Evidence map›Paper›PMID 26273684›Full record

ArticleAnnals of clinical and translational neurology2015

Aggregation of MBP in chronic demyelination.

Kati Frid, Ofira Einstein, Yael Friedman-Levi, Orli Binyamin, Tamir Ben-Hur, Ruth Gabizon

Open access · goldAbstract read
In one paragraph

Article in Annals of clinical and translational neurology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

32 citing papers in PubMed, 56 citations in OpenAlex.

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  18. Synaptic tau: A pathological or physiological phenomenon?Acta neuropathologica communications · 2021
    Review
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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 at 1 institution in 1 country.

Kati FridDepartment of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital Jerusalem, 91120, Israel.
Ofira EinsteinDepartment of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital Jerusalem, 91120, Israel.
Yael Friedman-LeviDepartment of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital Jerusalem, 91120, Israel.
Orli BinyaminDepartment of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital Jerusalem, 91120, Israel.
Tamir Ben-HurDepartment of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital Jerusalem, 91120, Israel.
Ruth GabizonDepartment of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital Jerusalem, 91120, Israel.
Hadassah Academic College · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectivesMisfolding of key disease proteins to an insoluble state is associated with most neurodegenerative conditions, such as prion, Parkinson, and Alzheimer's diseases. In this work, and by studying animal models of multiple sclerosis, we asked whether this is also the case for myelin basic protein (MBP) in the late and neurodegenerative phases of demyelinating diseases.

methodsTo this effect, we tested whether MBP, an essential myelin component, present prion-like properties in animal models of MS, as is the case for Cuprizone-induced chronic demyelination or chronic phases of Experimental Autoimmune Encephalomyelitis (EAE).

resultsWe show here that while total levels of MBP were not reduced following extensive demyelination, part of these molecules accumulated thereafter as aggregates inside oligodendrocytes or around neuronal cells. In chronic EAE, MBP precipitated concomitantly with Tau, a marker of diverse neurodegenerative conditions, including MS. Most important, analysis of fractions from Triton X-100 floatation gradients suggest that the lipid composition of brain membranes in chronic EAE differs significantly from that of naïve mice, an effect which may relate to oxidative insults and subsequently prevent the appropriate insertion and compaction of new MBP in the myelin sheath, thereby causing its misfolding and aggregation.

interpretationPrion-like aggregation of MBP following chronic demyelination may result from an aberrant lipid composition accompanying this pathological status. Such aggregation of MBP may contribute to neuronal damage that occurs in the progressive phase of MS.

Identifiers

PMID26273684
PMCPMC4531054
OpenAlexW1532949410

What OpenQuestion holds

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LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

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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.