Myosin V processivity: multiple kinetic pathways for head-to-head coordination. - Wikidata - awgldk - TriplyDB

Myosin V processivity: multiple kinetic pathways for head-to-head coordination.

Myosin V processivity: multiple kinetic pathways for head-to-head coordination.

http://www.wikidata.org/entity/Q37681953

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Mechanics of actomyosin bonds in different nucleotide states are tuned to muscle contraction Filming biomolecular processes by high-speed atomic force microscopy Actin structure-dependent stepping of myosin 5a and 10 during processive movement Flexural Stiffness of Myosin Va Subdomains as Measured from Tethered Particle Motion.Allosteric communication in myosin V: from small conformational changes to large directed movements APC/C and retinoblastoma interaction: cross-talk of retinoblastoma protein with the ubiquitin proteasome pathway Dwell time distributions of the molecular motor myosin V Strain Mediated Adaptation Is Key for Myosin Mechanochemistry: Discovering General Rules for Motor Activity Role for myosin-V motor proteins in the selective delivery of Kv channel isoforms to the membrane surface of cardiac myocytes Lever-arm mechanics of processive myosins Myosin Va molecular motors manoeuvre liposome cargo through suspended actin filament intersections in vitro.Label-free, all-optical detection, imaging, and tracking of a single protein Coarse-grained simulation of myosin-V movement.Adaptability of myosin V studied by simultaneous detection of position and orientation.Myosin Va maneuvers through actin intersections and diffuses along microtubules.Unconventional myosin traffic in cells reveals a selective actin cytoskeleton.Load and Pi control flux through the branched kinetic cycle of myosin V.Mechanochemical model for myosin V.Myosin Va and myosin VI coordinate their steps while engaged in an in vitro tug of war during cargo transport Full-length myosin Va exhibits altered gating during processive movement on actin.Design principles governing the motility of myosin V.Motor coupling through lipid membranes enhances transport velocities for ensembles of myosin Va Cooperative protofilament switching emerges from inter-motor interference in multiple-motor transport.Differential labeling of myosin V heads with quantum dots allows direct visualization of hand-over-hand processivity A force-dependent state controls the coordination of processive myosin V Vertebrate myosin VIIb is a high duty ratio motor adapted for generating and maintaining tension.Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin.Coupling of two non-processive myosin 5c dimers enables processive stepping along actin filaments.Mechanical characterization of one-headed myosin-V using optical tweezers.Simultaneous observation of tail and head movements of myosin V during processive motion.Holding the reins on myosin V.Force-dependent stepping kinetics of myosin-V.Phenomenological analysis of ATP dependence of motor proteins.Detailed tuning of structure and intramolecular communication are dispensable for processive motion of myosin VI.An elastically tethered viscous load imposes a regular gait on the motion of myosin-V. Simulation of the effect of transient force relaxation on a stochastic process.Two single-headed myosin V motors bound to a tetrameric adapter protein form a processive complex Quantum dot labeling strategies to characterize single-molecular motors.How myosin VI coordinates its heads during processive movement Myo4p is a monomeric myosin with motility uniquely adapted to transport mRNA A branched kinetic scheme describes the mechanochemical coupling of Myosin Va processivity in response to substrate.

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Myosin V processivity: multiple kinetic pathways for head-to-head coordination.

http://www.wikidata.org/entity/Q37681953

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 31 March 2004

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Myosin V processivity: multiple kinetic pathways for head-to-head coordination.

@en

Myosin V processivity: multiple kinetic pathways for head-to-head coordination.

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type

label

Myosin V processivity: multiple kinetic pathways for head-to-head coordination.

@en

Myosin V processivity: multiple kinetic pathways for head-to-head coordination.

@nl

prefLabel

Myosin V processivity: multiple kinetic pathways for head-to-head coordination.

@en

Myosin V processivity: multiple kinetic pathways for head-to-head coordination.

@nl

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PNAS.0307247101

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

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Myosin V processivity: multiple kinetic pathways for head-to-head coordination.

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P2093

Amy Armstrong

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

David M Warshaw

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

Elena B Krementsova

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

Guy G Kennedy

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

Kathleen M Trybus

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

P2860

Myosin-V is a processive actin-based motor

Griscelli syndrome restricted to hypopigmentation results from a melanophilin defect (GS3) or a MYO5A F-exon deletion (GS1)

Effect of ADP and ionic strength on the kinetic and motile properties of recombinant mouse myosin V

Myosin V exhibits a high duty cycle and large unitary displacement

Myosin V: regulation by calcium, calmodulin, and the tail domain

Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization

The unique properties of tonic smooth muscle emerge from intrinsic as well as intermolecular behaviors of Myosin molecules.

Direct long-term observation of kinesin processivity at low load.

Myosin learns to walk.

Role of the lever arm in the processive stepping of myosin V.

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5542-5546

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scholarly article

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10.1073/PNAS.0307247101

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15

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15056760

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397419

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