ArticleNature cell biology2006
Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro.
Article in Nature cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 141 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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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
141 citing papers in PubMed, 266 citations in OpenAlex.
- Feedback between filament spacing, crosslinker binding, and self-organization in cytoskeletal bundles.bioRxiv : the preprint server for biology · 2026Article
- Molecular Dynamics Simulations Provide Further Insights into the Allosteric Regulation of the Kinesin-5 Motor Domain by Loop 5.Journal of chemical information and modeling · 2026Article
- NovelBalkan journal of medical genetics : BJMG · 2025Article
- The rheology and interfacial properties of biomolecular condensates.Biophysical reviews · 2025Review
- Molecular design principles for bipolar spindle organization by two opposing motors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- A fine balance among key biophysical factors is required for recovery of bipolar mitotic spindle from monopolar and multipolar abnormalities.Molecular biology of the cell · 2023Article
- Determinant factors for residence time of kinesin motors at microtubule ends.Journal of biological physics · 2023Article
- Motor processivity and speed determine structure and dynamics of microtubule-motor assemblies.eLife · 2023Article
- Article
- KIF1A is kinetically tuned to be a superengaging motor under hindering loads.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Kinesin-5 Eg5 is essential for spindle assembly, chromosome stability and organogenesis in development.Cell death discovery · 2022Article
- Review
- Length-dependent poleward flux of sister kinetochore fibers promotes chromosome alignment.Cell reports · 2022Article
- Directly Measuring Forces within Reconstituted Active Microtubule Bundles.Journal of visualized experiments : JoVE · 2022Article
- Optical Control of Mitosis with a Photoswitchable Eg5 Inhibitor.Angewandte Chemie (International ed. in English) · 2022Article
- Microtubule Dumbbells to Assess the Effect of Force Geometry on Single Kinesin Motors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Effect of Kinesin-5 Tail Domain on Motor Dynamics for Antiparallel Microtubule Sliding.International journal of molecular sciences · 2021Article
- Mechanisms by Which Kinesin-5 Motors Perform Their Multiple Intracellular Functions.International journal of molecular sciences · 2021Review
- Retinal Features of Family Members With Familial Exudative Vitreoretinopathy Caused By Mutations in KIF11 Gene.Translational vision science & technology · 2021Article
81 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Eg5, a member of the kinesin superfamily of microtubule-based motors, is essential for bipolar spindle assembly and maintenance during mitosis, yet little is known about the mechanisms by which it accomplishes these tasks. Here, we used an automated optical trapping apparatus in conjunction with a novel motility assay that employed chemically modified surfaces to probe the mechanochemistry of Eg5. Individual dimers, formed by a recombinant human construct Eg5-513-5His, stepped processively along microtubules in 8-nm increments, with short run lengths averaging approximately eight steps. By varying the applied load (with a force clamp) and the ATP concentration, we found that the velocity of Eg5 was slower and less sensitive to external load than that of conventional kinesin, possibly reflecting the distinct demands of spindle assembly as compared with vesicle transport. The Eg5-513-5His velocity data were described by a minimal, three-state model where a force-dependent transition follows nucleotide binding.
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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.