Evidence map›Paper›PMID 25385183›Full record

ReviewThe Journal of cell biology2014

The contribution of αβ-tubulin curvature to microtubule dynamics.

Gary J Brouhard, Luke M Rice

Open access · bronzeAbstract readReview
In one paragraph

Review in The Journal of cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed
10.6field-weighted citation impact, top 1% 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

113 citing papers in PubMed, 207 citations in OpenAlex.

  1. Design and Pictet-Spengler enabled synthesis of carboxamide-substituted imidazo[1,2-Journal of enzyme inhibition and medicinal chemistry · 2026
    Article
  2. Article
  3. Review
  4. A cryo-EM processing pipeline for microtubules using CryoSPARC.Acta crystallographica. Section D, Structural biology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Imaging microtubule dynamics: A new frontier in biomarker development for neurodegenerative diseases.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Review
  9. Mechanisms of microtubule dynamics from single-molecule measurements.bioRxiv : the preprint server for biology · 2025
    Article
  10. Article
  11. Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

53 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 2 institutions in 2 countries.

Gary J BrouhardDepartment of Biology, McGill University, Montréal, Quebec, Canada H3A1B1 gary.brouhard@mcgill.ca luke.rice@utsouthwestern.edu.
Luke M RiceDepartment of Biophysics and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390 Department of Biophysics and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390 gary.brouhard@mcgill.ca luke.rice@utsouthwestern.edu.
McGill University · CAThe University of Texas Southwestern Medical Center · US

Funding

CONFORMATION & RECOGNITION IN MICROTUBLE DYNAMICSR01GM098543 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI RICE, LUKE W · 2011 to 2023
$4.2M
Canadian Institutes of Health Research MOP-111265NIGMS NIH HHS GM098543NIGMS NIH HHS R01 GM098543
6 · The paper itself

Abstract

Microtubules are dynamic polymers of αβ-tubulin that form diverse cellular structures, such as the mitotic spindle for cell division, the backbone of neurons, and axonemes. To control the architecture of microtubule networks, microtubule-associated proteins (MAPs) and motor proteins regulate microtubule growth, shrinkage, and the transitions between these states. Recent evidence shows that many MAPs exert their effects by selectively binding to distinct conformations of polymerized or unpolymerized αβ-tubulin. The ability of αβ-tubulin to adopt distinct conformations contributes to the intrinsic polymerization dynamics of microtubules. αβ-Tubulin conformation is a fundamental property that MAPs monitor and control to build proper microtubule networks.

Indexed as

AnimalsHumansMicrotubule-Associated ProteinsMicrotubulesProtein MultimerizationProtein StabilityProtein Structure, QuaternaryTubulinMicrotubule-Associated ProteinsTubulin

Identifiers

PMID25385183
PMCPMC4226729
OpenAlexW2036218826

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.