Evidence map›Paper›PMID 30318463›Full record

ArticleCell chemical biology2018

Monitoring Poly(ADP-ribosyl)glycohydrolase Activity with a Continuous Fluorescent Substrate.

Bryon S Drown, Tomohiro Shirai, Johannes Gregor Matthias Rack, Ivan Ahel, Paul J Hergenrother

Open access · bronzeAbstract read
In one paragraph

Article in Cell chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Fully protected pyrophosphatesChemical science · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
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 2 institutions in 2 countries.

Bryon S DrownDepartment of Chemistry and Institute for Genomic Biology, University of Illinois at Urbana-Champaign, 261 Roger Adams Lab Box 36-5, 600 S. Mathews Avenue, Urbana, IL 61801, USA.
Tomohiro ShiraiDepartment of Chemistry and Institute for Genomic Biology, University of Illinois at Urbana-Champaign, 261 Roger Adams Lab Box 36-5, 600 S. Mathews Avenue, Urbana, IL 61801, USA.
Johannes Gregor Matthias RackSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Ivan AhelSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Paul J HergenrotherDepartment of Chemistry and Institute for Genomic Biology, University of Illinois at Urbana-Champaign, 261 Roger Adams Lab Box 36-5, 600 S. Mathews Avenue, Urbana, IL 61801, USA. Electronic address: hergenro@illinois.edu.
University of Illinois Urbana-Champaign · USUniversity of Oxford · GB

Funding

Training Program at the Chemistry Biology InterfaceT32GM136629 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI Paul Hergenrother · 2020 to 2026
$4.5M
Identification of inhibitors of poly (ADP-ribose) glycohydrolase (PARG)R21CA212732 · NCI · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI HERGENROTHER, PAUL · 2017 to 2018
$353k
Cancer Research UK 22284Cancer Research UK C35050/A22284NCI NIH HHS R21 CA212732NIGMS NIH HHS T32 GM136629Wellcome TrustWellcome Trust 101794
6 · The paper itself

Abstract

The post-translational modification (PTM) and signaling molecule poly(ADP-ribose) (PAR) has an impact on diverse biological processes. This PTM is regulated by a series of ADP-ribosyl glycohydrolases (PARG enzymes) that cleave polymers and/or liberate monomers from their protein targets. Existing methods for monitoring these hydrolases rely on detection of the natural substrate, PAR, commonly achieved via radioisotopic labeling. Here we disclose a general substrate for monitoring PARG activity, TFMU-ADPr, which directly reports on total PAR hydrolase activity via release of a fluorophore; this substrate has excellent reactivity, generality (processed by the major PARG enzymes), stability, and usability. A second substrate, TFMU-IDPr, selectively reports on PARG activity only from the enzyme ARH3. Use of these probes in whole-cell lysate experiments has revealed a mechanism by which ARH3 is inhibited by cholera toxin. TFMU-ADPr and TFMU-IDPr are versatile tools for assessing small-molecule inhibitors in vitro and probing the regulation of ADP-ribosyl catabolic enzymes.

Indexed as

Enzyme AssaysCell Line, TumorEnzyme InhibitorsFluorescent DyesGlycoside HydrolasesHumansModels, MolecularMolecular ConformationSmall Molecule LibrariesSubstrate SpecificityEnzyme InhibitorsFluorescent DyesGlycoside Hydrolasespoly ADP-ribose glycohydrolaseSmall Molecule LibrariesARH3cholera toxinenzyme assayfluorescent probePARGpoly(ADP-ribose)

Identifiers

PMID30318463
PMCPMC6309520
OpenAlexW2896411544

What OpenQuestion holds

Textmetadata
LicenceTDM
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.