Evidence map›Paper›PMID 39062914›Full record

ArticleInternational journal of molecular sciences2024

Structural Basis for the Interaction between the Ezrin FERM-Domain and Human Aquaporins.

Helin Strandberg, Carl Johan Hagströmer, Balder Werin, Markus Wendler, Urban Johanson, Susanna Törnroth-Horsefield

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Ion channels and actin: A tale of two friends.Histology and histopathology · 2025
    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.

Helin StrandbergDepartment of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden.ORCID 0009-0005-5592-4926
Carl Johan HagströmerDepartment of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden.ORCID 0000-0002-2088-7281
Balder WerinDepartment of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden.
Markus WendlerDepartment of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden.ORCID 0009-0008-8293-745X
Urban JohansonDepartment of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden.ORCID 0000-0001-8862-128X
Susanna Törnroth-HorsefieldDepartment of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden.ORCID 0000-0002-9435-8243

Funding

Crafoord Foundation 2018-0916Swedish Research Council 2019-06106Swedish Research Council for Environment Agricultural Sciences and Spatial Planning 2017-01463
6 · The paper itself

Abstract

The Ezrin/Radixin/Moesin (ERM) family of proteins act as cross-linkers between the plasma membrane and the actin cytoskeleton. This mechanism plays an essential role in processes related to membrane remodeling and organization, such as cell polarization, morphogenesis and adhesion, as well as in membrane protein trafficking and signaling pathways. For several human aquaporin (AQP) isoforms, an interaction between the ezrin band

Indexed as

Aquaporin 2Aquaporin 5Cytoskeletal ProteinsProtein BindingAquaporinsBinding SitesEzrinHumansMembrane ProteinsMicrofilament ProteinsModels, MolecularProtein DomainsAQP2 protein, humanAQP5 protein, humanAquaporin 2Aquaporin 5AquaporinsCytoskeletal ProteinsEzrinMembrane ProteinsMicrofilament ProteinsmoesinradixinAquaporin 2Aquaporin 5ezrinFERMin silico modellingmembrane protein traffickingmicroscale thermophoresisprotein–protein interactions

Identifiers

PMID39062914
PMCPMC11277499

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.