Evidence map›Paper›PMID 30576923›Full record

ArticleRedox biology2019

Extra-mitochondrial Cu/Zn superoxide dismutase (Sod1) is dispensable for protection against oxidative stress but mediates peroxide signaling in Saccharomyces cerevisiae.

Claudia Montllor-Albalate, Alyson E Colin, Bindu Chandrasekharan, Naimah Bolaji, Joshua L Andersen, F Wayne Outten, Amit R Reddi

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2019. 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
2.2field-weighted citation impact, top 11% 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, 57 citations in OpenAlex.

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  17. Antioxidant Therapy in Cancer: Rationale and Progress.Antioxidants (Basel, Switzerland) · 2022
    Review
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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

7 authors at 3 institutions in 1 country.

Claudia Montllor-AlbalateSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Alyson E ColinSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Bindu ChandrasekharanSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Naimah BolajiDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA.
Joshua L AndersenDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT 84602, USA.
F Wayne OuttenDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA.
Amit R ReddiSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA; Parker Petit Institute for Bioengineering and Biosciences, Georgia Institute of Technology, Atlanta, GA 30332, USA. Electronic address: amit.reddi@chemistry.gatech.edu.
Georgia Institute of Technology · USUniversity of South Carolina · USBrigham Young University · US

Funding

Conformational dynamics and allosteric regulation during stress-responsive metallocofactor assemblyR01GM112919 · NIGMS · UNIVERSITY OF ALABAMA IN TUSCALOOSA · PI Patrick Frantom · 2015 to 2026
$2.8M
The Role of Cu/Zn Superoxide Dismutase (SOD1) in Redox SignalingR01GM118744 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI REDDI, AMIT RAM · 2016 to 2020
$1.6M
NIGMS NIH HHS R01 GM112919NIGMS NIH HHS R01 GM118744
6 · The paper itself

Abstract

Cu/Zn Superoxide Dismutase (Sod1) is a highly conserved and abundant metalloenzyme that catalyzes the disproportionation of superoxide radicals into hydrogen peroxide and molecular oxygen. As a consequence, Sod1 serves dual roles in oxidative stress protection and redox signaling by both scavenging cytotoxic superoxide radicals and producing hydrogen peroxide that can be used to oxidize and regulate the activity of downstream targets. However, the relative contributions of Sod1 to protection against oxidative stress and redox signaling are poorly understood. Using the model unicellular eukaryote, Baker's yeast, we found that only a small fraction of the total Sod1 pool is required for protection against superoxide toxicity and that this pool is localized to the mitochondrial intermembrane space. On the contrary, we find that much larger amounts of extra-mitochondrial Sod1 are critical for peroxide-mediated redox signaling. Altogether, our results force the re-evaluation of the physiological role of bulk Sod1 in redox biology; namely, we propose that the vast majority of Sod1 in yeast is utilized for peroxide-mediated signaling rather than superoxide scavenging.

Indexed as

Oxidative StressSignal TransductionHydrogen PeroxideOxidation-ReductionOxygenPeroxidesReactive Oxygen SpeciesSaccharomyces cerevisiaeSuperoxide Dismutase-1Hydrogen PeroxideOxygenPeroxidesReactive Oxygen SpeciesSuperoxide Dismutase-1Cu/Zn superoxide dismutaseHydrogen peroxideMitochondrial metabolismReactive oxygen speciesRedox signalingSuperoxide

Identifiers

PMID30576923
PMCPMC6302037
OpenAlexW2902985351

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.