ReviewPhotochemistry and photobiology
Fluorescent proteins: A journey from the cell to extreme environments in material science.
Review in Photochemistry and photobiology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed.
- Genetically encoded tools for tracking metabolites in live cells.Biochemical Society transactions · 2026Review
- Genetic Encoding of 3-Cyano-Tyrosine and Its Use in Controlling the Chromophore Isomeric State of the Fluorescent Protein mKate.International journal of molecular sciences · 2026Article
- Advances in Coumarin Fluorescent Probes for Medical Diagnostics: A Review of Recent Developments.Biosensors · 2026Review
- Fluorescent proteins: A journey from the cell to extreme environments in material science.Photochemistry and photobiologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
This review presents the progression from the use of fluorescent proteins (FPs) and chromoproteins as bioimaging labels and sensors to the strategic engineering of their properties for robust functionality in synthetic and non-biological environments. Specifically, engineered variants of the small ultra-red fluorescent protein (smURFP) were developed and optimized for optoacoustic imaging through structure-guided mutagenesis. Reversibly switchable genetically encoded indicators were also created to enhance bioimaging capabilities. To extend the applicability of such proteins to material science and enable their function in everyday applications-such as environmental sensors, encoders, or color components in textiles and electronics-their inherent stability limitations were addressed. For this purpose, supramolecular stabilization strategies, including genetically encoded macro-oligomerization techniques, were explored. These methods effectively enhanced the resilience of FPs under chemically challenging conditions, without compromising their photophysical properties. Finally, the exploration of circularly polarized luminescence (CPL) from FPs is discussed, and their potential as CPL emitters suitable for sustainable photonic applications is identified. Overall, the transformative potential of engineered FPs as essential components for applications beyond bioimaging is emphasized.
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Identifiers
What OpenQuestion holds
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.