ArticleNature structural & molecular biology2010
Single-molecule stepping and structural dynamics of myosin X.
Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
53 citing papers in PubMed, 105 citations in OpenAlex.
- Membrane-bound myosin IC drives the chiral rotation of the gliding actin filament around its longitudinal axis.Scientific reports · 2023Article
- Chiral growth of adherent filopodia.Biophysical journal · 2023Article
- The Antiparallel Coiled-Coil Domain Allows Multiple Forward Step Sizes of Myosin X.The journal of physical chemistry letters · 2023Article
- MYO10 regulates genome stability and cancer inflammation through mediating mitosis.Cell reports · 2023Article
- Mitochondria-associated myosin 19 processively transports mitochondria on actin tracks in living cells.The Journal of biological chemistry · 2022Article
- AAA+ proteins: one motor, multiple ways to work.Biochemical Society transactions · 2022Review
- Filopodia rotate and coil by actively generating twist in their actin shaft.Nature communications · 2022Article
- Parallel, linear, and subnanometric 3D tracking of microparticles with Stereo Darkfield Interferometry.Science advances · 2021Article
- Processivity and Velocity for Motors Stepping on Periodic Tracks.Biophysical journal · 2020Article
- Simultaneous tracking of two motor domains reveals near simultaneous steps and stutter steps of myosin 10 on actin filament bundles.Biochemical and biophysical research communications · 2020Article
- Tunneling Nanotubes and the Eye: Intercellular Communication and Implications for Ocular Health and Disease.BioMed research international · 2020Review
- Three-Dimensional Optical Tweezers Tracking Resolves Random Sideward Steps of the Kinesin-8 Kip3.Biophysical journal · 2018Article
- The Antiparallel Dimerization of Myosin X Imparts Bundle Selectivity for Processive Motility.Biophysical journal · 2018Article
- Myosin X is recruited to nascent focal adhesions at the leading edge and induces multi-cycle filopodial elongation.Scientific reports · 2017Article
- Three-Dimensional Localization of Single Molecules for Super-Resolution Imaging and Single-Particle Tracking.Chemical reviews · 2017Review
- Angular measurements of the dynein ring reveal a stepping mechanism dependent on a flexible stalk.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Deconvolution of Camera Instrument Response Functions.Biophysical journal · 2017Article
- Activated full-length myosin-X moves processively on filopodia with large steps toward diverse two-dimensional directions.Scientific reports · 2017Article
- MyTH4-FERM myosins in the assembly and maintenance of actin-based protrusions.Current opinion in cell biology · 2017Review
- Single molecule optical measurements of orientation and rotations of biological macromolecules.Methods and applications in fluorescence · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Myosin X is an unconventional myosin with puzzling motility properties. We studied the motility of dimerized myosin X using the single-molecule fluorescence techniques polTIRF, FIONA and Parallax to measure the rotation angles and three-dimensional position of the molecule during its walk. It was found that Myosin X steps processively in a hand-over-hand manner following a left-handed helical path along both single actin filaments and bundles. Its step size and velocity are smaller on actin bundles than individual filaments, suggesting myosin X often steps onto neighboring filaments in a bundle. The data suggest that a previously postulated single alpha-helical domain mechanically extends the lever arm, which has three IQ motifs, and either the neck-tail hinge or the tail is flexible. These structural features, in conjunction with the membrane- and microtubule-binding domains, enable myosin X to perform multiple functions on varied actin structures in cells.
Indexed as
Identifiers
What OpenQuestion holds
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.