ArticleBiophysical journal2010
Early aggregation steps in alpha-synuclein as measured by FCS and FRET: evidence for a contagious conformational change.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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Who cites it
74 citing papers in PubMed, 158 citations in OpenAlex.
- Microfluidic platform for understanding Parkinson's disease and α-synuclein conformation.Translational neurodegeneration · 2025Review
- Computational Fluid Dynamic Model Prediction of Enhanced Glymphatic Clearance in Response to Focused Ultrasound-Mediated Blood-Brain Barrier Opening.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Direct disassembly of α-syn preformed fibrils into α-syn monomers by an all-D-peptide.NPJ Parkinson's disease · 2025Article
- Comparative Analysis of Aggregation of β- and γ-Synucleins in Vertebrates.Biomolecules · 2025Article
- Criterion for Assessing Accumulated Neurotoxicity of Alpha-Synuclein Oligomers in Parkinson's Disease.International journal for numerical methods in biomedical engineering · 2025Article
- The role of RNA in the nanoscale organization of α-synuclein phase separation.NAR molecular medicine · 2025Article
- Astrocyte alterations in α-synucleinopathies.Frontiers in cellular neuroscience · 2025Review
- Unravelling γD-crystallin aggregation pathway to understand cataract formation using fluorescence correlation spectroscopy.Molecular vision · 2025Article
- Unravelling γD-crystallin aggregation pathway to understand cataract formation using fluorescence correlation spectroscopy.Molecular vision · 2025Article
- Targeting Protein Misfolding and Aggregation as a Therapeutic Perspective in Neurodegenerative Disorders.International journal of molecular sciences · 2024Review
- Article
- Toward the quantification of α-synuclein aggregates with digital seed amplification assays.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Experimental methods to study the structure and dynamics of intrinsically disordered regions in proteins.Current research in structural biology · 2024Review
- Single-photon microscopy to study biomolecular condensates.Nature communications · 2023Article
- Single-Molecule Detection of α-Synuclein Oligomers in Parkinson's Disease Patients Using Nanopores.ACS nano · 2023Article
- Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein.Scientific reports · 2023Article
- Dynein Dysfunction Prevents Maintenance of High Concentrations of Slow Axonal Transport Cargos at the Axon Terminal: A Computational Study.Journal of biomechanical engineering · 2023Article
- Single-Molecule Two-Color Coincidence Detection of Unlabeled alpha-Synuclein Aggregates.Angewandte Chemie (International ed. in English) · 2023Article
- Single-Molecule Two-Color Coincidence Detection of Unlabeled alpha-Synuclein Aggregates.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Article
- Effects of Mutations and Post-Translational Modifications on α-Synuclein In Vitro Aggregation.Journal of molecular biology · 2022Review
14 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The kinetics of aggregation of alpha-synuclein are usually studied by turbidity or Thio-T fluorescence. Here we follow the disappearance of monomers and the formation of early oligomers using fluorescence correlation spectroscopy. Alexa488-labeled A140C-synuclein was used as a fluorescent probe in trace amounts in the presence of excess unlabeled alpha-synuclein. Repeated short measurements produce a distribution of diffusion coefficients. Initially, a sharp peak is obtained corresponding to monomers, followed by a distinct transient population and the gradual formation of broader-sized distributions of higher oligomers. The kinetics of aggregation can be followed by the decreasing number of fast-diffusing species. Both the disappearance of fast-diffusing species and the appearance of turbidity can be fitted to the Finke-Watzky equation, but the apparent rate constants obtained are different. This reflects the fact that the disappearance of fast species occurs largely during the lag phase of turbidity development, due to the limited sensitivity of turbidity to the early aggregation process. The nucleation of the early oligomers is concentration-dependent and accompanied by a conformational change that precedes beta-structure formation, and can be visualized using fluorescence resonance energy transfer between the donor-labeled N-terminus and the acceptor-labeled cysteine in the mutant A140C.
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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.