Evidence map›Paper›PMID 39409036›Full record

ArticleInternational journal of molecular sciences2024

Small Molecules Inducing Autophagic Degradation of Expanded Polyglutamine Protein through Interaction with Both Mutant ATXN3 and LC3.

Te-Hsien Lin, Wan-Ling Chen, Shao-Fan Hsu, I-Cheng Chen, Chih-Hsin Lin, Kuo-Hsuan Chang, Yih-Ru Wu, Yi-Ru Chen, Ching-Fa Yao, Wenwei Lin and 2 more

Abstract read
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In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

12 authors.

Te-Hsien LinDepartment of Neurology, Chang-Gung Memorial Hospital, Chang-Gung University College of Medicine, Taoyuan 33302, Taiwan.
Wan-Ling ChenDepartment of Neurology, Chang-Gung Memorial Hospital, Chang-Gung University College of Medicine, Taoyuan 33302, Taiwan.
Shao-Fan HsuDepartment of Life Science, National Taiwan Normal University, Taipei 11677, Taiwan.
I-Cheng ChenDepartment of Life Science, National Taiwan Normal University, Taipei 11677, Taiwan.
Chih-Hsin LinDepartment of Neurology, Chang-Gung Memorial Hospital, Chang-Gung University College of Medicine, Taoyuan 33302, Taiwan.
Kuo-Hsuan ChangDepartment of Neurology, Chang-Gung Memorial Hospital, Chang-Gung University College of Medicine, Taoyuan 33302, Taiwan.ORCID 0000-0003-4972-9823
Yih-Ru WuDepartment of Neurology, Chang-Gung Memorial Hospital, Chang-Gung University College of Medicine, Taoyuan 33302, Taiwan.
Yi-Ru ChenDepartment of Chemistry, National Taiwan Normal University, Taipei 11677, Taiwan.ORCID 0000-0002-7969-8258
Ching-Fa YaoDepartment of Chemistry, National Taiwan Normal University, Taipei 11677, Taiwan.
Wenwei LinDepartment of Chemistry, National Taiwan Normal University, Taipei 11677, Taiwan.
Guey-Jen Lee-ChenDepartment of Life Science, National Taiwan Normal University, Taipei 11677, Taiwan.ORCID 0000-0003-4818-9917
Chiung-Mei ChenDepartment of Neurology, Chang-Gung Memorial Hospital, Chang-Gung University College of Medicine, Taoyuan 33302, Taiwan.ORCID 0000-0002-0769-0353

Funding

Chang Gung Memorial Hospital, Taoyuan, Taiwan CMRPG3M216Ministry of Science and Technology, Taiwan 110-2314-B-182A-071-MY3Ministry of Science and Technology, Taiwan 112-2811-B-182A-017
6 · The paper itself

Abstract

Polyglutamine (polyQ)-mediated spinocerebellar ataxia (SCA), including SCA1, 2, 3, 6, 7, and 17, are caused by mutant genes with expanded CAG repeats, leading to the intracellular accumulation of aggregated proteins, the production of reactive oxygen species, and cell death. Among SCA, SCA3 is caused by a mutation in the ATXN3 (ataxin-3) gene. In a circumstance of polyQ aggregation, the autophagic pathway is induced to degrade the aggregated proteins, thereby suppressing downstream deleterious effects and promoting neuronal survival. In this study, we tested the effects of synthetic indole (NC009-1, -2, -3, -6) and coumarin (LM-022, -031) derivatives as chemical chaperones to assist mutant ATXN3-Q

Indexed as

Ataxin-3AutophagyMicrotubule-Associated ProteinsPeptidesCell Line, TumorHumansIndolesMutationProtein BindingRepressor ProteinsAtaxin-3ATXN3 protein, humanIndolesMAP1LC3A protein, humanMicrotubule-Associated ProteinsPeptidespolyglutamineRepressor ProteinsATXN3autophagosome tetheringLC3polyglutamineSCA3 therapeuticsvenus-based BiFC

Identifiers

PMID39409036
PMCPMC11477298

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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.