Evidence map›Paper›PMID 20930138›Full record

ReviewJournal of cell science2010

Tubulin depolymerization may be an ancient biological motor.

J Richard McIntosh, Vladimir Volkov, Fazly I Ataullakhanov, Ekaterina L Grishchuk

Abstract readReview
In one paragraph

Review in Journal of cell science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

49 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Subcellular systems follow Onsager reciprocity.npj biomedical innovations · 2025
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Microtubule architecture in vitro and in cells revealed by cryo-electron tomography.Acta crystallographica. Section D, Structural biology · 2018
    Article
  15. Article
  16. Article
  17. Microtubule-based force generation.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2017
    Review
  18. Article
  19. Review
  20. Mitosis.Cold Spring Harbor perspectives in biology · 2016
    Review
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 at 4 institutions in 2 countries.

J Richard McIntoshDepartment of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309, USA. richard.mcintosh@colorado.edu
Vladimir Volkov
Fazly I Ataullakhanov
Ekaterina L Grishchuk
Center for Theoretical Problems of Physicochemical Pharmacology · RUFederal State Institution Hematology Research Center · RUUniversity of Colorado Boulder · USUniversity of Pennsylvania · US

Funding

WORKSHOPS AND TRAINING FOR IMAGE ANALYSIS USING IMODP41RR000592 · NCRR · UNIVERSITY OF COLORADO AT BOULDER · PI BASS, PETER W. · 1985 to 2011
$11.9M
NCRR NIH HHS P41 RR000592NCRR NIH HHS RR000592NIGMS NIH HHS GM033287
6 · The paper itself

Abstract

The motions of mitotic chromosomes are complex and show considerable variety across species. A wealth of evidence supports the idea that microtubule-dependent motor enzymes contribute to this variation and are important both for spindle formation and for the accurate completion of chromosome segregation. Motors that walk towards the spindle pole are, however, dispensable for at least some poleward movements of chromosomes in yeasts, suggesting that depolymerizing spindle microtubules can generate mitotic forces in vivo. Tubulin protofilaments that flare outward in association with microtubule shortening may be the origin of such forces, because they can move objects that are appropriately attached to a microtubule wall. For example, some kinetochore-associated proteins can couple experimental objects, such as microspheres, to shortening microtubules in vitro, moving them over many micrometers. Here, we review recent evidence about such phenomena, highlighting the force-generation mechanisms and different coupling strategies. We also consider bending filaments of the tubulin-like protein FtsZ, which form rings girding bacteria at their sites of cytokinesis. Mechanical similarities between these force-generation systems suggest a deep phylogenetic relationship between tubulin depolymerization in eukaryotic mitosis and FtsZ-mediated ring contraction in bacteria.

Indexed as

AnimalsBacteriaHumansMicrotubulesMitosisProtein MultimerizationTubulinTubulin

Identifiers

PMID20930138
PMCPMC2959111
OpenAlexW2005389292

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.