Evidence map›Paper›PMID 26381228›Full record

ArticleAntioxidants & redox signaling2016

A New Class of Thioredoxin-Related Protein Able to Bind Iron-Sulfur Clusters.

Hugo Bisio, Mariana Bonilla, Bruno Manta, Martín Graña, Valentina Salzman, Pablo S Aguilar, Vadim N Gladyshev, Marcelo A Comini, Gustavo Salinas

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Antioxidants & redox signaling, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. MitochondrialAntioxidants (Basel, Switzerland) · 2018
    Article
  3. 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.

Hugo Bisio1 Worm Biology Laboratory, Institut Pasteur de Montevideo, Montevideo, Uruguay .
Mariana Bonilla2 Redox Biology of Trypanosomes Laboratory, Institut Pasteur de Montevideo , Montevideo, Uruguay .
Bruno Manta2 Redox Biology of Trypanosomes Laboratory, Institut Pasteur de Montevideo , Montevideo, Uruguay .
Martín Graña3 Bioinformatics Unit, Institut Pasteur de Montevideo , Montevideo, Uruguay .
Valentina Salzman4 Cellular Membranes Laboratory, Institut Pasteur de Montevideo , Montevideo, Uruguay .
Pablo S Aguilar4 Cellular Membranes Laboratory, Institut Pasteur de Montevideo , Montevideo, Uruguay .
Vadim N Gladyshev5 Division of Genetics, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School , Boston, Massachusetts.
Marcelo A Comini2 Redox Biology of Trypanosomes Laboratory, Institut Pasteur de Montevideo , Montevideo, Uruguay .
Gustavo Salinas1 Worm Biology Laboratory, Institut Pasteur de Montevideo, Montevideo, Uruguay .

Funding

Functions of thioredoxin reductases and their targetsR37GM065204 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI GLADYSHEV, VADIM N. · 2011 to 2020
$4.0M
NIGMS NIH HHS R37 GM065204
6 · The paper itself

Abstract

aimsMembers of the thioredoxin (Trx) protein family participate mainly in redox pathways and have not been associated with Fe/S binding, in contrast to some closely related glutaredoxins (Grxs). Cestode parasites possess an unusual diversity of Trxs and Trx-related proteins with unexplored functions. In this study, we addressed the biochemical characterization of a new class of Trx-related protein (IsTRP) and a classical monothiol Grx (EgGrx5) from the human pathogen Echinococcus granulosus.

resultsThe dimeric form of IsTRP coordinates Fe INNOVATION: IsTRP is the first member from the Trx family to be reported to bind Fe/S. We disclose a novel mechanism of Fe/S coordination within the Trx folding unit, which renders the cluster highly resistant to oxidation-mediated disassembly.

conclusionWe demonstrate that IsTRP defines a new protein family within the Trx superfamily, confirm the conservation of function for class II Grx from nonphylogenetically related species, and highlight the versatility of the Trx folding unit to acquire Fe/S binding as a recurrent emergent function. Antioxid. Redox Signal. 00, 000-000.

Identifiers

PMID26381228
PMCPMC6913166

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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.