ArticleBiophysical journal2008
Kinesin steps do not alternate in size.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 30 citations in OpenAlex.
- CYK4 relaxes the bias in the off-axis motion by MKLP1 kinesin-6.Communications biology · 2021Article
- Kinesin and Dynein Mechanics: Measurement Methods and Research Applications.Journal of biomechanical engineering · 2018Review
- The Kinesin-8 Kip3 switches protofilaments in a sideward random walk asymmetrically biased by force.Biophysical journal · 2015Article
- Critical motor number for fractional steps of cytoskeletal filaments in gliding assays.PloS one · 2012Article
- Kinesin walks the line: single motors observed by atomic force microscopy.Biophysical journal · 2011Article
- Neck-linker docking coordinates the kinetics of kinesin's heads.Biophysical journal · 2011Article
- Two kinesins transport cargo primarily via the action of one motor: implications for intracellular transport.Biophysical journal · 2010Article
- On and around microtubules: an overview.Molecular biotechnology · 2009Review
- On the origin of kinesin limping.Biophysical journal · 2009Article
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 2 institutions in 1 country.
Funding
Abstract
Kinesin is a two-headed motor protein that transports cargo inside cells by moving stepwise on microtubules. Its exact trajectory along the microtubule is unknown: alternative pathway models predict either uniform 8-nm steps or alternating 7- and 9-nm steps. By analyzing single-molecule stepping traces from "limping" kinesin molecules, we were able to distinguish alternate fast- and slow-phase steps and thereby to calculate the step sizes associated with the motions of each of the two heads. We also compiled step distances from nonlimping kinesin molecules and compared these distributions against models predicting uniform or alternating step sizes. In both cases, we find that kinesin takes uniform 8-nm steps, a result that strongly constrains the allowed models.
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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.