scholarly article | Q13442814 |
P2093 | author name string | Sean X Sun | |
Ganhui Lan | |||
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Entropic elasticity of lambda-phage DNA | Q28247727 | ||
Unconstrained steps of myosin VI appear longest among known molecular motors | Q30476442 | ||
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A force-dependent state controls the coordination of processive myosin V | Q33223012 | ||
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Monte Carlo modeling of single-molecule cytoplasmic dynein | Q33922791 | ||
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ADP inhibition of myosin V ATPase activity | Q34173890 | ||
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Interhead distance measurements in myosin VI via SHRImP support a simplified hand-over-hand model | Q34350508 | ||
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Walking with myosin V. | Q36354001 | ||
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The unique insert in myosin VI is a structural calcium-calmodulin binding site. | Q37415026 | ||
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Elastic lever-arm model for myosin V | Q40334174 | ||
Mechanism of nucleotide binding to actomyosin VI: evidence for allosteric head-head communication | Q40536919 | ||
Class VI myosin moves processively along actin filaments backward with large steps | Q40758767 | ||
The core of the motor domain determines the direction of myosin movement | Q40784283 | ||
A simple theoretical model explains dynein's response to load | Q41814943 | ||
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 anchoring | Q44790017 | ||
Mechanochemical coupling of two substeps in a single myosin V motor | Q45001867 | ||
Load-dependent kinetics of myosin-V can explain its high processivity | Q46650611 | ||
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 properties | Q56894346 | ||
A single myosin head moves along an actin filament with regular steps of 5.3 nanometres | Q59063267 | ||
Brain myosin-V is a two-headed unconventional myosin with motor activity | Q70488210 | ||
Myosin steps backwards | Q73078828 | ||
A mechanical unfolding intermediate in an actin-crosslinking protein | Q75247106 | ||
Myosin VI steps via a hand-over-hand mechanism with its lever arm undergoing fluctuations when attached to actin | Q80341101 | ||
Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography | Q83177861 | ||
P433 | issue | 11 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 4002-4013 | |
P577 | publication date | 2006-09-08 | |
P1433 | published in | Biophysical Journal | Q2032955 |
P1476 | title | Flexible light-chain and helical structure of F-actin explain the movement and step size of myosin-VI. | |
P478 | volume | 91 |
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Q33780128 | Reverse 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 |
Q30494681 | Single-molecule stepping and structural dynamics of myosin X. |
Q85045885 | Switch between Large Hand-Over-Hand and Small Inchworm-like Steps in Myosin VI |