about
Kinesin-5: cross-bridging mechanism to targeted clinical therapyCoordinated hydrolysis explains the mechanical behavior of kinesin.Direct visualization of the microtubule lattice seam both in vitro and in vivoForce generation by kinesin and myosin cytoskeletal motor proteinsCoupling of kinesin ATP turnover to translocation and microtubule regulation: one engine, many machinesNavigation Strategies of Motor Proteins on Decorated TracksA single protofilament is sufficient to support unidirectional walking of dynein and kinesinMultiscale method for modeling binding phenomena involving large objects: application to kinesin motor domains motion along microtubules.Monte Carlo analysis of neck linker extension in kinesin molecular motorsEffects of surface passivation on gliding motility assaysDoublecortin recognizes the 13-protofilament microtubule cooperatively and tracks microtubule endsSingle cell optical imaging and spectroscopy.Distinct roles of doublecortin modulating the microtubule cytoskeleton.Three-dimensional structures of the flagellar dynein-microtubule complex by cryoelectron microscopy.Kinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains.Controlled and stochastic retention concentrates dynein at microtubule ends to keep endosomes on track.Two-dimensional tracking of ncd motility by back focal plane interferometry.Mechanical splitting of microtubules into protofilament bundles by surface-bound kinesin-1Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular MachinesFlexural rigidity of individual microtubules measured by a buckling force with optical trapsKinesin's neck-linker determines its ability to navigate obstacles on the microtubule surface3D motion of vesicles along microtubules helps them to circumvent obstacles in cellsDirectional loading of the kinesin motor molecule as it buckles a microtubule.Mechanochemical coupling of the motion of molecular motors to ATP hydrolysis.The force exerted by a single kinesin molecule against a viscous load.Motor protein mechanics: a stochastic model with minimal mechanochemical coupling.Single cytoplasmic dynein molecule movements: characterization and comparison with kinesin.Bidirectional helical motility of cytoplasmic dynein around microtubules.Structural and functional features of one- and two-headed biotinated kinesin derivatives.ncd and kinesin motor domains interact with both alpha- and beta-tubulin.Controlling self-assembly of microtubule spools via kinesin motor density.The force generated by a single kinesin molecule against an elastic load.Two-state displacement by the kinesin-14 Ncd stalkHybrid semiconducting polymer nanoparticles as polarization-sensitive fluorescent probesKinesin walks the line: single motors observed by atomic force microscopy.Structural comparison of dimeric Eg5, Neurospora kinesin (Nkin) and Ncd head-Nkin neck chimera with conventional kinesin.Large conformational changes in a kinesin motor catalyzed by interaction with microtubulesFlexible light-chain and helical structure of F-actin explain the movement and step size of myosin-VI.High-resolution tracking of microtubule motility driven by a single kinesin motor.Kinesin motor mechanics: binding, stepping, tracking, gating, and limping.
P2860
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P2860
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Kinesin follows the microtubule's protofilament axis
@ast
Kinesin follows the microtubule's protofilament axis
@en
type
label
Kinesin follows the microtubule's protofilament axis
@ast
Kinesin follows the microtubule's protofilament axis
@en
prefLabel
Kinesin follows the microtubule's protofilament axis
@ast
Kinesin follows the microtubule's protofilament axis
@en
P2860
P356
P1476
Kinesin follows the microtubule's protofilament axis
@en
P2093
P2860
P304
P356
10.1083/JCB.121.5.1083
P407
P577
1993-06-01T00:00:00Z