ArticleScientific reports2015
Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson's disease patients.
Article in Scientific reports, 2015. 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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53 citing papers in PubMed, 97 citations in OpenAlex.
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- Molecular polymorphism of tau aggregates in Pick's disease.Neurobiology of disease · 2025Article
- Nanoplasmonic Infrared Microarray Sensor Enabling Structural Protein Biomarker-Based Drug Screening for Neurodegenerative Diseases.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Expanding our understanding of synucleinopathies: proteinopathy, proteinopenia, and lipidopathy.The FEBS journal · 2025Review
- FTIR-based molecular fingerprinting for the rapid classification of dengue and chikungunya from human sera using machine learning: an observational study.The Lancet regional health. Southeast Asia · 2025Article
- Conformational Switch in the Alpha-Synuclein C-Terminal Domain Directs Its Fibril Polymorphs.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- The Neuroprotective Effects of Agmatine on Parkinson's Disease: Focus on Oxidative Stress, Inflammation and Molecular Mechanisms.Inflammation · 2025Review
- Label-free Aβ plaque detection in Alzheimer's disease brain tissue using infrared microscopy and neural networks.Heliyon · 2025Article
- Effect of Extraction Methods and Preheat Treatments on the Functional Properties of Pumpkin Seed Protein Concentrate.ACS food science & technology · 2025Article
- RXR nuclear receptor signaling modulates lipid metabolism and triggers lysosomal clearance of alpha-synuclein in neuronal models of synucleinopathy.Cellular and molecular life sciences : CMLS · 2024Article
- Role of Lipids in the Pathogenesis of Parkinson's Disease.International journal of molecular sciences · 2024Review
- Pathological mechanisms and treatment of sporadic Parkinson's disease: past, present, and future.Journal of neural transmission (Vienna, Austria : 1996) · 2024Review
- Molecular Behavior of α-Synuclein Is Associated with Membrane Transport, Lipid Metabolism, and Ubiquitin-Proteasome Pathways in Lewy Body Disease.International journal of molecular sciences · 2024Article
- Synthetic β-sheets mimicking fibrillar and oligomeric structures for evaluation of spectral X-ray scattering technique for biomarker quantification.Cell & bioscience · 2024Article
- Linking acetylated α-Tubulin redistribution to α-Synuclein pathology in brain of Parkinson's disease patients.NPJ Parkinson's disease · 2024Article
- Defining a Lewy Body: Running Up the Hill of Shifting Definitions and Evolving Concepts.Journal of Parkinson's disease · 2024Review
- Artificial intelligence-coupled plasmonic infrared sensor for detection of structural protein biomarkers in neurodegenerative diseases.Science advances · 2023Article
- Phosphatidylinositol-3,4,5-trisphosphate interacts with alpha-synuclein and initiates its aggregation and formation of Parkinson's disease-related fibril polymorphism.Acta neuropathologica · 2023Article
- Biomolecular alterations detected in multiple sclerosis skin fibroblasts using Fourier transform infrared spectroscopy.Frontiers in cellular neuroscience · 2023Article
- Monitoring α-synuclein aggregation.Neurobiology of disease · 2023Review
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Authors and funding
13 authors at 5 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Lewy bodies (LBs), which mainly consist of α-synuclein (α-syn), are neuropathological hallmarks of patients with Parkinson's disease (PD). The fine structure of LBs is unknown, and LBs cannot be made artificially. Nevertheless, many studies have described fibrillisation using recombinant α-syn purified from E. coli. An extremely fundamental problem is whether the structure of LBs is the same as that of recombinant amyloid fibrils. Thus, we used synchrotron Fourier transform infrared micro-spectroscopy (FTIRM) to analyse the fine structure of LBs in the brain of PD patients. Our results showed a shift in the infrared spectrum that indicates abundance of a β-sheet-rich structure in LBs. Also, 2D infrared mapping of LBs revealed that the content of the β-sheet structure is higher in the halo than in the core, and the core contains a large amount of proteins and lipids.
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