Evidence map›Paper›PMID 38450250›Full record

ArticleFrontiers in cell and developmental biology2024

A bipartite NLS motif mediates the nuclear import of

Zoltán Kovács, Csaba Bajusz, Anikó Szabó, Péter Borkúti, Balázs Vedelek, Réka Benke, Zoltán Lipinszki, Ildikó Kristó, Péter Vilmos

Open access · goldAbstract read
In one paragraph

Article in Frontiers in cell and developmental biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. ERM proteins support perinuclear actin rim formation.Frontiers in cell and developmental biology · 2025
    Article
  3. Article
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 2 institutions in 1 country.

Zoltán Kovács *HUN-REN Biological Research Centre, Szeged, Hungary.
Csaba Bajusz *HUN-REN Biological Research Centre, Szeged, Hungary.
Anikó SzabóHUN-REN Biological Research Centre, Szeged, Hungary.
Péter BorkútiHUN-REN Biological Research Centre, Szeged, Hungary.
Balázs VedelekHUN-REN Biological Research Centre, Szeged, Hungary.
Réka BenkeHUN-REN Biological Research Centre, Szeged, Hungary.
Zoltán LipinszkiHUN-REN Biological Research Centre, Institute of Biochemistry, MTA SZBK Lendület Laboratory of Cell Cycle Regulation, Szeged, Hungary.
Ildikó Kristó *HUN-REN Biological Research Centre, Szeged, Hungary.
Péter Vilmos *HUN-REN Biological Research Centre, Szeged, Hungary.
HUN-REN Szegedi Biológiai Kutatóközpont · HUInstitute of Biochemistry · HU

Funding

DROSOPHILA GENOMICS RESOURCE CENTERP40OD010949 · OD · TRUSTEES OF INDIANA UNIVERSITY · PI Andrew Zelhof · 2012 to 2026
$9.4M
NIH HHS P40 OD010949
6 · The paper itself

Abstract

The ERM protein family, which consists of three closely related proteins in vertebrates, ezrin, radixin, and moesin (ERM), is an ancient and important group of cytoplasmic actin-binding and organizing proteins. With their FERM domain, ERMs bind various transmembrane proteins and anchor them to the actin cortex through their C-terminal F-actin binding domain, thus they are major regulators of actin dynamics in the cell. ERMs participate in many fundamental cellular processes, such as phagocytosis, microvilli formation, T-cell activation and tumor metastasis. We have previously shown that, besides its cytoplasmic activities, the single ERM protein of

Indexed as

DrosophilaERMimportinmoesinNLSnucleusphosphorylationPIP2

Identifiers

PMID38450250
PMCPMC10915024
OpenAlexW4392002986

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.