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High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformationsElectrostatically biased binding of kinesin to microtubulesThe forward and backward stepping processes of kinesin are gated by ATP bindingDirect observation of the binding state of the kinesin head to the microtubule.Single molecule measurements and molecular motorsPressure-induced changes in the structure and function of the kinesin-microtubule complex.Mechanical characterization of one-headed myosin-V using optical tweezers.One-dimensional Brownian motion of charged nanoparticles along microtubules: a model system for weak binding interactions.Mechanism of processive movement of monomeric and dimeric kinesin molecules.Unwinding forward and sliding back: an intermittent unwinding mode of the BLM helicase.Retrograde NGF axonal transport--motor coordination in the unidirectional motility regimeKinesin motor mechanics: binding, stepping, tracking, gating, and limping.Effects of Obstacles on the Dynamics of Kinesins, Including Velocity and Run Length, Predicted by a Model of Two Dimensional Motion.Kinesin is an evolutionarily fine-tuned molecular ratchet-and-pawl device of decisively locked direction.Mechanical control of the directional stepping dynamics of the kinesin motor.The Kinesin-1 Chemomechanical Cycle: Stepping Toward a Consensus.Dwell time symmetry in random walks and molecular motors.Energetics of kinesin-1 stepping mechanism.Mechanical design of translocating motor proteins.Fundamental and functional aspects of mesoscopic architectures with examples in physics, cell biology, and chemistry.How single molecule detection measures the dynamic actions of life.Directional fidelity of nanoscale motors and particles is limited by the 2nd law of thermodynamics--via a universal equality.Operation modes of the molecular motor kinesin.Generic maps of optimality reveal two chemomechanical coupling regimes for motor proteins: from F1-ATPase and kinesin to myosin and cytoplasmic dynein.Unbinding of Kinesin from Microtubule in the Strongly Bound States Enhances under Assisting Forces.A stochastic automaton model for simulating kinesin processivity.Properties of tug-of-war model for cargo transport by molecular motors.Parsing the roles of neck-linker docking and tethered head diffusion in the stepping dynamics of kinesin.Discrete Step Sizes of Molecular Motors Lead to Bimodal Non-Gaussian Velocity Distributions under Force.Role of directional fidelity in multiple aspects of extreme performance of the F(1)-ATPase motor.Processivity of dimeric kinesin-1 molecular motors
P2860
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P2860
description
2005 nî lūn-bûn
@nan
2005 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Entropy rectifies the Brownian steps of kinesin.
@ast
Entropy rectifies the Brownian steps of kinesin.
@en
type
label
Entropy rectifies the Brownian steps of kinesin.
@ast
Entropy rectifies the Brownian steps of kinesin.
@en
prefLabel
Entropy rectifies the Brownian steps of kinesin.
@ast
Entropy rectifies the Brownian steps of kinesin.
@en
P2093
P2860
P356
P1476
Entropy rectifies the Brownian steps of kinesin
@en
P2093
Toshio Yanagida
Yoshiharu Ishii
Yuichi Taniguchi
P2860
P2888
P304
P356
10.1038/NCHEMBIO741
P577
2005-10-09T00:00:00Z