Kinesin takes one 8-nm step for each ATP that it hydrolyzes.
about
KIF1D is a fast non-processive kinesin that demonstrates novel K-loop-dependent mechanochemistry.RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free systemFilopodia act as phagocytic tentacles and pull with discrete steps and a load-dependent velocity.Coupling of kinesin ATP turnover to translocation and microtubule regulation: one engine, many machinesA kinesin motor in a force-producing conformationThe structure of apo-kinesin bound to tubulin links the nucleotide cycle to movementMolecular dissection of the microtubule depolymerizing activity of mitotic centromere-associated kinesinMCAK, a Kin I kinesin, increases the catastrophe frequency of steady-state HeLa cell microtubules in an ATP-dependent manner in vitroMolecular motors: thermodynamics and the random walkMotor domain phosphorylation modulates kinesin-1 transportThe distance that kinesin-1 holds its cargo from the microtubule surface measured by fluorescence interference contrast microscopy.Transport of beads by several kinesin motorsKinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains.Processive movement by a kinesin heterodimer with an inactivating mutation in one head.Direct measurements of kinesin torsional properties reveal flexible domains and occasional stalk reversals during stepping.Mechanical splitting of microtubules into protofilament bundles by surface-bound kinesin-1Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular MachinesRapid double 8-nm steps by a kinesin mutant.Novel ways to determine kinesin-1's run length and randomness using fluorescence microscopy.Magnet polepiece design for uniform magnetic force on superparamagnetic beads.Energetic cost of building a virus.Analysis of video-based microscopic particle trajectories using Kalman filtering.The conformational cycle of kinesin.A dynamical model of kinesin-microtubule motility assaysEquilibrium and transition between single- and double-headed binding of kinesin as revealed by single-molecule mechanics.Thermodynamic properties of the kinesin neck-region docking to the catalytic core.Kinesins at a glanceRevealingly odd couplesOn the hand-over-hand mechanism of kinesinProcessive movement of single 22S dynein molecules occurs only at low ATP concentrations.A universal pathway for kinesin stepping.One-dimensional deterministic transport in neurons measured by dispersion-relation phase spectroscopyLethal kinesin mutations reveal amino acids important for ATPase activation and structural coupling.Cytoplasmic dynein transports cargos via load-sharing between the heads.Highly loaded behavior of kinesins increases the robustness of transport under high resisting loadsCoordination between motor domains in processive kinesins.Examining kinesin processivity within a general gating framework.Kinesin motor mechanics: binding, stepping, tracking, gating, and limping.Walking motion of an overdamped active particle in a ratchet potential.Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism.
P2860
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P2860
Kinesin takes one 8-nm step for each ATP that it hydrolyzes.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
Kinesin takes one 8-nm step for each ATP that it hydrolyzes.
@en
Kinesin takes one 8-nm step for each ATP that it hydrolyzes.
@nl
type
label
Kinesin takes one 8-nm step for each ATP that it hydrolyzes.
@en
Kinesin takes one 8-nm step for each ATP that it hydrolyzes.
@nl
prefLabel
Kinesin takes one 8-nm step for each ATP that it hydrolyzes.
@en
Kinesin takes one 8-nm step for each ATP that it hydrolyzes.
@nl
P2860
P356
P1476
Kinesin takes one 8-nm step for each ATP that it hydrolyzes.
@en
P2093
P2860
P304
P356
10.1074/JBC.274.6.3667
P407
P577
1999-02-01T00:00:00Z