ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2012
SIRT1 protects against α-synuclein aggregation by activating molecular chaperones.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 106 papers, 2 of them syntheses that pooled it.
What it found
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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.
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.
Who cites it
106 citing papers in PubMed, 2 syntheses or guidelines pooled it, 207 citations in OpenAlex.
- Sirtuin Acetylation and Deacetylation: a Complex Paradigm in Neurodegenerative Disease.Molecular neurobiology · 2021Pooled it
- Pooled it
- Rs2015 Polymorphism in miRNA Target Site of Sirtuin2 Gene Is Associated with the Risk of Parkinson's Disease in Chinese Han Population.BioMed research international · 2019Trial
- From synaptic development to degeneration: a narrative review of small molecule strategies targeting alpha-synuclein in Parkinson's disease.Metabolic brain disease · 2026Review
- Investigating the Interplay Between the Nrf2/Keap1/HO-1/SIRT-1 Pathway and the p75NTR/PI3K/Akt/MAPK Cascade in Neurological Disorders: Mechanistic Insights and Therapeutic Innovations.Molecular neurobiology · 2025Review
- Activation and inhibition of sirtuins: From bench to bedside.Medicinal research reviews · 2025Review
- SIRT1 exerts protective effects by inhibiting endoplasmic reticulum stress and NF-κB signaling pathways.Frontiers in cell and developmental biology · 2024Review
- Role ofDiagnostics (Basel, Switzerland) · 2023Article
- Article
- Changes in α-Synuclein Posttranslational Modifications in an AAV-Based Mouse Model of Parkinson's Disease.International journal of molecular sciences · 2023Article
- Review
- Brain insulin resistance linked Alzheimer's and Parkinson's disease pathology: An undying implication of epigenetic and autophagy modulation.Inflammopharmacology · 2023Review
- SIRT1 pathway in Parkinson's disease: a faraway snapshot but so close.Inflammopharmacology · 2023Review
- Dysregulation of miR-543 in Parkinson's disease: Impact on the neuroprotective gene SIRT1.Neuropathology and applied neurobiology · 2023Article
- Natural Bioactive Products as Epigenetic Modulators for Treating Neurodegenerative Disorders.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Alpha synuclein post translational modifications: potential targets for Parkinson's disease therapy?Frontiers in molecular neuroscience · 2023Review
- Genetic modifiers of synucleinopathies-lessons from experimental models.Oxford open neuroscience · 2023Review
- Sirtuins and redox signaling interplay in neurogenesis, neurodegenerative diseases, and neural cell reprogramming.Frontiers in neuroscience · 2023Review
- Sirt2 promotes white matter oligodendrogenesis during development and in models of neonatal hypoxia.Nature communications · 2022Article
- Cdk5 phosphorylation-induced SIRT2 nuclear translocation promotes the death of dopaminergic neurons in Parkinson's disease.NPJ Parkinson's disease · 2022Article
46 more citing papers are in PubMed but not listed here.
Corrections and comments
- Retraction · 2016-04-06Manipulation of Images · Unreliable Image ·
- Commented on by
- Retracted
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
α-Synuclein is a key molecule in the pathogenesis of synucleinopathy including dementia with Lewy bodies, Parkinson's disease, and multiple system atrophy. Sirtuins are NAD(+)-dependent protein deacetylases that are highly conserved and counter aging in lower organisms. We show that the life span of a mouse model with A53T α-synuclein mutation is increased by overexpressing SIRT1 and decreased by knocking out SIRT1 in brain. Furthermore, α-synuclein aggregates are reduced in the brains of mice with SIRT1 overexpression and increased by SIRT1 deletion. We show that SIRT1 deacetylates HSF1 (heat shock factor 1) and increases HSP70 RNA and protein levels, but only in the brains of mice with A53T and SIRT1 expression. Thus, SIRT1 responds to α-synuclein aggregation-induced stress by activating molecular chaperones to protect against disease.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.