(Q33942984)

30 July 2017

title

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

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30 July 2017

Yasuda R

1

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30 July 2017

Noji H

2

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30 July 2017

Yoshida M

3

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30 July 2017

Kinosita K Jr

4

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30 July 2017

Itoh H

5

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30 July 2017

language of work or name

English

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publication date

1 April 2001

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30 July 2017

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30 July 2017

volume

410

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30 July 2017

issue

6831

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30 July 2017

page(s)

898-904

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

30 July 2017

cites work

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Catalytic site forms and controls in ATP synthase catalysis

21 January 2018

1 reference

Hypothesis. The mechanism of ATP synthase. Conformational change by rotation of the beta-subunit

21 January 2018

1 reference

Molecular mechanics of protonmotive F0F1 ATPases. Rolling well and turnstile hypothesis

21 January 2018

1 reference

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

21 January 2018

1 reference

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

21 January 2018

1 reference

Direct observation of the rotation of F1-ATPase

21 January 2018

1 reference

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

21 January 2018

1 reference

Abrupt changes in flagellar rotation observed by laser dark-field microscopy

21 January 2018

1 reference

Structural origins of high-affinity biotin binding to streptavidin

21 January 2018

1 reference

Atomic structure and chemistry of human serum albumin

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

The alpha 3 beta 3 gamma complex of the F1-ATPase from thermophilic Bacillus PS3 containing the alpha D261N substitution fails to dissociate inhibitory MgADP from a catalytic site when ATP binds to noncatalytic sites

21 January 2018

1 reference

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

21 January 2018

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The alpha3beta3gamma subcomplex of the F1-ATPase from the thermophilic bacillus PS3 with the betaT165S substitution does not entrap inhibitory MgADP in a catalytic site during turnover

21 January 2018

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Bi-site activation occurs with the native and nucleotide-depleted mitochondrial F1-ATPase

21 January 2018

1 reference

The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution

21 January 2018

1 reference

Energy transduction in the F1 motor of ATP synthase

21 January 2018

1 reference

Synthesis of ATP from ADP and inorganic phosphate at the myosin-subfragment 1 active site.

21 January 2018

1 reference

Three conformational states of scallop myosin S1

21 January 2018

1 reference

A structural change in the kinesin motor protein that drives motility

21 January 2018

1 reference

Force production by single kinesin motors

21 January 2018

1 reference

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

21 January 2018

1 reference

Intersubunit rotation in active F-ATPase

21 January 2018

1 reference

The loose coupling mechanism in molecular machines of living cells

21 January 2018

1 reference

7 January 2021

Stepwise motion of an actin filament over a small number of heavy meromyosin molecules is revealed in an in vitro motility assay

1 reference

7 January 2021

The reversal of the myosin and actomyosin ATPase reactions and the free energy of ATP binding to myosin

1 reference

7 January 2021

Structure and function in GroEL-mediated protein folding

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7 January 2021

Innocuous labeling of the subfragment-2 region of skeletal muscle heavy meromyosin with a fluorescent polyacrylamide nanobead and visualization of individual heavy meromyosin molecules

1 reference

7 January 2021

Identifiers

DOI

10.1038/35073513

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Dimensions Publication ID

30 July 2017

1022691195

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