(Q34769108)

4 August 2017

title

Resolving stepping rotation in Thermus thermophilus H(+)-ATPase/synthase with an essentially drag-free probe (English)

1 reference

4 August 2017

Thermus thermophilus

1 reference

Shou Furuike

1

1 reference

4 August 2017

Masahiro Nakano

2

1 reference

4 August 2017

Kengo Adachi

3

1 reference

4 August 2017

Hiroyuki Noji

4

1 reference

4 August 2017

Kazuhiko Kinosita

5

1 reference

4 August 2017

Ken Yokoyama

6

1 reference

4 August 2017

language of work or name

English

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publication date

1 January 2011

1 reference

4 August 2017

published in

Nature Communications

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4 August 2017

volume

2

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4 August 2017

page(s)

233

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Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported

4 August 2017

copyright license

start time

8 March 2011

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

0 references

cites work

36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

Torque generation and elastic power transmission in the rotary F(O)F(1)-ATPase.

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

ATP hydrolysis and synthesis of a rotary motor V-ATPase from Thermus thermophilus

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

Dodecamer rotor ring defines H+/ATP ratio for ATP synthesis of prokaryotic V-ATPase from Thermus thermophilus.

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

Rotation, structure, and classification of prokaryotic V-ATPase.

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

Rotation scheme of V1-motor is different from that of F1-motor.

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

Direct observation of base-pair stepping by RNA polymerase

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

Activation of pausing F1 motor by external force

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

ATP-driven stepwise rotation of FoF1-ATP synthase

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

Mechanically driven ATP synthesis by F1-ATPase

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

Evidence for rotation of V1-ATPase.

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

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

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

Structure-function relationships of A-, F- and V-ATPases.

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

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

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

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

7 July 2018

2 references

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

7 July 2018

https://api.crossref.org/works/10.1038%2FNCOMMS1215

ATP synthase: an electrochemical transducer with rotatory mechanics

21 January 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

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

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

Direct observation of kinesin stepping by optical trapping interferometry

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

Thermus thermophilus membrane-associated ATPase. Indication of a eubacterial V-type ATPase

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3072102

Subunit arrangement in V-ATPase from Thermus thermophilus

7 July 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS1215

Rotation of the proteolipid ring in the V-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS1215

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS1215

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS1215

V-ATPase of Thermus thermophilus is inactivated during ATP hydrolysis but can synthesize ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS1215

V-Type H+-ATPase/synthase from a thermophilic eubacterium, Thermus thermophilus. Subunit structure and operon

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS1215

Effect of external torque on the ATP-driven rotation of F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS1215

Acceleration of the ATP-binding rate of F1-ATPase by forcible forward rotation

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS1215

Stimulation of F(1)-ATPase activity by sodium dodecyl sulfate

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS1215

Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/21407199

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1038/NCOMMS1215

1 reference

Dimensions Publication ID

4 August 2017

0 references

0 references

1 reference

4 August 2017

1 reference