Evidence map›Paper›PMID 29674711›Full record

ReviewNature reviews. Molecular cell biology2018

Microtubule dynamics: an interplay of biochemistry and mechanics.

Gary J Brouhard, Luke M Rice

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 266 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
266citing papers in PubMed, 1 pooled it
30.2field-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

266 citing papers in PubMed, 1 synthesis or guideline pooled it, 565 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. CLASP2 promotes repair of kinesin-1 damage to the microtubule lattice.bioRxiv : the preprint server for biology · 2026
    Article
  12. Article
  13. Tubulin flux at spastin-induced nanodamage sites regulates microtubule rescue frequency and EB1 lifetimes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  14. Article
  15. Article
  16. Chemical reviews · 2026
    Review
  17. Article
  18. Review
  19. Review
  20. A cryo-EM processing pipeline for microtubules using CryoSPARC.Acta crystallographica. Section D, Structural biology · 2026
    Article

206 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. gary.brouhard@mcgill.ca.ORCID 0000-0001-9101-1247
Luke M RiceDepartment of Biophysics, University of Texas Southwestern, Dallas, TX, USA. Luke.Rice@UTSouthwestern.edu.ORCID 0000-0001-6551-3307
McGill University · CASouthwestern Medical Center · US

Funding

CONFORMATION & RECOGNITION IN MICROTUBLE DYNAMICSR01GM098543 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI RICE, LUKE W · 2011 to 2023
$4.2M
NIGMS NIH HHS R01 GM098543
6 · The paper itself

Abstract

Microtubules are dynamic polymers of αβ-tubulin that are essential for intracellular organization, organelle trafficking and chromosome segregation. Microtubule growth and shrinkage occur via addition and loss of αβ-tubulin subunits, which are biochemical processes. Dynamic microtubules can also engage in mechanical processes, such as exerting forces by pushing or pulling against a load. Recent advances at the intersection of biochemistry and mechanics have revealed the existence of multiple conformations of αβ-tubulin subunits and their central role in dictating the mechanisms of microtubule dynamics and force generation. It has become apparent that microtubule-associated proteins (MAPs) selectively target specific tubulin conformations to regulate microtubule dynamics, and mechanical forces can also influence microtubule dynamics by altering the balance of tubulin conformations. Importantly, the conformational states of tubulin dimers are likely to be coupled throughout the lattice: the conformation of one dimer can influence the conformation of its nearest neighbours, and this effect can propagate over longer distances. This coupling provides a long-range mechanism by which MAPs and forces can modulate microtubule growth and shrinkage. These findings provide evidence that the interplay between biochemistry and mechanics is essential for the cellular functions of microtubules.

Indexed as

Biological TransportHumansMicrotubule-Associated ProteinsMicrotubulesOrganellesTubulinMicrotubule-Associated ProteinsTubulin

Identifiers

PMID29674711
PMCPMC6019280
OpenAlexW2799809717

What OpenQuestion holds

Textmetadata
LicenceTDM
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.