Evidence map›Paper›PMID 32845139›Full record

ArticleBiochemistry2020

Can Selenoenzymes Resist Electrophilic Modification? Evidence from Thioredoxin Reductase and a Mutant Containing α-Methylselenocysteine.

Emma J Ste Marie, Robert J Wehrle, Daniel J Haupt, Neil B Wood, Albert van der Vliet, Michael J Previs, Douglas S Masterson, Robert J Hondal

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. 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

8 authors.

Emma J Ste MarieDepartment of Biochemistry, University of Vermont, 89 Beaumont Avenue, Burlington, Vermont 05405, United States.
Robert J WehrleSchool of Mathematics and Natural Sciences, Chemistry and Biochemistry, University of Southern Mississippi, 118 College Drive, Hattiesburg, Mississippi 39406, United States.
Daniel J HauptDepartment of Chemistry, Discovery Hall, University of Vermont, 82 University Place, Burlington, Vermont 05405, United States.
Neil B WoodDepartment of Molecular Physiology & Biophysics, University of Vermont, 89 Beaumont Avenue, Burlington, Vermont 05405, United States.
Albert van der VlietDepartment of Pathology and Laboratory Medicine, University of Vermont, 149 Beaumont Avenue, Burlington, Vermont 05405, United States.
Michael J PrevisDepartment of Molecular Physiology & Biophysics, University of Vermont, 89 Beaumont Avenue, Burlington, Vermont 05405, United States.
Douglas S MastersonSchool of Mathematics and Natural Sciences, Chemistry and Biochemistry, University of Southern Mississippi, 118 College Drive, Hattiesburg, Mississippi 39406, United States.
Robert J HondalDepartment of Biochemistry, University of Vermont, 89 Beaumont Avenue, Burlington, Vermont 05405, United States.ORCID 0000-0002-1466-2852

Funding

HEMOSTASIS &THROMBOSIS PROGRAM FOR ACADEMIC TRAINEEST32HL007594 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI KELM, ROBERT J · 1985 to 2015
$4.6M
Selenocyanate as a novel treatment of cystic fibrosis lung diseaseR01HL141146 · NHLBI · NATIONAL JEWISH HEALTH · PI DAY, BRIAN J, HONDAL, ROBERT J · 2019 to 2022
$1.6M
NHLBI NIH HHS R01 HL141146NHLBI NIH HHS T32 HL007594
6 · The paper itself

Abstract

Selenocysteine (Sec) is the 21st proteogenic amino acid in the genetic code. Incorporation of Sec into proteins is a complex and bioenergetically costly process that evokes the following question: "Why did nature choose selenium?" An answer that has emerged over the past decade is that Sec confers resistance to irreversible oxidative inactivation by reactive oxygen species. Here, we explore the question of whether this concept can be broadened to include resistance to reactive electrophilic species (RES) because oxygen and related compounds are merely a subset of RES. To test this hypothesis, we inactivated mammalian thioredoxin reductase (Sec-TrxR), a mutant containing α-methylselenocysteine [(αMe)Sec-TrxR], and a cysteine ortholog TrxR (Cys-TrxR) with various electrophiles, including acrolein, 4-hydroxynonenal, and curcumin. Our results show that the acrolein-inactivated Sec-TrxR and the (αMe)Sec-TrxR mutant could regain 25% and 30% activity, respectively, when incubated with 2 mM H

Indexed as

MutationCysteineHumansOxidation-ReductionSelenium OxidesSelenocysteineSelenoproteinsThioredoxin-Disulfide ReductaseThioredoxinsCysteineSelenium OxidesSelenocysteineselenomethylselenocysteineSelenoproteinsselenoxideThioredoxin-Disulfide ReductaseThioredoxins

Identifiers

PMID32845139
PMCPMC7509987

What OpenQuestion holds

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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.