Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase (Q27618304)

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The ATP synthase--a splendid molecular machine

21 January 2018

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Direct observation of the rotation of F1-ATPase

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

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

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Arrangement of the multicopy H+-translocating subunit c in the membrane sector of the Escherichia coli F1F0 ATP synthase.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Subunit organization and structure in the F0 sector of Escherichia coli F1F0 ATP synthase

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Topographical structure of membrane-bound Escherichia coli F1F0 ATP synthase in aqueous buffer

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

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

21 January 2018

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ATP synthase: a tentative structural model

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Energy transduction in ATP synthase

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

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.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

The stalk region of the Escherichia coli ATP synthase. Tyrosine 205 of the gamma subunit is in the interface between the F1 and F0 parts and can interact with both the epsilon and c oligomer.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

The UNC operon nucleotide sequence, regulation and structure of ATP-synthase

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

The second stalk composed of the b- and delta-subunits connects F0 to F1 via an alpha-subunit in the Escherichia coli ATP synthase

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

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

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Reconstitution of the Fo complex of Escherichia coli ATP synthase from isolated subunits. Varying the number of essential carboxylates by co-incorporation of wild-type and mutant subunit c after purification in organic solvent.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Generation of impossible cross-peaks between bulk water and biomolecules in solution NMR.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Torsion angle dynamics for NMR structure calculation with the new program DYANA

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

MOLMOL: a program for display and analysis of macromolecular structures

21 January 2018

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Chemical shifts as a tool for structure determination

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

The preference of tryptophan for membrane interfaces.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Characterization and modeling of membrane proteins using sequence analysis

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Architecture of helix bundle membrane proteins: an analysis of cytochrome c oxidase from bovine mitochondria

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

The functions of tryptophan residues in membrane proteins

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Aromatic-aromatic interaction: a mechanism of protein structure stabilization

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Direct indication for the existence of a double stalk in CF 0 F 1 1 1Edited by J. Karn

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Intersubunit rotation in active F-ATPase

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Genetic fusions of subunit c in the F0 sector of H+-transporting ATP synthase. Functional dimers and trimers and determination of stoichiometry by cross-linking analysis

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Energy, Life, and ATP (Nobel Lecture)

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

ATP Synthesis by Rotary Catalysis (Nobel lecture)

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Molecular imaging of Escherichia coli F0F1-ATPase in reconstituted membranes using atomic force microscopy

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

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

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

ATP synthase's second stalk comes into focus

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Structure of the membrane-embedded F0 part of F1F0 ATP synthase from Escherichia coli as inferred from labeling with 3-(Trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

The subunit delta-subunit b domain of the Escherichia coli F1F0 ATPase. The B subunits interact with F1 as a dimer and through the delta subunit

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Formation of the b subunit dimer is necessary for interaction with F1-ATPase

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Characterization of a b2delta complex from Escherichia coli ATP synthase

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Functional effects and cross-reactivity of antibody to purified subunit b (uncF protein) of Escherichia coli proton-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.22.15598

Helix packing in membrane proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.22.15598