Evidence map›Paper›PMID 36829940›Full record

ArticleAntioxidants (Basel, Switzerland)2023

A Buried Water Network Modulates the Activity of the

Geqing Wang, Jilong Qin, Anthony D Verderosa, Lilian Hor, Carlos Santos-Martin, Jason J Paxman, Jennifer L Martin, Makrina Totsika, Begoña Heras

Open access · goldAbstract read
In one paragraph

Article in Antioxidants (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.3field-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

6 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Accelerated Hydration Site Localization and Thermodynamic Profiling.Journal of chemical information and modeling · 2025
    Article
  5. Article
  6. 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 3 institutions in 1 country.

Geqing WangDepartment of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086, Australia.
Jilong QinCentre for Immunology and Infection Control, School of Biomedical Sciences, Queensland University of Technology, Brisbane, QLD 4000, Australia.ORCID 0000-0002-5867-6332
Anthony D VerderosaCentre for Immunology and Infection Control, School of Biomedical Sciences, Queensland University of Technology, Brisbane, QLD 4000, Australia.
Lilian HorDepartment of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086, Australia.
Carlos Santos-MartinDepartment of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086, Australia.
Jason J PaxmanDepartment of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086, Australia.ORCID 0000-0002-1418-5910
Jennifer L MartinGriffith Institute for Drug Discovery, Griffith University, Nathan, QLD 4111, Australia.
Makrina TotsikaCentre for Immunology and Infection Control, School of Biomedical Sciences, Queensland University of Technology, Brisbane, QLD 4000, Australia.ORCID 0000-0003-2468-0293
Begoña HerasDepartment of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086, Australia.
La Trobe University · AUQueensland University of Technology · AUGriffith University · AU

Funding

Australian Research Council DP180102987, DP190101613, DP210100673, FT130100580National Health and Medical Research Council GNT1143638, GNT1144046
6 · The paper itself

Abstract

The formation of disulphide bonds is an essential step in the folding of many proteins that enter the secretory pathway; therefore, it is not surprising that eukaryotic and prokaryotic organisms have dedicated enzymatic systems to catalyse this process. In bacteria, one such enzyme is disulphide bond-forming protein A (DsbA), a thioredoxin-like thiol oxidase that catalyses the oxidative folding of proteins required for virulence and fitness. A large body of work on DsbA proteins, particularly

Indexed as

bacterial pathogenesisdisulphideprotein foldingredox regulationthioredoxin

Identifiers

PMID36829940
PMCPMC9952396
OpenAlexW4319316084

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.