|
1
|
Coupling of rotation and catalysis in F(1)-ATPase revealed by single-molecule imaging and manipulation.
|
Cell
|
2007
|
4.09
|
|
2
|
Mechanically driven ATP synthesis by F1-ATPase.
|
Nature
|
2004
|
3.45
|
|
3
|
Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation.
|
Nat Struct Mol Biol
|
2004
|
3.23
|
|
4
|
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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Proc Natl Acad Sci U S A
|
2003
|
2.65
|
|
5
|
Myosin V is a left-handed spiral motor on the right-handed actin helix.
|
Nat Struct Biol
|
2002
|
1.95
|
|
6
|
Direct observation of the myosin Va recovery stroke that contributes to unidirectional stepping along actin.
|
PLoS Biol
|
2011
|
1.57
|
|
7
|
Myosin V walks by lever action and Brownian motion.
|
Science
|
2007
|
1.54
|
|
8
|
ATP-driven stepwise rotation of FoF1-ATP synthase.
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Proc Natl Acad Sci U S A
|
2005
|
1.43
|
|
9
|
Activation of pausing F1 motor by external force.
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Proc Natl Acad Sci U S A
|
2005
|
1.41
|
|
10
|
One rotary mechanism for F1-ATPase over ATP concentrations from millimolar down to nanomolar.
|
Biophys J
|
2004
|
1.40
|
|
11
|
Axle-less F1-ATPase rotates in the correct direction.
|
Science
|
2008
|
1.36
|
|
12
|
Chemo-mechanical coupling in F(1)-ATPase revealed by catalytic site occupancy during catalysis.
|
Biophys J
|
2010
|
1.35
|
|
13
|
The ATP-waiting conformation of rotating F1-ATPase revealed by single-pair fluorescence resonance energy transfer.
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Proc Natl Acad Sci U S A
|
2003
|
1.34
|
|
14
|
Unconstrained steps of myosin VI appear longest among known molecular motors.
|
Biophys J
|
2004
|
1.24
|
|
15
|
Resolving stepping rotation in Thermus thermophilus H(+)-ATPase/synthase with an essentially drag-free probe.
|
Nat Commun
|
2011
|
1.08
|
|
16
|
F1-ATPase changes its conformations upon phosphate release.
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J Biol Chem
|
2002
|
1.07
|
|
17
|
Torque generation and utilization in motor enzyme F0F1-ATP synthase: half-torque F1 with short-sized pushrod helix and reduced ATP Synthesis by half-torque F0F1.
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J Biol Chem
|
2011
|
1.05
|
|
18
|
Controlled rotation of the F₁-ATPase reveals differential and continuous binding changes for ATP synthesis.
|
Nat Commun
|
2012
|
1.03
|
|
19
|
Temperature dependence of the rotation and hydrolysis activities of F1-ATPase.
|
Biophys J
|
2008
|
1.01
|
|
20
|
The rotor tip inside a bearing of a thermophilic F1-ATPase is dispensable for torque generation.
|
Biophys J
|
2006
|
0.94
|
|
21
|
Activation and stiffness of the inhibited states of F1-ATPase probed by single-molecule manipulation.
|
J Biol Chem
|
2010
|
0.94
|
|
22
|
Neither helix in the coiled coil region of the axle of F1-ATPase plays a significant role in torque production.
|
Biophys J
|
2008
|
0.93
|
|
23
|
Single-molecule imaging of rotation of F1-ATPase.
|
Methods Enzymol
|
2003
|
0.91
|
|
24
|
Efficient ATP synthesis by thermophilic Bacillus FoF1-ATP synthase.
|
FEBS J
|
2011
|
0.88
|
|
25
|
Effect of epsilon subunit on the rotation of thermophilic Bacillus F1-ATPase.
|
FEBS Lett
|
2009
|
0.88
|
|
26
|
Kinetic equivalence of transmembrane pH and electrical potential differences in ATP synthesis.
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J Biol Chem
|
2012
|
0.86
|
|
27
|
Torque generation in F1-ATPase devoid of the entire amino-terminal helix of the rotor that fills half of the stator orifice.
|
Biophys J
|
2011
|
0.83
|
|
28
|
Stimulation of F(1)-ATPase activity by sodium dodecyl sulfate.
|
Biochim Biophys Acta
|
2010
|
0.80
|
|
29
|
Direct observation of strand passage by DNA-topoisomerase and its limited processivity.
|
PLoS One
|
2012
|
0.80
|
|
30
|
A giant liposome for single-molecule observation of conformational changes in membrane proteins.
|
Biochim Biophys Acta
|
2009
|
0.79
|
|
31
|
Visualization of RecA filaments and DNA by fluorescence microscopy.
|
J Biochem
|
2007
|
0.76
|