ArticleScientific reports2018
Characterization of Split Fluorescent Protein Variants and Quantitative Analyses of Their Self-Assembly Process.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 28 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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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.
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Who cites it
28 citing papers in PubMed, 51 citations in OpenAlex.
- Intensity modulation of trichromatic split fluorescent proteins for live cell mapping.Cell reports methods · 2026Article
- Bipartite Genetically Encoded Biosensors to Sense Calcium Ion Dynamics at Membrane-Membrane Contact Sites.Analytical chemistry · 2025Article
- Immobilization and enhancement of a heterodimeric fluorescence biosensor in fibrous protein biomaterials.Protein science : a publication of the Protein Society · 2025Article
- DNA-Regulated Multi-Protein Complement Control.Journal of the American Chemical Society · 2024Article
- Article
- FAST, a method based on split-GFP for the detection in solution of proteins synthesized in cell-free expression systems.Scientific reports · 2024Article
- Article
- Fluorescent biosensors illuminate the spatial regulation of cell signaling across scales.The Biochemical journal · 2023Review
- A single-domain green fluorescent protein catenane.Nature communications · 2023Article
- CRISPR-Cas9-Mediated Knock-In Approach to Insert the GFPMethods in molecular biology (Clifton, N.J.) · 2023Article
- Assessment of oligomerization of bacterial micro-compartment shell components with the tripartite GFP reporter technology.PloS one · 2023Article
- Generalized Bioluminescent Platform To Observe and Track Cellular Interactions.Bioconjugate chemistry · 2022Article
- The expanding role of split protein complementation in opsin-free optogenetics.Current opinion in pharmacology · 2022Review
- Review
- Article
- Engineering an efficient and bright split Corynactis californica green fluorescent protein.Scientific reports · 2021Article
- Split-wrmScarlet and split-sfGFP: tools for faster, easier fluorescent labeling of endogenous proteins in Caenorhabditis elegans.Genetics · 2021Article
- Challenges facing quantitative large-scale optical super-resolution, and some simple solutions.iScience · 2021Review
- Multiplexed labeling of cellular proteins with split fluorescent protein tags.Communications biology · 2021Article
- Tracking exogenous intracellular casp-3 using split GFP.Protein science : a publication of the Protein Society · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many biotechniques use complementary split-fluorescent protein (sFPs) fragments to visualize protein-protein interactions, image cells by ensemble or single molecule fluorescence microscopy, or assemble nanomaterials and protein superstructures. Yet, the reassembly mechanisms of sFPs, including fragment binding rates, folding, chromophore maturation and overall photophysics remain poorly characterized. Here, we evolved asymmetric and self-complementing green, yellow and cyan sFPs together with their full-length equivalents (flFPs) and described their biochemical and photophysical properties in vitro and in cells. While re-assembled sFPs have spectral properties similar to flFPs, they display slightly reduced quantum yields and fluorescence lifetimes due to a less sturdy β-barrel structure. The complementation of recombinant sFPs expressed in vitro follows a conformational selection mechanism whereby the larger sFP fragments exist in a monomer-dimer equilibrium and only monomers are competent for fluorescence complementation. This bimolecular fragment interaction involves a slow and irreversible binding step, followed by chromophore maturation at a rate similar to that of flFPs. When expressed as fusion tags in cells, sFPs behave as monomers directly activated with synthetic complementary fragments. This study resulted in the development of sFP color variants having improved maturation kinetics, brightness, and photophysics for fluorescence microscopy imaging of cellular processes, including single molecule detection.
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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.