(Q36226177)

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Large conformational changes of the epsilon subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme

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Europe PubMed Central

PMC publication ID

12 August 2017

Large conformational changes of the epsilon subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme (English)

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

author name string

S P Tsunoda

1

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Europe PubMed Central

PMC publication ID

12 August 2017

A J Rodgers

2

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Europe PubMed Central

PMC publication ID

12 August 2017

R Aggeler

3

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

M C Wilce

4

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

M Yoshida

5

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

R A Capaldi

6

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Europe PubMed Central

PMC publication ID

12 August 2017

language of work or name

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publication date

29 May 2001

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Europe PubMed Central

PMC publication ID

12 August 2017

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

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Europe PubMed Central

PMC publication ID

12 August 2017

98

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Europe PubMed Central

PMC publication ID

12 August 2017

12

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

6560-6564

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

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

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Structure of the gamma-epsilon complex of ATP synthase

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Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging

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Coupling H(+) transport to rotary catalysis in F-type ATP synthases: structure and organization of the transmembrane rotary motor

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Molecular architecture of the rotary motor in ATP synthase

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Direct observation of the rotation of epsilon subunit in F1-ATPase

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Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli

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Thermophilic F1-ATPase is activated without dissociation of an endogenous inhibitor, epsilon subunit.

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The ATP synthase--a splendid molecular machine

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Direct observation of the rotation of F1-ATPase

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Nucleotide-dependent movement of the epsilon subunit between alpha and beta subunits in the Escherichia coli F1F0-type ATPase

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

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Identifiers

10.1073/PNAS.111128098

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

2001PNAS...98.6560T

0 references

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

ResearchGate publication ID

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