Evidence map›Paper›PMID 29706546›Full record

ArticleCell2018

Pervasive Protein Thermal Stability Variation during the Cell Cycle.

Isabelle Becher, Amparo Andrés-Pons, Natalie Romanov, Frank Stein, Maike Schramm, Florence Baudin, Dominic Helm, Nils Kurzawa, André Mateus, Marie-Therese Mackmull and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
11.5field-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

134 citing papers in PubMed, 246 citations in OpenAlex.

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  4. Mass spectrometry proteomics for studying mitostasis.Protein science : a publication of the Protein Society · 2026
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74 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

15 authors at 2 institutions in 1 country.

Isabelle BecherGenome Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
Amparo Andrés-PonsStructural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
Natalie RomanovStructural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
Frank SteinProteomics Core Facility, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
Maike SchrammGenome Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
Florence BaudinStructural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
Dominic HelmProteomics Core Facility, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
Nils KurzawaGenome Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
André MateusGenome Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
Marie-Therese MackmullStructural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
Athanasios TypasGenome Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
Christoph W MüllerStructural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
Peer BorkStructural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany; Max Delbrück Center for Molecular Medicine, 13125 Berlin, Germany; Molecular Medicine Partnership Unit, 69120 Heidelberg, Germany; Department of Bioinformatics, Biocenter, University of Würzburg, 97074 Würzburg, Germany. Electronic address: bork@embl.de.
Martin BeckStructural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany; Cell Biology and Biophysics Unit, European Molecular Biology Laboratory 69117 Heidelberg, Germany. Electronic address: martin.beck@embl.de.
Mikhail M SavitskiGenome Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany. Electronic address: mikhail.savitski@embl.de.
European Molecular Biology Laboratory · DEEuropean Molecular Biology Laboratory · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Quantitative mass spectrometry has established proteome-wide regulation of protein abundance and post-translational modifications in various biological processes. Here, we used quantitative mass spectrometry to systematically analyze the thermal stability and solubility of proteins on a proteome-wide scale during the eukaryotic cell cycle. We demonstrate pervasive variation of these biophysical parameters with most changes occurring in mitosis and G1. Various cellular pathways and components vary in thermal stability, such as cell-cycle factors, polymerases, and chromatin remodelers. We demonstrate that protein thermal stability serves as a proxy for enzyme activity, DNA binding, and complex formation in situ. Strikingly, a large cohort of intrinsically disordered and mitotically phosphorylated proteins is stabilized and solubilized in mitosis, suggesting a fundamental remodeling of the biophysical environment of the mitotic cell. Our data represent a rich resource for cell, structural, and systems biologists interested in proteome regulation during biological transitions.

Indexed as

Cell CycleChromatin Assembly and DisassemblyCluster AnalysisDNAHeLa CellsHot TemperatureHumansMass SpectrometryMitosisPhosphorylationProtein Processing, Post-TranslationalProtein StabilityProteomeProteomicsRNA Polymerase IISolubilityDNAProteomeRNA Polymerase IIcell cycleproteomicsthermal proteome profiling

Identifiers

PMID29706546
PMCPMC5998384
OpenAlexW2800980602

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.