Evidence map›Paper›PMID 23891152›Full record

ArticleChemistry & biology2013

Peroxiredoxin-1 from the human hookworm Ancylostoma ceylanicum forms a stable oxidized decamer and is covalently inhibited by conoidin A.

Jennifer B Nguyen, Christopher D Pool, Christina Y B Wong, Rebecca S Treger, David L Williams, Michael Cappello, Wendy A Lea, Anton Simeonov, Jon J Vermeire, Yorgo Modis

Abstract read
In one paragraph

Article in Chemistry & biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.4field-weighted citation impact, top 23% 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

26 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. The Role of Peroxiredoxins in the Regulation of Sepsis.Antioxidants (Basel, Switzerland) · 2022
    Review
  9. Frontiers in cellular and infection microbiology · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Real-time monitoring of peroxiredoxin oligomerization dynamics in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. 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

10 authors at 3 institutions in 1 country.

Jennifer B NguyenDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Christopher D Pool
Christina Y B Wong
Rebecca S Treger
David L Williams
Michael Cappello
Wendy A Lea
Anton Simeonov
Jon J Vermeire
Yorgo Modis
Yale University · USNational Institutes of Health · USRush University Medical Center · US

Funding

X-RAY ANALYSIS OF PROTEIN STRUCTURE AND FUNCTIONP01GM022778 · NIGMS · YALE UNIVERSITY · PI BREAKER, RONALD R · 1985 to 2019
$26.1M
PREDOCTORAL PROGRAM IN BIOPHYSICST32GM008283 · NIGMS · YALE UNIVERSITY · PI XIONG, YONG · 1988 to 2022
$10.5M
NIAID NIH HHS K22 AI08476NIGMS NIH HHS P01 GM022778NIGMS NIH HHS T32 GM008283NIGMS NIH HHS T32 GM08283
6 · The paper itself

Abstract

Hookworms are parasitic nematodes that have a devastating impact on global health, particularly in developing countries. We report a biochemical and structural analysis of a peroxiredoxin from the hookworm Ancylostoma ceylanicum, AcePrx-1. Peroxiredoxins provide antioxidant protection and act as signaling molecules and chaperones. AcePrx-1 is expressed in adult hookworms and can be inactivated by 2,3-bis(bromomethyl)quinoxaline-1,4-dioxide (conoidin A). Conoidin A inactivates AcePrx-1 by alkylating or crosslinking the catalytic cysteines, while maintaining the enzyme in the "locally unfolded" conformation. Irreversible oxidation of the resolving cysteine may contribute additional inhibitory activity. A crystal structure of oxidized AcePrx-1 reveals a disulfide-linked decamer. A helix macrodipole near the active site increases the reactivity of the catalytic cysteines to conoidin A. This work demonstrates the promise of conoidin compounds as probes to evaluate peroxiredoxins as drug targets in human parasites.

Indexed as

Amino Acid SequenceAncylostomaAncylostomiasisAnimalsCatalytic DomainCrystallography, X-RayHumansModels, MolecularMolecular Sequence DataOxidation-ReductionPeroxiredoxinsProtein ConformationProtein MultimerizationQuinoxalinesconoidin APeroxiredoxinsQuinoxalines

Identifiers

PMID23891152
PMCPMC3755041
OpenAlexW2013880933

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.