Evidence map›Paper›PMID 38424171›Full record

ArticleNature chemical biology2024

In situ analysis of osmolyte mechanisms of proteome thermal stabilization.

Monika Pepelnjak, Britta Velten, Nicolas Näpflin, Tatjana von Rosen, Umberto Capasso Palmiero, Jeong Hoon Ko, Heather D Maynard, Paolo Arosio, Eilika Weber-Ban, Natalie de Souza and 2 more

Abstract read
In one paragraph

Article in Nature chemical biology, 2024. 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. Trimethylamine-N-oxide: the microbial cue in immune-mediated disorders.Trends in endocrinology and metabolism: TEM · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Hydration ofMolecules (Basel, Switzerland) · 2024
    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

12 authors.

Monika PepelnjakDepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.ORCID 0000-0001-8502-1772
Britta VeltenDivision of Computational Genomics and Systems Genetics, German Cancer Research Center (DKFZ), Heidelberg, Germany.ORCID 0000-0002-8397-3515
Nicolas NäpflinDepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.ORCID 0000-0001-6845-7400
Tatjana von RosenDepartment of Biology, Institute of Molecular Biology & Biophysics, ETH Zurich, Zurich, Switzerland.
Umberto Capasso PalmieroDepartment of Chemistry and Applied Biosciences, Institute of Chemical and Bioengineering, ETH Zurich, Zurich, Switzerland.
Jeong Hoon KoDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA, USA.ORCID 0000-0003-2000-3789
Heather D MaynardDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA, USA.ORCID 0000-0003-3692-6289
Paolo ArosioDepartment of Chemistry and Applied Biosciences, Institute of Chemical and Bioengineering, ETH Zurich, Zurich, Switzerland.ORCID 0000-0002-2740-1205
Eilika Weber-BanDepartment of Biology, Institute of Molecular Biology & Biophysics, ETH Zurich, Zurich, Switzerland.ORCID 0000-0002-5773-9274
Natalie de SouzaDepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Wolfgang HuberGenome Biology Unit, European Molecular Biological Laboratory, Heidelberg, Germany.ORCID 0000-0002-0474-2218
Paola PicottiDepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland. picotti@imsb.biol.ethz.ch.ORCID 0000-0002-4109-3552

Funding

EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) 866004Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (Swiss National Science Foundation) 51NF40_180541
6 · The paper itself

Abstract

Organisms use organic molecules called osmolytes to adapt to environmental conditions. In vitro studies indicate that osmolytes thermally stabilize proteins, but mechanisms are controversial, and systematic studies within the cellular milieu are lacking. We analyzed Escherichia coli and human protein thermal stabilization by osmolytes in situ and across the proteome. Using structural proteomics, we probed osmolyte effects on protein thermal stability, structure and aggregation, revealing common mechanisms but also osmolyte- and protein-specific effects. All tested osmolytes (trimethylamine N-oxide, betaine, glycerol, proline, trehalose and glucose) stabilized many proteins, predominantly via a preferential exclusion mechanism, and caused an upward shift in temperatures at which most proteins aggregated. Thermal profiling of the human proteome provided evidence for intrinsic disorder in situ but also identified potential structure in predicted disordered regions. Our analysis provides mechanistic insight into osmolyte function within a complex biological matrix and sheds light on the in situ prevalence of intrinsically disordered regions.

Indexed as

Escherichia coliProtein StabilityProteomeBetaineEscherichia coli ProteinsGlucoseGlycerolHumansMethylaminesProlineProteomicsTemperatureTrehaloseBetaineEscherichia coli ProteinsGlucoseGlycerolMethylaminesProlineProteomeTrehalosetrimethyloxamine

Identifiers

PMID38424171
PMCPMC11288892

What Socratic 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 Socratic graph.