Evidence map›Paper›PMID 29320700›Full record

ArticleBiophysical journal2018

Role of Phosphorylation in Moesin Interactions with PIP

Quentin Lubart, Helene Vitet, Fabien Dalonneau, Aline Le Roy, Mathieu Kowalski, Morgane Lourdin, Christine Ebel, Marianne Weidenhaupt, Catherine Picart

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Charge-dependent interactions of monomeric and filamentous actin with lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. Review
  6. Article
  7. 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

9 authors at 4 institutions in 1 country.

Quentin LubartCNRS UMR 5628 (LMGP), University Grenoble Alpes, CEA, CNRS, Grenoble, France; Institut National Polytechnique de Grenoble, University Grenoble Alpes, CEA, CNRS, Grenoble, France.
Helene VitetCNRS UMR 5628 (LMGP), University Grenoble Alpes, CEA, CNRS, Grenoble, France; Institut National Polytechnique de Grenoble, University Grenoble Alpes, CEA, CNRS, Grenoble, France.
Fabien DalonneauCNRS UMR 5628 (LMGP), University Grenoble Alpes, CEA, CNRS, Grenoble, France; Institut National Polytechnique de Grenoble, University Grenoble Alpes, CEA, CNRS, Grenoble, France.
Aline Le RoyInstitut de Biologie Structurale (IBS), University Grenoble Alpes, CEA, CNRS, Grenoble, France.
Mathieu KowalskiCNRS UMR 5628 (LMGP), University Grenoble Alpes, CEA, CNRS, Grenoble, France; Institut National Polytechnique de Grenoble, University Grenoble Alpes, CEA, CNRS, Grenoble, France.
Morgane LourdinCNRS UMR 5628 (LMGP), University Grenoble Alpes, CEA, CNRS, Grenoble, France; Institut National Polytechnique de Grenoble, University Grenoble Alpes, CEA, CNRS, Grenoble, France.
Christine EbelInstitut de Biologie Structurale (IBS), University Grenoble Alpes, CEA, CNRS, Grenoble, France.
Marianne WeidenhauptCNRS UMR 5628 (LMGP), University Grenoble Alpes, CEA, CNRS, Grenoble, France; Institut National Polytechnique de Grenoble, University Grenoble Alpes, CEA, CNRS, Grenoble, France.
Catherine PicartCNRS UMR 5628 (LMGP), University Grenoble Alpes, CEA, CNRS, Grenoble, France; Institut National Polytechnique de Grenoble, University Grenoble Alpes, CEA, CNRS, Grenoble, France. Electronic address: catherine.picart@grenoble-inp.fr.
Commissariat à l'Énergie Atomique et aux Énergies Alternatives · FRCentre National de la Recherche Scientifique · FRUniversité Grenoble Alpes · FRCEA Grenoble · FR

Funding

European Research Council 259370
6 · The paper itself

Abstract

Moesin, a protein of the ezrin, radixin, and moesin family, which links the plasma membrane to the cytoskeleton, is involved in multiple physiological and pathological processes, including viral budding and infection. Its interaction with the plasma membrane occurs via a key phosphoinositide, the phosphatidyl(4,5)inositol-bisphosphate (PIP

Indexed as

Membranes, ArtificialMicrofilament ProteinsMicrotubulesPhosphatidylinositol 4,5-DiphosphatePhosphorylationProtein BindingProtein MultimerizationMembranes, ArtificialMicrofilament ProteinsmoesinPhosphatidylinositol 4,5-Diphosphate

Identifiers

PMID29320700
PMCPMC5912500
OpenAlexW2784329532

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.