Evidence map›Paper›PMID 37749234›Full record

ArticleNature chemistry2023

The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibrils.

Miriam Linsenmeier, Lenka Faltova, Chiara Morelli, Umberto Capasso Palmiero, Charlotte Seiffert, Andreas M Küffner, Dorothea Pinotsi, Jiangtao Zhou, Raffaele Mezzenga, Paolo Arosio

Open access · hybridAbstract read
In one paragraph

Article in Nature chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
25.4field-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

96 citing papers in PubMed, 166 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. α-Synuclein Forms Distinct Micelle-Like Assemblies at Low Ionic Strengths.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. bioRxiv : the preprint server for biology · 2026
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

36 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

Miriam LinsenmeierDepartment of Chemistry and Applied Sciences, Institute for Chemical and Bioengineering, ETH Zurich, Zurich, Switzerland.
Lenka FaltovaDepartment of Chemistry and Applied Sciences, Institute for Chemical and Bioengineering, ETH Zurich, Zurich, Switzerland.
Chiara MorelliDepartment of Chemistry and Applied Sciences, Institute for Chemical and Bioengineering, ETH Zurich, Zurich, Switzerland.
Umberto Capasso PalmieroDepartment of Chemistry and Applied Sciences, Institute for Chemical and Bioengineering, ETH Zurich, Zurich, Switzerland.
Charlotte SeiffertDepartment of Chemistry and Applied Sciences, Institute for Chemical and Bioengineering, ETH Zurich, Zurich, Switzerland.ORCID 0000-0002-3080-0864
Andreas M KüffnerDepartment of Chemistry and Applied Sciences, Institute for Chemical and Bioengineering, ETH Zurich, Zurich, Switzerland.
Dorothea PinotsiScientific Center for Optical and Electron Microscopy, ETH Zurich, Zurich, Switzerland.
Jiangtao ZhouDepartment for Health Sciences and Technology, Institute of Food, Nutrition and Health, ETH Zurich, Zurich, Switzerland.ORCID 0000-0003-4248-2207
Raffaele MezzengaDepartment for Health Sciences and Technology, Institute of Food, Nutrition and Health, ETH Zurich, Zurich, Switzerland.ORCID 0000-0002-5739-2610
Paolo ArosioDepartment of Chemistry and Applied Sciences, Institute for Chemical and Bioengineering, ETH Zurich, Zurich, Switzerland. paolo.arosio@chem.ethz.ch.ORCID 0000-0002-2740-1205
ETH Zurich · CH

Funding

EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) 101002094
6 · The paper itself

Abstract

The maturation of liquid-like protein condensates into amyloid fibrils has been associated with several neurodegenerative diseases. However, the molecular mechanisms underlying this liquid-to-solid transition have remained largely unclear. Here we analyse the amyloid formation mediated by condensation of the low-complexity domain of hnRNPA1, a protein involved in amyotrophic lateral sclerosis. We show that phase separation and fibrillization are connected but distinct processes that are modulated by different regions of the protein sequence. By monitoring the spatial and temporal evolution of amyloid formation we demonstrate that the formation of fibrils does not occur homogeneously inside the droplets but is promoted at the interface of the condensates. We further show that coating the interface of the droplets with surfactant molecules inhibits fibril formation. Our results reveal that the interface of biomolecular condensates of hnRNPA1 promotes fibril formation, therefore suggesting interfaces as a potential novel therapeutic target against the formation of aberrant amyloids mediated by condensation.

Indexed as

AmyloidHeterogeneous Nuclear Ribonucleoprotein A1HumansProtein DomainsAmyloidHeterogeneous Nuclear Ribonucleoprotein A1hnRNPA1 protein, human

Identifiers

PMID37749234
PMCPMC10533390
OpenAlexW4387025523

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.