Evidence map›Paper›PMID 36814382›Full record

ArticleBiophysical journal2023

FERM domains recruit ample PI(4,5)P

Thomas Ehret, Tim Heißenberg, Svenja de Buhr, Camilo Aponte-Santamaría, Claudia Steinem, Frauke Gräter

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. On the mechanism of ezrin activation.Biophysical journal · 2026
    Article
  2. Article
  3. On the Mechanism of Ezrin Activation.bioRxiv : the preprint server for biology · 2025
    Article
  4. Review
  5. 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

6 authors.

Thomas EhretHeidelberg Institute for Theoretical Studies (HITS), Heidelberg, Germany.
Tim HeißenbergInstitute of Organic and Biomolecular Chemistry, University of Göttingen, Göttingen, Germany; Max Planck School Matter to Life, Heidelberg and Göttingen, Germany.
Svenja de BuhrHeidelberg Institute for Theoretical Studies (HITS), Heidelberg, Germany.
Camilo Aponte-SantamaríaHeidelberg Institute for Theoretical Studies (HITS), Heidelberg, Germany.
Claudia SteinemInstitute of Organic and Biomolecular Chemistry, University of Göttingen, Göttingen, Germany; Max Planck School Matter to Life, Heidelberg and Göttingen, Germany. Electronic address: csteine@gwdg.de.
Frauke GräterHeidelberg Institute for Theoretical Studies (HITS), Heidelberg, Germany; Max Planck School Matter to Life, Heidelberg and Göttingen, Germany; Interdisciplinary Center for Scientific Computing (IWR), Heidelberg University, Heidelberg, Germany. Electronic address: frauke.graeter@h-its.org.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The four-point-one ezrin-radixin-moesin homology (FERM) protein domain is a multifunctional protein-lipid binding site, constituting an integral part of numerous membrane-associated proteins. Its interaction with the lipid phosphatidylinositol-4,5-bisphosphate (PIP

Indexed as

FERM DomainsLipid BilayersBinding SitesCell MembraneFocal Adhesion Protein-Tyrosine KinasesPhosphatidylinositol 4,5-DiphosphateProtein BindingFocal Adhesion Protein-Tyrosine KinasesLipid BilayersPhosphatidylinositol 4,5-Diphosphate

Identifiers

PMID36814382
PMCPMC10111351

What OpenQuestion holds

Textmetadata
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.