ArticleBiophysical journal1999
Actin motion on microlithographically functionalized myosin surfaces and tracks.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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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
13 citing papers in PubMed.
- Surface Topography Induces and Orients Nematic Swarms of Active Filaments: Considerations for Lab-On-A-Chip Devices.ACS applied nano materials · 2024Article
- Exploitation of Engineered Light-Switchable Myosin XI for Nanotechnological Applications.ACS nano · 2023Article
- Through the Eyes of Creators: Observing Artificial Molecular Motors.ACS nanoscience Au · 2022Review
- Comparative analysis of widely used methods to remove nonfunctional myosin heads for the in vitro motility assay.Journal of muscle research and cell motility · 2018Article
- Motor-like DNA motion due to an ATP-hydrolyzing protein under nanoconfinement.Scientific reports · 2018Article
- Parallel computation with molecular-motor-propelled agents in nanofabricated networks.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Translational actomyosin research: fundamental insights and applications hand in hand.Journal of muscle research and cell motility · 2012Review
- Antibodies covalently immobilized on actin filaments for fast myosin driven analyte transport.PloS one · 2012Article
- Self-organization of motor-propelled cytoskeletal filaments at topographically defined borders.Journal of biomedicine & biotechnology · 2012Article
- Two-stage capture employing active transport enables sensitive and fast biosensors.Nano letters · 2010Article
- A smart dust biosensor powered by kinesin motors.Nature nanotechnology · 2009Article
- Controlling the direction of kinesin-driven microtubule movements along microlithographic tracks.Biophysical journal · 2001Article
- Actomyosin interactions in a novel single muscle fiber in vitro motility assay.Journal of muscle research and cell motility · 2000Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High-resolution e-beam patterning exposure of the surface of poly[(tert-butyl-methacrylate)-co-(methyl methacrylate)]-a common e-beam and deep-UV resist used in semiconductor microlithography-induced sharp changes in the surface hydrophobicity. These differences in hydrophobicity resulted in the selective attachment of heavy meromyosin to hydrophobic, unexposed surfaces. The movement of the actin filaments on myosin-rich and myosin-poor surfaces was statistically characterized in terms of velocity, acceleration, and angle of movement. The actin filaments have a smooth motion on myosin-rich surfaces and an uneven motion on myosin-poor surfaces. Interestingly, an excess of myosin sites has a slowing, albeit mild effect on the motion of the actin filaments. It was also found that the myosin-rich/myosin-poor boundary has an alignment-enforcement effect, especially for the filaments approaching the border from the myosin-rich side. Based on these results, we discuss the feasibility of building purposefully designed molecular motor arrays and the testing of the hypotheses regarding the functioning of the molecular motors.
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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.