Evidence map›Paper›PMID 16382238›Full record

ArticleNature2006

A lever-arm rotation drives motility of the minus-end-directed kinesin Ncd.

Nicholas F Endres, Craig Yoshioka, Ronald A Milligan, Ronald D Vale

Abstract read
In one paragraph

Article in Nature, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
–field-weighted citation impact
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

64 citing papers in PubMed.

  1. Article
  2. Motor-driven microtubule diffusion in a photobleached dynamical coordinate system.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Modeling processive motion of kinesin-13 MCAK and kinesin-14 Cik1-Kar3 molecular motors.Protein science : a publication of the Protein Society · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Motor Proteins.Cold Spring Harbor perspectives in biology · 2018
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Working stroke of the kinesin-14, ncd, comprises two substeps of different direction.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article

4 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

4 authors.

Nicholas F EndresThe Howard Hughes Medical Institute, and the Department of Cellular and Molecular Pharmacology, University of California San Francisco, 600 16th Street, San Francisco, California 94107, USA.
Craig Yoshioka
Ronald A Milligan
Ronald D Vale

Funding

STRUCTURE/FUNCTION OF MOLECULAR MOTORSP01AR042895 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI COOKE, ROGER A · 1994 to 2008
$9.8M
Howard Hughes Medical InstituteNIAMS NIH HHS P01 AR042895
6 · The paper itself

Abstract

Kinesins are microtubule-based motor proteins that power intracellular transport. Most kinesin motors, exemplified by Kinesin-1, move towards the microtubule plus end, and the structural changes that govern this directional preference have been described. By contrast, the nature and timing of the structural changes underlying the minus-end-directed motility of Kinesin-14 motors (such as Drosophila Ncd) are less well understood. Using cryo-electron microscopy, here we demonstrate that a coiled-coil mechanical element of microtubule-bound Ncd rotates approximately 70 degrees towards the minus end upon ATP binding. Extending or shortening this coiled coil increases or decreases velocity, respectively, without affecting ATPase activity. An unusual Ncd mutant that lacks directional preference shows unstable nucleotide-dependent conformations of its coiled coil, underscoring the role of this mechanical element in motility. These results show that the force-producing conformational change in Ncd occurs on ATP binding, as in other kinesins, but involves the swing of a lever-arm mechanical element similar to that described for myosins.

Indexed as

RotationAdenosine TriphosphateAnimalsCryoelectron MicroscopyDrosophila ProteinsKinesinsMicrotubulesModels, BiologicalModels, MolecularMutationProtein ConformationStructure-Activity RelationshipAdenosine TriphosphateDrosophila ProteinsKinesinsncd protein, Drosophila

Identifiers

PMID16382238
PMCPMC2851630

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.