Evidence map›Paper›PMID 35102205›Full record

ArticleScientific reports2022

Sulfotransferase 4A1 activity facilitates sulfate-dependent cellular protection to oxidative stress.

Evan J Brettrager, Arthur W Meehan, Charles N Falany, Robert C A M van Waardenburg

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Zymolyase Treatment ofDNA and cell biology · 2024
    Article
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  8. Review
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

4 authors at 1 institution in 1 country.

Evan J BrettragerDepartment of Pharmacology and Toxicology, University of Alabama at Birmingham, 155 Volker Hall, 1720 2nd Ave S., Birmingham, AL, 35294-0019, USA.
Arthur W MeehanDepartment of Pharmacology and Toxicology, University of Alabama at Birmingham, 155 Volker Hall, 1720 2nd Ave S., Birmingham, AL, 35294-0019, USA.
Charles N FalanyDepartment of Pharmacology and Toxicology, University of Alabama at Birmingham, 155 Volker Hall, 1720 2nd Ave S., Birmingham, AL, 35294-0019, USA.
Robert C A M van WaardenburgDepartment of Pharmacology and Toxicology, University of Alabama at Birmingham, 155 Volker Hall, 1720 2nd Ave S., Birmingham, AL, 35294-0019, USA. rvanwaar@uab.edu.
University of Alabama at Birmingham · US

Funding

Analysis of SULT4A1 in protein interactionsR21NS116312 · NINDS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI VAN WAARDENBURG, ROBERT C.A.M. · 2020 to 2020
$408k
NINDS NIH HHS R21 NS116312
6 · The paper itself

Abstract

Sulfotransferase 4A1 (SULT4A1) is an orphan member of the cytosolic SULT superfamily that contains enzymes that catalyze the sulfonation of hydrophobic drugs and hormones. SULT4A1 has been assessed through all classical SULT approaches yet no SULT activity has been reported. To ascertain SULT4A1 function and activity, we utilized Saccharomyces cerevisiae as a model system, which exhibits no endogenous SULT activity nor possesses SULT-related genes. We observed that ectopic SULT4A1 expression in yeast displays similar subcellular localization as reported in mouse neurons and observed that SULT4A1 is associated with the outer mitochondria membrane. SULT4A1 expression stimulates colony formation and protects these cells from hydrogen peroxide and metabolism-associated oxidative stress. These SULT4A1-mediated phenotypes are dependent on extracellular sulfate that is converted in yeast to PAPS, the universal sulfonate donor for SULT activity. Thus, heterologous SULT4A1 expression in yeast is correctly distributed and functional, and SULT4A1 antioxidant activity is sulfate dependent supporting the concept that SULT4A1 has sulfate-associated activity.

Indexed as

Oxidative StressSaccharomyces cerevisiaeSulfotransferasesAnimalsHumansHydrogen PeroxideMicePhosphoadenosine PhosphosulfateSulfatesHydrogen PeroxidePhosphoadenosine PhosphosulfateSulfatesSulfotransferasesSULT4A1 protein, human

Identifiers

PMID35102205
PMCPMC8803991
OpenAlexW4210445005

What OpenQuestion holds

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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.