ArticleBiophysical journal2005
Biased binding of single molecules and continuous movement of multiple molecules of truncated single-headed kinesin.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Intracellular cargo transport by single-headed kinesin motors.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Step Sizes and Rate Constants of Single-headed Cytoplasmic Dynein Measured with Optical Tweezers.Scientific reports · 2018Article
- Article
- Cytoplasmic dynein moves through uncoordinated stepping of the AAA+ ring domains.Science (New York, N.Y.) · 2012Article
- Article
- Electrostatically biased binding of kinesin to microtubules.PLoS biology · 2011Article
- Mechanism of processive movement of monomeric and dimeric kinesin molecules.International journal of biological sciences · 2010Review
- Single molecular observation of self-regulated kinesin motility.Biochemistry · 2010Article
- Unidirectional Brownian motion observed in an in silico single molecule experiment of an actomyosin motor.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Kinesin motor mechanics: binding, stepping, tracking, gating, and limping.Biophysical journal · 2007Review
- High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations.The EMBO journal · 2006Article
- Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro.Nature cell biology · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conventional kinesin has a double-headed structure consisting of two motor domains and moves processively along a microtubule using the two heads cooperatively. The movement of single and multiple truncated heads of Drosophila kinesin was measured using a laser trap and nanometer detecting apparatus. Single molecules of single-headed kinesin bound to the microtubules with a 3.5 nm biased displacement toward the plus end of the microtubule. The position of these single-headed kinesin molecules bound to a microtubule did not change until they had dissociated, indicating that single kinesin heads utilize nonprocessive movement processes. Two molecules of single-headed kinesin moved continuously along a microtubule with a lower velocity and force than that of single molecules of double-headed kinesin. The biased binding of the heads determines the directionality of movement, whereas two molecules of single-headed kinesin move continuously without dissociation from a microtubule.
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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.