Evidence map›Paper›PMID 32371922›Full record

ArticleScientific reports2020

Comprehensive analysis of posttranslational protein modifications in aging of subcellular compartments.

Tim Baldensperger, Michael Eggen, Jonas Kappen, Patrick R Winterhalter, Thorsten Pfirrmann, Marcus A Glomb

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

26 citing papers in PubMed, 51 citations in OpenAlex.

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  8. In-ovo imaging using ostrich eggs: biodistribution of F-18-FDG in ostrich embryos.Experimental biology and medicine (Maywood, N.J.) · 2025
    Article
  9. Review
  10. Therapy-Induced Senescence: Novel Approaches for Markers Identification.International journal of molecular sciences · 2024
    Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Biomarkers of aging.Science China. Life sciences · 2023
    Review
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  17. Article
  18. Article
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  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

6 authors at 1 institution in 1 country.

Tim BaldenspergerInstitute of Chemistry, Food Chemistry, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str. 2, 06120, Halle/Saale, Germany.
Michael EggenInstitute of Chemistry, Food Chemistry, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str. 2, 06120, Halle/Saale, Germany.
Jonas KappenInstitute of Chemistry, Food Chemistry, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str. 2, 06120, Halle/Saale, Germany.
Patrick R WinterhalterClinic for Heart Surgery, Martin-Luther-University Halle-Wittenberg, Ernst-Grube Str. 40, 06120, Halle/Saale, Germany.
Thorsten PfirrmannInstitute of Physiological Chemistry, Martin-Luther-University Halle-Wittenberg, Hollystr. 1, 06114, Halle/Saale, Germany.
Marcus A GlombInstitute of Chemistry, Food Chemistry, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str. 2, 06120, Halle/Saale, Germany. marcus.glomb@chemie.uni-halle.de.
Martin Luther University Halle-Wittenberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymatic and non-enzymatic posttranslational protein modifications by oxidation, glycation and acylation are key regulatory mechanisms in hallmarks of aging like inflammation, altered epigenetics and decline in proteostasis. In this study a mouse cohort was used to monitor changes of posttranslational modifications in the aging process. A protocol for the extraction of histones, cytosolic and mitochondrial proteins from mouse liver was developed and validated. In total, 6 lysine acylation structures, 7 advanced glycation endproducts, 6 oxidative stress markers, and citrullination were quantitated in proteins of subcellular compartments using HPLC-MS/MS. Methionine sulfoxide, acetylation, formylation, and citrullination were the most abundant modifications. Histone proteins were extraordinary high modified and non-enzymatic modifications accumulated in all subcellular compartments during the aging process. Compared to acetylation of histone proteins which gave between 350 and 305 µmol/mol leucine equivalents in young and old animals, modifications like acylation, glycation, and citrullination raised to 43%, 20%, and 18% of acetylation, respectively. On the other hand there was an age related increase of selected oxidative stress markers by up to 150%. The data and patterns measured in this study are mandatory for further studies and will strongly facilitate understanding of the molecular mechanisms in aging.

Indexed as

Cellular SenescenceProtein Processing, Post-TranslationalAcetylationChromatography, LiquidCitrullinationGlycosylationIntracellular SpaceLiverOrganellesOxidative StressSubcellular Fractions

Identifiers

PMID32371922
PMCPMC7200742
OpenAlexW3023749540

What OpenQuestion holds

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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.