Evidence map›Paper›PMID 15722432›Full record

ArticleBiophysical journal2005

A molecular-mechanical model of the microtubule.

Maxim I Molodtsov, Elena A Ermakova, Emmanuil E Shnol, Ekaterina L Grishchuk, J Richard McIntosh, Fazly I Ataullakhanov

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

48 citing papers in PubMed, 121 citations in OpenAlex.

  1. 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
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  5. Review
  6. Beyond the GTP-cap: Elucidating the molecular mechanisms of microtubule catastrophe.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  7. Article
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  10. Article
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  15. Article
  16. Article
  17. Direct observation of individual tubulin dimers binding to growing microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Article
  19. TensorCalculator: exploring the evolution of mechanical stress in the CCMV capsid.Journal of physics. Condensed matter : an Institute of Physics journal · 2018
    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

6 authors at 4 institutions in 2 countries.

Maxim I MolodtsovMolecular, Cellular, and Developmental Biology Department, University of Colorado, Boulder, Colorado, USA.
Elena A Ermakova
Emmanuil E Shnol
Ekaterina L Grishchuk
J Richard McIntosh
Fazly I Ataullakhanov
University of Colorado Boulder · USInstitute of Mathematical Problems of Biology · RULomonosov Moscow State University · RUSemenov Institute of Chemical Physics · RU

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 GM33787NIGMS NIH HHS R01 GM033787
6 · The paper itself

Abstract

Dynamic instability of MTs is thought to be regulated by biochemical transformations within tubulin dimers that are coupled to the hydrolysis of bound GTP. Structural studies of nucleotide-bound tubulin dimers have recently provided a concrete basis for understanding how these transformations may contribute to MT dynamic instability. To analyze these ideas, we have developed a molecular-mechanical model in which structural and biochemical properties of tubulin are used to predict the shape and stability of MTs. From simple and explicit features of tubulin, we define bond energy relationships and explore the impact of their variations on integral MT properties. This modeling provides quantitative predictions about the GTP cap. It specifies important mechanical features underlying MT instability and shows that this property does not require GTP-hydrolysis to alter the strength of tubulin-tubulin bonds. The MT plus end is stabilized by at least two layers of GTP-tubulin subunits, whereas the minus end requires at least one; this and other differences between the ends are explained by asymmetric force balances. Overall, this model provides a new link between the biophysical characteristics of tubulin and the physiological behavior of MTs. It will also be useful in building a more complete description of MT dynamics and mechanics.

Indexed as

BiochemistryBiophysicsDimerizationGuanosine DiphosphateGuanosine TriphosphateHydrolysisMicrotubule-Associated ProteinsMicrotubule ProteinsMicrotubulesModels, MolecularModels, StatisticalModels, TheoreticalTubulinGuanosine DiphosphateGuanosine TriphosphateMicrotubule-Associated ProteinsMicrotubule ProteinsTubulin

Identifiers

PMID15722432
PMCPMC1305467
OpenAlexW2088603374

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.