ArticleMolecular systems biology2018
LuTHy: a double-readout bioluminescence-based two-hybrid technology for quantitative mapping of protein-protein interactions in mammalian cells.
Article in Molecular systems biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed.
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- Variant characterization in the intrinsically disordered human proteome.Nature structural & molecular biology · 2026Article
- Cysteine string protein α and a link between rare and common neurodegenerative dementias.NPJ dementia · 2025Review
- TPepPro: a deep learning model for predicting peptide-protein interactions.Bioinformatics (Oxford, England) · 2024Article
- A comprehensive two-hybrid analysis to explore themSystems · 2024Article
- Molecular architecture of synaptic vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- AI Promoted Virtual Screening, Structure-Based Hit Optimization, and Synthesis of Novel COVID-19 S-RBD Domain Inhibitors.Journal of chemical information and modeling · 2024Article
- MACC1 revisited - an in-depth review of a master of metastasis.Biomarker research · 2024Review
- A TBK1 variant causes autophagolysosomal and motoneuron pathology without neuroinflammation in mice.The Journal of experimental medicine · 2024Article
- AI-guided pipeline for protein-protein interaction drug discovery identifies a SARS-CoV-2 inhibitor.Molecular systems biology · 2024Article
- Systematic discovery of protein interaction interfaces using AlphaFold and experimental validation.Molecular systems biology · 2024Article
- Delineation of functional subdomains of Huntingtin protein and their interaction with HAP40.Structure (London, England : 1993) · 2023Article
- A systematic approach to identify host targets and rapidly deliver broad-spectrum antivirals.Molecular therapy : the journal of the American Society of Gene Therapy · 2022Article
- Dynamics of huntingtin protein interactions in the striatum identifies candidate modifiers of Huntington disease.Cell systems · 2022Article
- The macrophage odorant receptor Olfr78 mediates the lactate-induced M2 phenotype of tumor-associated macrophages.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Ccdc103 promotes myeloid cell proliferation and migration independent of motile cilia.Disease models & mechanisms · 2021Article
- Split Intein-Mediated Protein Ligation for detecting protein-protein interactions and their inhibition.Nature communications · 2020Article
- Maximizing binary interactome mapping with a minimal number of assays.Nature communications · 2019Article
- Structured Methods for reproducible science.Molecular systems biology · 2018Article
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Abstract
Information on protein-protein interactions (PPIs) is of critical importance for studying complex biological systems and developing therapeutic strategies. Here, we present a double-readout bioluminescence-based two-hybrid technology, termed LuTHy, which provides two quantitative scores in one experimental procedure when testing binary interactions. PPIs are first monitored in cells by quantification of bioluminescence resonance energy transfer (BRET) and, following cell lysis, are again quantitatively assessed by luminescence-based co-precipitation (LuC). The double-readout procedure detects interactions with higher sensitivity than traditional single-readout methods and is broadly applicable, for example, for detecting the effects of small molecules or disease-causing mutations on PPIs. Applying LuTHy in a focused screen, we identified 42 interactions for the presynaptic chaperone CSPα, causative to adult-onset neuronal ceroid lipofuscinosis (ANCL), a progressive neurodegenerative disease. Nearly 50% of PPIs were found to be affected when studying the effect of the disease-causing missense mutations L115R and ∆L116 in CSPα with LuTHy. Our study presents a robust, sensitive research tool with high utility for investigating the molecular mechanisms by which disease-associated mutations impair protein activity in biological systems.
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