Loop L5 acts as a conformational latch in the mitotic kinesin Eg5 - Wikidata - wikimedia - TriplyDB

Loop L5 acts as a conformational latch in the mitotic kinesin Eg5

Loop L5 acts as a conformational latch in the mitotic kinesin Eg5

http://www.wikidata.org/entity/Q24627077

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Analysis of the interaction of the Eg5 Loop5 with the nucleotide site Force generation by kinesin and myosin cytoskeletal motor proteins 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.Kinesin-5 allosteric inhibitors uncouple the dynamics of nucleotide, microtubule, and neck-linker binding sites.Kinesin-2 KIF3AB exhibits novel ATPase characteristics Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines A universal pathway for kinesin stepping.Synthesis and characterization of tritylthioethanamine derivatives with potent KSP inhibitory activity.The loop 5 element structurally and kinetically coordinates dimers of the human kinesin-5, Eg5.Microtubule capture by mitotic kinesin centromere protein E (CENP-E).The structural kinetics of switch-1 and the neck linker explain the functions of kinesin-1 and Eg5.Loop L5 assumes three distinct orientations during the ATPase cycle of the mitotic kinesin Eg5: a transient and time-resolved fluorescence study.Discovery of Novel Allosteric Eg5 Inhibitors Through Structure-Based Virtual Screening.The Kinesin-5 Chemomechanical Cycle Is Dominated by a Two-heads-bound State.The yeast kinesin-5 Cin8 interacts with the microtubule in a noncanonical manner.Heterodimerization of Kinesin-2 KIF3AB Modulates Entry into the Processive Run.Structural basis of small molecule ATPase inhibition of a human mitotic kinesin motor protein.Kinesin motility is driven by subdomain dynamics.Src family kinase phosphorylation of the motor domain of the human kinesin-5, Eg5.Biallelic variants in KIF14 cause intellectual disability with microcephaly.Chemical Genetics Approach to Engineer Kinesins with Sensitivity towards a Small-Molecule Inhibitor of Eg5.A posttranslational modification of the mitotic kinesin Eg5 that enhances its mechanochemical coupling and alters its mitotic function.Intraflagellar transport velocity is governed by the number of active KIF17 and KIF3AB motors and their motility properties under load.

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P2860

Loop L5 acts as a conformational latch in the mitotic kinesin Eg5

http://www.wikidata.org/entity/Q24627077

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2011 nî lūn-bûn

@nan

2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Loop L5 acts as a conformational latch in the mitotic kinesin Eg5

@ast

Loop L5 acts as a conformational latch in the mitotic kinesin Eg5

@en

Loop L5 acts as a conformational latch in the mitotic kinesin Eg5

@nl

type

label

Loop L5 acts as a conformational latch in the mitotic kinesin Eg5

@ast

Loop L5 acts as a conformational latch in the mitotic kinesin Eg5

@en

Loop L5 acts as a conformational latch in the mitotic kinesin Eg5

@nl

prefLabel

Loop L5 acts as a conformational latch in the mitotic kinesin Eg5

@ast

Loop L5 acts as a conformational latch in the mitotic kinesin Eg5

@en

Loop L5 acts as a conformational latch in the mitotic kinesin Eg5

@nl

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JBC.M110.192930

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Journal of Biological Chemistry

P1476

Loop L5 acts as a conformational latch in the mitotic kinesin Eg5

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Carolyn Moores

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

Jeremie Vendome

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

Steven S Rosenfeld

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

William M Behnke-Parks

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Zoltan Maliga

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P2860

Allosteric drug discrimination is coupled to mechanochemical changes in the kinesin-5 motor core.

The conserved L5 loop establishes the pre-powerstroke conformation of the Kinesin-5 motor, eg5

ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism

ATPase mechanism of Eg5 in the absence of microtubules: insight into microtubule activation and allosteric inhibition by monastrol

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

Switch-based mechanism of kinesin motors

ATPase Cycle of the Nonmotile Kinesin NOD Allows Microtubule End Tracking and Drives Chromosome Movement

9-Angström structure of a microtubule-bound mitotic motor

UCSF Chimera--a visualization system for exploratory research and analysis

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

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10.1074/JBC.M110.192930

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