Evidence map›Paper›PMID 40299727›Full record

ArticleThe FEBS journal2025

On the synergy between myelin proteins P0, MBP, and P2 in peripheral nerve major dense line formation.

Oda C Krokengen, Arne Raasakka, Martin Berg Klenow, Antara Pal, Øystein Hetland, Anna Mularski, Salla Ruskamo, Jan Skov Pedersen, Adam Cohen Simonsen, Petri Kursula

Abstract read
In one paragraph

Article in The FEBS journal, 2025. 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. Review
  2. 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

10 authors.

Oda C KrokengenDepartment of Biomedicine, University of Bergen, Norway.
Arne RaasakkaDepartment of Biomedicine, University of Bergen, Norway.ORCID https://orcid.org/0000-0002-9443-9959
Martin Berg KlenowDepartment of Physics, Chemistry and Pharmacy, University of Southern Denmark, Odense, Denmark.
Antara PalDepartment of Chemistry, Interdisciplinary Nanoscience Center, Aarhus University, Denmark.
Øystein HetlandDepartment of Biomedicine, University of Bergen, Norway.
Anna MularskiDepartment of Physics, Chemistry and Pharmacy, University of Southern Denmark, Odense, Denmark.
Salla RuskamoFaculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Finland.
Jan Skov PedersenDepartment of Chemistry, Interdisciplinary Nanoscience Center, Aarhus University, Denmark.
Adam Cohen SimonsenDepartment of Physics, Chemistry and Pharmacy, University of Southern Denmark, Odense, Denmark.
Petri KursulaDepartment of Biomedicine, University of Bergen, Norway.ORCID https://orcid.org/0000-0001-8529-3751

Funding

Formas 2019-02496Horizon 2020 Framework Programme MOSBRI-2022-137Jane and Aatos Erkko FoundationNorges Forskningsråd 245828Norges Forskningsråd 245922Norges Forskningsråd 324877Swedish Governmental Agency for Innovation Systems 2018-04969Swedish Research Council 2018-07152University of Bergen (Norway)
6 · The paper itself

Abstract

The proper formation and function of the myelin sheath, a proteolipid membrane multilayer, relies on the coordinated action of several key myelin proteins. We studied how proteins from the peripheral myelin cytoplasmic apposition-myelin basic protein (MBP), the cytoplasmic tail of myelin protein zero (P0ct), and peripheral myelin protein 2 (P2)-interact with each other and with myelin-like membranes using various techniques, such as small-angle X-ray diffraction, differential scanning calorimetry (DSC), surface plasmon resonance (SPR), and electron and live epifluorescence microscopy. DSC revealed changes in lipid interactions depending on the protein combination, with altered membrane fluidity and stability. These results were supported by SPR, which indicated that the myelin proteins may compete for membrane surface binding. Analysis of the Bragg peaks induced by the myelin proteins in lipidic environments showed both lamellar and nonlamellar phases in protein-lipid complexes, indicating the formation of nanoscale structures that may be relevant for myelin assembly. Microscopy experiments showed the formation of new membrane structures with each of the proteins separately and together. Our data indicate both synergy and competition between the three main proteins residing in the peripheral nervous system myelin major dense line. The observed direct effects of myelin proteins on lipid membrane structure and properties may be relevant to their function in myelinating cells as well as their role in myelin disorders.

Indexed as

Myelin Basic ProteinMyelin P0 ProteinMyelin P2 ProteinMyelin SheathPeripheral NervesAnimalsCalorimetry, Differential ScanningSurface Plasmon ResonanceX-Ray DiffractionMyelin Basic ProteinMyelin P0 ProteinMyelin P2 Proteinmolecular structuremultilayermyelinprotein–membrane interactionssynergy

Identifiers

PMID40299727
PMCPMC12326912

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.