Evidence map›Paper›PMID 19802390›Full record

ArticlePloS one2009

Rules governing selective protein carbonylation.

Etienne Maisonneuve, Adrien Ducret, Pierre Khoueiry, Sabrina Lignon, Sonia Longhi, Emmanuel Talla, Sam Dukan

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

62 citing papers in PubMed, 142 citations in OpenAlex.

  1. Chemical Carbonylation of Arginine in Peptides and Proteins.Journal of the American Chemical Society · 2025
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  8. Chemiexcitation: Mammalian Photochemistry in the DarkPhotochemistry and photobiology · 2023
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  14. Functionalized AuCommunications chemistry · 2021
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  16. Methionine Redox Homeostasis in Protein Quality Control.Frontiers in molecular biosciences · 2021
    Review
  17. Dienone Compounds: Targets and Pharmacological Responses.Journal of medicinal chemistry · 2020
    Article
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  20. Proteomic analysis of the monkey hippocampus for elucidating ischemic resistance.Journal of clinical biochemistry and nutrition · 2020
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2 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

7 authors at 3 institutions in 1 country.

Etienne MaisonneuveLaboratoire de Chimie Bactérienne - Aix Marseille Université - UPR 9043-CNRS, 31, Chemin Joseph Aiguier, Marseille, France.
Adrien Ducret
Pierre Khoueiry
Sabrina Lignon
Sonia Longhi
Emmanuel Talla
Sam Dukan
Centre National de la Recherche Scientifique · FRAix-Marseille Université · FRArchitecture et Fonction des Macromolécules Biologiques · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundCarbonyl derivatives are mainly formed by direct metal-catalysed oxidation (MCO) attacks on the amino-acid side chains of proline, arginine, lysine and threonine residues. For reasons unknown, only some proteins are prone to carbonylation. METHODOLOGY/PRINCIPAL

findingswe used mass spectrometry analysis to identify carbonylated sites in: BSA that had undergone in vitro MCO, and 23 carbonylated proteins in Escherichia coli. The presence of a carbonylated site rendered the neighbouring carbonylatable site more prone to carbonylation. Most carbonylated sites were present within hot spots of carbonylation. These observations led us to suggest rules for identifying sites more prone to carbonylation. We used these rules to design an in silico model (available at http://www.lcb.cnrs-mrs.fr/CSPD/), allowing an effective and accurate prediction of sites and of proteins more prone to carbonylation in the E. coli proteome. CONCLUSIONS/SIGNIFICANCE: We observed that proteins evolve to either selectively maintain or lose predicted hot spots of carbonylation depending on their biological function. As our predictive model also allows efficient detection of carbonylated proteins in Bacillus subtilis, we believe that our model may be extended to direct MCO attacks in all organisms.

Indexed as

Protein CarbonylationAmino Acid SequenceArginineBacillus subtilisBiochemistryCarbonCatalysisEscherichia coliHumansLysineMass SpectrometryMetalsMolecular Sequence DataOxygenProlineProteinsArginineCarbonLysineMetalsOxygenProlineProteinsSerum AlbuminThreonine

Identifiers

PMID19802390
PMCPMC2751825
OpenAlexW2031235464

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.