Controlled rotation of the F₁-ATPase reveals differential and continuous binding changes for ATP synthesis. (Q30525177)

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12 February 2020

title

Controlled rotation of the F₁-ATPase reveals differential and continuous binding changes for ATP synthesis (English)

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2

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author name string

Kengo Adachi

1

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12 February 2020

Masasuke Yoshida

3

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12 February 2020

Takayuki Nishizaka

4

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12 February 2020

Kazuhiko Kinosita

5

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12 February 2020

language of work or name

English

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publication date

1 January 2012

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12 February 2020

published in

Nature Communications

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volume

3

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page(s)

1022

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Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported

12 February 2020

copyright license

start time

1 January 2012

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April 2022 Public Data File from Crossref

copyright status

copyrighted

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describes a project that uses

ImageJ

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11 June 2022

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inferred from PubMed Central ID database lookup

cites work

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Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation

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Catalysis and rotation of F1 motor: cleavage of ATP at the catalytic site occurs in 1 ms before 40 degree substep rotation

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The ATP-waiting conformation of rotating F1-ATPase revealed by single-pair fluorescence resonance energy transfer

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The 2'-O- and 3'-O-Cy3-EDA-ATP(ADP) complexes with myosin subfragment-1 are spectroscopically distinct

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12 December 2020

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12 December 2020

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12 December 2020

Identifiers

DOI

10.1038/NCOMMS2026

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22929779 AND SRC:MED&resulttype=core&format=json

Dimensions Publication ID

12 February 2020

ADS bibcode

2012NatCo...3.1022A

0 references

0 references

1 reference

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12 February 2020

PubMed publication ID

22929779

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22929779 AND SRC:MED&resulttype=core&format=json