Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging (Q35155735)

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

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instance of

scholarly article

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Europe PubMed Central

PubMed publication ID

10840052

retrieved

6 August 2017

title

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

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stated in

Europe PubMed Central

PubMed publication ID

10840052

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6 August 2017

main subject

visualization

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author name string

K Adachi

series ordinal

1

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Europe PubMed Central

PubMed publication ID

10840052

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6 August 2017

R Yasuda

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2

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Europe PubMed Central

PubMed publication ID

10840052

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6 August 2017

H Noji

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3

1 reference

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Europe PubMed Central

PubMed publication ID

10840052

retrieved

6 August 2017

H Itoh

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4

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Europe PubMed Central

PubMed publication ID

10840052

retrieved

6 August 2017

Y Harada

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5

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stated in

Europe PubMed Central

PubMed publication ID

10840052

retrieved

6 August 2017

M Yoshida

series ordinal

6

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10840052

retrieved

6 August 2017

K Kinosita

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7

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stated in

Europe PubMed Central

PubMed publication ID

10840052

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6 August 2017

language of work or name

English

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publication date

1 June 2000

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Europe PubMed Central

PubMed publication ID

10840052

retrieved

6 August 2017

published in

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

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stated in

Europe PubMed Central

PubMed publication ID

10840052

retrieved

6 August 2017

volume

97

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stated in

Europe PubMed Central

PubMed publication ID

10840052

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6 August 2017

issue

13

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Europe PubMed Central

PubMed publication ID

10840052

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6 August 2017

page(s)

7243-7247

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Europe PubMed Central

PubMed publication ID

10840052

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6 August 2017

cites work

F1-ATPase: a highly efficient rotary ATP machine

1 reference

stated in

PubMed Central

reference URL

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13 July 2018

A rotary molecular motor that can work at near 100% efficiency

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PubMed Central

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13 July 2018

Real time imaging of rotating molecular machines

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PubMed Central

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13 July 2018

Single-fluorophore imaging with an unmodified epifluorescence microscope and conventional video camera

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PubMed Central

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13 July 2018

Energy transduction in the F1 motor of ATP synthase

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13 July 2018

F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps

1 reference

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PubMed Central

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Myosin conformational states determined by single fluorophore polarization

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The ATP synthase--a splendid molecular machine

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13 July 2018

Rotation of a gamma-epsilon subunit domain in the Escherichia coli F1F0-ATP synthase complex. The gamma-epsilon subunits are essentially randomly distributed relative to the alpha3beta3delta domain in the intact complex.

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13 July 2018

Axial rotation of sliding actin filaments revealed by single-fluorophore imaging

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13 July 2018

Direct observation of the rotation of F1-ATPase

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13 July 2018

ATP hydrolysis by membrane-bound Escherichia coli F0F1 causes rotation of the gamma subunit relative to the beta subunits

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13 July 2018

Real time imaging of single fluorophores on moving actin with an epifluorescence microscope

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

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

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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Catalytic activity of the alpha3beta3gamma complex of F1-ATPase without noncatalytic nucleotide binding site

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Analysis of time-dependent change of Escherichia coli Fl-ATPase activity and its relationship with apparent negative cooperativity

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Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution

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Intersubunit rotation in active F-ATPase

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Three-stepped rotation of subunits gamma and epsilon in single molecules of F-ATPase as revealed by polarized, confocal fluorometry

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The loose coupling mechanism in molecular machines of living cells

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Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay

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Kinetics of adenosine triphosphate hydrolysis by shortening myofibrils from rabbit psoas muscle

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Single Molecule Dynamics Studied by Polarization Modulation

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10840052

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12 December 2020

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Identifiers

DOI

10.1073/PNAS.120174297

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10840052

retrieved

6 August 2017

ADS bibcode

2000PNAS...97.7243A

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PMC publication ID

16530

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10840052

retrieved

6 August 2017

PubMed publication ID

10840052

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10840052

retrieved

6 August 2017

ResearchGate publication ID

12478343

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