Evidence map›Paper›PMID 25415053›Full record

ArticleeLife2014

High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation.

Zhiguo Shang, Kaifeng Zhou, Chen Xu, Roseann Csencsits, Jared C Cochran, Charles V Sindelar

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

86 citing papers in PubMed, 155 citations in OpenAlex.

  1. Article
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  7. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  8. Tether-scanning the kinesin motor domain reveals a core mechanical action.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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26 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 1 country.

Zhiguo ShangDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, United States.
Kaifeng ZhouDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, United States.
Chen XuDepartment of Biology, Brandeis University, Waltham, United States.
Roseann CsencsitsLife Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, United States.
Jared C CochranDepartment of Molecular and Cellular Biochemistry, Indiana University, Bloomington, United States.
Charles V SindelarDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, United States.
Yale University · USBrandeis University · USIndiana University Bloomington · USLawrence Berkeley National Laboratory · US

Funding

Structural basis of motility by dimeric kinesin motor proteinsR01GM110530 · NIGMS · YALE UNIVERSITY · PI SINDELAR, CHARLES VAUGHN · 2014 to 2023
$3.0M
NIGMS NIH HHS R01 GM110530NIGMS NIH HHS R01 GM 110530-01
6 · The paper itself

Abstract

Microtubule-based transport by the kinesin motors, powered by ATP hydrolysis, is essential for a wide range of vital processes in eukaryotes. We obtained insight into this process by developing atomic models for no-nucleotide and ATP states of the monomeric kinesin motor domain on microtubules from cryo-EM reconstructions at 5-6 Å resolution. By comparing these models with existing X-ray structures of ADP-bound kinesin, we infer a mechanistic scheme in which microtubule attachment, mediated by a universally conserved 'linchpin' residue in kinesin (N255), triggers a clamshell opening of the nucleotide cleft and accompanying release of ADP. Binding of ATP re-closes the cleft in a manner that tightly couples to translocation of cargo, via kinesin's 'neck linker' element. These structural transitions are reminiscent of the analogous nucleotide-exchange steps in the myosin and F1-ATPase motors and inform how the two heads of a kinesin dimer 'gate' each other to promote coordinated stepping along microtubules.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateBinding SitesBiomechanical PhenomenaHumansKinesinsMicrotubulesModels, MolecularMutant ProteinsNucleotidesPoint MutationProtein Structure, SecondaryProtein Structure, TertiaryAdenosine DiphosphateAdenosine TriphosphateKinesinsMutant ProteinsNucleotidesbiophysicscryo-EMhumankinesinmolecular motorsmyosinstructural biology

Identifiers

PMID25415053
PMCPMC4383081
OpenAlexW2110213040

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.