The role of the stalk in the coupling mechanism of F1F0-ATPases (Q40764078)

23 September 2017

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title

The role of the stalk in the coupling mechanism of F1F0-ATPases (English)

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ORCID Public Data File 2021

23 September 2017

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author name string

Walker JE

series ordinal

1

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PubMed ID

8206156

23 September 2017

Collinson IR

series ordinal

2

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PubMed ID

8206156

23 September 2017

language of work or name

English

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publication date

1 June 1994

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23 September 2017

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23 September 2017

346

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23 September 2017

1

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23 September 2017

39-43

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The stalk connecting the F1 and F0 domains of ATP synthase visualized by electron microscopy of unstained specimens

23 September 2017

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ATP synthesis in mitochondria

21 January 2018

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

21 January 2018

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

21 January 2018

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Chemiosmotic coupling in oxidative and photosynthetic phosphorylation

21 January 2018

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Structural aspects of proton-pumping ATPases

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The atp operon: nucleotide sequence of the promoter and the genes for the membrane proteins, and the delta subunit of Escherichia coli ATP-synthase

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E. coli F1-ATPase interacts with a membrane protein component of a proton channel

21 January 2018

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Subunit b of the membrane moiety (F0) of ATP synthase (F1F0) from Escherichia coli is indispensable for H+ translocation and binding of the water-soluble F1 moiety

21 January 2018

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Added subunit beta of CF1 as well as gamma/delta/epsilon restore photophosphorylation in partially CF1-depleted thylakoids

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Asymmetry and structural changes in ECF1 examined by cryoelectronmicroscopy.

21 January 2018

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Amino acid sequence of bovine heart coupling factor 6

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Molecular cloning of cDNA for the import precursor of human coupling factor 6 of H(+)-ATP synthase in mitochondria

21 January 2018

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ATP synthase from bovine mitochondria. The characterization and sequence analysis of two membrane-associated sub-units and of the corresponding cDNAs.

21 January 2018

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cDNA cloning and sequencing for the import precursor of subunit B in H(+)-ATP synthase from rat mitochondria

21 January 2018

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Subunit 4 of ATP synthase (F0F1) from yeast mitochondria. Purification, amino-acid composition and partial N-terminal sequence

21 January 2018

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Molecular cloning of cDNA for the import precursor of human subunit B of H(+)-ATP synthase in mitochondria

21 January 2018

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cDNA cloning for and preparation of antibodies against subunit d of H(+)-ATP synthase in rat mitochondria

21 January 2018

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Stoichiometry of the oligomycin-sensitivity-conferring protein (OSCP) in the mitochondrial F0F1-ATPase determined by an immunoelectrotransfer blot technique

21 January 2018

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Role of the carboxyl-terminal region of the PVP protein (F0I subunit) in the H+ conduction of F0F1 H+-ATP synthase of bovine heart mitochondria

21 January 2018

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Complete amino acid sequence of subunit e of rat liver mitochondrial H(+)-ATP synthase

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Possible functions of chains of catalysts

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Organization and sequences of genes for the subunits of ATP synthase in the thermophilic cyanobacterium Synechococcus 6716.

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Interactions between the oligomycin sensitivity conferring protein (OSCP) and beef heart mitochondrial F1-ATPase. 1. Study of the binding parameters with a chemically radiolabeled OSCP

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11 October 2022

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Cell-membrane ultrastructure. Low-temperature electron microsopy and x-ray diffraction studies of lipoprotein components in lamellar systems

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11 October 2022

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Studies on the mitochondrial adenosine triphosphatase system. IV. Purification and characterization of the oligomycin sensitivity conferring protein

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11 October 2022

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Cross-linking of bovine mitochondrial H+-ATPase by copper--o-phenanthroline. Interaction of the oligomycin-sensitivity-conferring protein with a 24-kDa protein

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11 October 2022

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ATP synthesis by oxidative phosphorylation

1 reference

11 October 2022

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Identifiers

DOI

10.1016/0014-5793(94)00368-8

1 reference

23 September 2017

1 reference

PubMed ID

8206156