Evidence map›Paper›PMID 34116477›Full record

ReviewDNA repair2021

ADP-ribosylation of DNA and RNA.

Joséphine Groslambert, Evgeniia Prokhorova, Ivan Ahel

Open access · hybridAbstract readReview
In one paragraph

Review in DNA repair, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

68 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
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8 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

3 authors at 1 institution in 1 country.

Joséphine GroslambertSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.
Evgeniia ProkhorovaSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.
Ivan AhelSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom. Electronic address: ivan.ahel@path.ox.ac.uk.
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/R007195/1Cancer Research UK 22284Cancer Research UK C35050/A22284Wellcome Trust 101794Wellcome Trust 210634Wellcome Trust 210634/Z/18/Z
6 · The paper itself

Abstract

ADP-ribosylation is a chemical modification of macromolecules found across all domains of life and known to regulate a variety of cellular processes. Notably, it has a well-established role in the DNA damage response. While it was historically known as a post-translational modification of proteins, recent studies have shown that nucleic acids can also serve as substrates of reversible ADP-ribosylation. More precisely, ADP-ribosylation of DNA bases, phosphorylated DNA ends and phosphorylated RNA ends have been reported. We will discuss these three types of modification in details. In a variety of bacterial species, including Mycobacterium tuberculosis, ADP-ribosylation of thymidine has emerged as the mode of action of a toxin-antitoxin system named DarTG, with the resultant products perceived as DNA damage by the cell. On the other hand, mammalian DNA damage sensors PARP1, PARP2 and PARP3 were shown to ADP-ribosylate phosphorylated ends of double-stranded DNA in vitro. Additionally, TRPT1 and several PARP enzymes, including PARP10, can add ADP-ribose to the 5'-phosphorylated end of single-stranded RNA in vitro, representing a novel RNA capping mechanism. Together, these discoveries have led to the emergence of a new and exciting research area, namely DNA and RNA ADP-ribosylation, that is likely to have far-reaching implications for the fields of DNA repair, replication and epigenetics.

Indexed as

ADP-RibosylationDNA DamageDNA RepairAnimalsCell Cycle ProteinsDNAHumansPhosphorylationPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesProto-Oncogene ProteinsRNACell Cycle ProteinsDNAPARP10 protein, humanPARP1 protein, humanPARP2 protein, humanPARP3 protein, humanPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesProto-Oncogene ProteinsRNAADP-ribosylationDNA damage responseDNA modificationPARPRNA modification

Identifiers

PMID34116477
PMCPMC8385414
OpenAlexW3169751507

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.