Kinesin-microtubule binding depends on both nucleotide state and loading direction. - Wikidata - awgldk - TriplyDB

Kinesin-microtubule binding depends on both nucleotide state and loading direction.

Kinesin-microtubule binding depends on both nucleotide state and loading direction.

http://www.wikidata.org/entity/Q34027513

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Kinesin's biased stepping mechanism: amplification of neck linker zippering Collective dynamics of processive cytoskeletal motors Are coiled-coils of dimeric kinesins unwound during their walking on microtubule?The Mechanochemical Cycle of Mammalian Kinesin-2 KIF3A/B under Load.Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosensing at multiple AAA domains.The forward and backward stepping processes of kinesin are gated by ATP binding Modulation of kinesin binding by the C-termini of tubulin.Adhesion through single peptide aptamers.Identification of a strong binding site for kinesin on the microtubule using mutant analysis of tubulin.Two distinct modes of processive kinesin movement in mixtures of ATP and AMP-PNP.Mechanism of cooperative behaviour in systems of slow and fast molecular motors.Oatp1a1 requires PDZK1 to traffic to the plasma membrane by selective recruitment of microtubule-based motor proteins.Novel ways to determine kinesin-1's run length and randomness using fluorescence microscopy.Crystal structure of Zen4 in the apo state reveals a missing conformation of kinesin.Asymmetric friction of nonmotor MAPs can lead to their directional motion in active microtubule networks.Equilibrium 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.The sliding filament model: 1972-2004.Revealingly odd couples Backsteps induced by nucleotide analogs suggest the front head of kinesin is gated by strain On the hand-over-hand mechanism of kinesin A seesaw model for intermolecular gating in the kinesin motor protein Highly loaded behavior of kinesins increases the robustness of transport under high resisting loads Kinesin motor mechanics: binding, stepping, tracking, gating, and limping.N-terminal kinesins: many and various.Quasiperiodic distribution of rigor cross-bridges along a reconstituted thin filament in a skeletal myofibril.Kinetics of nucleotide-dependent structural transitions in the kinesin-1 hydrolysis cycle.To step or not to step? How biochemistry and mechanics influence processivity in Kinesin and Eg5.Load-dependent ADP binding to myosins V and VI: implications for subunit coordination and function.Directed Binding of Gliding Bacterium, Mycoplasma mobile, Shown by Detachment Force and Bond Lifetime.Energetics of kinesin-1 stepping mechanism.Walking the walk: how kinesin and dynein coordinate their steps.Insights into the mechanisms of myosin and kinesin molecular motors from the single-molecule unbinding force measurements.Bidirectional cargo transport: moving beyond tug of war.Coordination of molecular motors: from in vitro assays to intracellular dynamics.Key residues on microtubule responsible for activation of kinesin ATPase.Processivity of kinesin motility is enhanced on increasing temperature.Bifurcation of velocity distributions in cooperative transport of filaments by fast and slow motors.Design principles governing chemomechanical coupling of kinesin.Kinesin's front head is gated by the backward orientation of its neck linker.

P2860

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P2860

Kinesin-microtubule binding depends on both nucleotide state and loading direction.

http://www.wikidata.org/entity/Q34027513

description

2002 nî lūn-bûn

@nan

2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի ապրիլին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

@zh-hk

2002年論文

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2002年論文

@zh-tw

2002年论文

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name

Kinesin-microtubule binding depends on both nucleotide state and loading direction.

@ast

Kinesin-microtubule binding depends on both nucleotide state and loading direction.

@en

Kinesin-microtubule binding depends on both nucleotide state and loading direction.

@nl

type

label

Kinesin-microtubule binding depends on both nucleotide state and loading direction.

@ast

Kinesin-microtubule binding depends on both nucleotide state and loading direction.

@en

Kinesin-microtubule binding depends on both nucleotide state and loading direction.

@nl

prefLabel

Kinesin-microtubule binding depends on both nucleotide state and loading direction.

@ast

Kinesin-microtubule binding depends on both nucleotide state and loading direction.

@en

Kinesin-microtubule binding depends on both nucleotide state and loading direction.

@nl

P1433

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Kinesin-microtubule binding depends on both nucleotide state and loading direction.

@en

P2093

Junichiro Yajima

http://www.w3.org/2001/XMLSchema#string

Kenji Kawaguchi

http://www.w3.org/2001/XMLSchema#string

Masaki Edamatsu

http://www.w3.org/2001/XMLSchema#string

Shin'ichi Ishiwata

http://www.w3.org/2001/XMLSchema#string

Sotaro Uemura

http://www.w3.org/2001/XMLSchema#string

Yoko Yano Toyoshima

http://www.w3.org/2001/XMLSchema#string

P2860

A protein factor essential for microtubule assembly

Switch-based mechanism of kinesin motors

Kinesin and ncd bind through a single head to microtubules and compete for a shared MT binding site

The way things move: looking under the hood of molecular motor proteins

A structural change in the kinesin motor protein that drives motility

Kinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains.

Nucleotide-dependent single- to double-headed binding of kinesin.

Mechanics of single kinesin molecules measured by optical trapping nanometry

Characterization of single actomyosin rigor bonds: load dependence of lifetime and mechanical properties.

Preparation of marked microtubules for the assay of the polarity of microtubule-based motors by fluorescence.

P304

5977-5981

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P31

scholarly article

P356

10.1073/PNAS.092546199

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P407

P433

9

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P478

99

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2002-04-16T00:00:00Z

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11407361

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P698

11959922

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P932

122887

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