ArticleeLife2017
Structural basis of cooperativity in kinesin revealed by 3D reconstruction of a two-head-bound state on microtubules.
Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Neck region-microtubule interactions direct counterclockwise stepping of kinesin-1.Biophysical journal · 2026Article
- Kinetic regulation of kinesin's two motor domains coordinates its stepping along microtubules.eLife · 2025Article
- Noncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin.Science advances · 2024Article
- Structure challenges in the multivalency of Tau-microtubule interactions.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Direct observation of motor protein stepping in living cells using MINFLUX.Science (New York, N.Y.) · 2023Article
- Multi-curve fitting and tubulin-lattice signal removal for structure determination of large microtubule-based motors.Journal of structural biology · 2022Article
- Magic-angle-spinning NMR structure of the kinesin-1 motor domain assembled with microtubules reveals the elusive neck linker orientation.Nature communications · 2022Article
- Structural basis of mechano-chemical coupling by the mitotic kinesin KIF14.Nature communications · 2021Article
- Structure Determination of Microtubules and Pili: Past, Present, and Future Directions.Frontiers in molecular biosciences · 2021Review
- How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1.International journal of molecular sciences · 2020Review
- Synthetic biology approaches to dissecting linear motor protein function: towards the design and synthesis of artificial autonomous protein walkers.Biophysical reviews · 2020Review
- Dynamic and asymmetric fluctuations in the microtubule wall captured by high-resolution cryoelectron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Hyper-Molecules: on the Representation and Recovery of Dynamical Structures for Applications in Flexible Macro-Molecules in Cryo-EM.Inverse problems · 2020Article
- A microtubule RELION-based pipeline for cryo-EM image processing.Journal of structural biology · 2020Article
- Shaft Function of Kinesin-1's α4 Helix in the Processive Movement.Cellular and molecular bioengineering · 2019Article
- Article
- An allosteric propofol-binding site in kinesin disrupts kinesin-mediated processive movement on microtubules.The Journal of biological chemistry · 2018Article
- KIF15 nanomechanics and kinesin inhibitors, with implications for cancer chemotherapeutics.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments.The Journal of biological chemistry · 2018Article
- Kinesin-2 motors: Kinetics and biophysics.The Journal of biological chemistry · 2018Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The detailed basis of walking by dimeric molecules of kinesin along microtubules has remained unclear, partly because available structural methods have been unable to capture microtubule-bound intermediates of this process. Utilizing novel electron cryomicroscopy methods, we solved structures of microtubule-attached, dimeric kinesin bound to an ATP analog. We find that under these conditions, the kinesin dimer can attach to the microtubule with either one or two motor domains, and we present sub-nanometer resolution reconstructions of both states. The former structure reveals a novel kinesin conformation that revises the current understanding of how ATP binding is coupled to forward stepping of the motor. The latter structure indicates how tension between the two motor domains keeps their cycles out of phase in order to stimulate directional motility. The methods presented here pave the way for future structural studies of a variety of challenging macromolecules that bind to microtubules and other filaments.
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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.