Evidence map›Paper›PMID 31842403›Full record

ReviewCells2019

The Enigmatic Function of PARP1: From PARylation Activity to PAR Readers.

Tatiana Kamaletdinova, Zahra Fanaei-Kahrani, Zhao-Qi Wang

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
6.7field-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

92 citing papers in PubMed, 164 citations in OpenAlex.

  1. Trial
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  4. Article
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  10. Review
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  12. PARylation promotes acute kidney injuryActa pharmaceutica Sinica. B · 2025
    Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
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  19. Article
  20. Single-molecule analysis of PARP1-G-quadruplex interaction.bioRxiv : the preprint server for biology · 2025
    Article

32 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.

Tatiana KamaletdinovaLeibniz Institute on Aging-Fritz-Lipmann Institute (FLI), Beutenbergstrasse 11, 07745 Jena, Germany.
Zahra Fanaei-KahraniLeibniz Institute on Aging-Fritz-Lipmann Institute (FLI), Beutenbergstrasse 11, 07745 Jena, Germany.
Zhao-Qi WangLeibniz Institute on Aging-Fritz-Lipmann Institute (FLI), Beutenbergstrasse 11, 07745 Jena, Germany.ORCID 0000-0002-8336-3485
Leibniz Institute on Aging - Fritz Lipmann Institute (FLI) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Poly(ADP-ribosyl)ation (PARylation) is catalysed by poly(ADP-ribose) polymerases (PARPs, also known as ARTDs) and then rapidly removed by degrading enzymes. Poly(ADP-ribose) (PAR) is produced from PARylation and provides a delicate and spatiotemporal interaction scaffold for numerous target proteins. The PARylation system, consisting of PAR synthesizers and erasers and PAR itself and readers, plays diverse roles in the DNA damage response (DDR), DNA repair, transcription, replication, chromatin remodeling, metabolism, and cell death. Despite great efforts by scientists in biochemistry, cell and molecular biology, genetics, and pharmacology over the last five decades, the biology of PARPs and PARylation remains enigmatic. In this review, we summarize the current understanding of the biological function of PARP1 (ARTD1), the founding member of the PARP family, focusing on the inter-dependent or -independent nature of different functional domains of the PARP1 protein. We also discuss the readers of PAR, whose function may transduce signals and coordinate the cellular processes, which has recently emerged as a new research avenue for PARP biology. We aim to provide some perspective on how future research might disentangle the biology of PARylation by dissecting the structural and functional relationship of PARP1, a major effector of the PARPs family.

Indexed as

AnimalsChromatin Assembly and DisassemblyDNA DamageDNA RepairHumansPoly (ADP-Ribose) Polymerase-1Poly ADP RibosylationProtein DomainsSignal TransductionPoly (ADP-Ribose) Polymerase-1PARPAR binderPAR-binding motifPARP1PARylation activity

Identifiers

PMID31842403
PMCPMC6953017
OpenAlexW2995207917

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.