Noncovalent PAR Binding Guides Proteins to PARP1-Mediated PARylation.

Arthur Fischbach, Klara Bangert, Alexander Bürkle, Aswin Mangerich

Abstract read

In one paragraph

Article in ACS chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

–field-weighted citation impact

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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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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

4 authors.

Arthur FischbachMax Planck Institute for Biology of Ageing, Molecular Genetics of Ageing Department, 50931 Cologne, Germany.

Klara BangertMolecular Toxicology, Department of Biology, University of Konstanz, 78457 Konstanz, Germany.

Alexander BürkleMolecular Toxicology, Department of Biology, University of Konstanz, 78457 Konstanz, Germany.

Aswin MangerichMolecular Toxicology, Department of Biology, University of Konstanz, 78457 Konstanz, Germany.ORCID 0000-0001-9742-2338

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Poly(ADP-ribosyl)ation (PARylation) is a highly dynamic post-translational modification mediated by poly(ADP-ribose) polymerases (PARPs), influencing DNA damage response, transcription, and cell death. Previously, we showed that noncovalent interactions between PAR and the intrinsically disordered regions (IDPRs) of the p53 C-terminal domain (CTD) mediate the PARP1-dependent covalent modification of its target proteins. In this study, we test whether this mechanism also applies to noncovalent interactions involving the highly basic RGG IDPR of the FUS protein, as well as to domains lacking IDPRs, such as WWE, PBZ, and the macrodomain. We employed a chemical biology approach using a fluorescently labeled NAD

Indexed as

Poly Adenosine Diphosphate RibosePoly (ADP-Ribose) Polymerase-1Poly ADP RibosylationHumansProtein BindingProtein DomainsTumor Suppressor Protein p53PARP1 protein, humanPoly Adenosine Diphosphate RibosePoly (ADP-Ribose) Polymerase-1Tumor Suppressor Protein p53

Identifiers

PMID41824896

DOI10.1021/acschembio.5c01021

PMCPMC13097088

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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.