ArticleBiophysical journal2017
Enzyme-Triggered Dissociation of a FRET-Based Protein Biosensor Monitored by Synchrotron SAXS.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 8 citations in OpenAlex.
- Next-Generation Genetically Encoded Fluorescent Biosensors Illuminate Cell Signaling and Metabolism.Annual review of biophysics · 2024Review
- FRET Based Biosensor: Principle Applications Recent Advances and Challenges.Diagnostics (Basel, Switzerland) · 2023Review
- Structural Analysis of a Genetically Encoded FRET Biosensor by SAXS and MD Simulations.Sensors (Basel, Switzerland) · 2021Article
- Design of a chromogenic substrate for elastase based on split GFP system-Proof of concept for colour switch sensors.Biotechnology reports (Amsterdam, Netherlands) · 2019Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein biosensors are widely used for the monitoring of metabolite concentration and enzymatic activities inside living cells and in in vitro applications. Neutrophil elastase (NE) is a serine protease of relevance in inflammatory diseases whose activity can lead to pathological conditions if unregulated. This study focuses on the structural characterization of a biosensor for NE activity based on Förster resonance energy transfer (FRET). The cleavage by NE results in dissociation of the FRET fluorescent protein pair and alteration of the fluorescent emission spectrum. We have used small angle x-ray scattering at a high intensity synchrotron source, combined with model-free analysis of the scattering data, to demonstrate the structure of the biosensor and the effect of its exposure to NE on size and shape. These investigations, together with biochemical studies, established the nanostructure-activity relationship that may contribute to the detailed understanding of the FRET-based biosensor and guide the rational design of new biosensor constructs.
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Registered trials
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