36013-36016

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The ATP synthase--a splendid molecular machine

12 November 2017

cites work

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ATP synthase--a marvellous rotary engine of the cell.

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Inhibitory properties of endogenous subunit ϵ in the Escherichia coli F1 ATPase

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Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy

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Crystal structure of the ϵ subunit of the proton-translocating ATP synthase from Escherichia coli

21 January 2018

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

21 January 2018

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Thermophilic F1-ATPase is activated without dissociation of an endogenous inhibitor, epsilon subunit.

21 January 2018

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Epsilon subunit, an endogenous inhibitor of bacterial F(1)-ATPase, also inhibits F(0)F(1)-ATPase

21 January 2018

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Movement of the helical domain of the epsilon subunit is required for the activation of thermophilic F1-ATPase

21 January 2018

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The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution

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Structure of the gamma-epsilon complex of ATP synthase

21 January 2018

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The role of the betaDELSEED motif of F1-ATPase: propagation of the inhibitory effect of the epsilon subunit

21 January 2018

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Large conformational changes of the epsilon subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme

21 January 2018

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The regulatory functions of the gamma and epsilon subunits from chloroplast CF1 are transferred to the core complex, alpha3beta3, from thermophilic bacterial F1.

21 January 2018

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Catalytic properties of Escherichia coli F1-ATPase depleted of endogenous nucleotides.

21 January 2018

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Characterization of the inhibitory (epsilon) subunit of the proton-translocating adenosine triphosphatase from Escherichia coli

21 January 2018

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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

21 January 2018

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The epsilon subunit of the F(1)F(0) complex of Escherichia coli. cross-linking studies show the same structure in situ as when isolated

21 January 2018

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The carboxyl terminus of the epsilon subunit of the chloroplast ATP synthase is exposed during illumination

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M306140200

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12 November 2017

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