ArticleJournal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology2009
Early stages for Parkinson's development: alpha-synuclein misfolding and aggregation.
Article in Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Impact of Gender and Race on Gastrointestinal Diseases in Patients With Parkinson's Disease: A Nationwide Analysis.JGH open : an open access journal of gastroenterology and hepatology · 2026Article
- Interplay between α-synuclein and parkin genes: Insights of Parkinson's disease.Molecular biology reports · 2024Review
- Designing and Formulation of Nanocarriers for "Alzheimer's and Parkinson's" Early Detection and Therapy.CNS & neurological disorders drug targets · 2024Review
- Early stages of misfolding of PAP248-286 at two different pH values: An insight from molecular dynamics simulations.Computational and structural biotechnology journal · 2022Article
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- Proteostasis Failure in Neurodegenerative Diseases: Focus on Oxidative Stress.Oxidative medicine and cellular longevity · 2020Review
- AFM Probing of Amyloid-Beta 42 Dimers and Trimers.Frontiers in molecular biosciences · 2020Article
- Probing the Basis of α-Synuclein Aggregation by Comparing Simulations to Single-Molecule Experiments.Biophysical journal · 2019Article
- Early stages of aggregation of engineered α-synuclein monomers and oligomers in solution.Scientific reports · 2019Article
- A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptides.Protein science : a publication of the Protein Society · 2018Article
- High-speed atomic force microscopy reveals structural dynamics of α-synuclein monomers and dimers.The Journal of chemical physics · 2018Article
- Single-Molecule Force Spectroscopy Studies of APOBEC3A-Single-Stranded DNA Complexes.Biochemistry · 2016Article
- Probing of Amyloid Aβ (14-23) Trimers by Single-Molecule Force Spectroscopy.Jacobs journal of molecular and translational medicine · 2016Article
- Drug Delivery Systems for Imaging and Therapy of Parkinson's Disease.Current neuropharmacology · 2016Review
- APOBEC3G Interacts with ssDNA by Two Modes: AFM Studies.Scientific reports · 2015Article
- Effect of pH on the Aggregation of α-syn12 Dimer in Explicit Water by Replica-Exchange Molecular Dynamics Simulation.International journal of molecular sciences · 2015Article
- Role of monomer arrangement in the amyloid self-assembly.Biochimica et biophysica acta · 2015Article
- Preconditioning as a potential strategy for the prevention of Parkinson's disease.Molecular neurobiology · 2015Review
- Amyloid misfolding, aggregation, and the early onset of protein deposition diseases: insights from AFM experiments and computational analyses.AIMS molecular science · 2015Article
- The structure of misfolded amyloidogenic dimers: computational analysis of force spectroscopy data.Biophysical journal · 2014Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Misfolding and aggregation of proteins are common threads linking a number of important human health problems, including various neurodegenerative disorders such as Parkinson's disease in particular. The first and perhaps most important elements in most neurodegenerative processes are misfolding and aggregation of specific proteins. Despite the crucial importance of protein misfolding and abnormal interactions, very little is currently known about the molecular mechanism underlying these processes. Factors that lead to protein misfolding and aggregation in vitro are poorly understood, in addition to the complexities involved in the formation of protein nanoparticles with different morphologies (e.g. nanopores and other species) in vivo. A clear understanding of the molecular mechanisms of misfolding and aggregation will facilitate rational approaches to prevent protein misfolding mediated pathologies. To accomplish this goal and to elucidate the mechanism of protein misfolding, we developed a novel nanotechnology tool capable of detecting protein misfolding. We applied single molecule probing technique to characterize misfolding and self-assembly of alpha-synuclein dimers, which is the very first step of the aggregation process. Using AFM force spectroscopy approach, we were able to detect protein misfolding via enhanced interprotein interaction. Moreover, such an important characteristic as the lifetime of dimers formed by misfolded alpha-synuclein was measured. These data suggest that compared to highly dynamic monomeric forms, alpha-synuclein dimers are practically static and thus can play a role of aggregation nuclei for the formation of aggregates. Importantly, two different dissociation channels were detected suggesting that aggregation process can follow different pathways. The application of these findings for understanding of the aggregation phenomenon and the development of the disease is discussed.
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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.