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 (Q37578098)

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scientific article published on December 1984

Language	Label	Description	Also known as
English	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	scientific article published on December 1984

Statements

scholarly article

1 reference

Europe PubMed Central

21 August 2017

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 (English)

1 reference

Europe PubMed Central

21 August 2017

Escherichia coli

1 reference

based on heuristic

inferred from title

author name string

Schneider E

1

1 reference

Europe PubMed Central

21 August 2017

Altendorf K

2

1 reference

Europe PubMed Central

21 August 2017

language of work or name

0 references

publication date

1 December 1984

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Europe PubMed Central

21 August 2017

Proceedings of the National Academy of Sciences of the United States of America

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Europe PubMed Central

21 August 2017

81

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Europe PubMed Central

21 August 2017

23

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Europe PubMed Central

21 August 2017

7279-7283

1 reference

Europe PubMed Central

21 August 2017

Delipidation of bacteriorhodopsin and reconstitution with exogenous phospholipid.

1 reference

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Purification and properties of reconstitutively active and inactive adenosinetriphosphatase from Escherichia coli

1 reference

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23 August 2017

Purification of the carbodiimide-reactive protein component of the ATP energy-transducing system of Escherichia coli

1 reference

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23 August 2017

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

1 reference

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14 September 2017

Structure and function of proton-translocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches

1 reference

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The proton-ATPase of bacteria and mitochondria

1 reference

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Purification of the DCCD-reactive protein of the energy-transducing adenosine triphosphatase complex fromEscherichia coli

1 reference

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14 September 2017

Identification of the DCCD-reactive protein of the energy transducing adenosinetriphosphatase complex fromEscherichia coli

1 reference

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6 Analysis of products of mitochondrial protein synthesis in yeast: Genetic and biochemical aspects

1 reference

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28 September 2017

Membrane integration and function of the three F0 subunits of the ATP synthase of Escherichia coli K12.

1 reference

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28 September 2017

The topology of the proton translocating F0 component of the ATP synthase from E. coli K12: studies with proteases

1 reference

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

1 reference

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25 June 2018

The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit δ of the membrane bound ATP synthase of Escherichia coli

1 reference

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25 June 2018

Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from : Prediction of the primary structure of F0 subunits

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392129

25 June 2018

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

1 reference

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25 June 2018

Conformational change of the α subunit of Escherichia coli F1 ATPase: ATP changes the trypsin sensitivity of the subunit

1 reference

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1 September 2018

Amino acid replacement in dicyclohexylcarbodiimide-reactive proteins from mutant strains of Escherichia coli defective in the energy-transducing ATPase complex

1 reference

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12 December 2020

based on heuristic

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Reconstitution of the purified proton conductor (F0) of the adenosine triphosphatase complex from Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/6209711

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The proteolipid subunit of the chloroplast adenosine triphosphatase complex. Reconstitution and demonstration of proton-conductive properties

1 reference

https://pubmed.ncbi.nlm.nih.gov/6209711

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The isolated of F0ofescherichia coliATP-synthase is reconstitutively active in H+-conduction and ATP-dependent energy-transduction

1 reference

https://pubmed.ncbi.nlm.nih.gov/6209711

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

ATP-synthetase complex (F1F0) from Escherichia coli. Purification and characterization of subunits A and B of the F0 part

1 reference

https://pubmed.ncbi.nlm.nih.gov/6209711

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

ATP Synthetase (F1F0) of Escherichia coli K-12. High-Yield Preparation of Functional F0 by Hydrophobic Affinity Chromatography

1 reference

https://pubmed.ncbi.nlm.nih.gov/6209711

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

An Asp—Asn substitution in the proteolipid subnit of the ATP‐synthase from Escherichia coli leads to a non‐functional proton channel

1 reference

https://pubmed.ncbi.nlm.nih.gov/6209711

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Integration of F1 and the membrane sector of the proton-ATPase of Escherichia coli. Role of subunit “b” (uncF protein)

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/6209711

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

https://pubmed.ncbi.nlm.nih.gov/6209711

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Chemical modification of the F0 part of the ATP synthase (F1F0) from Escherichia coli. Effects on proton conduction and F1 binding

1 reference

https://pubmed.ncbi.nlm.nih.gov/6209711

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.81.23.7279

1 reference

Europe PubMed Central

21 August 2017

1984PNAS...81.7279S

0 references

1 reference

Europe PubMed Central

21 August 2017

1 reference

Europe PubMed Central

21 August 2017

ResearchGate publication ID

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