Direct observation of the rotation of F1-ATPase (Q29615360)

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scientific article (publication date: 20 March 1997)

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English	Direct observation of the rotation of F1-ATPase	scientific article (publication date: 20 March 1997)

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Direct observation of the rotation of F1-ATPase (English)

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PubMed

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author name string

Noji H

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1

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PubMed

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Yasuda R

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2

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Yoshida M

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3

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Kinosita K Jr

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4

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language of work or name

English

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publication date

20 March 1997

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published in

Nature

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volume

386

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issue

6622

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page(s)

299-302

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Single myosin molecule mechanics: piconewton forces and nanometre steps

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Single-molecule analysis of the actomyosin motor using nano-manipulation

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Transcription against an applied force

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Bacteria Swim by Rotating their Flagellar Filaments

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

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Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism

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

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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

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Intersubunit rotation in active F-ATPase

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Molecular switch of F0F1-ATP synthase, G-protein, and other ATP-driven enzymes

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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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The loose coupling mechanism in molecular machines of living cells

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The proton flux through the bacterial flagellar motor

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Expression of the wild-type and the Cys-/Trp-less α3β3γ complex of thermophilic F1-ATPase in Escherichia coli

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

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

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The force exerted by a single kinesin molecule against a viscous load

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Identifiers

DOI

10.1038/386299A0

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PubMed

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30 April 2017

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

650215

Dimensions Publication ID

1031410497

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release_a6yp7ojstfbppgkexve5qjk4oy

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OpenCitations bibliographic resource ID

650215

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

650215

PubMed publication ID

9069291

2 references

stated in

PubMed

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9069291

retrieved

30 April 2017

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

650215

ResearchGate publication ID

14143706

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