H+ transport and coupling by the F0 sector of the ATP synthase: insights into the molecular mechanism of function (Q35235377)

7 August 2017

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title

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

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7 August 2017

R. H. Fillingame

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1331039

14 September 2022

language of work or name

English

1 reference

National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=1331039

14 September 2022

publication date

1 October 1992

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Journal of Bioenergetics and Biomembranes

7 August 2017

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7 August 2017

24

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7 August 2017

5

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7 August 2017

485-491

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https://scigraph.springernature.com/pub.10.1007/bf00762366

7 August 2017

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cites work

Subunit interactions within the chloroplast ATP synthase (CF0-CF1) as deduced by specific depletion of CF0 polypeptides

1 reference

12 December 2020

Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit.

1 reference

12 December 2020

H+-ATPase activity of Escherichia coli F1F0 is blocked after reaction of dicyclohexylcarbodiimide with a single proteolipid (subunit c) of the F0 complex.

1 reference

12 December 2020

The mechanism and regulation of ATP synthesis by F1-ATPases

1 reference

12 December 2020

Deletions in hydrophilic domains of subunit a from the Escherichia coli F1F0-ATP synthase interfere with membrane insertion or F0 assembly

1 reference

12 December 2020

Mutations in three of the putative transmembrane helices of subunit a of the Escherichia coli F1F0-ATPase disrupt ATP-driven proton translocation.

1 reference

12 December 2020

The essential carboxyl group in subunit c of the F1F0 ATP synthase can be moved and H(+)-translocating function retained

1 reference

12 December 2020

Topology, organization, and function of the psi subunit in the F0 sector of the H+-ATPase of Escherichia coli

1 reference

12 December 2020

Cross-linking and labeling of the Escherichia coli F1F0-ATP synthase reveal a compact hydrophilic portion of F0 close to an F1 catalytic subunit

1 reference

12 December 2020

A topological analysis of subunit alpha from Escherichia coli F1F0-ATP synthase predicts eight transmembrane segments

1 reference

12 December 2020

Conserved polar loop region of Escherichia coli subunit c of the F1F0 H+-ATPase. Glutamine 42 is not absolutely essential, but substitutions alter binding and coupling of F1 to F0.

1 reference

12 December 2020

The sodium ion translocating adenosinetriphosphatase of Propionigenium modestum pumps protons at low sodium ion concentrations

1 reference

12 December 2020

Mutation of alanine 24 to serine in subunit c of the Escherichia coli F1F0-ATP synthase reduces reactivity of aspartyl 61 with dicyclohexylcarbodiimide

1 reference

12 December 2020

Topological studies suggest that the pathway of the protons through F0 is provided by amino acid residues accessible from the lipid phase

1 reference

12 December 2020

The polar domain of the b subunit of Escherichia coli F1F0-ATPase forms an elongated dimer that interacts with the F1 sector

1 reference

12 December 2020

The transmembrane topology of the a [corrected] subunit from the ATPase in Escherichia coli analyzed by PhoA protein fusions

1 reference

12 December 2020

Mutational analysis of the function of the a-subunit of the F0F1-APPase of Escherichia coli

1 reference

12 December 2020

Stoichiometry of subunits in the H+-ATPase complex of Escherichia coli.

1 reference

12 December 2020

Essential residues in the polar loop region of subunit c of Escherichia coli F1F0 ATP synthase defined by random oligonucleotide-primed mutagenesis

1 reference

12 December 2020

Mutations in the conserved proline 43 residue of the uncE protein (subunit c) of Escherichia coli F1F0-ATPase alter the coupling of F1 to F0.

1 reference

12 December 2020

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

1 reference

12 December 2020

H+-ATPase of Escherichia coli. An uncE mutation impairing coupling between F1 and Fo but not Fo-mediated H+ translocation.

1 reference

12 December 2020

ATP synthesis by oxidative phosphorylation

1 reference

12 December 2020

The Proton-Translocating Pumps of Oxidative Phosphorylation

1 reference

12 December 2020

The proton pore in the Escherichia coli F0F1-ATPase: a requirement for arginine at position 210 of the a-subunit

1 reference

12 December 2020

Identifiers

DOI

10.1007/BF00762366

1 reference

release_woynkzp25bb3jbfiy5j4ztljhq

7 August 2017

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/woynkzp25bb3jbfiy5j4ztljhq

24 November 2022

mapped directly with Wikidata item

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