Direct observation of the binding state of the kinesin head to the microtubule.
about
Force and premature binding of ADP can regulate the processivity of individual Eg5 dimersShedding light on protein folding, structural and functional dynamics by single molecule studiesThe Mechanochemical Cycle of Mammalian Kinesin-2 KIF3A/B under Load.Kinesin, 30 years later: Recent insights from structural studiesAn improved optical tweezers assay for measuring the force generation of single kinesin molecules.Molecular plasmonics for biology and nanomedicine.Direct measurements of kinesin torsional properties reveal flexible domains and occasional stalk reversals during stepping.Kinesin processivity is gated by phosphate releaseKinesin's step dissected with single-motor FRET.Crystal structure of Zen4 in the apo state reveals a missing conformation of kinesin.Phenomenological analysis of ATP dependence of motor proteins.Covalent immobilization of microtubules on glass surfaces for molecular motor force measurements and other single-molecule assays.Kinesin walks the line: single motors observed by atomic force microscopy.Effect of (2)H and (18)O water isotopes in kinesin-1 gliding assay.A universal pathway for kinesin stepping.Cytoplasmic dynein transports cargos via load-sharing between the heads.Optical tweezers study life under tensionExamining kinesin processivity within a general gating framework.Effects of Obstacles on the Dynamics of Kinesins, Including Velocity and Run Length, Predicted by a Model of Two Dimensional Motion.Ribosomal protein S1 unwinds double-stranded RNA in multiple steps.Kinetics of nucleotide-dependent structural transitions in the kinesin-1 hydrolysis cycle.The Kinesin-1 Chemomechanical Cycle: Stepping Toward a Consensus.Modular aspects of kinesin force generation machineryA modified active Brownian dynamics model using asymmetric energy conversion and its application to the molecular motor system.Recent developments in single-molecule DNA mechanics.Motor proteins and molecular motors: how to operate machines at the nanoscale.Geological constraints on the origin of oxygenic photosynthesis.Moving into the cell: single-molecule studies of molecular motors in complex environments.Walking molecules.Kinesin backsteps.Role of kinesin-1 in the pathogenesis of SPG10, a rare form of hereditary spastic paraplegia.Engineered, harnessed, and hijacked: synthetic uses for cytoskeletal systems.Processive cytoskeletal motors studied with single-molecule fluorescence techniques.Myosin V is a biological Brownian machine.Ensemble velocity of non-processive molecular motors with multiple chemical statesKinesin's front head is gated by the backward orientation of its neck linker.Strain through the neck linker ensures processive runs: a DNA-kinesin hybrid nanomachine study.Cargo transportation by two species of motor protein.Measurement of Force-Dependent Release Rates of Cytoskeletal Motors.Kinesin rotates unidirectionally and generates torque while walking on microtubules.
P2860
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P2860
Direct observation of the binding state of the kinesin head to the microtubule.
description
2009 nî lūn-bûn
@nan
2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Direct observation of the binding state of the kinesin head to the microtubule.
@ast
Direct observation of the binding state of the kinesin head to the microtubule.
@en
type
label
Direct observation of the binding state of the kinesin head to the microtubule.
@ast
Direct observation of the binding state of the kinesin head to the microtubule.
@en
prefLabel
Direct observation of the binding state of the kinesin head to the microtubule.
@ast
Direct observation of the binding state of the kinesin head to the microtubule.
@en
P2860
P356
P1433
P1476
Direct observation of the binding state of the kinesin head to the microtubule.
@en
P2093
Nicholas R Guydosh
P2860
P2888
P304
P356
10.1038/NATURE08259
P407
P577
2009-08-19T00:00:00Z
P5875
P6179
1038169689