Evidence map›Paper›PMID 41745748›Full record

ArticleToxins2026

ADP-Ribosylation of Cytidine: A Novel Nucleic Acid Modification Reversed by NADAR Hydrolases.

Petra Mikolčević, Andrea Hloušek-Kasun, Marion Schuller, Yang Lu, Elena Pirović, Ivan Ahel, Andreja Mikoč

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Toxins, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Petra MikolčevićDivision of Molecular Biology, Ruđer Bošković Institute, 10000 Zagreb, Croatia.
Andrea Hloušek-KasunInstitute of Chemistry, University of Graz, 8010 Graz, Austria.
Marion SchullerMax Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Yang LuSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Elena PirovićDivision of Molecular Biology, Ruđer Bošković Institute, 10000 Zagreb, Croatia.
Ivan AhelSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0002-9446-3756
Andreja MikočDivision of Molecular Biology, Ruđer Bošković Institute, 10000 Zagreb, Croatia.

Funding

Biotechnology and Biological Sciences Research Council BB/R007195/1Biotechnology and Biological Sciences Research Council BB/W016613/1Cancer Research UK C35050/A22284Wellcome Trust 210634Wellcome Trust 223107Wellcome Trust 302632
6 · The paper itself

Abstract

ADP-ribosylation of nucleic acids is a modification found in both eukaryotes and bacteria, where it contributes to genome maintenance but can also serve as a toxic mechanism used by bacterial toxins to disrupt essential cellular processes. This modification is catalysed by ADP-ribosyltransferases and can be reversed by antagonistic ADP-ribosylgylcohydrolase enzymes. To date, ADP-ribosylation of nucleic acid bases has been described only for adenosine, guanosine, and thymidine. Here we report the ADP-ribosylation of cytidine, catalysed by members of the pierisin family of bacterial toxins-ScARP (SCO5461) and Scabin. We also show that ADP-ribosylation of cytidine is reversible through removal by certain NADAR family proteins, including NADAR proteins from the bacterium

Indexed as

ADP-ribosylationcytidineNADARScARP/SCO5461SCO5665Streptomyces

Identifiers

PMID41745748
PMCPMC12945103

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.