Evidence map›Paper›PMID 29234005›Full record

ArticleNature communications2017

Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase.

Jeannette Abplanalp, Mario Leutert, Emilie Frugier, Kathrin Nowak, Roxane Feurer, Jiro Kato, Hans V A Kistemaker, Dmitri V Filippov, Joel Moss, Amedeo Caflisch and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

81 citing papers in PubMed, 123 citations in OpenAlex.

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  11. Mitotic chromatin marking governs asymmetric segregation of DNA damage.bioRxiv : the preprint server for biology · 2024
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21 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

11 authors at 3 institutions in 3 countries.

Jeannette AbplanalpDepartment of Molecular Mechanisms of Disease, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.ORCID http://orcid.org/0000-0003-4516-5899
Mario LeutertDepartment of Molecular Mechanisms of Disease, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.ORCID http://orcid.org/0000-0001-7921-4017
Emilie FrugierDepartment of Biochemistry, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.
Kathrin NowakDepartment of Molecular Mechanisms of Disease, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.
Roxane FeurerDepartment of Molecular Mechanisms of Disease, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.
Jiro KatoLaboratory of Translational Research, National Heart, Lung and Blood Institute, NIH, Bethesda, MD, 20892-1590, USA.
Hans V A KistemakerLeiden Institute of Chemistry, Department of Bio-organic Synthesis, Leiden University, Einsteinweg 55, 2333 CC, Leiden, The Netherlands.
Dmitri V FilippovLeiden Institute of Chemistry, Department of Bio-organic Synthesis, Leiden University, Einsteinweg 55, 2333 CC, Leiden, The Netherlands.
Joel MossLaboratory of Translational Research, National Heart, Lung and Blood Institute, NIH, Bethesda, MD, 20892-1590, USA.
Amedeo CaflischDepartment of Biochemistry, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.
Michael O HottigerDepartment of Molecular Mechanisms of Disease, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland. michael.hottiger@dmmd.uzh.ch.ORCID http://orcid.org/0000-0002-7323-2270
University of Zurich · CHLeiden University · NLNational Heart Lung and Blood Institute · US

Funding

ADP-ribosylation CyclesZIAHL000659 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI MOSS, JOEL · 2009 to 2025
$29.8M
6 · The paper itself

Abstract

ADP-ribosylation is a posttranslational modification that exists in monomeric and polymeric forms. Whereas the writers (e.g. ARTD1/PARP1) and erasers (e.g. PARG, ARH3) of poly-ADP-ribosylation (PARylation) are relatively well described, the enzymes involved in mono-ADP-ribosylation (MARylation) have been less well investigated. While erasers for the MARylation of glutamate/aspartate and arginine have been identified, the respective enzymes with specificity for serine were missing. Here we report that, in vitro, ARH3 specifically binds and demodifies proteins and peptides that are MARylated. Molecular modeling and site-directed mutagenesis of ARH3 revealed that numerous residues are critical for both the mono- and the poly-ADP-ribosylhydrolase activity of ARH3. Notably, a mass spectrometric approach showed that ARH3-deficient mouse embryonic fibroblasts are characterized by a specific increase in serine-ADP-ribosylation in vivo under untreated conditions as well as following hydrogen peroxide stress. Together, our results establish ARH3 as a serine mono-ADP-ribosylhydrolase and as an important regulator of the basal and stress-induced ADP-ribosylome.

Indexed as

ADP-RibosylationAnimalsCell Line, TumorEnzyme AssaysGene Knockout TechniquesGlycoside HydrolasesHumansHydrogen PeroxideMass SpectrometryMiceModels, MolecularMutagenesis, Site-DirectedPoly (ADP-Ribose) Polymerase-1ProteomicsSerineADPRS protein, humanGlycoside HydrolasesHydrogen PeroxidePARP1 protein, humanPoly (ADP-Ribose) Polymerase-1Serine

Identifiers

PMID29234005
PMCPMC5727137
OpenAlexW2772487490

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.