Evidence map›Paper›PMID 37326024›Full record

ArticleNucleic acids research2023

Updated protein domain annotation of the PARP protein family sheds new light on biological function.

Marcin J Suskiewicz, Deeksha Munnur, Øyvind Strømland, Ji-Chun Yang, Laura E Easton, Chatrin Chatrin, Kang Zhu, Domagoj Baretić, Stéphane Goffinont, Marion Schuller and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
14.3field-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

43 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  3. NMR study of human macroPARPs domains:Biomolecular NMR assignments · 2026
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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

16 authors at 3 institutions in 3 countries.

Marcin J SuskiewiczCentre de Biophysique Moléculaire, CNRS UPR 4301, Orléans, France.ORCID 0000-0002-3279-6571
Deeksha MunnurSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Øyvind StrømlandSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Ji-Chun YangMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Laura E EastonMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Chatrin ChatrinSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Kang ZhuSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Domagoj BaretićSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Stéphane GoffinontCentre de Biophysique Moléculaire, CNRS UPR 4301, Orléans, France.
Marion SchullerSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Wing-Fung WuMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Jonathan M ElkinsCentre for Medicines Discovery, University of Oxford, Oxford OX3 7DQ, UK.
Dragana AhelSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Sumana SanyalSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
David NeuhausMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.ORCID 0000-0002-8561-7485
Ivan AhelSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0002-9446-3756
University of Oxford · GBMRC Laboratory of Molecular Biology · GBCentre National de la Recherche Scientifique · FR

Funding

Biotechnology and Biological Sciences Research Council BB/R007195/1Medical Research Council MC_U105178934Medical Research Council U105178934Wellcome Trust 210634Wellcome Trust 210634/Z/18/ZWellcome Trust 220776/Z/20/ZWellcome Trust 223107
6 · The paper itself

Abstract

AlphaFold2 and related computational tools have greatly aided studies of structural biology through their ability to accurately predict protein structures. In the present work, we explored AF2 structural models of the 17 canonical members of the human PARP protein family and supplemented this analysis with new experiments and an overview of recent published data. PARP proteins are typically involved in the modification of proteins and nucleic acids through mono or poly(ADP-ribosyl)ation, but this function can be modulated by the presence of various auxiliary protein domains. Our analysis provides a comprehensive view of the structured domains and long intrinsically disordered regions within human PARPs, offering a revised basis for understanding the function of these proteins. Among other functional insights, the study provides a model of PARP1 domain dynamics in the DNA-free and DNA-bound states and enhances the connection between ADP-ribosylation and RNA biology and between ADP-ribosylation and ubiquitin-like modifications by predicting putative RNA-binding domains and E2-related RWD domains in certain PARPs. In line with the bioinformatic analysis, we demonstrate for the first time PARP14's RNA-binding capability and RNA ADP-ribosylation activity in vitro. While our insights align with existing experimental data and are probably accurate, they need further validation through experiments.

Indexed as

Poly(ADP-ribose) Polymerase InhibitorsPoly(ADP-ribose) PolymerasesADP-RibosylationHumansProtein DomainsRNAPoly(ADP-ribose) Polymerase InhibitorsPoly(ADP-ribose) PolymerasesRNA

Identifiers

PMID37326024
PMCPMC10450202
OpenAlexW4380870307

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.