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Two rotary motors in F-ATP synthase are elastically coupled by a flexible rotor and a stiff stator stalk.Domain compliance and elastic power transmission in rotary F(O)F(1)-ATPaseOne-step selection of Vaccinia virus-binding DNA aptamers by MonoLEXThe torque of rotary F-ATPase can unfold subunit gamma if rotor and stator are cross-linked.Torque generation and elastic power transmission in the rotary F(O)F(1)-ATPase.Twisting and subunit rotation in single F(O)(F1)-ATP synthase.The uniqueness of subunit α of mycobacterial F-ATP synthases: An evolutionary variant for niche adaptation.Functional halt positions of rotary FOF1-ATPase correlated with crystal structures.Power Stroke Angular Velocity Profiles of Archaeal A-ATP Synthase Versus Thermophilic and Mesophilic F-ATP Synthase Molecular Motors.Evidence of a folding intermediate in RNase H from single-molecule FRET experiments.Conformational dynamics of the rotary subunit F in the A3 B3 DF complex of Methanosarcina mazei Gö1 A-ATP synthase monitored by single-molecule FRET.The molecular motor F-ATP synthase is targeted by the tumoricidal protein HAMLET.Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP SynthasesThe regulatory subunit ε in Escherichia coli FOF1-ATP synthaseThe structural features of Acetobacterium woodii F-ATP synthase reveal the importance of the unique subunit γ-loop in Na+ translocation and ATP synthesis
P50
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Hendrik Sielaff
@ast
Hendrik Sielaff
@en
Hendrik Sielaff
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Hendrik Sielaff
@nl
Hendrik Sielaff
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type
label
Hendrik Sielaff
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Hendrik Sielaff
@en
Hendrik Sielaff
@es
Hendrik Sielaff
@nl
Hendrik Sielaff
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prefLabel
Hendrik Sielaff
@ast
Hendrik Sielaff
@en
Hendrik Sielaff
@es
Hendrik Sielaff
@nl
Hendrik Sielaff
@sl
P106
P21
P31
P496
0000-0001-5231-7286