Flexible light-chain and helical structure of F-actin explain the movement and step size of myosin-VI.

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Flexible light-chain and helical structure of F-actin explain the movement and step size of myosin-VI. is …
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scholarly articleQ13442814

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P356DOI10.1529/BIOPHYSJ.106.089888
P932PMC publication ID1635660
P698PubMed publication ID16963511
P5875ResearchGate publication ID6826460

P2093author name stringSean X Sun
Ganhui Lan
P2860cites workMyosin-V is a processive actin-based motorQ22003739
Myosin VI is an actin-based motor that moves backwardsQ22010643
Three myosin V structures delineate essential features of chemo-mechanical transductionQ24310086
Myosin VI is a processive motor with a large step sizeQ24555089
Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin headQ27618317
A structural state of the myosin V motor without bound nucleotideQ27642224
Entropic elasticity of lambda-phage DNAQ28247727
Unconstrained steps of myosin VI appear longest among known molecular motorsQ30476442
The structure of the myosin VI motor reveals the mechanism of directionality reversalQ30490997
A force-dependent state controls the coordination of processive myosin VQ33223012
Myosins: a diverse superfamilyQ33866577
Monte Carlo modeling of single-molecule cytoplasmic dyneinQ33922791
Holding the reins on myosin V.Q34048256
ADP inhibition of myosin V ATPase activityQ34173890
A simple kinetic model describes the processivity of myosin-vQ34180584
The physics of molecular motorsQ34285697
Interhead distance measurements in myosin VI via SHRImP support a simplified hand-over-hand modelQ34350508
From continuum Fokker-Planck models to discrete kinetic modelsQ34351006
Myosin VI: cellular functions and motor propertiesQ34357378
Role of the lever arm in the processive stepping of myosin V.Q34392475
Myosin-V, a versatile motor for short-range vesicle transportQ35009600
Myosin-V stepping kinetics: a molecular model for processivityQ35207228
Design and regulation of the AAA+ microtubule motor dyneinQ35705280
Relating biochemistry and function in the myosin superfamilyQ35705378
Kinesin follows the microtubule's protofilament axisQ36232866
Walking with myosin V.Q36354001
The kinetic mechanism of myosin V.Q36700327
The unique insert in myosin VI is a structural calcium-calmodulin binding site.Q37415026
Dynamics of myosin-V processivityQ40317802
Elastic lever-arm model for myosin VQ40334174
Mechanism of nucleotide binding to actomyosin VI: evidence for allosteric head-head communicationQ40536919
Class VI myosin moves processively along actin filaments backward with large stepsQ40758767
The core of the motor domain determines the direction of myosin movementQ40784283
A simple theoretical model explains dynein's response to loadQ41814943
Kinetic mechanism and regulation of myosin VI.Q43651972
The gated gait of the processive molecular motor, myosin V.Q43820585
The mechanism of myosin VI translocation and its load-induced anchoringQ44790017
Mechanochemical coupling of two substeps in a single myosin V motorQ45001867
Load-dependent kinetics of myosin-V can explain its high processivityQ46650611
A flexible domain is essential for the large step size and processivity of myosin VI.Q47391271
Fluorescence imaging with one nanometer accuracy: application to molecular motors.Q50761313
The elasticity of alpha-helices.Q51393846
The light chain composition of chicken brain myosin-Va: calmodulin, myosin-II essential light chains, and 8-kDa dynein light chain/PIN.Q52144362
Myosin VI: cellular functions and motor propertiesQ56894346
A single myosin head moves along an actin filament with regular steps of 5.3 nanometresQ59063267
Brain myosin-V is a two-headed unconventional myosin with motor activityQ70488210
Myosin steps backwardsQ73078828
A mechanical unfolding intermediate in an actin-crosslinking proteinQ75247106
Myosin VI steps via a hand-over-hand mechanism with its lever arm undergoing fluctuations when attached to actinQ80341101
Three-dimensional structure of the myosin V inhibited state by cryoelectron tomographyQ83177861
P433issue11
P407language of work or nameEnglishQ1860
P304page(s)4002-4013
P577publication date2006-09-08
P1433published inBiophysical JournalQ2032955
P1476titleFlexible light-chain and helical structure of F-actin explain the movement and step size of myosin-VI.
P478volume91

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cites work (P2860)
Q37360986Chapter 23: Stochastic modeling methods in cell biology
Q43199321Comprehensive physical mechanism of two-headed biomotor myosin V.
Q35990181Engineered myosin VI motors reveal minimal structural determinants of directionality and processivity.
Q44871950Kinematics of the lever arm swing in myosin VI.
Q28743071Lever-arm mechanics of processive myosins
Q34398441Mechanical response and conformational amplification in α-helical coiled coils.
Q37382357Motor proteins and molecular motors: how to operate machines at the nanoscale
Q92655586Myosin V executes steps of variable length via structurally constrained diffusion
Q42149706Myosin VI walks "wiggly" on actin with large and variable tilting
Q50912175Path ensembles and path sampling in nonequilibrium stochastic systems.
Q33780128Reverse 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 scattering
Q30494681Single-molecule stepping and structural dynamics of myosin X.
Q85045885Switch between Large Hand-Over-Hand and Small Inchworm-like Steps in Myosin VI