Evidence map›Paper›PMID 15767580›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Force production by depolymerizing microtubules: a theoretical study.

M I Molodtsov, E L Grishchuk, A K Efremov, J R McIntosh, F I Ataullakhanov

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

50 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Microtubule dynamics are defined by conformations and stability of clustered protofilaments.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Responsive Supramolecular Polymers for Diagnosis and Treatment.International journal of molecular sciences · 2024
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Molecular photoswitches mediating the strain-driven disassembly of supramolecular tubules.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. Article
  15. Article
  16. Article
  17. Microtubule-based force generation.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2017
    Review
  18. Article
  19. Article
  20. Article
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

5 authors at 2 institutions in 2 countries.

M I MolodtsovDepartment of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309, USA.
E L Grishchuk
A K Efremov
J R McIntosh
F I Ataullakhanov
Institute of Theoretical and Experimental Biophysics · RUUniversity of Colorado Boulder · US

Funding

MICROTUBULE POLYMERIZATION AND DYNAMICS IN VIVOR01GM033787 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI MCINTOSH, JOHN RICHARD · 1985 to 2017
$6.5M
NIGMS NIH HHS GM 33787NIGMS NIH HHS R01 GM033787
6 · The paper itself

Abstract

Chromosome movement during mitosis is powered in part by energy released through the depolymerization of kinetochore microtubules (MTs). Strong but indirect evidence suggests the existence of a specialized coupling between kinetochores and MT plus ends that enables this transduction of chemical energy into mechanical work. Analysis of this phenomenon is important for learning how energy is stored within the MT lattice, how it is transduced, and how efficient the process can be, given coupling devices of different designs. Here we use a recently developed molecular-mechanical model of MTs to examine the mechanism of disassembly dependent force generation. Our approach is based on changes in tubulin dimer conformation that occur during MT disassembly. We find that all of the energy of polymerization-associated GTP hydrolysis can be stored as deformations of the longitudinal bonds between tubulin dimers, and its optimal use does not require the weakening of lateral bonds between dimers. Maximum utilization of this stored energy and, hence, the generation of the strongest possible force, is achieved by a protofilament power-stroke mechanism, so long as the coupling device does not restrict full dissociation of the lateral bonds between tubulin dimers.

Indexed as

Models, BiologicalBiomechanical PhenomenaDimerizationEnergy MetabolismGuanosine TriphosphateKinetochoresMicrotubulesProtein Structure, QuaternaryThermodynamicsTubulinGuanosine TriphosphateTubulin

Identifiers

PMID15767580
PMCPMC555502
OpenAlexW2110748079

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.