Evidence map›Paper›PMID 40320462›Full record

ArticleScientific reports2025

Effect of hydrogen sulfide on alpha-synuclein aggregation and cell viability.

Elena A Ostrakhovitch, Eun-Suk Song, Johannah E Stegemann, Michael McLeod, Tritia R Yamasaki

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

5 authors.

Elena A OstrakhovitchDepartment of Neurology, University of Kentucky, 740 South Limestone St., Ste. J401, Lexington, KY, 40536-0284, USA.
Eun-Suk SongDepartment of Neurology, University of Kentucky, 740 South Limestone St., Ste. J401, Lexington, KY, 40536-0284, USA.
Johannah E StegemannDepartment of Neurology, University of Kentucky, 740 South Limestone St., Ste. J401, Lexington, KY, 40536-0284, USA.
Michael McLeodDepartment of Neurology, University of Kentucky, 740 South Limestone St., Ste. J401, Lexington, KY, 40536-0284, USA.
Tritia R YamasakiDepartment of Neurology, University of Kentucky, 740 South Limestone St., Ste. J401, Lexington, KY, 40536-0284, USA. tyamasaki@uky.edu.

Funding

WKU Lead Faculty AwardP20GM103436 · NIGMS · UNIVERSITY OF LOUISVILLE · PI ERIC C ROUCHKA · 2012 to 2026
$60.1M
Sustained eIF5A hypusination at the core of brain metabolic dysfunction in TDP-43 proteinopathiesP20GM148326 · NIGMS · UNIVERSITY OF KENTUCKY · PI Patrick G Sullivan · 2023 to 2026
$10.6M
UKNeu-PREP: University of Kentucky Neuroscience Postbaccalaureate Research Education ProgramR25NS130963 · NINDS · UNIVERSITY OF KENTUCKY · PI BRADLEY, LUKE H, GENSEL, JOHN C · 2023 to 2025
$1.1M
BLRD VA IK2 BX004883Kentucky IDeA Networks of Biomedical Research Excellence 5P20GM103436-24NIGMS NIH HHS P20 GM103436NIGMS NIH HHS P20 GM148326NINDS NIH HHS R25 NS130963U.S. Department of Veterans Affairs 5IK2BX004883
6 · The paper itself

Abstract

Parkinson's disease (PD) is a progressive neurodegenerative movement disorder characterized by nigrostriatal degeneration and aggregation of α-synuclein (α-Syn) with accumulation of insoluble aggregates in Lewy bodies. Familial mutations in α-Syn are associated with the development of PD. Accumulation of insoluble aggregates results in neuronal toxicity. Identification of compounds that inhibit seeding activity of α-Syn is of great importance. Here we investigate the potential of H2S donor, sodium hydrosulfide (NaHS), to inhibit α-Syn aggregation. We examined the effect of NaHS on fibril growth kinetics and the structural change of α-Syn fibrils formed by self-seeding and cross-seeding of wild-type (wt) and PD familial α-Syn mutations. NaHS slowed both self- and cross-seeded A53T α-Syn fibril formation but not wild-type fibril formation. We observed a decrease in the formed fibril length in vitro. We examined the effect on fibril formation within cells. NaHS significantly reduced the number and filament length of formed oligomers in an α-Syn overexpressing cell model. Furthermore, NaHS rescued viability of A53T α-Syn overexpressing cells seeded with wt- and mutant preformed fibrils. These results support a conformation-specific effect of hydrogen sulfide on alpha-synuclein aggregation and cell viability which deserves further exploration for therapeutic potential.

Indexed as

alpha-SynucleinHydrogen SulfideProtein AggregatesProtein Aggregation, PathologicalCell SurvivalHumansMutationParkinson DiseaseSulfidesalpha-SynucleinHydrogen SulfideProtein Aggregatessodium bisulfideSulfidesHydrogen sulfideParkinson diseaseProtein aggregationα-Synuclein

Identifiers

PMID40320462
PMCPMC12050307

What Socratic holds

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LicenceCC BY
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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 Socratic graph.