Evidence map›Paper›PMID 26437877›Full record

ArticleNature communications2015

Kinesin-5 is a microtubule polymerase.

Yalei Chen, William O Hancock

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed, 1 pooled it
4.7field-weighted citation impact, top 4% 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

63 citing papers in PubMed, 1 synthesis or guideline pooled it, 113 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. KIF11 UFMylation Maintains Photoreceptor Cilium Integrity and Retinal Homeostasis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. IncreasediScience · 2022
    Article
  18. The cell cycle, cancer development and therapy.Molecular biology reports · 2022
    Review
  19. Article
  20. Review

3 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

2 authors at 1 institution in 1 country.

Yalei ChenDepartment of Biomedical Engineering, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.
William O HancockDepartment of Biomedical Engineering, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.
Pennsylvania State University · US

Funding

Molecular mechanism of kinesin motilityR01GM076476 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI HANCOCK, WILLIAM OLAF · 2006 to 2019
$3.5M
Kinesin and +TIP-based microtubule steeringR01GM100076 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI HANCOCK, WILLIAM OLAF · 2012 to 2015
$1.7M
NIGMS NIH HHS R01 GM076476NIGMS NIH HHS R01GM076476NIGMS NIH HHS R01 GM100076NIGMS NIH HHS R01GM100076
6 · The paper itself

Abstract

Kinesin-5 slides antiparallel microtubules during spindle assembly, and regulates the branching of growing axons. Besides the mechanical activities enabled by its tetrameric configuration, the specific motor properties of kinesin-5 that underlie its cellular function remain unclear. Here by engineering a stable kinesin-5 dimer and reconstituting microtubule dynamics in vitro, we demonstrate that kinesin-5 promotes microtubule polymerization by increasing the growth rate and decreasing the catastrophe frequency. Strikingly, microtubules growing in the presence of kinesin-5 have curved plus ends, suggesting that the motor stabilizes growing protofilaments. Single-molecule fluorescence experiments reveal that kinesin-5 remains bound to the plus ends of static microtubules for 7 s, and tracks growing microtubule plus ends in a manner dependent on its processivity. We propose that kinesin-5 pauses at microtubule plus ends and enhances polymerization by stabilizing longitudinal tubulin-tubulin interactions, and that these activities underlie the ability kinesin-5 to slide and stabilize microtubule bundles in cells.

Indexed as

AnimalsDimerizationDrosophilaDrosophila ProteinsIn Vitro TechniquesKinesinsMicrotubule-Associated ProteinsMicrotubulesTubulinTubulin ModulatorsXenopus laevisXenopus ProteinsDrosophila ProteinsKIF11 protein, XenopusKinesinsKlp61F protein, DrosophilaMicrotubule-Associated ProteinsTubulinTubulin ModulatorsXenopus Proteins

Identifiers

PMID26437877
PMCPMC4600729
OpenAlexW2253382748

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.