ArticleChembiochem : a European journal of chemical biology2020
Engineering of a Red Fluorogenic Protein/Merocyanine Complex for Live-Cell Imaging.
Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- Photoisomerization detected in a fully wavelength-tunable rhodopsin mimic system.Acta crystallographica. Section D, Structural biology · 2026Article
- Regulation of Absorption and Emission in a Protein/Fluorophore Complex.ACS chemical biology · 2024Article
- Light controlled reversible Michael addition of cysteine: a new tool for dynamic site-specific labeling of proteins.The Analyst · 2023Article
- Design of Large Stokes Shift Fluorescent Proteins Based on Excited State Proton Transfer of an Engineered Photobase.Journal of the American Chemical Society · 2021Article
- Next-Generation Fluorogen-Based Reporters and Biosensors for Advanced Bioimaging.International journal of molecular sciences · 2019Review
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Authors and funding
8 authors.
Funding
Abstract
A reengineered human cellular retinol binding protein II (hCRBPII), a 15-kDa protein belonging to the intracellular lipid binding protein (iLBP) family, generates a highly fluorescent red pigment through the covalent linkage of a merocyanine aldehyde to an active site lysine residue. The complex exhibits "turn-on" fluorescence, due to a weakly fluorescent aldehyde that "lights up" with subsequent formation of a strongly fluorescent merocyanine dye within the binding pocket of the protein. Cellular penetration of merocyanine is rapid, and fluorophore maturation is nearly instantaneous. The hCRBPII/merocyanine complex displays high quantum yield, low cytotoxicity, specificity in labeling organelles, and compatibility in both cancer cell lines and yeast cells. The hCRBPII/merocyanine tag is brighter than most common red fluorescent proteins.
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Registered trials
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