ArticleActa neuropathologica2008
Characterization of antibodies that selectively detect alpha-synuclein in pathological inclusions.
Article in Acta neuropathologica, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 82 citations in OpenAlex.
- The pesticide chlorpyrifos increases the risk of Parkinson's disease.Molecular neurodegeneration · 2025Article
- Differential role of C-terminal truncations on alpha-synuclein pathology and Lewy body formation.NPJ Parkinson's disease · 2025Article
- Development and validation of an expanded antibody toolset that captures alpha-synuclein pathological diversity in Lewy body diseases.NPJ Parkinson's disease · 2023Article
- Evaluation of an Adoptive Cellular Therapy-Based Vaccine in a Transgenic Mouse Model of α-synucleinopathy.ACS chemical neuroscience · 2023Article
- Revisiting the specificity and ability of phospho-S129 antibodies to capture alpha-synuclein biochemical and pathological diversity.NPJ Parkinson's disease · 2022Article
- Opportunities and challenges of alpha-synuclein as a potential biomarker for Parkinson's disease and other synucleinopathies.NPJ Parkinson's disease · 2022Review
- Collusion of α-Synuclein and Aβ aggravating co-morbidities in a novel prion-type mouse model.Molecular neurodegeneration · 2021Article
- Multiple system atrophy-associated oligodendroglial protein p25α stimulates formation of novel α-synuclein strain with enhanced neurodegenerative potential.Acta neuropathologica · 2021Article
- In vivo aggregation of presynaptic alpha-synuclein is not influenced by its phosphorylation at serine-129.Neurobiology of disease · 2021Article
- Age-related increase of alpha-synuclein oligomers is associated with motor disturbances in L61 transgenic mice.Neurobiology of aging · 2021Article
- Investigating the presence of doubly phosphorylated α-synuclein at tyrosine 125 and serine 129 in idiopathic Lewy body diseases.Brain pathology (Zurich, Switzerland) · 2020Article
- The center of olfactory bulb-seeded α-synucleinopathy is the limbic system and the ensuing pathology is higher in male than in female mice.Brain pathology (Zurich, Switzerland) · 2019Article
- Slow Progressive Accumulation of Oligodendroglial Alpha-Synuclein (α-Syn) Pathology in Synthetic α-Syn Fibril-Induced Mouse Models of Synucleinopathy.Journal of neuropathology and experimental neurology · 2019Article
- Human myeloperoxidase (hMPO) is expressed in neurons in the substantia nigra in Parkinson's disease and in the hMPO-α-synuclein-A53T mouse model, correlating with increased nitration and aggregation of α-synuclein and exacerbation of motor impairment.Free radical biology & medicine · 2019Article
- Oxidative stress in vagal neurons promotes parkinsonian pathology and intercellular α-synuclein transfer.The Journal of clinical investigation · 2019Article
- Parkinsonian GM2 synthase knockout mice lacking mature gangliosides develop urinary dysfunction and neurogenic bladder.Experimental neurology · 2019Article
- Physiological C-terminal truncation of α-synuclein potentiates the prion-like formation of pathological inclusions.The Journal of biological chemistry · 2018Article
- Localized Induction of Wild-Type and Mutant Alpha-Synuclein Aggregation Reveals Propagation along Neuroanatomical Tracts.Journal of virology · 2018Article
- Induction of the Immunoproteasome Subunit Lmp7 Links Proteostasis and Immunity in α-Synuclein Aggregation Disorders.EBioMedicine · 2018Article
- Reversible Conformational Conversion of α-Synuclein into Toxic Assemblies by Glucosylceramide.Neuron · 2018Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Sensitive detection of alpha-synuclein (alpha-syn) pathology is important in the diagnosis of disorders like Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy and in providing better insights into the etiology of these diseases. Several monoclonal antibodies that selectively react with aggregated alpha-syn in pathological inclusions and reveal extensive and underappreciated alpha-syn pathology in the brains of diseased patients were previously reported by Duda et al. (Ann Neurol 52:205-210, 2002). We sought to characterize the specificity of some of these antibodies (Syn 505, Syn 506 and Syn 514); using C-terminal and N-terminal truncations of alpha-syn, all three antibodies were determined to require N-terminal epitopes that minimally comprise amino acids 2-4, but possibly extend to amino acid 12 of alpha-syn. The selectivity of these antibodies was further assessed using biochemical analysis of human brains and reactivity to altered recombinant alpha-syn proteins with duplication variants of amino acids 1-12. In addition, by expressing wild-type or a double mutant (E46K/A53T) of alpha-syn in cultured cells and by comparing their immunoreactivities to another antibody (SNL-4), which has a similar primary epitope, it was determined that Syn 505, Syn 506 and Syn 514 recognize conformational variants of alpha-syn that is enhanced by the presence of the double mutations. These studies indicate that antibodies Syn 505, Syn 506 and Syn 514 preferentially recognize N-terminal epitopes in complex conformations, consistent with the dramatic conformational change associated with the polymerization of alpha-synuclein into amyloid fibrils that form pathological inclusions.
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