ArticleBiophysical journal2006
Flexible light-chain and helical structure of F-actin explain the movement and step size of myosin-VI.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- Kinematics of the lever arm swing in myosin VI.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Motor proteins and molecular motors: how to operate machines at the nanoscale.Journal of physics. Condensed matter : an Institute of Physics journal · 2013Review
- Lever-arm mechanics of processive myosins.Biophysical journal · 2011Review
- Mechanical response and conformational amplification in α-helical coiled coils.Biophysical journal · 2010Article
- Single-molecule stepping and structural dynamics of myosin X.Nature structural & molecular biology · 2010Article
- Engineered myosin VI motors reveal minimal structural determinants of directionality and processivity.Journal of molecular biology · 2009Article
- 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.Journal of molecular biology · 2009Article
- Myosin VI walks "wiggly" on actin with large and variable tilting.Molecular cell · 2007Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myosin-VI is a dimeric isoform of unconventional myosins. Single molecule experiments indicate that myosin-VI and myosin-V are processive molecular motors, but travel toward opposite ends of filamentous actin. Structural studies show several differences between myosin-V and VI, including a significant difference in the light-chain domain connecting the motor domains. Combining the measured kinetics of myosin-VI with the elasticity of the light chains, and the helical structure of F-actin, we compare and contrast the motility of myosin-VI with myosin-V. We show that the elastic properties of the light-chain domain control the stepping behavior of these motors. Simple models incorporating the motor elastic energy can quantitatively capture most of the observed data. Implications of our result for other processive motors are discussed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.