Evidence map›Paper›PMID 30234483›Full record

ArticleeLife2018

Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner.

Feng-Ching Tsai, Aurelie Bertin, Hugo Bousquet, John Manzi, Yosuke Senju, Meng-Chen Tsai, Laura Picas, Stephanie Miserey-Lenkei, Pekka Lappalainen, Emmanuel Lemichez and 2 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

38 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. On the mechanism of ezrin activation.Biophysical journal · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. SARS-CoV-2 S assembly into virions facilitated by host ERM proteins.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. On the Mechanism of Ezrin Activation.bioRxiv : the preprint server for biology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Turn-On Protein Switches for Controlling Actin Binding in Cells.bioRxiv : the preprint server for biology · 2023
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review
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

12 authors at 3 institutions in 2 countries.

Feng-Ching Tsai *Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, Paris, France.ORCID https://orcid.org/0000-0002-6869-5254
Aurelie Bertin *Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, Paris, France.
Hugo BousquetSorbonne Université, Paris, France.
John ManziLaboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, Paris, France.
Yosuke SenjuProgram in Cell and Molecular Biology, Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
Meng-Chen TsaiUniversité Côte d'Azur, CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.
Laura PicasInstitut de Recherche en Infectiologie de Montpellier (IRIM), CNRS UMR 9004, Montpellier, France.
Stephanie Miserey-LenkeiSorbonne Université, Paris, France.
Pekka LappalainenProgram in Cell and Molecular Biology, Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
Emmanuel LemichezDépartement de Microbiologie, Unité des Toxines Bactériennes, Université Paris Descartes, Institut Pasteur, Paris, France.ORCID http://orcid.org/0000-0001-9080-7761
Evelyne Coudrier *Sorbonne Université, Paris, France.ORCID http://orcid.org/0000-0001-6011-8922
Patricia Bassereau *Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, Paris, France.ORCID http://orcid.org/0000-0002-8544-6778
Centre National de la Recherche Scientifique · FRUniversity of Helsinki · FIInstitut Pasteur · FR

Funding

Agence Nationale de la Recherche ANR-15-CE18-0016Agence Nationale de la Recherche ANR-15-CE18-0016-03European Molecular Biology Organization ALTF 1527-2014H2020 European Research Council 339847H2020 Marie Skłodowska-Curie Actions H2020-MSCA-IF-2014Human Frontier Science Program RGP0005/2016Investments for the Future LABEX SIGNALIFE ANR-11-LABX-0028-01
6 · The paper itself

Abstract

One challenge in cell biology is to decipher the biophysical mechanisms governing protein enrichment on curved membranes and the resulting membrane deformation. The ERM protein ezrin is abundant and associated with cellular membranes that are flat, positively or negatively curved. Using

Indexed as

Protein ConformationActinsCell MembraneCytoskeletal ProteinsEzrinLipid BilayersMutant ProteinsPhosphorylationProtein BindingProtein DomainsActinsCytoskeletal ProteinsEzrinLipid BilayersMutant Proteinscellular protrusionsezrinezrin-membrane interactionI-BAR domain proteinsmembrane curvaturephosphorylationphysics of living systems

Identifiers

PMID30234483
PMCPMC6167055
OpenAlexW2952164723

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.