Evidence map›Paper›PMID 32973451›Full record

ArticleFrontiers in cellular neuroscience2020

The CNS Myelin Proteome: Deep Profile and Persistence After Post-mortem Delay.

Olaf Jahn, Sophie B Siems, Kathrin Kusch, Dörte Hesse, Ramona B Jung, Thomas Liepold, Marina Uecker, Ting Sun, Hauke B Werner

Open access · goldAbstract read
In one paragraph

Article in Frontiers in cellular neuroscience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed, 1 pooled it
4.5field-weighted citation impact, top 4% 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

52 citing papers in PubMed, 1 synthesis or guideline pooled it, 95 citations in OpenAlex.

  1. Pooled it
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  3. A canineProceedings of the National Academy of Sciences of the United States of America · 2026
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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

9 authors at 1 institution in 1 country.

Olaf JahnProteomics Group, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
Sophie B SiemsDepartment of Neurogenetics, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
Kathrin KuschDepartment of Neurogenetics, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
Dörte HesseProteomics Group, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
Ramona B JungDepartment of Neurogenetics, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
Thomas LiepoldProteomics Group, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
Marina UeckerProteomics Group, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
Ting SunDepartment of Neurogenetics, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
Hauke B WernerDepartment of Neurogenetics, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
Max Planck Institute of Experimental Medicine · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myelin membranes are dominated by lipids while the complexity of their protein composition has long been considered to be low. However, numerous additional myelin proteins have been identified since. Here we revisit the proteome of myelin biochemically purified from the brains of healthy c56Bl/6N-mice utilizing complementary proteomic approaches for deep qualitative and quantitative coverage. By gel-free, label-free mass spectrometry, the most abundant myelin proteins PLP, MBP, CNP, and MOG constitute 38, 30, 5, and 1% of the total myelin protein, respectively. The relative abundance of myelin proteins displays a dynamic range of over four orders of magnitude, implying that PLP and MBP have overshadowed less abundant myelin constituents in initial gel-based approaches. By comparisons with published datasets we evaluate to which degree the CNS myelin proteome correlates with the mRNA and protein abundance profiles of myelin and oligodendrocytes. Notably, the myelin proteome displays only minor changes if assessed after a post-mortem delay of 6 h. These data provide the most comprehensive proteome resource of CNS myelin so far and a basis for addressing proteomic heterogeneity of myelin in mouse models and human patients with white matter disorders.

Indexed as

autopsycentral nervous system (CNS)demyelinationlabel-free proteomicsmyelin proteomeoligodendrocytepost-mortem delaytranscriptome

Identifiers

PMID32973451
PMCPMC7466725
OpenAlexW3066361405

What OpenQuestion holds

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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.