Evidence map›Paper›PMID 28463568›Full record

ArticleAntioxidants & redox signaling2017

The Enzymatic and Structural Basis for Inhibition of Echinococcus granulosus Thioredoxin Glutathione Reductase by Gold(I).

Gustavo Salinas, Wei Gao, Yang Wang, Mariana Bonilla, Long Yu, Andrey Novikov, Veridiana G Virginio, Henrique B Ferreira, Marisol Vieites, Vadim N Gladyshev and 2 more

Abstract read
In one paragraph

Article in Antioxidants & redox signaling, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.2field-weighted citation impact, top 15% 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

10 citing papers in PubMed, 19 citations in OpenAlex.

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  5. Structure ofInternational journal of molecular sciences · 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

12 authors at 4 institutions in 5 countries.

Gustavo Salinas1 Worm Biology Lab, Institut Pasteur de Montevideo , Montevideo, Uruguay .
Wei Gao3 Department of Biomedical Research, National Jewish Health , Denver, Colorado.
Yang Wang3 Department of Biomedical Research, National Jewish Health , Denver, Colorado.
Mariana Bonilla2 Cátedra de Inmunología, Facultad de Química, Instituto de Higiene, Universidad de la República , Montevideo, Uruguay .
Long Yu3 Department of Biomedical Research, National Jewish Health , Denver, Colorado.
Andrey Novikov3 Department of Biomedical Research, National Jewish Health , Denver, Colorado.
Veridiana G Virginio7 Laboratório de Genômica Estrutural e Funcional, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul , Porto Alegre, RS, Brazil .
Henrique B Ferreira7 Laboratório de Genômica Estrutural e Funcional, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul , Porto Alegre, RS, Brazil .
Marisol Vieites8 Cátedra de Química Inorgánica, Facultad de Química, Universidad de la República , Montevideo, Uruguay .
Vadim N Gladyshev9 Brigham and Women's Hospital , Harvard Medical School, Boston, Massachusetts.
Dinorah Gambino8 Cátedra de Química Inorgánica, Facultad de Química, Universidad de la República , Montevideo, Uruguay .
Shaodong Dai3 Department of Biomedical Research, National Jewish Health , Denver, Colorado.
National Jewish Health · USUniversidad de la República de Uruguay · UYUniversidade Federal do Rio Grande do Sul · BRBrigham and Women's Hospital · US

Funding

Molecular Mechanisms of Immune ToleranceT32AI074491 · NIAID · NATIONAL JEWISH HEALTH · PI CAMBIER, JOHN C, PELANDA, ROBERTA · 2009 to 2023
$4.1M
Molecular Basis of T Cell Recognition of Metal IonsR01ES025797 · NIEHS · UNIVERSITY OF COLORADO DENVER · PI DAI, SHAODONG · 2015 to 2019
$1.8M
Heavy Metal Induced AutoimmunityR21ES025885 · NIEHS · UNIVERSITY OF COLORADO DENVER · PI DAI, SHAODONG · 2017 to 2018
$432k
NIEHS NIH HHS R01 ES025797NIEHS NIH HHS R21 ES025885
6 · The paper itself

Abstract

aimsNew drugs are needed to treat flatworm infections that cause severe human diseases such as schistosomiasis. The unique flatworm enzyme thioredoxin glutathione reductase (TGR), structurally different from the human enzyme, is a key drug target. Structural studies of the flatworm Echinococcus granulosus TGR, free and complexed with Au

resultsAu INNOVATION: The identification of a primary site for gold binding and the structural model provide a basis for gold compound optimization through scaffold adjustments.

conclusionsThe structural study revealed that TGR functions are achieved not only through a mobile Sec-containing redox center but also by rotation of the Grx domain and distinct binding sites for Grx domain and thioredoxin. The conserved Cys

Indexed as

AnimalsBinding SitesCysteineEchinococcus granulosusEnzyme InhibitorsGlutaredoxinsHelminth ProteinsModels, MolecularMultienzyme ComplexesMutationNADH, NADPH OxidoreductasesOrganogold CompoundsProtein BindingProtein ConformationCysteineEnzyme InhibitorsGlutaredoxinsHelminth ProteinsMultienzyme ComplexesNADH, NADPH OxidoreductasesOrganogold Compoundsthioredoxin glutathione reductaseEchinococcusflatwormglutaredoxingoldselenocysteineselenoproteinthioredoxin glutathione reductase

Identifiers

PMID28463568
PMCPMC5678357
OpenAlexW2611550378

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.