Evidence map›Paper›PMID 26928936›Full record

ArticleNature chemical biology2016

Direct observation of intermediate states during the stepping motion of kinesin-1.

Hiroshi Isojima, Ryota Iino, Yamato Niitani, Hiroyuki Noji, Michio Tomishige

Abstract read
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In one paragraph

Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
11.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

66 citing papers in PubMed, 158 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
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  6. Article
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  8. Article
  9. Article
  10. Article
  11. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  12. Article
  13. Review
  14. Article
  15. Tracking Single Kinesin in Live Cells Using MINFLUX.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  16. Article
  17. Review
  18. Visualizing Single V-ATPase Rotation Using Janus Nanoparticles.bioRxiv : the preprint server for biology · 2024
    Article
  19. Article
  20. A Model for Chemomechanical Coupling of Kinesin-3 Motor.Cellular and molecular bioengineering · 2024
    Article

6 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Hiroshi IsojimaDepartment of Applied Physics, School of Engineering, The University of Tokyo, Tokyo, Japan.
Ryota IinoOkazaki Institute for Integrative Bioscience, Institute for Molecular Science, National Institutes of Natural Sciences, Aichi, Japan.ORCID http://orcid.org/0000-0003-0110-5704
Yamato NiitaniDepartment of Applied Physics, School of Engineering, The University of Tokyo, Tokyo, Japan.
Hiroyuki NojiDepartment of Applied Chemistry, School of Engineering, The University of Tokyo, Tokyo, Japan.
Michio TomishigeDepartment of Applied Physics, School of Engineering, The University of Tokyo, Tokyo, Japan.
The University of Tokyo · JPNational Institutes of Natural Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The dimeric motor protein kinesin-1 walks along microtubules by alternatingly hydrolyzing ATP and moving two motor domains ('heads'). Nanometer-precision single-molecule studies demonstrated that kinesin takes regular 8-nm steps upon hydrolysis of each ATP; however, the intermediate states between steps have not been directly visualized. Here, we employed high-temporal resolution dark-field microscopy to directly visualize the binding and unbinding of kinesin heads to or from microtubules during processive movement. Our observations revealed that upon unbinding from microtubules, the labeled heads were displaced rightward and underwent tethered diffusive movement. Structural and kinetic analyses of wild-type and mutant kinesins with altered neck linker lengths provided evidence that rebinding of the unbound head to the rear-binding site is prohibited by a tension increase in the neck linker and that ATP hydrolysis by the leading head is suppressed when both heads are bound to the microtubule, thereby explaining how the two heads coordinate to move in a hand-over-hand manner.

Indexed as

Adenosine TriphosphateBiotinylationEscherichia coliGoldKinesinsKineticsMicroscopy, FluorescenceMicrotubulesModels, BiologicalMovementMutationOptical TweezersProtein BindingProtein ConformationProtein MultimerizationProtein TransportAdenosine TriphosphateGoldKinesins

Identifiers

PMID26928936
OpenAlexW2291768908

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.