ArticleJournal of the American Chemical Society2014
Genetically encoded optochemical probes for simultaneous fluorescence reporting and light activation of protein function with two-photon excitation.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
What it found
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Who cites it
72 citing papers in PubMed, 167 citations in OpenAlex.
- Photocaged FLP recombinase for precise spatio-temporal control of gene expression.Nucleic acids research · 2026Article
- Genetically encoded green-light-responsive photocaged lysine for sequential control of protein function.Chemical science · 2026Article
- Coumarin-Based Photolabile Solid Support Facilitates Nonchromatographic Purification of RNA Oligonucleotides.The Journal of organic chemistry · 2025Article
- Engineering unnatural cells with a 21st amino acid as a living epigenetic sensor.Nature communications · 2025Article
- A hydrophobic photouncaging reaction to profile the lipid droplet interactome in tissues.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion.Chemical reviews · 2025Review
- Strategies to Expand the Genetic Code of Mammalian Cells.Chemical reviews · 2025Review
- BeyondChemical reviews · 2025Review
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Noncanonical Amino Acid Tools and Their Application to Membrane Protein Studies.Chemical reviews · 2024Review
- Engineering Pyrrolysine Systems for Genetic Code Expansion and Reprogramming.Chemical reviews · 2024Review
- Cellular Site-Specific Incorporation of Noncanonical Amino Acids in Synthetic Biology.Chemical reviews · 2024Review
- Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids.Chemical reviews · 2024Review
- Genetically Encoded Lysine Analogues with Differential Light Sensitivity for Activation of Protein Function.ChemPhotoChem · 2024Article
- Applications of genetic code expansion technology in eukaryotes.Protein & cell · 2024Review
- Visible Light-Induced Specific Protein Reaction Delineates Early Stages of Cell Adhesion.Journal of the American Chemical Society · 2023Article
- Isoform-specific optical activation of kinase function reveals p38-ERK signaling crosstalk.RSC chemical biology · 2023Article
- Visible light-induced specific protein reaction delineates early stages of cell adhesion.bioRxiv : the preprint server for biology · 2023Article
- Genetically Encoded Aminocoumarin Lysine for Optical Control of Protein-Nucleotide Interactions in Zebrafish Embryos.ACS chemical biology · 2023Article
- Regulation of IL-24/IL-20R2 complex formation using photocaged tyrosines and UV light.Frontiers in molecular biosciences · 2023Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
The site-specific incorporation of three new coumarin lysine analogues into proteins was achieved in bacterial and mammalian cells using an engineered pyrrolysyl-tRNA synthetase system. The genetically encoded coumarin lysines were successfully applied as fluorescent cellular probes for protein localization and for the optical activation of protein function. As a proof-of-principle, photoregulation of firefly luciferase was achieved in live cells by caging a key lysine residue, and excellent OFF to ON light-switching ratios were observed. Furthermore, two-photon and single-photon optochemical control of EGFP maturation was demonstrated, enabling the use of different, potentially orthogonal excitation wavelengths (365, 405, and 760 nm) for the sequential activation of protein function in live cells. These results demonstrate that coumarin lysines are a new and valuable class of optical probes that can be used for the investigation and regulation of protein structure, dynamics, function, and localization in live cells. The small size of coumarin, the site-specific incorporation, the application as both a light-activated caging group and as a fluorescent probe, and the broad range of excitation wavelengths are advantageous over other genetically encoded photocontrol systems and provide a precise and multifunctional tool for cellular biology.
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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.