Evidence map›Paper›PMID 31892536›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Proteome-wide observation of the phenomenon of life on the edge of solubility.

Giulia Vecchi, Pietro Sormanni, Benedetta Mannini, Andrea Vandelli, Gian Gaetano Tartaglia, Christopher M Dobson, F Ulrich Hartl, Michele Vendruscolo

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed, 3 pooled it
7.8field-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

75 citing papers in PubMed, 3 syntheses or guidelines pooled it, 167 citations in OpenAlex.

  1. Shift of the insoluble content of the proteome in the aging mouse brain.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Pooled it
  2. Pooled it
  3. Pooled it
  4. Protein rheostasis: quality control in metastable proteomes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  5. Translation fidelity mechanisms and their changes in aging.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Dissecting the effects of single amino acid substitutions in SARS-CoV-2 Mpro.Protein science : a publication of the Protein Society · 2025
    Article
  12. Candidate transmission survival genome ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Review
  15. Article
  16. Review
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  18. Article
  19. Leveraging a large language model to predict protein phase transition: A physical, multiscale, and interpretable approach.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Article

15 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

8 authors at 4 institutions in 4 countries.

Giulia VecchiCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom.
Pietro SormanniCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom.ORCID 0000-0002-6228-2221
Benedetta ManniniCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom.ORCID 0000-0001-6812-7348
Andrea VandelliGene Function and Evolution, Centre for Genomic Regulation (CRG), The Barcelona Institute of Science and Technology (BIST), 08003 Barcelona, Spain.
Gian Gaetano TartagliaDepartment of Neuroscience and Brain Technologies, Istituto Italiano di Tecnologia, 16163 Genoa, Italy.ORCID 0000-0001-7524-6310
Christopher M DobsonCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom.
F Ulrich HartlDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Michele VendruscoloCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom; mv245@cam.ac.uk.ORCID 0000-0002-3616-1610
University of Cambridge · GBCentre for Genomic Regulation · ESInstitució Catalana de Recerca i Estudis Avançats · ESMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To function effectively proteins must avoid aberrant aggregation, and hence they are expected to be expressed at concentrations safely below their solubility limits. By analyzing proteome-wide mass spectrometry data of

Indexed as

AgingAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsHomeostasisMass SpectrometryMolecular ChaperonesProtein AggregatesProtein FoldingProteomeSolubilityCaenorhabditis elegans ProteinsMolecular ChaperonesProtein AggregatesProteomeprotein aggregationprotein homeostasisprotein misfolding diseases

Identifiers

PMID31892536
PMCPMC6969518
OpenAlexW2998302976

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.