Evidence map›Paper›PMID 32284610›Full record

ArticleNature methods2020

Meltome atlas-thermal proteome stability across the tree of life.

Anna Jarzab, Nils Kurzawa, Thomas Hopf, Matthias Moerch, Jana Zecha, Niels Leijten, Yangyang Bian, Eva Musiol, Melanie Maschberger, Gabriele Stoehr and 15 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature methods, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 148 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
148citing papers in PubMed, 3 pooled it
12.6field-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

148 citing papers in PubMed, 3 syntheses or guidelines pooled it, 286 citations in OpenAlex.

  1. Pooled it
  2. 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
  3. Pooled it
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  13. Decoding the Hot-Mitochondrion Paradox.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  14. Mass spectrometry proteomics for studying mitostasis.Protein science : a publication of the Protein Society · 2026
    Review
  15. Article
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88 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

25 authors at 5 institutions in 3 countries.

Anna Jarzab *Chair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany.ORCID http://orcid.org/0000-0002-1059-9147
Nils Kurzawa *Genome Biology Unit, EMBL, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-7846-2817
Thomas Hopf *OmicScouts GmbH, Freising, Germany.
Matthias MoerchDepartment of Microbiology, Technical University of Munich, Freising, Germany.
Jana ZechaChair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany.ORCID http://orcid.org/0000-0002-8767-6294
Niels LeijtenBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands.ORCID http://orcid.org/0000-0002-7305-7249
Yangyang BianChair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany.
Eva MusiolMolecular Nutrition Unit, Technical University of Munich, Freising, Germany.
Melanie MaschbergerOmicScouts GmbH, Freising, Germany.
Gabriele StoehrOmicScouts GmbH, Freising, Germany.
Isabelle BecherGenome Biology Unit, EMBL, Heidelberg, Germany.ORCID http://orcid.org/0000-0001-7170-2235
Charlotte DalyChair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany.
Patroklos SamarasChair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany.ORCID http://orcid.org/0000-0001-6042-1585
Julia MergnerChair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany.
Britta SpanierChair of Nutritional Physiology, Technical University of Munich, Freising, Germany.
Angel AngelovDepartment of Microbiology, Technical University of Munich, Freising, Germany.ORCID http://orcid.org/0000-0002-9228-0817
Thilo WernerCellzome, Heidelberg, Germany.
Marcus BantscheffCellzome, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-8343-8977
Mathias WilhelmChair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany.ORCID http://orcid.org/0000-0002-9224-3258
Martin KlingensporMolecular Nutrition Unit, Technical University of Munich, Freising, Germany.
Simone LemeerBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands.ORCID http://orcid.org/0000-0002-6230-9471
Wolfgang LieblDepartment of Microbiology, Technical University of Munich, Freising, Germany.
Hannes HahneOmicScouts GmbH, Freising, Germany. hannes.hahne@omicscouts.com.ORCID http://orcid.org/0000-0003-3601-0051
Mikhail M SavitskiGenome Biology Unit, EMBL, Heidelberg, Germany. mikhail.savitski@embl.de.ORCID http://orcid.org/0000-0003-2011-9247
Bernhard KusterChair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany. kuster@tum.de.ORCID http://orcid.org/0000-0002-9094-1677
Technical University of Munich · DEEuropean Molecular Biology Organization · DELeibniz-Institute for Food Systems Biology at the Technical University of Munich · DEUtrecht University · NLOnslow Memorial Hospital · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have used a mass spectrometry-based proteomic approach to compile an atlas of the thermal stability of 48,000 proteins across 13 species ranging from archaea to humans and covering melting temperatures of 30-90 °C. Protein sequence, composition and size affect thermal stability in prokaryotes and eukaryotic proteins show a nonlinear relationship between the degree of disordered protein structure and thermal stability. The data indicate that evolutionary conservation of protein complexes is reflected by similar thermal stability of their proteins, and we show examples in which genomic alterations can affect thermal stability. Proteins of the respiratory chain were found to be very stable in many organisms, and human mitochondria showed close to normal respiration at 46 °C. We also noted cell-type-specific effects that can affect protein stability or the efficacy of drugs. This meltome atlas broadly defines the proteome amenable to thermal profiling in biology and drug discovery and can be explored online at http://meltomeatlas.proteomics.wzw.tum.de:5003/ and http://www.proteomicsdb.org.

Indexed as

Gene Expression RegulationTransition TemperatureAnimalsElectron Transport Chain Complex ProteinsHumansMitochondriaProkaryotic CellsProteinsProtein StabilityProteomeSoftwareSpecies SpecificityElectron Transport Chain Complex ProteinsProteinsProteome

Identifiers

PMID32284610
OpenAlexW3015921770

What OpenQuestion holds

Textmetadata
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.