ArticleThe journal of physical chemistry letters2018
Different Conformational Subensembles of the Intrinsically Disordered Protein α-Synuclein in Cells.
Article in The journal of physical chemistry letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 51 citations in OpenAlex.
- Controlling interfacial protein adsorption, desorption and aggregation in biomolecular condensates.Nature communications · 2025Article
- Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Exploring α-Syn's Functions Through Ablation Models: Physiological and Pathological Implications.Cellular and molecular neurobiology · 2025Review
- Interplay between lipid droplets and alpha-synuclein: implication in Parkinson's disease pathogenesis.Frontiers in molecular neuroscience · 2025Review
- The role of biomolecular condensates in protein aggregation.Nature reviews. Chemistry · 2024Review
- 14-3-3τ as a Modulator of Early α-Synuclein Multimerization and Amyloid Formation.ACS chemical neuroscience · 2024Article
- Exploring Intra- and Inter-Regional Interactions in the IDP α-Synuclein Using smFRET and MD Simulations.Biomacromolecules · 2023Article
- Dissecting the Self-assembly Dynamics of Imperfect Repeats in α-Synuclein.Journal of chemical information and modeling · 2023Article
- The Interplay between α-Synuclein and Microglia in α-Synucleinopathies.International journal of molecular sciences · 2023Review
- Potential role of N6-methyladenosine modification in the development of Parkinson's disease.Frontiers in cell and developmental biology · 2023Review
- Biomolecular condensates can both accelerate and suppress aggregation of α-synuclein.Science advances · 2022Article
- A comprehensive mini-review on amyloidogenesis of different SARS-CoV-2 proteins and its effect on amyloid formation in various host proteins.3 Biotech · 2022Review
- Interactions between SARS-CoV-2 N-Protein and α-Synuclein Accelerate Amyloid Formation.ACS chemical neuroscience · 2022Article
- Deciphering the Structure and Formation of Amyloids in Neurodegenerative Diseases With Chemical Biology Tools.Frontiers in chemistry · 2022Review
- α-Synuclein-mediated neurodegeneration in Dementia with Lewy bodies: the pathobiology of a paradox.Cell & bioscience · 2021Review
- The role of neuroimaging in Parkinson's disease.Journal of neurochemistry · 2021Review
- Exploiting Complex Fluorophore Interactions to Monitor Virus Capsid Disassembly.Molecules (Basel, Switzerland) · 2021Article
- In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligomers.PloS one · 2021Article
- Alpha-Synuclein Aggregation in Parkinson's Disease.Frontiers in medicine · 2021Review
- α-Synuclein: An All-Inclusive Trip Around its Structure, Influencing Factors and Applied Techniques.Frontiers in chemistry · 2021Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The intrinsically disordered protein α-synuclein (αS) is thought to play an important role in cellular membrane processes. Although in vitro experiments indicate that this initially disordered protein obtains structure upon membrane binding, NMR and EPR studies in cells could not single out any conformational subensemble. Here we microinjected small amounts of αS, labeled with a Förster resonance energy transfer (FRET) pair, into SH-SY5Y cells to investigate conformational changes upon membrane binding. Our FRET studies show a clear conformational difference between αS in the cytosol and when bound to small vesicles. The identification of these different conformational subensembles inside cells resolves the apparent contradiction between in vitro and in vivo experiments and shows that at least two different conformational subensembles of αS exist in cells. The existence of conformational subensembles supports the idea that αS can obtain different functions which can possibly be dynamically addressed with changing intracellular physicochemical conditions.
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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.