ArticleScientific reports2017
High-Resolution Imaging of a Single Gliding Protofilament of Tubulins by HS-AFM.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 26 citations in OpenAlex.
- Nano-Scale Video Imaging of Motility Machinery by High-Speed Atomic Force Microscopy.Biomolecules · 2025Review
- Can repetitive mechanical motion cause structural damage to axons?Frontiers in molecular neuroscience · 2024Review
- Regulation of microtubule dynamics, mechanics and function through the growing tip.Nature reviews. Molecular cell biology · 2021Review
- Molecular swarm robots: recent progress and future challenges.Science and technology of advanced materials · 2020Review
- Synchronous operation of biomolecular engines.Biophysical reviews · 2020Review
- A bio-pen for direct writing of single molecules on user-functionalized surfaces.Nanoscale advances · 2020Article
- Radial alignment of microtubules through tubulin polymerization in an evaporating droplet.PloS one · 2020Article
- [Progress in the applications of high-speed atomic force microscopy in cell biology].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2018Review
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In vitro gliding assay of microtubules (MTs) on kinesins has provided us with valuable biophysical and chemo-mechanical insights of this biomolecular motor system. Visualization of MTs in an in vitro gliding assay has been mainly dependent on optical microscopes, limited resolution of which often render them insufficient sources of desired information. In this work, using high speed atomic force microscopy (HS-AFM), which allows imaging with higher resolution, we monitored MTs and protofilaments (PFs) of tubulins while gliding on kinesins. Moreover, under the HS-AFM, we also observed splitting of gliding MTs into single PFs at their leading ends. The split single PFs interacted with kinesins and exhibited translational motion, but with a slower velocity than the MTs. Our investigation at the molecular level, using the HS-AFM, would provide new insights to the mechanics of MTs in dynamic systems and their interaction with motor proteins.
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