ArticleTraffic (Copenhagen, Denmark)2009
Diffusive movement of processive kinesin-1 on microtubules.
Article in Traffic (Copenhagen, Denmark), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed, 50 citations in OpenAlex.
- KLP-6 is a kinesin superfamily protein resistant to ADP inhibition.Communications biology · 2026Article
- Kinesin-1 is highly flexible and adopts an open conformation in the absence of cargo.iScience · 2026Article
- Kinesin-1 autoinhibition tunes cargo transport by motor ensembles.Biophysical journal · 2025Article
- Nesprin-2 coordinates opposing microtubule motors during nuclear migration in neurons.The Journal of cell biology · 2024Article
- Unraveling the interplay of kinesin-1, tau, and microtubules in neurodegeneration associated with Alzheimer's disease.Frontiers in cellular neuroscience · 2024Review
- Interaction of Tau with Kinesin-1: Effect of Kinesin-1 Heavy Chain Elimination on Autophagy-Mediated Mutant Tau Degradation.Biomedicines · 2023Article
- Effect of detachment of motor protein from track on its transport.Journal of biological physics · 2022Article
- Mitochondria-adaptor TRAK1 promotes kinesin-1 driven transport in crowded environments.Nature communications · 2020Article
- Junctional sarcoplasmic reticulum motility in adult mouse ventricular myocytes.American journal of physiology. Cell physiology · 2020Article
- MAP7 regulates organelle transport by recruiting kinesin-1 to microtubules.The Journal of biological chemistry · 2019Article
- Phragmoplast Orienting Kinesin 2 Is a Weak Motor Switching between Processive and Diffusive Modes.Biophysical journal · 2018Article
- The axonal transport motor kinesin-2 navigates microtubule obstacles via protofilament switching.Traffic (Copenhagen, Denmark) · 2017Article
- The mitotic kinesin-14 KlpA contains a context-dependent directionality switch.Nature communications · 2017Article
- Distinct Interaction Modes of the Kinesin-13 Motor Domain with the Microtubule.Biophysical journal · 2016Article
- Bidirectional cargo transport: moving beyond tug of war.Nature reviews. Molecular cell biology · 2014Review
- Transport and diffusion of Tau protein in neurons.Cellular and molecular life sciences : CMLS · 2014Review
- Phosphorylation of myosin regulatory light chain has minimal effect on kinetics and distribution of orientations of cross bridges of rabbit skeletal muscle.American journal of physiology. Regulatory, integrative and comparative physiology · 2014Article
- Motor domain phosphorylation modulates kinesin-1 transport.The Journal of biological chemistry · 2013Article
- Kinetochore kinesin CENP-E is a processive bi-directional tracker of dynamic microtubule tips.Nature cell biology · 2013Article
- Kinesin-8 is a low-force motor protein with a weakly bound slip state.Biophysical journal · 2013Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The processive motor kinesin-1 moves unidirectionally toward the plus end of microtubules. This process can be visualized by total internal reflection fluorescence microscopy of kinesin bound to a carboxylated quantum dot (Qdot), which acts both as cargo and label. Surprisingly, when kinesin is bound to an anti-HIS Qdot, it shows diffusive movement on microtubules, which decreased in favor of processive runs with increasing salt concentration. This observation implies that kinesin movement on microtubules is governed by its conformation, as it is well established that kinesin undergoes a salt-dependent transition from a folded (inactive) to an extended (active) molecule. A truncated kinesin lacking the last 75 amino acids (kinesin-Delta C) showed both processive and diffusive movement on microtubules. The extent of each behavior depends on the relative amounts of ADP and ATP, with purely diffusive movement occurring in ADP alone. Taken together, these data imply that folded kinesin.ADP can exist in a state that diffuses along the microtubule lattice without expending energy. This mechanism may facilitate the ability of kinesin to pick up cargo, and/or allow the kinesin/cargo complex to stay bound after encountering obstacles.
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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.