Evidence map›Paper›PMID 33894202›Full record

ArticleThe Journal of biological chemistry

Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions.

Yasin Pourfarjam, Zhijun Ma, Igor Kurinov, Joel Moss, In-Kwon Kim

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 56% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Review
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

5 authors at 3 institutions in 1 country.

Yasin PourfarjamDepartment of Chemistry, University of Cincinnati, Cincinnati, Ohio, USA.
Zhijun MaDepartment of Chemistry, University of Cincinnati, Cincinnati, Ohio, USA.
Igor KurinovDepartment of Chemistry and Chemical Biology, NE-CAT APS, Cornell University, Argonne, Illinois, USA.
Joel MossPulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, USA.
In-Kwon KimDepartment of Chemistry, University of Cincinnati, Cincinnati, Ohio, USA. Electronic address: kimiw@ucmail.uc.edu.
University of Cincinnati · USArgonne National Laboratory · USNational Institutes of Health · US

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI MALCOLM S. CAPEL · 2018 to 2026
$34.2M
ADP-ribosylation CyclesZIAHL000659 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI MOSS, JOEL · 2009 to 2025
$29.8M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
Reversal of residue-specific ADP-ribosylations by ADP-ribosyl-acceptor hydrolasesR01GM141226 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KIM, IN-KWON · 2021 to 2024
$1.4M
NIGMS NIH HHS P30 GM124165NIGMS NIH HHS R01 GM141226NIH HHS S10 OD021527
6 · The paper itself

Abstract

ADP-ribosylation is a reversible and site-specific post-translational modification that regulates a wide array of cellular signaling pathways. Regulation of ADP-ribosylation is vital for maintaining genomic integrity, and uncontrolled accumulation of poly(ADP-ribosyl)ation triggers a poly(ADP-ribose) (PAR)-dependent release of apoptosis-inducing factor from mitochondria, leading to cell death. ADP-ribosyl-acceptor hydrolase 3 (ARH3) cleaves PAR and mono(ADP-ribosyl)ation at serine following DNA damage. ARH3 is also a metalloenzyme with strong metal selectivity. While coordination of two magnesium ions (Mg

Indexed as

DNA DamageGlycoside HydrolasesHumansHydrolysisMagnesiumModels, MolecularPoly Adenosine Diphosphate RiboseProtein ConformationSubstrate SpecificityADPRS protein, humanGlycoside HydrolasesMagnesiumPoly Adenosine Diphosphate RiboseADP-ribosylationARH3hydrolysismetal specificityPARP1

Identifiers

PMID33894202
PMCPMC8141533
OpenAlexW3152957108

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.