Evidence map›Paper›PMID 33073387›Full record

ArticleThe EMBO journal2020

Protein structure, amino acid composition and sequence determine proteome vulnerability to oxidation-induced damage.

Roger L Chang, Julian A Stanley, Matthew C Robinson, Joel W Sher, Zhanwen Li, Yujia A Chan, Ashton R Omdahl, Ruddy Wattiez, Adam Godzik, Sabine Matallana-Surget

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

23 citing papers in PubMed, 48 citations in OpenAlex.

  1. Eukaryogenesis From FECA to LECA: Radical Steps Along the Way.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
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  15. Thiol Reductases inAntioxidants (Basel, Switzerland) · 2022
    Review
  16. Review
  17. Water is a preservative of microbes.Microbial biotechnology · 2022
    Article
  18. Manganese Utilization inFrontiers in cell and developmental biology · 2022
    Review
  19. Review
  20. Review
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

10 authors at 4 institutions in 3 countries.

Roger L ChangDepartment of Systems Biology, Blavatnik Institute at Harvard Medical School, Boston, MA, USA.ORCID 0000-0003-1630-6584
Julian A StanleyDepartment of Systems Biology, Blavatnik Institute at Harvard Medical School, Boston, MA, USA.
Matthew C RobinsonDepartment of Systems Biology, Blavatnik Institute at Harvard Medical School, Boston, MA, USA.
Joel W SherDepartment of Systems Biology, Blavatnik Institute at Harvard Medical School, Boston, MA, USA.
Zhanwen LiDivision of Biomedical Sciences, University of California Riverside School of Medicine, Riverside, CA, USA.
Yujia A ChanDepartment of Systems Biology, Blavatnik Institute at Harvard Medical School, Boston, MA, USA.
Ashton R OmdahlDepartment of Systems Biology, Blavatnik Institute at Harvard Medical School, Boston, MA, USA.
Ruddy WattiezDepartment of Proteomics and Microbiology, Research Institute for Biosciences, University of Mons, Mons, Belgium.
Adam GodzikDivision of Biomedical Sciences, University of California Riverside School of Medicine, Riverside, CA, USA.
Sabine Matallana-SurgetDivision of Biological and Environmental Sciences, Faculty of Natural Sciences, University of Stirling, Stirling, UK.ORCID 0000-0002-6023-3215
Harvard University · USUniversity of California, Riverside · USUniversity of Mons · BEUniversity of Stirling · GB

Funding

Fonds De La Recherche Scientifique - FNRS (FNRS)Life Sciences Research Foundation (LSRF) GBMF 2550.04
6 · The paper itself

Abstract

Oxidative stress alters cell viability, from microorganism irradiation sensitivity to human aging and neurodegeneration. Deleterious effects of protein carbonylation by reactive oxygen species (ROS) make understanding molecular properties determining ROS susceptibility essential. The radiation-resistant bacterium Deinococcus radiodurans accumulates less carbonylation than sensitive organisms, making it a key model for deciphering properties governing oxidative stress resistance. We integrated shotgun redox proteomics, structural systems biology, and machine learning to resolve properties determining protein damage by γ-irradiation in Escherichia coli and D. radiodurans at multiple scales. Local accessibility, charge, and lysine enrichment accurately predict ROS susceptibility. Lysine, methionine, and cysteine usage also contribute to ROS resistance of the D. radiodurans proteome. Our model predicts proteome maintenance machinery, and proteins protecting against ROS are more resistant in D. radiodurans. Our findings substantiate that protein-intrinsic protection impacts oxidative stress resistance, identifying causal molecular properties.

Indexed as

AgingBacterial ProteinsComputational BiologyDeinococcusEscherichia coliHumansMachine LearningNeurodegenerative DiseasesOxidation-ReductionOxidative StressProtein ConformationProtein Processing, Post-TranslationalProteomeProteomicsReactive Oxygen SpeciesSequence Analysis, ProteinBacterial ProteinsProteomeReactive Oxygen SpeciesDeinococcus radioduransoxidative stressprotein carbonylradioresistancestructural systems biology

Identifiers

PMID33073387
PMCPMC7705453
OpenAlexW3092731370

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.