Evidence map›Paper›PMID 37703374›Full record

ArticleScience advances2023

PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities.

Nina Đukić, Øyvind Strømland, Jonas Damgaard Elsborg, Deeksha Munnur, Kang Zhu, Marion Schuller, Chatrin Chatrin, Pulak Kar, Lena Duma, Osamu Suyari and 15 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
15.4field-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

46 citing papers in PubMed, 67 citations in OpenAlex.

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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

25 authors at 5 institutions in 5 countries.

Nina ĐukićSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0009-0004-6120-6421
Øyvind StrømlandSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0003-2841-4638
Jonas Damgaard ElsborgProteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.ORCID 0000-0002-1506-4280
Deeksha MunnurSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0003-0888-3859
Kang ZhuSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0003-2623-3331
Marion SchullerSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0002-1551-0359
Chatrin ChatrinSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0002-5666-3175
Pulak KarSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Lena DumaSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0003-4373-5106
Osamu SuyariSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0009-0008-3258-8722
Johannes Gregor Matthias RackSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0001-8341-6439
Domagoj BaretićSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0001-7049-3961
Dorian Richard Kenneth CrudgingtonSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0002-0716-0782
Joséphine GroslambertSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0002-3254-2854
Gerissa FowlerMedical Research Council Human Immunology Unit, Medical Research Council Weatherall Institute of Molecular Medicine, Radcliffe Department of Medicine, University of Oxford, Oxford OX3 9DS, UK.ORCID 0000-0001-9801-2613
Sven WijngaardenLeiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC Leiden, Netherlands.ORCID 0000-0002-6449-4113
Evgeniia ProkhorovaSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0002-5467-5586
Jan RehwinkelMedical Research Council Human Immunology Unit, Medical Research Council Weatherall Institute of Molecular Medicine, Radcliffe Department of Medicine, University of Oxford, Oxford OX3 9DS, UK.ORCID 0000-0003-3841-835X
Herwig SchülerCenter for Molecular Protein Science, Department of Chemistry, Lund University, 22100 Lund, Sweden.ORCID 0000-0003-4059-3501
Dmitri V FilippovLeiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC Leiden, Netherlands.ORCID 0000-0002-6978-7425
Sumana SanyalSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0002-6230-5366
Dragana AhelSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0002-7042-156X
Michael L NielsenProteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.ORCID 0000-0002-0067-9039
Rebecca SmithSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0002-1658-5635
Ivan AhelSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.ORCID 0000-0002-9446-3756
University of Oxford · GBLeiden University · NLUniversity of Copenhagen · DKLund University · SEUniversity of Exeter · GB

Funding

Medical Research Council MC_UU_00008/8Medical Research Council MR/V033417/1Medical Research Council MR/X007472/1Wellcome Trust 210634/Z/18/Z
6 · The paper itself

Abstract

PARP14 is a mono-ADP-ribosyl transferase involved in the control of immunity, transcription, and DNA replication stress management. However, little is known about the ADP-ribosylation activity of PARP14, including its substrate specificity or how PARP14-dependent ADP-ribosylation is reversed. We show that PARP14 is a dual-function enzyme with both ADP-ribosyl transferase and hydrolase activity acting on both protein and nucleic acid substrates. In particular, we show that the PARP14 macrodomain 1 is an active ADP-ribosyl hydrolase. We also demonstrate hydrolytic activity for the first macrodomain of PARP9. We reveal that expression of a PARP14 mutant with the inactivated macrodomain 1 results in a marked increase in mono(ADP-ribosyl)ation of proteins in human cells, including PARP14 itself and antiviral PARP13, and displays specific cellular phenotypes. Moreover, we demonstrate that the closely related hydrolytically active macrodomain of SARS2 Nsp3, Mac1, efficiently reverses PARP14 ADP-ribosylation in vitro and in cells, supporting the evolution of viral macrodomains to counteract PARP14-mediated antiviral response.

Indexed as

COVID-19TransferasesAntiviral AgentsHumansHydrolasesPoly(ADP-ribose) Polymerase InhibitorsPoly(ADP-ribose) PolymerasesAntiviral AgentsHydrolasesPARP14 protein, humanPoly(ADP-ribose) Polymerase InhibitorsPoly(ADP-ribose) PolymerasesTransferases

Identifiers

PMID37703374
PMCPMC10499325
OpenAlexW4386719093

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.