Evidence map›Paper›PMID 38295165›Full record

ArticleScience advances2024

N-glycosylation as a eukaryotic protective mechanism against protein aggregation.

Ramon Duran-Romaña, Bert Houben, Matthias De Vleeschouwer, Nikolaos Louros, Matthew P Wilson, Gert Matthijs, Joost Schymkowitz, Frederic Rousseau

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
9.1field-weighted citation impact, top 1% 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

25 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  4. Revealing the Biological Effect of theJournal of the American Chemical Society · 2026
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  13. Journal of virology · 2025
    Article
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  16. Chemical Synthesis of Medin via a Removable Aggregation-Suppressing Linker.Journal of peptide science : an official publication of the European Peptide Society · 2025
    Article
  17. Review
  18. Article
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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

8 authors at 2 institutions in 1 country.

Ramon Duran-RomañaSwitch Laboratory, VIB Center for Brain and Disease Research, 3000 Leuven, Belgium.ORCID 0000-0002-2020-8672
Bert HoubenSwitch Laboratory, VIB Center for Brain and Disease Research, 3000 Leuven, Belgium.ORCID 0000-0002-6750-011X
Matthias De VleeschouwerSwitch Laboratory, VIB Center for Brain and Disease Research, 3000 Leuven, Belgium.ORCID 0000-0001-6889-1928
Nikolaos LourosSwitch Laboratory, VIB Center for Brain and Disease Research, 3000 Leuven, Belgium.ORCID 0000-0002-4030-1022
Matthew P WilsonLaboratory for Molecular Diagnosis, Center for Human Genetics, KU Leuven, 3000 Leuven, Belgium.
Gert MatthijsLaboratory for Molecular Diagnosis, Center for Human Genetics, KU Leuven, 3000 Leuven, Belgium.
Joost SchymkowitzSwitch Laboratory, VIB Center for Brain and Disease Research, 3000 Leuven, Belgium.ORCID 0000-0003-2020-0168
Frederic RousseauSwitch Laboratory, VIB Center for Brain and Disease Research, 3000 Leuven, Belgium.ORCID 0000-0002-9189-7399
VIB-KU Leuven Center for Brain & Disease Research · BEVIB-KU Leuven Center for Cancer Biology · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tendency for proteins to form aggregates is an inherent part of every proteome and arises from the self-assembly of short protein segments called aggregation-prone regions (APRs). While posttranslational modifications (PTMs) have been implicated in modulating protein aggregation, their direct role in APRs remains poorly understood. In this study, we used a combination of proteome-wide computational analyses and biophysical techniques to investigate the potential involvement of PTMs in aggregation regulation. Our findings reveal that while most PTM types are disfavored near APRs, N-glycosylation is enriched and evolutionarily selected, especially in proteins prone to misfolding. Experimentally, we show that N-glycosylation inhibits the aggregation of peptides in vitro through steric hindrance. Moreover, mining existing proteomics data, we find that the loss of N-glycans at the flanks of APRs leads to specific protein aggregation in Neuro2a cells. Our findings indicate that, among its many molecular functions, N-glycosylation directly prevents protein aggregation in higher eukaryotes.

Indexed as

Protein AggregatesProteomeGlycosylationPeptidesProtein Processing, Post-TranslationalPeptidesProtein AggregatesProteome

Identifiers

PMID38295165
PMCPMC10830103
OpenAlexW4391418240

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.