Evidence map›Paper›PMID 31266751›Full record

ArticleDrug metabolism and disposition: the biological fate of chemicals2019

SULT4A1 Protects Against Oxidative-Stress Induced Mitochondrial Dysfunction in Neuronal Cells.

Mohammed I Hossain, Joshua M Marcus, Jun Hee Lee, Patrick L Garcia, Jean-Philippe Gagné, Guy G Poirier, Charles N Falany, Shaida A Andrabi

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Drug metabolism and disposition: the biological fate of chemicals, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. 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

8 authors at 1 institution in 2 countries.

Mohammed I HossainDepartments of Pharmacology and Toxicology (M.I.H., J.M.M., J.H.L., P.L.G., C.N.F., S.A.A.) and Neurology (S.A.A.), University of Alabama at Birmingham, Birmingham, Alabama; and Centre de recherche du CHU de Québec, Faculté de Médecine, Université Laval, Québec, Canada (J.-P.G., G.G.P.).
Joshua M MarcusDepartments of Pharmacology and Toxicology (M.I.H., J.M.M., J.H.L., P.L.G., C.N.F., S.A.A.) and Neurology (S.A.A.), University of Alabama at Birmingham, Birmingham, Alabama; and Centre de recherche du CHU de Québec, Faculté de Médecine, Université Laval, Québec, Canada (J.-P.G., G.G.P.).
Jun Hee LeeDepartments of Pharmacology and Toxicology (M.I.H., J.M.M., J.H.L., P.L.G., C.N.F., S.A.A.) and Neurology (S.A.A.), University of Alabama at Birmingham, Birmingham, Alabama; and Centre de recherche du CHU de Québec, Faculté de Médecine, Université Laval, Québec, Canada (J.-P.G., G.G.P.).
Patrick L GarciaDepartments of Pharmacology and Toxicology (M.I.H., J.M.M., J.H.L., P.L.G., C.N.F., S.A.A.) and Neurology (S.A.A.), University of Alabama at Birmingham, Birmingham, Alabama; and Centre de recherche du CHU de Québec, Faculté de Médecine, Université Laval, Québec, Canada (J.-P.G., G.G.P.).
Jean-Philippe GagnéDepartments of Pharmacology and Toxicology (M.I.H., J.M.M., J.H.L., P.L.G., C.N.F., S.A.A.) and Neurology (S.A.A.), University of Alabama at Birmingham, Birmingham, Alabama; and Centre de recherche du CHU de Québec, Faculté de Médecine, Université Laval, Québec, Canada (J.-P.G., G.G.P.).
Guy G PoirierDepartments of Pharmacology and Toxicology (M.I.H., J.M.M., J.H.L., P.L.G., C.N.F., S.A.A.) and Neurology (S.A.A.), University of Alabama at Birmingham, Birmingham, Alabama; and Centre de recherche du CHU de Québec, Faculté de Médecine, Université Laval, Québec, Canada (J.-P.G., G.G.P.).
Charles N FalanyDepartments of Pharmacology and Toxicology (M.I.H., J.M.M., J.H.L., P.L.G., C.N.F., S.A.A.) and Neurology (S.A.A.), University of Alabama at Birmingham, Birmingham, Alabama; and Centre de recherche du CHU de Québec, Faculté de Médecine, Université Laval, Québec, Canada (J.-P.G., G.G.P.).
Shaida A AndrabiDepartments of Pharmacology and Toxicology (M.I.H., J.M.M., J.H.L., P.L.G., C.N.F., S.A.A.) and Neurology (S.A.A.), University of Alabama at Birmingham, Birmingham, Alabama; and Centre de recherche du CHU de Québec, Faculté de Médecine, Université Laval, Québec, Canada (J.-P.G., G.G.P.) sandrabi@uab.edu.ORCID 0000-0002-4083-1998
University of Alabama at Birmingham · US

Funding

Training Program in Cell, Molecular, and Developmental BiologyT32GM008111 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI YODER, BRADLEY K. · 1985 to 2022
$5.4M
Poly (ADP-ribose) Mediates Cell Death in Stroke by Inhibiting Glucose MetabolismR01NS086953 · NINDS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI ANDRABI, SHAIDA A. · 2015 to 2019
$1.7M
NIGMS NIH HHS T32 GM008111NINDS NIH HHS R01 NS086953
6 · The paper itself

Abstract

Sulfotransferase 4A1 (SULT4A1), a member of cytosolic sulfotransferases (SULT), is exclusively expressed in neurons with no known function. Severe phenotype and early postnatal death in SULT4A1 knockout mice revealed that SULT4A1 is an essential neuronal protein. Localization of SULT4A1 in different cytosolic compartments, including mitochondria, suggests multiple roles for this protein. We observed that knockdown of SULT4A1 results in the accumulation of reactive oxygen species in primary cortical neurons, suggesting a potential role of SULT4A1 in regulating redox homeostasis. Expression of SULT4A1 in the human neuroblastoma SH-SY5Y cells revealed a defused but nonuniform staining pattern in the cytoplasm, with increased density around mitochondria. Subcellular fractionation of SULT4A1 expressing SH-SY5Y cells confirms the presence of SULT4A1 in mitochondrial fractions. SULT4A1 expressing cells display significant protection against H

Indexed as

AnimalsApoptosisCell Line, TumorCerebral CortexCloning, MolecularHumansMembrane Potential, MitochondrialMiceMice, KnockoutMitochondriaNeuronsOxidative StressPrimary Cell CultureReactive Oxygen SpeciesRecombinant ProteinsSulfotransferasesReactive Oxygen SpeciesRecombinant ProteinsSulfotransferasesSULT4A1 protein, humanSult4a1 protein, mouse

Identifiers

PMID31266751
PMCPMC6694224
OpenAlexW2955463971

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.