ArticleMethods in enzymology2019
Utilizing split-NanoLuc luciferase fragments as luminescent probes for protein solubility in living cells.
Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Rapid, expression-free bacteriophage-based specific detection of target bacteria by conditional release of encapsidated reporter molecules.Bioengineering & translational medicine · 2026Article
- Targeting papillomavirus infections: high-throughput screening reveals an effective inhibitor of cutaneous β-HPV types.Journal of virology · 2025Article
- Review
- A Luminescence-Based System for Identification of Genetically Encodable Inhibitors of Protein Aggregation.ACS omega · 2020Article
- A luminescence-based assay for monitoring changes in alpha-synuclein aggregation in living cells.RSC advances · 2020Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein misfolding and aggregation is now recognized as a hallmark of numerous human diseases. Standard bioanalytical techniques for monitoring protein aggregation generally rely on small molecules that provide an optical readout of fibril formation. While these methods have been useful for mechanistic studies, additional approaches are required to probe the equilibrium between soluble and insoluble protein within living systems. Such approaches could provide platforms for the identification of inhibitors of protein aggregation as well as a means to investigate the effect of mutations on protein aggregation in model systems. In this chapter, we provide detailed protocols for employing split-NanoLuc luciferase (Nluc) fragments to monitor changes in protein solubility in bacterial and mammalian cells. This sensitive luminesce-based assay can report upon changes in protein solubility induced by inhibitors and disease-relevant mutations.
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