Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism.
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Mechanistic analysis of the mitotic kinesin Eg5.Processive movement of single kinesins on crowded microtubules visualized using quantum dots.Identification of a strong binding site for kinesin on the microtubule using mutant analysis of tubulin.Transport of beads by several kinesin motorsA kinesin-13 mutant catalytically depolymerizes microtubules in ADPProcessive movement by a kinesin heterodimer with an inactivating mutation in one head.Mechanism of cooperative behaviour in systems of slow and fast molecular motors.Diffusive movement of processive kinesin-1 on microtubulesKinesin processivity is gated by phosphate releaseKinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular MachinesKinesin crouches to sprint but resists pushingThe tethered motor domain of a kinesin-microtubule complex catalyzes reversible synthesis of bound ATP.Backsteps induced by nucleotide analogs suggest the front head of kinesin is gated by strainA universal pathway for kinesin stepping.Examining kinesin processivity within a general gating framework.Kinesin motor mechanics: binding, stepping, tracking, gating, and limping.To step or not to step? How biochemistry and mechanics influence processivity in Kinesin and Eg5.Modelling microtubule patterns.A modified active Brownian dynamics model using asymmetric energy conversion and its application to the molecular motor system.Secondary structure and compliance of a predicted flexible domain in kinesin-1 necessary for cooperation of motors.Molecular motors: not quite like clockworkModels of protein linear molecular motors for dynamic nanodevices.The kinesin-13 MCAK has an unconventional ATPase cycle adapted for microtubule depolymerization.The Kinesin-8 Kip3 switches protofilaments in a sideward random walk asymmetrically biased by force.Alternating site ATPase pathway of rat conventional kinesin.Intramolecular strain coordinates kinesin stepping behavior along microtubules.Design principles governing chemomechanical coupling of kinesin.Kinesin's front head is gated by the backward orientation of its neck linker.Myosin V: Chemomechanical-coupling ratchet with load-induced mechanical slipNeck-linker docking coordinates the kinetics of kinesin's heads.Distinct functions of elongation factor G in ribosome recycling and translocation.Operation modes of the molecular motor kinesin.Unbinding of Kinesin from Microtubule in the Strongly Bound States Enhances under Assisting Forces.Kinesin rotates unidirectionally and generates torque while walking on microtubules.A self-powered kinesin-microtubule system for smart cargo delivery.Model for hand-over-hand motion of molecular motors.Kinesin-2 motors: Kinetics and biophysics.Network Complexity and Parametric Simplicity for Cargo Transport by Two Molecular Motors
P2860
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P2860
Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism.
@ast
Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism.
@en
type
label
Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism.
@ast
Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism.
@en
prefLabel
Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism.
@ast
Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism.
@en
P2860
P356
P1476
Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism
@en
P2093
Rutilio H Clark
William R Schief
P2860
P304
P356
10.1073/PNAS.0304369101
P407
P577
2004-01-20T00:00:00Z