The unique insert in myosin VI is a structural calcium-calmodulin binding site.
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How are the cellular functions of myosin VI regulated within the cell?Calcium can mobilize and activate myosin-VIPrecise positioning of myosin VI on endocytic vesicles in vivoMyosin VI Dimerization Triggers an Unfolding of a Three-Helix Bundle in Order to Extend Its ReachStructure of androcam supports specialized interactions with myosin VIStrain Mediated Adaptation Is Key for Myosin Mechanochemistry: Discovering General Rules for Motor ActivityUnconstrained steps of myosin VI appear longest among known molecular motors.The power stroke of myosin VI and the basis of reverse directionality.The structure of the myosin VI motor reveals the mechanism of directionality reversalHead of myosin IX binds calmodulin and moves processively toward the plus-end of actin filaments.Myosin Va and myosin VI coordinate their steps while engaged in an in vitro tug of war during cargo transportReverse conformational changes of the light chain-binding domain of myosin V and VI processive motor heads during and after hydrolysis of ATP by small-angle X-ray solution scatteringMyosin VI: an innovative motor that challenged the swinging lever arm hypothesisStructure of the light chain-binding domain of myosin VInsight into the role of Ca2+-binding protein 5 in vesicle exocytosis.Detailed tuning of structure and intramolecular communication are dispensable for processive motion of myosin VI.Flexible light-chain and helical structure of F-actin explain the movement and step size of myosin-VI.Myosin VI deafness mutation prevents the initiation of processive runs on actinThe unique insert at the end of the myosin VI motor is the sole determinant of directionality.Myosin VI has a one track mind versus myosin Va when moving on actin bundles or at an intersection.Long single alpha-helical tail domains bridge the gap between structure and function of myosin VI.Actin filament dynamics in the actomyosin VI complex is regulated allosterically by calcium-calmodulin light chainSingle-molecule fluorescence to study molecular motors.Myosin light chains: Teaching old dogs new tricksThe cortical acto-Myosin network: from diffusion barrier to functional gateway in the transport of neurosecretory vesicles to the plasma membrane.Cargo-binding makes a wild-type single-headed myosin-VI move processively.Myosin VI walks "wiggly" on actin with large and variable tilting.Formation of salt bridges mediates internal dimerization of myosin VI medial tail domain.Real-time measurement of myosin-nucleotide noncovalent complexes by electrospray ionization mass spectrometry.Myosin VI walks hand-over-hand along actin.Androcam is a tissue-specific light chain for myosin VI in the Drosophila testis.Myosin VI: cellular functions and motor properties
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P2860
The unique insert in myosin VI is a structural calcium-calmodulin binding site.
description
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 22 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
The unique insert in myosin VI is a structural calcium-calmodulin binding site.
@en
The unique insert in myosin VI is a structural calcium-calmodulin binding site.
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type
label
The unique insert in myosin VI is a structural calcium-calmodulin binding site.
@en
The unique insert in myosin VI is a structural calcium-calmodulin binding site.
@nl
prefLabel
The unique insert in myosin VI is a structural calcium-calmodulin binding site.
@en
The unique insert in myosin VI is a structural calcium-calmodulin binding site.
@nl
P2093
P2860
P50
P356
P1476
The unique insert in myosin VI is a structural calcium-calmodulin binding site
@en
P2093
Alain Van Dorsselaer
Amber L Wells
Anne Houdusse
H Lee Sweeney
Jocelyn Nolt
Li-Qiong Chen
Noëlle Potier
Steve Rosenfeld
Zhaohui Yang
P2860
P304
P356
10.1073/PNAS.0306892101
P407
P577
2004-03-22T00:00:00Z