Activation and stiffness of the inhibited states of F1-ATPase probed by single-molecule manipulation. (Q40101560)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20154086%20AND%20SRC:MED&resulttype=core&format=json

18 January 2020

title

Activation and stiffness of the inhibited states of F1-ATPase probed by single-molecule manipulation (English)

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18 January 2020

2

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18 January 2020

author name string

Ei-ichiro Saita

1

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18 January 2020

Toshiharu Suzuki

3

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18 January 2020

Boris A Feniouk

4

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18 January 2020

Kazuhiko Kinosita

5

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18 January 2020

Masasuke Yoshida

6

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18 January 2020

language of work or name

English

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publication date

12 February 2010

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Journal of Biological Chemistry

18 January 2020

published in

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18 January 2020

volume

285

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18 January 2020

issue

15

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18 January 2020

page(s)

11411-11417

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Essentials for ATP synthesis by F1F0 ATP synthases

18 January 2020

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Structures of the thermophilic F1-ATPase subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1

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The regulator of the F1 motor: inhibition of rotation of cyanobacterial F1-ATPase by the epsilon subunit.

22 September 2017

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Microsecond time scale rotation measurements of single F1-ATPase molecules

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22 September 2017

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Pause and rotation of F(1)-ATPase during catalysis

22 September 2017

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ATP synthase--a marvellous rotary engine of the cell.

22 September 2017

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Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase

22 September 2017

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Purine but not pyrimidine nucleotides support rotation of F(1)-ATPase.

22 September 2017

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Structure of the gamma-epsilon complex of ATP synthase

22 September 2017

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Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex

22 September 2017

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

22 September 2017

1 reference

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

22 September 2017

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

22 September 2017

1 reference

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Direct observation of the rotation of F1-ATPase

22 September 2017

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The H+/ATP coupling ratio of the ATP synthase from thiol-modulated chloroplasts and two cyanobacterial strains is four

22 September 2017

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

22 September 2017

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

22 September 2017

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Mechanism of inhibition by C-terminal alpha-helices of the epsilon subunit of Escherichia coli FoF1-ATP synthase.

22 September 2017

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Cross-linking of two beta subunits in the closed conformation in F1-ATPase

17 June 2018

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The critical electric potential difference for photophosphorylation. Its relation to the chemiosmotic hypothesis and to the triggering requirements of the ATPase system

17 June 2018

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Effect of epsilon subunit on the rotation of thermophilic Bacillus F1-ATPase

17 June 2018

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Role of the epsilon subunit of thermophilic F1-ATPase as a sensor for ATP.

20 August 2018

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Coupling of rotation and catalysis in F(1)-ATPase revealed by single-molecule imaging and manipulation.

20 August 2018

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Chemical modification of mono-cysteine mutants allows a more global look at conformations of the epsilon subunit of the ATP synthase from Escherichia coli.

20 August 2018

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Regulatory interplay between proton motive force, ADP, phosphate, and subunit epsilon in bacterial ATP synthase

20 August 2018

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Probing conformations of the beta subunit of F0F1-ATP synthase in catalysis

20 August 2018

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Stochastic high-speed rotation of Escherichia coli ATP synthase F1 sector: the epsilon subunit-sensitive rotation

20 August 2018

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20 August 2018

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Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase

20 August 2018

1 reference

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Highly coupled ATP synthesis by F1-ATPase single molecules

20 August 2018

1 reference

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The characteristics of the (alpha V371C)3(beta R337C)3 gamma double mutant subcomplex of the TF1-ATPase indicate that the catalytic site at the alpha TP-beta TP interface with bound MgADP in crystal structures of MF1 represents a catalytic site cont

20 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2857019

Rotor/Stator interactions of the epsilon subunit in Escherichia coli ATP synthase and implications for enzyme regulation.

20 August 2018

1 reference

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Proton-powered subunit rotation in single membrane-bound F0F1-ATP synthase.

20 August 2018

1 reference

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F0F1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of epsilon subunit in response to proton motive force and ADP/ATP balance

20 August 2018

1 reference

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Isolated epsilon subunit of thermophilic F1-ATPase binds ATP.

20 August 2018

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The role of the betaDELSEED motif of F1-ATPase: propagation of the inhibitory effect of the epsilon subunit

20 August 2018

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Movement of the helical domain of the epsilon subunit is required for the activation of thermophilic F1-ATPase

20 August 2018

1 reference

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Epsilon subunit, an endogenous inhibitor of bacterial F(1)-ATPase, also inhibits F(0)F(1)-ATPase

20 August 2018

1 reference

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Slow binding of ATP to noncatalytic nucleotide binding sites which accelerates catalysis is responsible for apparent negative cooperativity exhibited by the bovine mitochondrial F1-ATPase.

20 August 2018

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Powering the flagellar motor of Escherichia coli with an external voltage source

20 August 2018

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Crossref

https://api.crossref.org/works/10.1074%2FJBC.M109.099143

The activity of the ATP synthase from Escherichia coli is regulated by the transmembrane proton motive force

21 January 2018

1 reference

12 December 2020

Effects of P 1 and ADP on ATPase activity in chloroplasts

1 reference

12 December 2020

Interactions of inorganic phosphate with spinach coupling factor 1. Effects on ATPase and ADP binding activities

1 reference

12 December 2020

Tightly bound adenosine diphosphate, which inhibits the activity of mitochondrial F1-ATPase, is located at the catalytic site of the enzyme

1 reference

12 December 2020

Activation of the H(+)-ATP synthase in the photosynthetic bacterium Rhodobacter capsulatus

1 reference

12 December 2020

Rotation of the epsilon subunit during catalysis by Escherichia coli FOF1-ATP synthase

1 reference

12 December 2020

F1-ATPase rotates by an asymmetric, sequential mechanism using all three catalytic subunits

1 reference

12 December 2020

Effect of the epsilon-subunit on nucleotide binding to Escherichia coli F1-ATPase catalytic sites

1 reference

12 December 2020

Energy-linked binding of Pi is required for continuous steady-state proton-translocating ATP hydrolysis catalyzed by F0.F1 ATP synthase

1 reference

12 December 2020

Identifiers

DOI

10.1074/JBC.M109.099143

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20154086%20AND%20SRC:MED&resulttype=core&format=json

18 January 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20154086%20AND%20SRC:MED&resulttype=core&format=json

18 January 2020

PubMed publication ID

20154086

1 reference