Evidence map›Paper›PMID 34152627›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2021

Comparative Nucleosomal Reactivity of 5-Formyl-Uridine and 5-Formyl-Cytidine.

Leander Simon Runtsch, Michael Stadlmeier, Alexander Schön, Markus Müller, Thomas Carell

Open access · hybridAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Mitochondria regulate MR1 protein expression and produce self-metabolites that activate MR1-restricted T cells.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Comparative Nucleosomal Reactivity of 5-Formyl-Uridine and 5-Formyl-Cytidine.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021
    Article
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

5 authors at 1 institution in 1 country.

Leander Simon RuntschDepartment of Chemistry, Ludwig-Maximilians-Universität München, Butenandtstr. 5-13, 81377, Munich, Germany.
Michael StadlmeierDepartment of Chemistry, Ludwig-Maximilians-Universität München, Butenandtstr. 5-13, 81377, Munich, Germany.
Alexander SchönDepartment of Chemistry, Ludwig-Maximilians-Universität München, Butenandtstr. 5-13, 81377, Munich, Germany.
Markus MüllerDepartment of Chemistry, Ludwig-Maximilians-Universität München, Butenandtstr. 5-13, 81377, Munich, Germany.
Thomas CarellDepartment of Chemistry, Ludwig-Maximilians-Universität München, Butenandtstr. 5-13, 81377, Munich, Germany.ORCID http://orcid.org/0000-0001-7898-2831
Ludwig-Maximilians-Universität München · DE

Funding

Deutsche Forschungsgemeinschaft 325871075Deutsche Forschungsgemeinschaft 893547839H2020 European Research Council 741912H2020 Marie Skłodowska-Curie Actions 765266Verband der Chemischen Industrie DoktorandenstipendiumVolkswagen Foundation
6 · The paper itself

Abstract

5-Formyl-deoxyuridine (fdU) and 5-formyl-deoxycytidine (fdC) are formyl-containing nucleosides that are created by oxidative stress in differentiated cells. While fdU is almost exclusively an oxidative stress lesion formed from deoxythymidine (T), the situation for fdC is more complex. Next to formation as an oxidative lesion, it is particularly abundant in stem cells, where it is more frequently formed in an epigenetically important oxidation reaction performed by α-ketoglutarate dependent TET enzymes from 5-methyl-deoxycytidine (mdC). Recently, it was shown that genomic fdC and fdU can react with the ϵ-aminogroups of nucleosomal lysines to give Schiff base adducts that covalently link nucleosomes to genomic DNA. Here, we show that fdU features a significantly higher reactivity towards lysine side chains compared with fdC. This result shows that depending on the amounts of fdC and fdU, oxidative stress may have a bigger impact on nucleosome binding than epigenetics.

Indexed as

Epigenesis, GeneticNucleosomesDNAOxidation-ReductionUridineDNANucleosomesUridineDNA damageDNA histone adductsDNA repairepigeneticsnucleosomes

Identifiers

PMID34152627
PMCPMC8518870
OpenAlexW3173457774

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.