Allosteric inhibition of kinesin-5 modulates its processive directional motility. - Wikidata - awgldk - TriplyDB

Allosteric inhibition of kinesin-5 modulates its processive directional motility.

Allosteric inhibition of kinesin-5 modulates its processive directional motility.

http://www.wikidata.org/entity/Q34554785

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Kinesin-5: cross-bridging mechanism to targeted clinical therapy A nonmotor microtubule binding site in kinesin-5 is required for filament crosslinking and sliding NSC 622124 inhibits human Eg5 and other kinesins via interaction with the conserved microtubule-binding site Microtubule cross-linking triggers the directional motility of kinesin-5 Force and premature binding of ADP can regulate the processivity of individual Eg5 dimers Kinesin-5 regulates the growth of the axon by acting as a brake on its microtubule array.TPX2 Inhibits Eg5 by Interactions with Both Motor and Microtubule.The Structural Basis of Force Generation by the Mitotic Motor Kinesin-5 "Snapshots"of Ispinesib-induced Conformational Changes in the Mitotic Kinesin Eg5 Comprehensive structural model of the mechanochemical cycle of a mitotic motor highlights molecular adaptations in the kinesin family.Directional switching of the kinesin Cin8 through motor coupling.XMAP215 is a processive microtubule polymerase.Diffusive movement of processive kinesin-1 on microtubules Costal2 functions as a kinesin-like protein in the hedgehog signal transduction pathway Dynamic reorganization of Eg5 in the mammalian spindle throughout mitosis requires dynein and TPX2.Embedding dual function into molecular motors through collective motion Mammalian Kinesin-3 motors are dimeric in vivo and move by processive motility upon release of autoinhibition.Insights into the Mechanical Properties of the Kinesin Neck Linker Domain from Sequence Analysis and Molecular Dynamics Simulations The homotetrameric kinesin-5 KLP61F preferentially crosslinks microtubules into antiparallel orientations.Phosphorylation by Cdk1 increases the binding of Eg5 to microtubules in vitro and in Xenopus egg extract spindles Novel ways to determine kinesin-1's run length and randomness using fluorescence microscopy.Opposite-polarity motors activate one another to trigger cargo transport in live cells How kinesin motor proteins drive mitotic spindle function: Lessons from molecular assays.Microtubule organization by the antagonistic mitotic motors kinesin-5 and kinesin-14 Spindle pole mechanics studied in mitotic asters: dynamic distribution of spindle forces through compliant linkages.Interhead tension determines processivity across diverse N-terminal kinesins.Eg5 steps it up!Mutation of the MAP kinase DYF-5 affects docking and undocking of kinesin-2 motors and reduces their speed in the cilia of Caenorhabditis elegans The loop 5 element structurally and kinetically coordinates dimers of the human kinesin-5, Eg5.Load-dependent release limits the processive stepping of the tetrameric Eg5 motor.Biased Brownian motion as a mechanism to facilitate nanometer-scale exploration of the microtubule plus end by a kinesin-8.To step or not to step? How biochemistry and mechanics influence processivity in Kinesin and Eg5.A chimeric kinesin-1 head/kinesin-5 tail motor switches between diffusive and processive motility CENP-E combines a slow, processive motor and a flexible coiled coil to produce an essential motile kinetochore tether Distinct Interaction Modes of the Kinesin-13 Motor Domain with the Microtubule.The diffusive interaction of microtubule binding proteins.Mechanical properties of spindle poles are symmetrically balanced.Mitotic functions of kinesin-5.Metaphase Spindle Assembly.Moving into the cell: single-molecule studies of molecular motors in complex environments.

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Allosteric inhibition of kinesin-5 modulates its processive directional motility.

http://www.wikidata.org/entity/Q34554785

description

2006 nî lūn-bûn

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2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի օգոստոսին հրատարակված գիտական հոդված

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2006年の論文

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年學術文章

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name

Allosteric inhibition of kinesin-5 modulates its processive directional motility.

@ast

Allosteric inhibition of kinesin-5 modulates its processive directional motility.

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Allosteric inhibition of kinesin-5 modulates its processive directional motility.

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type

label

Allosteric inhibition of kinesin-5 modulates its processive directional motility.

@ast

Allosteric inhibition of kinesin-5 modulates its processive directional motility.

@en

Allosteric inhibition of kinesin-5 modulates its processive directional motility.

@nl

prefLabel

Allosteric inhibition of kinesin-5 modulates its processive directional motility.

@ast

Allosteric inhibition of kinesin-5 modulates its processive directional motility.

@en

Allosteric inhibition of kinesin-5 modulates its processive directional motility.

@nl

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Nature Chemical Biology

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Allosteric inhibition of kinesin-5 modulates its processive directional motility

@en

P2093

Benjamin H Kwok

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

Jeffrey H Kim

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

Lukas C Kapitein

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

Tarun M Kapoor

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P2860

A bipolar kinesin

The bipolar kinesin, KLP61F, cross-links microtubules within interpolar microtubule bundles of Drosophila embryonic mitotic spindles

Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker

Inhibition of a mitotic motor protein: where, how, and conformational consequences

Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen

Evidence that monastrol is an allosteric inhibitor of the mitotic kinesin Eg5

The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends

Microtubules as a target for anticancer drugs

Mitotic spindle organization by a plus-end-directed microtubule motor

A structural model for monastrol inhibition of dimeric kinesin Eg5.

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480-485

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scholarly article

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10.1038/NCHEMBIO812

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9

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2

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Christoph F Schmidt

Erwin J.G. Peterman

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2006-08-06T00:00:00Z

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6895105

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16892050

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