Evidence map›Paper›PMID 29068682›Full record

ArticleJournal of the American Chemical Society2017

Activity-Based Probes for Isoenzyme- and Site-Specific Functional Characterization of Glutathione S-Transferases.

Ethan G Stoddard, Bryan J Killinger, Reji N Nair, Natalie C Sadler, Regan F Volk, Samuel O Purvine, Anil K Shukla, Jordan N Smith, Aaron T Wright

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Short divalent ethacrynic amides as pro-inhibitors of glutathioneJournal of enzyme inhibition and medicinal chemistry · 2022
    Article
  5. Article
  6. Article
  7. Functionalised Cofactor Mimics for Interactome Discovery and Beyond.Angewandte Chemie (International ed. in English) · 2022
    Review
  8. Gut CommensalmBio · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. 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

9 authors at 1 institution in 1 country.

Ethan G StoddardChemical Biology and Exposure Sciences, Biological Sciences Division, Pacific Northwest National Laboratory , 902 Battelle Boulevard, Richland, Washington 99352, United States.
Bryan J KillingerChemical Biology and Exposure Sciences, Biological Sciences Division, Pacific Northwest National Laboratory , 902 Battelle Boulevard, Richland, Washington 99352, United States.
Reji N NairChemical Biology and Exposure Sciences, Biological Sciences Division, Pacific Northwest National Laboratory , 902 Battelle Boulevard, Richland, Washington 99352, United States.
Natalie C SadlerChemical Biology and Exposure Sciences, Biological Sciences Division, Pacific Northwest National Laboratory , 902 Battelle Boulevard, Richland, Washington 99352, United States.
Regan F VolkChemical Biology and Exposure Sciences, Biological Sciences Division, Pacific Northwest National Laboratory , 902 Battelle Boulevard, Richland, Washington 99352, United States.
Samuel O PurvineChemical Biology and Exposure Sciences, Biological Sciences Division, Pacific Northwest National Laboratory , 902 Battelle Boulevard, Richland, Washington 99352, United States.
Anil K ShuklaChemical Biology and Exposure Sciences, Biological Sciences Division, Pacific Northwest National Laboratory , 902 Battelle Boulevard, Richland, Washington 99352, United States.
Jordan N SmithChemical Biology and Exposure Sciences, Biological Sciences Division, Pacific Northwest National Laboratory , 902 Battelle Boulevard, Richland, Washington 99352, United States.
Aaron T WrightChemical Biology and Exposure Sciences, Biological Sciences Division, Pacific Northwest National Laboratory , 902 Battelle Boulevard, Richland, Washington 99352, United States.ORCID 0000-0002-3172-5253
Battelle · US

Funding

Research Experience and Training Coordination CoreP42ES016465 · NIEHS · OREGON STATE UNIVERSITY · PI Susan C Tilton · 2009 to 2026
$52.5M
Equipment Supplement Request for a Research Resource for Ultra-sensitive High Throughput ProteomicsP41GM103493 · NIGMS · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2012 to 2022
$22.6M
Department of Energy DE-AC06-76RL01830NIEHS NIH HHS P42 ES016465NIGMS NIH HHS P41 GM103493
6 · The paper itself

Abstract

Glutathione S-transferases (GSTs) comprise a diverse family of phase II drug metabolizing enzymes whose shared function is the conjugation of reduced glutathione (GSH) to endo- and xenobiotics. Although the conglomerate activity of these enzymes can be measured, the isoform-specific contribution to the metabolism of xenobiotics in complex biological samples has not been possible. We have developed two activity-based probes (ABPs) that characterize active GSTs in mammalian tissues. The GST active site is composed of a GSH binding "G site" and a substrate binding "H site". Therefore, we developed (1) a GSH-based photoaffinity probe (GSTABP-G) to target the "G site", and (2) an ABP designed to mimic a substrate molecule and have "H site" activity (GSTABP-H). The GSTABP-G features a photoreactive moiety for UV-induced covalent binding to GSTs and GSH-binding enzymes. The GSTABP-H is a derivative of a known mechanism-based GST inhibitor that binds within the active site and inhibits GST activity. Validation of probe targets and "G" and "H" site specificity was carried out using a series of competition experiments in the liver. Herein, we present robust tools for the characterization of enzyme- and active site-specific GST activity in mammalian model systems.

Indexed as

AnimalsBinding SitesCatalytic DomainGlutathioneGlutathione TransferaseHumansIsoenzymesLiverLungMicePhotoaffinity LabelsProtein BindingGlutathioneGlutathione TransferaseIsoenzymesPhotoaffinity Labels

Identifiers

PMID29068682
PMCPMC6279235
OpenAlexW2766465725

What OpenQuestion holds

Textmetadata
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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.