Evidence map›Paper›PMID 32085570›Full record

ReviewCells2020

Flexible Players within the Sheaths: The Intrinsically Disordered Proteins of Myelin in Health and Disease.

Arne Raasakka, Petri Kursula

Erratum issuedOpen access · goldAbstract readReview
In one paragraph

Review in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  8. Electrical Forces Improve Memory in Old Age.Reviews of physiology, biochemistry and pharmacology · 2025
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  18. Emerging cellular themes in leukodystrophies.Frontiers in cell and developmental biology · 2022
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 2 countries.

Arne RaasakkaDepartment of Biomedicine, University of Bergen, Jonas Lies vei 91, NO-5009 Bergen, Norway.
Petri KursulaDepartment of Biomedicine, University of Bergen, Jonas Lies vei 91, NO-5009 Bergen, Norway.
University of Bergen · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myelin ensheathes selected axonal segments within the nervous system, resulting primarily in nerve impulse acceleration, as well as mechanical and trophic support for neurons. In the central and peripheral nervous systems, various proteins that contribute to the formation and stability of myelin are present, which also harbor pathophysiological roles in myelin disease. Many myelin proteins have common attributes, including small size, hydrophobic segments, multifunctionality, longevity, and regions of intrinsic disorder. With recent advances in protein biophysical characterization and bioinformatics, it has become evident that intrinsically disordered proteins (IDPs) are abundant in myelin, and their flexible nature enables multifunctionality. Here, we review known myelin IDPs, their conservation, molecular characteristics and functions, and their disease relevance, along with open questions and speculations. We place emphasis on classifying the molecular details of IDPs in myelin, and we correlate these with their various functions, including susceptibility to post-translational modifications, function in protein-protein and protein-membrane interactions, as well as their role as extended entropic chains. We discuss how myelin pathology can relate to IDPs and which molecular factors are potentially involved.

Indexed as

AnimalsHumansIntrinsically Disordered ProteinsMiceMultiple SclerosisMyelin ProteinsMyelin SheathPeripheral Nervous System DiseasesProtein FoldingProtein Interaction MapsProtein Processing, Post-TranslationalSignal TransductionIntrinsically Disordered ProteinsMyelin Proteinsintrinsically disordered proteinmultiple sclerosismyelinmyelinationperipheral neuropathiesprotein foldingprotein–membrane interactionprotein–protein interaction

Identifiers

PMID32085570
PMCPMC7072810
OpenAlexW3004220601

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.