ArticlePloS one2012
Quantitative analysis of α-synuclein solubility in living cells using split GFP complementation.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Article
- Dynamic behaviors of α-synuclein and tau in the cellular context: New mechanistic insights and therapeutic opportunities in neurodegeneration.Neurobiology of disease · 2019Review
- The center of olfactory bulb-seeded α-synucleinopathy is the limbic system and the ensuing pathology is higher in male than in female mice.Brain pathology (Zurich, Switzerland) · 2019Article
- Development and Applications of Superfolder and Split Fluorescent Protein Detection Systems in Biology.International journal of molecular sciences · 2019Review
- A Split Transcriptional Repressor That Links Protein Solubility to an Orthogonal Genetic Circuit.ACS synthetic biology · 2018Article
- Endoplasmic Reticulum Stress Response in Arabidopsis Roots.Frontiers in plant science · 2017Article
- Structure-Based Drug Discovery for Prion Disease Using a Novel Binding Simulation.EBioMedicine · 2016Article
- Characterization of aggregate/aggresome structures formed by polyhedrin of Bombyx mori nucleopolyhedrovirus.Scientific reports · 2015Article
- Article
- Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs).Chemical reviews · 2014Review
- Chemical induction of Hsp70 reduces α-synuclein aggregation in neuroglioma cells.ACS chemical biology · 2013Article
- Environmental stresses induce misfolded protein aggregation in plant cells in a microtubule-dependent manner.International journal of molecular sciences · 2013Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Presently incurable, Parkinson's disease (PD) is the most common neurodegenerative movement disorder and affects 1% of the population over 60 years of age. The hallmarks of PD pathogenesis are the loss of dopaminergic neurons in the substantia nigra pars compacta, and the occurrence of proteinaceous cytoplasmic inclusions (Lewy bodies) in surviving neurons. Lewy bodies are mainly composed of the pre-synaptic protein alpha-synuclein (αsyn), an intrinsically unstructured, misfolding-prone protein with high propensity to aggregate. Quantifying the pool of soluble αsyn and monitoring αsyn aggregation in living cells is fundamental to study the molecular mechanisms of αsyn-induced cytotoxicity and develop therapeutic strategies to prevent αsyn aggregation. In this study, we report the use of a split GFP complementation assay to quantify αsyn solubility. Particularly, we investigated a series of naturally occurring and rationally designed αsyn variants and showed that this method can be used to study how αsyn sequence specificity affects its solubility. Furthermore, we demonstrated the utility of this assay to explore the influence of the cellular folding network on αsyn solubility. The results presented underscore the utility of the split GFP assay to quantify αsyn solubility in living cells.
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