Evidence map›Paper›PMID 22500803›Full record

ArticleCell2012

EBs recognize a nucleotide-dependent structural cap at growing microtubule ends.

Sebastian P Maurer, Franck J Fourniol, Gergő Bohner, Carolyn A Moores, Thomas Surrey

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 234 papers.

0numbers the graph read from it
0cells of the map it votes in
234citing papers in PubMed
14.9field-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

234 citing papers in PubMed, 397 citations in OpenAlex.

  1. Microtubule Engagement by the WD40-Containing Tail of Kinesin-4 KIF21B.bioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. 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
  6. Article
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  10. The microtubule GTP-tubulin cap size is modulated during cell division.bioRxiv : the preprint server for biology · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. 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
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

174 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

5 authors at 4 institutions in 2 countries.

Sebastian P MaurerCancer Research UK London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3LY, UK.
Franck J Fourniol
Gergő Bohner
Carolyn A Moores
Thomas Surrey
Cancer Research UK · GBEuropean Molecular Biology Laboratory · DEInstitute of Structural and Molecular Biology · GBThe Honourable Society of Lincoln's Inn · GB

Funding

Cancer Research UK 14256Medical Research Council MR/J000973/1Wellcome Trust WT079605Wellcome Trust WT085945
6 · The paper itself

Abstract

Growing microtubule ends serve as transient binding platforms for essential proteins that regulate microtubule dynamics and their interactions with cellular substructures. End-binding proteins (EBs) autonomously recognize an extended region at growing microtubule ends with unknown structural characteristics and then recruit other factors to the dynamic end structure. Using cryo-electron microscopy, subnanometer single-particle reconstruction, and fluorescence imaging, we present a pseudoatomic model of how the calponin homology (CH) domain of the fission yeast EB Mal3 binds to the end regions of growing microtubules. The Mal3 CH domain bridges protofilaments except at the microtubule seam. By binding close to the exchangeable GTP-binding site, the CH domain is ideally positioned to sense the microtubule's nucleotide state. The same microtubule-end region is also a stabilizing structural cap protecting the microtubule from depolymerization. This insight supports a common structural link between two important biological phenomena, microtubule dynamic instability and end tracking.

Indexed as

Amino Acid SequenceCryoelectron MicroscopyMicrotubule-Associated ProteinsMicrotubulesModels, MolecularMolecular Sequence DataProtein Structure, TertiarySchizosaccharomycesSchizosaccharomyces pombe ProteinsSequence AlignmentTubulinMal3 protein, S pombeMicrotubule-Associated ProteinsSchizosaccharomyces pombe ProteinsTubulin

Identifiers

PMID22500803
PMCPMC3368265
OpenAlexW2044820159

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.