(Q44548841)

English

Interacting helical surfaces of the transmembrane segments of subunits a and c' of the yeast V-ATPase defined by disulfide-mediated cross-linking

scientific article published on 12 August 2003

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scholarly article

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Europe PubMed Central

4 December 2017

Interacting helical surfaces of the transmembrane segments of subunits a and c' of the yeast V-ATPase defined by disulfide-mediated cross-linking (English)

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Europe PubMed Central

4 December 2017

transmembrane protein

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author name string

Shoko Kawasaki-Nishi

1

1 reference

Europe PubMed Central

4 December 2017

Tsuyoshi Nishi

2

1 reference

Europe PubMed Central

4 December 2017

Michael Forgac

3

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Europe PubMed Central

4 December 2017

language of work or name

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publication date

12 August 2003

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Europe PubMed Central

4 December 2017

Journal of Biological Chemistry

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Europe PubMed Central

4 December 2017

278

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Europe PubMed Central

4 December 2017

43

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Europe PubMed Central

4 December 2017

41908-41913

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Europe PubMed Central

4 December 2017

The vacuolar (H+)-ATPases--nature's most versatile proton pumps

1 reference

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21 January 2018

Structure and properties of the vacuolar (H+)-ATPases

1 reference

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21 January 2018

Atp6i-deficient mice exhibit severe osteopetrosis due to loss of osteoclast-mediated extracellular acidification.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Subunit interactions in the clathrin-coated vesicle vacuolar (H(+))-ATPase complex.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

cDNA sequence encoding the 16-kDa proteolipid of chromaffin granules implies gene duplication in the evolution of H+-ATPases

1 reference

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21 January 2018

VMA11 and VMA16 encode second and third proteolipid subunits of the Saccharomyces cerevisiae vacuolar membrane H+-ATPase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

The rotary binding change mechanism of ATP synthases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Synthase (H(+) ATPase): coupling between catalysis, mechanical work, and proton translocation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Direct observation of the rotation of F1-ATPase

1 reference

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21 January 2018

Molecular architecture of the rotary motor in ATP synthase

1 reference

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21 January 2018

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

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(O) sector of Escherichia coli ATP synthase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

The b and delta subunits of the Escherichia coli ATP synthase interact via residues in their C-terminal regions.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Visualization of a peripheral stalk in V-type ATPase: evidence for the stator structure essential to rotational catalysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Structure of the vacuolar ATPase by electron microscopy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Cysteine-directed cross-linking to subunit B suggests that subunit E forms part of the peripheral stalk of the vacuolar H+-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Localization of subunits D, E, and G in the yeast V-ATPase complex using cysteine-mediated cross-linking to subunit B.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Evidence for rotation of V1-ATPase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Subunit rotation of vacuolar-type proton pumping ATPase: relative rotation of the G and C subunits

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Rotation of the proteolipid ring in the V-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Improved method for high efficiency transformation of intact yeast cells

1 reference

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21 January 2018

Assembly of the yeast vacuolar H+-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Interacting helical faces of subunits a and c in the F1Fo ATP synthase of Escherichia coli defined by disulfide cross-linking

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

The first putative transmembrane segment of subunit c" (Vma16p) of the yeast V-ATPase is not necessary for function

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Mutational analysis of the catalytic subunit of the yeast vacuolar proton-translocating ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Mutational analysis of yeast vacuolar H(+)-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Expression and localization of the mouse homologue of the yeast V-ATPase 21-kDa Subunit c" (Vma16p).

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Helical interactions and membrane disposition of the 16-kDa proteolipid subunit of the vacuolar H(+)-ATPase analyzed by cysteine replacement mutagenesis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Structural biology. Proton-powered turbine of a plant motor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Molecular architecture of the undecameric rotor of a bacterial Na+-ATP synthase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Three-dimensional structure of the vacuolar ATPase proton channel by electron microscopy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Gene duplication as a means for altering H+/ATP ratios during the evolution of FoF1 ATPases and synthases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Site-directed mutagenesis of the 100-kDa subunit (Vph1p) of the yeast vacuolar (H+)-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Mutagenic analysis of the F0 stator subunits

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Mutations in subunit C of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Coupling proton movements to c-ring rotation in F(1)F(o) ATP synthase: aqueous access channels and helix rotations at the a-c interface

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Structural changes linked to proton translocation by subunit c of the ATP synthase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Intersubunit rotation in active F-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308026200

21 January 2018

Identifiers

10.1074/JBC.M308026200

1 reference

Europe PubMed Central

4 December 2017

1 reference

Europe PubMed Central

4 December 2017

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