Evidence map›Paper›PMID 26234155›Full record

ArticleCell2015

Mechanistic Origin of Microtubule Dynamic Instability and Its Modulation by EB Proteins.

Rui Zhang, Gregory M Alushin, Alan Brown, Eva Nogales

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 280 papers.

0numbers the graph read from it
0cells of the map it votes in
280citing papers in PubMed
26.3field-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

280 citing papers in PubMed, 478 citations in OpenAlex.

  1. Review
  2. Article
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  13. A cryo-EM processing pipeline for microtubules using CryoSPARC.Acta crystallographica. Section D, Structural biology · 2026
    Article
  14. Article
  15. Article
  16. Review
  17. Degradation of the Molecular Basis of Life During the Aging Process.International journal of molecular sciences · 2026
    Review
  18. Article
  19. Article
  20. The microtubule GTP-tubulin cap size is modulated during cell division.bioRxiv : the preprint server for biology · 2026
    Article

220 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

4 authors at 4 institutions in 2 countries.

Rui ZhangLife Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Gregory M AlushinBiophysics Graduate Program, University of California, Berkeley, Berkeley, CA 94720, USA.
Alan BrownMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Eva NogalesLife Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA 94720, USA. Electronic address: enogales@lbl.gov.
Howard Hughes Medical Institute · USLawrence Berkeley National Laboratory · USMRC Laboratory of Molecular Biology · GBUniversity of California, Berkeley · US

Funding

TUBULIN STRUCTURE BY ELECTRON CRYSTALLOGRAPHYP01GM051487 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI CATE, JAMIE H · 1994 to 2018
$27.6M
MOLECULAR BIOPHYSICS TRAINING GRANTT32GM008295 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HURLEY, JAMES H, WEMMER, DAVID E · 1989 to 2022
$8.1M
Howard Hughes Medical InstituteMedical Research Council MC_U105184332NIGMS NIH HHS GM051487NIGMS NIH HHS P01 GM051487NIGMS NIH HHS T32 GM008295
6 · The paper itself

Abstract

Microtubule (MT) dynamic instability is driven by GTP hydrolysis and regulated by microtubule-associated proteins, including the plus-end tracking end-binding protein (EB) family. We report six cryo-electron microscopy (cryo-EM) structures of MTs, at 3.5 Å or better resolution, bound to GMPCPP, GTPγS, or GDP, either decorated with kinesin motor domain after polymerization or copolymerized with EB3. Subtle changes around the E-site nucleotide during hydrolysis trigger conformational changes in α-tubulin around an "anchor point," leading to global lattice rearrangements and strain generation. Unlike the extended lattice of the GMPCPP-MT, the EB3-bound GTPγS-MT has a compacted lattice that differs in lattice twist from that of the also compacted GDP-MT. These results and the observation that EB3 promotes rapid hydrolysis of GMPCPP suggest that EB proteins modulate structural transitions at growing MT ends by recognizing and promoting an intermediate state generated during GTP hydrolysis. Our findings explain both EBs end-tracking behavior and their effect on microtubule dynamics.

Indexed as

Amino Acid SequenceAnimalsCryoelectron MicroscopyCrystallography, X-RayMicrotubule-Associated ProteinsMicrotubulesModels, MolecularMolecular Sequence DataSequence AlignmentSus scrofaMicrotubule-Associated Proteins

Identifiers

PMID26234155
PMCPMC4537847
OpenAlexW1785817244

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.