Evidence map›Paper›PMID 29480802›Full record

ArticleeLife2018

Serine is the major residue for ADP-ribosylation upon DNA damage.

Luca Palazzo, Orsolya Leidecker, Evgeniia Prokhorova, Helen Dauben, Ivan Matic, Ivan Ahel

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 160 papers.

0numbers the graph read from it
0cells of the map it votes in
160citing papers in PubMed
10.9field-weighted citation impact, top 1% 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

160 citing papers in PubMed, 237 citations in OpenAlex.

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100 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

6 authors at 2 institutions in 2 countries.

Luca Palazzo *Sir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.ORCID http://orcid.org/0000-0002-5556-5549
Orsolya Leidecker *Max Planck Institute for Biology of Ageing, Cologne, Germany.ORCID http://orcid.org/0000-0001-5315-014X
Evgeniia Prokhorova *Sir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.ORCID http://orcid.org/0000-0002-5467-5586
Helen DaubenMax Planck Institute for Biology of Ageing, Cologne, Germany.
Ivan MaticMax Planck Institute for Biology of Ageing, Cologne, Germany.ORCID http://orcid.org/0000-0003-0170-7991
Ivan AhelSir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.ORCID http://orcid.org/0000-0002-9446-3756
Max Planck Institute for Biology of Ageing · DEUniversity of Oxford · GB

Funding

Cancer Research UK 22284Cancer Research UK C35050/A22284European Research Council 281739Marie Curie 657501Wellcome Trust 101794
6 · The paper itself

Abstract

Poly(ADP-ribose) polymerases (PARPs) are a family of enzymes that synthesise ADP-ribosylation (ADPr), a reversible modification of proteins that regulates many different cellular processes. Several mammalian PARPs are known to regulate the DNA damage response, but it is not clear which amino acids in proteins are the primary ADPr targets. Previously, we reported that ARH3 reverses the newly discovered type of ADPr (ADPr on serine residues; Ser-ADPr) and developed tools to analyse this modification (Fontana et al., 2017). Here, we show that Ser-ADPr represents the major fraction of ADPr synthesised after DNA damage in mammalian cells and that globally Ser-ADPr is dependent on HPF1, PARP1 and ARH3. In the absence of HPF1, glutamate/aspartate becomes the main target residues for ADPr. Furthermore, we describe a method for site-specific validation of serine ADP-ribosylated substrates in cells. Our study establishes serine as the primary form of ADPr in DNA damage signalling.

Indexed as

ADP-RibosylationDNA DamageCarrier ProteinsCell LineGlycoside HydrolasesHumansNuclear ProteinsPoly (ADP-Ribose) Polymerase-1SerineADPRS protein, humanCarrier ProteinsGlycoside HydrolasesHPF1 protein, humanNuclear ProteinsPARP1 protein, humanPoly (ADP-Ribose) Polymerase-1SerineADP-ribosylationARH3biochemistrychemical biologyDNA damageDNA repairenzymehumanPARP

Identifiers

PMID29480802
PMCPMC5837557
OpenAlexW2788939638

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.