Evidence map›Paper›PMID 33022891›Full record

ArticleMolecular systems biology2020

Aggregation and disaggregation features of the human proteome.

Tomi A Määttä, Mandy Rettel, Sindhuja Sridharan, Dominic Helm, Nils Kurzawa, Frank Stein, Mikhail M Savitski

Abstract read
In one paragraph

Article in Molecular systems biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Article
  2. Global Analysis of Aggregation Determinants in Small Protein Domains.bioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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

7 authors.

Tomi A MäättäGenome Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
Mandy RettelProteomics Core Facility, European Molecular Biology Laboratory, Heidelberg, Germany.
Sindhuja SridharanGenome Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
Dominic HelmProteomics Core Facility, European Molecular Biology Laboratory, Heidelberg, Germany.
Nils KurzawaGenome Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.ORCID 0000-0002-7846-2817
Frank SteinProteomics Core Facility, European Molecular Biology Laboratory, Heidelberg, Germany.ORCID 0000-0001-9695-1692
Mikhail M SavitskiGenome Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.ORCID 0000-0003-2011-9247

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein aggregates have negative implications in disease. While reductionist experiments have increased our understanding of aggregation processes, the systemic view in biological context is still limited. To extend this understanding, we used mass spectrometry-based proteomics to characterize aggregation and disaggregation in human cells after non-lethal heat shock. Aggregation-prone proteins were enriched in nuclear proteins, high proportion of intrinsically disordered regions, high molecular mass, high isoelectric point, and hydrophilic amino acids. During recovery, most aggregating proteins disaggregated with a rate proportional to the aggregation propensity: larger loss in solubility was counteracted by faster disaggregation. High amount of intrinsically disordered regions were associated with faster disaggregation. However, other characteristics enriched in aggregating proteins did not correlate with the disaggregation rates. In addition, we analyzed changes in protein thermal stability after heat shock. Soluble remnants of aggregated proteins were more thermally stable compared with control condition. Therefore, our results provide a rich resource of heat stress-related protein solubility data and can foster further studies related to protein aggregation diseases.

Indexed as

Cell LineCell NucleusCell SurvivalFluorescent Antibody TechniqueHeat-Shock ResponseHistonesHumansMass SpectrometryMolecular WeightNuclear ProteinsProtein BiosynthesisProtein FoldingProteomeSolubilityHistonesNuclear ProteinsProteomeaggregationdisaggregationheat shockproteomicsthermal proteome profiling

Identifiers

PMID33022891
PMCPMC7538195

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.