ArticleNature communications2023
Structural and photophysical characterization of the small ultra-red fluorescent protein.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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
10 citing papers in PubMed, 14 citations in OpenAlex.
- Serpin-driven green camouflage and NIR fluorescence in frogs.Science advances · 2026Article
- Emerging trends of fluorescence lifetime imaging microscopy (FLIM): advances, challenges, and prospects.Biophysics reports · 2026Article
- Host-specific fluorescence dynamics in legume-rhizobium symbiosis during nodulation.Applied and environmental microbiology · 2026Article
- Hyperspectral reporters for long-distance and wide-area detection of gene expression in living bacteria.Nature biotechnology · 2026Article
- Feeling the vibes: Vibrational spectroscopic imaging of biomolecular assemblies in their natural environment.Applied physics reviews · 2025Article
- Engineering a Bright Near-Infrared Fluorescent Protein by Screening a Comprehensive Phenotypic Landscape.bioRxiv : the preprint server for biology · 2025Article
- Characterization and structural basis for the brightness of mCLIFY: A novel monomeric and circularly permuted bright yellow fluorescent protein.Biophysical journal · 2025Article
- Protocol for CRISPR-based endogenous protein tagging in mammalian cells.STAR protocols · 2024Article
- Characterization and structural basis for the brightness of mCLIFY: a novel monomeric and circularly permuted bright yellow fluorescent protein.Research square · 2024Article
- More than double the fun with two-photon excitation microscopy.Communications biology · 2024Review
Corrections and comments
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Authors and funding
16 authors at 11 institutions in 2 countries.
Funding
Abstract
The small Ultra-Red Fluorescent Protein (smURFP) represents a new class of fluorescent protein with exceptional photostability and brightness derived from allophycocyanin in a previous directed evolution. Here, we report the smURFP crystal structure to better understand properties and enable further engineering of improved variants. We compare this structure to the structures of allophycocyanin and smURFP mutants to identify the structural origins of the molecular brightness. We then use a structure-guided approach to develop monomeric smURFP variants that fluoresce with phycocyanobilin but not biliverdin. Furthermore, we measure smURFP photophysical properties necessary for advanced imaging modalities, such as those relevant for two-photon, fluorescence lifetime, and single-molecule imaging. We observe that smURFP has the largest two-photon cross-section measured for a fluorescent protein, and that it produces more photons than organic dyes. Altogether, this study expands our understanding of the smURFP, which will inform future engineering toward optimal FPs compatible with whole organism studies.
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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.