ArticleCell reports2019
Quantitative Characterization of α-Synuclein Aggregation in Living Cells through Automated Microfluidics Feedback Control.
Article in Cell reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed.
- Concentration-dependent mutational scanning probes the cellular folding landscape of α-synuclein in yeast.Protein science : a publication of the Protein Society · 2026Article
- Microfluidic platform for understanding Parkinson's disease and α-synuclein conformation.Translational neurodegeneration · 2025Review
- Concentration-Dependent Mutational Scanning Probes the Cellular Folding Landscape of α-Synuclein in Yeast.bioRxiv : the preprint server for biology · 2025Article
- Integrating bioengineering, super-resolution microscopy and mechanobiology in autophagy research: addendum to the guidelines (4th edition).Autophagy · 2025Article
- α-synuclein and tau: interactions, cross-seeding, and the redefinition of synucleinopathies as complex proteinopathies.Frontiers in neuroscience · 2025Review
- Neuropathogenesis-on-chips for neurodegenerative diseases.Nature communications · 2024Review
- Deep model predictive control of gene expression in thousands of single cells.Nature communications · 2024Article
- Sporadic SNCA mutations A18T and A29S exhibit variable effects on protein aggregation, cell viability and oxidative stress.Molecular biology reports · 2023Article
- Neurodegenerative disease-associated inclusion bodies are cleared by selective autophagy in budding yeast.Autophagy reports · 2023Article
- Monitoring α-synuclein aggregation.Neurobiology of disease · 2023Review
- Enabling reactive microscopy with MicroMator.Nature communications · 2022Article
- Cybergenetic control of microbial community composition.Frontiers in bioengineering and biotechnology · 2022Review
- Exploiting Information and Control Theory for Directing Gene Expression in Cell Populations.Frontiers in microbiology · 2022Review
- Rapid prototyping and design of cybergenetic single-cell controllers.Nature communications · 2021Article
- Review
- Automatic synchronisation of the cell cycle in budding yeast through closed-loop feedback control.Nature communications · 2021Article
- ChipSeg: An Automatic Tool to Segment Bacterial and Mammalian Cells Cultured in Microfluidic Devices.ACS omega · 2021Article
- Functional roles of microbial cell-to-cell heterogeneity and emerging technologies for analysis and control.Current opinion in microbiology · 2020Review
- From Synaptic Protein to Prion: The Long and Controversial Journey of α-Synuclein.Frontiers in synaptic neuroscience · 2020Review
- Proteostasis of α-Synuclein and Its Role in the Pathogenesis of Parkinson's Disease.Frontiers in cellular neuroscience · 2020Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aggregation of α-synuclein and formation of inclusions are hallmarks of Parkinson's disease (PD). Aggregate formation is affected by cellular environment, but it has been studied almost exclusively in cell-free systems. We quantitatively analyzed α-synuclein inclusion formation and clearance in a yeast cell model of PD expressing either wild-type (WT) α-synuclein or the disease-associated A53T mutant from the galactose (Gal)-inducible promoter. A computer-controlled microfluidics device regulated α-synuclein in cells by means of closed-loop feedback control. We demonstrated that inclusion formation is strictly concentration dependent and that the aggregation threshold of the A53T mutant is about half of the WT α-synuclein (56%). We chemically modulated the proteasomal and autophagic pathways and demonstrated that autophagy is the main determinant of A53T α-synuclein inclusions' clearance. In addition to proposing a technology to overcome current limitations in dynamically regulating protein expression levels, our results contribute to the biology of PD and have relevance for therapeutic applications.
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Registered trials
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