ArticleScientific reports2017
Split GFP technologies to structurally characterize and quantify functional biomolecular interactions of FTD-related proteins.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Loss of TDP-43 oligomerization or RNA binding elicits distinct aggregation patterns.The EMBO journal · 2023Article
- Article
- Monomerization of TDP-43 is a key determinant for inducing TDP-43 pathology in amyotrophic lateral sclerosis.Science advances · 2023Article
- Tau protein binds to the P53 E3 ubiquitin ligase MDM2.Scientific reports · 2023Article
- Sequestration of LINE-1 in cytosolic aggregates by MOV10 restricts retrotransposition.EMBO reports · 2022Article
- Parkinson's disease motor symptoms rescue by CRISPRa-reprogramming astrocytes into GABAergic neurons.EMBO molecular medicine · 2022Article
- Monitoring the interactions between alpha-synuclein and Tau in vitro and in vivo using bimolecular fluorescence complementation.Scientific reports · 2022Article
- SARS-CoV-2 variants as super cell fusers: cause or consequence of COVID-19 severity?The EMBO journal · 2021Article
- In vivo Validation of Bimolecular Fluorescence Complementation (BiFC) to Investigate Aggregate Formation in Amyotrophic Lateral Sclerosis (ALS).Molecular neurobiology · 2021Article
- Tau affects P53 function and cell fate during the DNA damage response.Communications biology · 2020Article
- The Role of RNA in HIV-1 Vif-Mediated Degradation of APOBEC3H.Journal of molecular biology · 2019Article
- Development and Applications of Superfolder and Split Fluorescent Protein Detection Systems in Biology.International journal of molecular sciences · 2019Review
- Design of a chromogenic substrate for elastase based on split GFP system-Proof of concept for colour switch sensors.Biotechnology reports (Amsterdam, Netherlands) · 2019Article
- Structural Insights Into TDP-43 and Effects of Post-translational Modifications.Frontiers in molecular neuroscience · 2019Review
- Genetically Encoded Fluorescent Biosensors Illuminate the Spatiotemporal Regulation of Signaling Networks.Chemical reviews · 2018Review
- Phosphorylation of nuclear Tau is modulated by distinct cellular pathways.Scientific reports · 2018Article
- Tdp-25 Routing to Autophagy and Proteasome Ameliorates its Aggregation in Amyotrophic Lateral Sclerosis Target Cells.Scientific reports · 2018Article
- Recent Insights on Alzheimer's Disease Originating from Yeast Models.International journal of molecular sciences · 2018Review
- Analysis of the substrate recognition state of TDP-43 to single-stranded DNA using fluorescence correlation spectroscopy.Biochemistry and biophysics reports · 2018Article
- Using High-Throughput Animal or Cell-Based Models to Functionally Characterize GWAS Signals.Current genetic medicine reports · 2018Review
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9 authors.
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Abstract
Protein multimerization in physiological and pathological conditions constitutes an intrinsic trait of proteins related to neurodegeneration. Recent evidence shows that TDP-43, a RNA-binding protein associated with frontotemporal dementia and amyotrophic lateral sclerosis, exists in a physiological and functional nuclear oligomeric form, whose destabilization may represent a prerequisite for misfolding, toxicity and subsequent pathological deposition. Here we show the parallel implementation of two split GFP technologies, the GFP bimolecular and trimolecular fluorescence complementation (biFC and triFC) in the context of TDP-43 self-assembly. These techniques coupled to a variety of assays based on orthogonal readouts allowed us to define the structural determinants of TDP-43 oligomerization in a qualitative and quantitative manner. We highlight the versatility of the GFP biFC and triFC technologies for studying the localization and mechanisms of protein multimerization in the context of neurodegeneration.
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