Evidence map›Paper›PMID 29907568›Full record

ArticleThe Journal of biological chemistry2018

Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition.

Yasin Pourfarjam, Jessica Ventura, Igor Kurinov, Ahra Cho, Joel Moss, In-Kwon Kim

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

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

22 citing papers in PubMed.

  1. Article
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  4. Switch-like compaction of poly(ADP-ribose) upon cation binding.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

6 authors.

Yasin PourfarjamFrom the Department of Chemistry, University of Cincinnati, Cincinnati, Ohio 45221.
Jessica VenturaFrom the Department of Chemistry, University of Cincinnati, Cincinnati, Ohio 45221.
Igor KurinovCornell University, Department of Chemistry and Chemical Biology, Northeastern Collaborative Access Team Advanced Photon Source (NE-CAT APS), Argonne, Illinois 60439, and.
Ahra ChoFrom the Department of Chemistry, University of Cincinnati, Cincinnati, Ohio 45221.
Joel MossPulmonary Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892.
In-Kwon KimFrom the Department of Chemistry, University of Cincinnati, Cincinnati, Ohio 45221, in-kwon.kim@uc.edu.ORCID 0000-0002-2779-9735

Funding

ADP-ribosylation CyclesZIAHL000659 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI MOSS, JOEL · 2009 to 2025
$29.8M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
NIGMS NIH HHS P41 GM103403NIH HHS S10 OD021527
6 · The paper itself

Abstract

ADP-ribosyl-acceptor hydrolase 3 (ARH3) plays important roles in regulation of poly(ADP-ribosyl)ation, a reversible post-translational modification, and in maintenance of genomic integrity. ARH3 degrades poly(ADP-ribose) to protect cells from poly(ADP-ribose)-dependent cell death, reverses serine mono(ADP-ribosyl)ation, and hydrolyzes

Indexed as

Protein ConformationAdenosine Diphosphate RiboseAmino Acid SequenceCatalysisCatalytic DomainCrystallography, X-RayGlycoside HydrolasesHumansHydrolysisModels, MolecularSequence HomologySubstrate SpecificityAdenosine Diphosphate RiboseADPRS protein, humanGlycoside HydrolasesADP-ribosylationARH3conformational changehydrolasePARP1structural biologysubstrate specificity

Identifiers

PMID29907568
PMCPMC6093245

What OpenQuestion holds

Textmetadata
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.