ArticleJournal of Parkinson's disease2023
Specific Detection of Physiological S129 Phosphorylated α-Synuclein in Tissue Using Proximity Ligation Assay.
Article in Journal of Parkinson's disease, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 9 citations in OpenAlex.
- α-Synuclein blocks endoplasmic reticulum co-translational protein translocation early in Parkinson's disease.Nature communications · 2026Article
- Seeing Invisible Oligomers: Rethinking α-Synuclein Pathology Through Proximity Ligation Assay.Movement disorders : official journal of the Movement Disorder Society · 2026Review
- Post-translational Modifications in Proteins: Prediction Methods, Biological Functions, and Diseases.MedComm · 2026Review
- Ten-Year Retrospective Study on the Diagnostic Value of Three-Site Skin Biopsy for Detecting pS129-α-Synuclein Biomarker: Cervical and Leg Dual-Site Biopsy as an Effective and Less Invasive Alternative.European journal of neurology · 2026Article
- Microfluidic platform for understanding Parkinson's disease and α-synuclein conformation.Translational neurodegeneration · 2025Review
- Micro- and nanoscale biosensing technologies for early diagnosis of Parkinson's disease.Mikrochimica acta · 2025Review
- Phosphorylated α-synuclein in CSF and plasma does not reflect synucleinopathy.NPJ Parkinson's disease · 2025Article
- Physiological roles of α-synuclein serine-129 phosphorylation - not an oxymoron.Trends in neurosciences · 2024Review
- An immunoassay for the quantification of phosphorylated α-synuclein at serine 129 in human cerebrospinal fluid.Bioanalysis · 2024Article
- α-Synuclein serine129 phosphorylation - the physiology of pathology.Molecular neurodegeneration · 2023Article
- Development of a Novel Electrochemiluminescence ELISA for Quantification of α-Synuclein Phosphorylated at SerACS chemical neuroscience · 2023Article
- Monitoring α-synuclein aggregation.Neurobiology of disease · 2023Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
backgroundSynucleinopathies are a group of neurodegenerative disorders that are pathologically characterized by intracellular aggregates called Lewy bodies. Lewy bodies are primarily composed of α-synuclein (asyn) protein, which is mostly phosphorylated at serine 129 (pS129) when aggregated and therefore used as a marker for pathology. Currently commercial antibodies against pS129 asyn stain aggregates well but in healthy brains cross react with other proteins, thus making it difficult to specifically detect physiological pS129 asyn.
objectiveTo develop a staining procedure that detects endogenous and physiological relevant pS129 asyn with high specificity and low background.
methodsWe used the fluorescent and brightfield in situ proximity ligation assay (PLA) to specifically detect pS129 asyn in cell culture, mouse, and human brain sections.
resultsThe pS129 asyn PLA specifically stained physiological and soluble pS129 asyn in cell culture, mouse brain sections, and human brain tissue without significant cross-reactivity or background signal. However, this technique was not successful in detecting Lewy bodies in human brain tissue.
conclusionWe successfully developed a novel PLA method that can, in the future, be used on in vitro and in vivo samples as a tool to explore and better understand the cellular localization and function of pS129 asyn in health and disease.
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Registered trials
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