ArticleProtein science : a publication of the Protein Society2013
Structural basis of fluorescence quenching in caspase activatable-GFP.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- Engineering fusion enzymes for enhanced catalysis and stability: strategies and biotechnological applications.Molecular biology reports · 2026Review
- Exploring Water Beyond the Solvent: Insights into Density Fluctuations and EGFP Unfolding via Luminescence Thermometry.The journal of physical chemistry. B · 2025Article
- GeoEvoBuilder: A deep learning framework for efficient functional and thermostable protein design.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Chemogenetic and optogenetic strategies for spatiotemporal control of split-enzyme-based calcium recording.bioRxiv : the preprint server for biology · 2025Article
- Protein Engineering for Spatiotemporally Resolved Cellular Monitoring.Annual review of analytical chemistry (Palo Alto, Calif.) · 2025Review
- Evaluating the specificity of flavivirus proteases in Aedes aegypti cells for dengue virus 2-derived cleavage sites.PloS one · 2024Article
- Modular Bioorthogonal Lipid Nanoparticle Modification Platforms for Cardiac Homing.Journal of the American Chemical Society · 2023Article
- A highly sensitive NanoLuc-based protease biosensor for detecting apoptosis and SARS-CoV-2 infection.Scientific reports · 2023Article
- Pressure and temperature dependence of fluorescence anisotropy of green fluorescent protein.RSC advances · 2022Article
- Article
- Tracking exogenous intracellular casp-3 using split GFP.Protein science : a publication of the Protein Society · 2021Article
- Controlling Optical and Catalytic Activity of Genetically Engineered Proteins by Ultrasound.Angewandte Chemie (International ed. in English) · 2021Article
- MeasuringGenetics · 2020Article
- A fluorescence-activatable reporter of flavivirus NS2B-NS3 protease activity enables live imaging of infection in single cells and viral plaques.The Journal of biological chemistry · 2020Article
- Development of a fluorescence-based cellular apoptosis reporter.Methods and applications in fluorescence · 2018Article
- The Use ofFrontiers in veterinary science · 2018Review
- Live Cell Reporter Systems for Positive-Sense Single Strand RNA Viruses.Applied biochemistry and biotechnology · 2016Review
- A tunable, modular approach to fluorescent protease-activated reporters.Biophysical journal · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Apoptosis is critical for organismal homeostasis and a wide variety of diseases. Caspases are the ultimate executors of the apoptotic programmed cell death pathway. As caspases play such a central role in apoptosis, there is significant demand for technologies to monitor caspase function. We recently developed a caspase activatable-GFP (CA-GFP) reporter. CA-GFP is unique due to its "dark" state, where chromophore maturation of the GFP is inhibited by the presence of a C-terminal peptide. Here we show that chromophore maturation is prevented because CA-GFP does not fold into the robust β-barrel of GFP until the peptide has been cleaved by active caspase. Both CA-GFP and GFP₁₋₁₀ , a split form of GFP lacking the 11th strand, have similar secondary structure, different from mature GFP. A similar susceptibility to proteolytic digestion indicates that this shared structure is not the robust, fully formed GFP β-barrel. We have developed a model that suggests that as CA-GFP is translated in vivo it follows the same folding path as wild-type GFP; however, the presence of the appended peptide does not allow CA-GFP to form the barrel of the fully matured GFP. CA-GFP is therefore held in a "pro-folding" intermediate state until the peptide is released, allowing it to continue folding into the mature barrel geometry. This new understanding of the structural basis of the dark state of the CA-GFP reporter will enable manipulation of this mechanism in the development of reporter systems for any number of cellular processes involving proteases and potentially other enzymes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.