ArticleChemPhotoChem2024
Genetically Encoded Lysine Analogues with Differential Light Sensitivity for Activation of Protein Function.
Article in ChemPhotoChem, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
The trial behind it
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Who cites it
3 citing papers in PubMed.
- Light-responsive DNA nanostructures.Nature reviews. Chemistry · 2026Review
- Genetically encoded green-light-responsive photocaged lysine for sequential control of protein function.Chemical science · 2026Article
- Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion.Chemical reviews · 2025Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Genetically encoded unnatural amino acids are versatile tools for controlling protein function, but options for regulating multiple proteins in a single experiment are limited. Here, we report the genetic encoding of two new photocaged lysine derivatives, 1-(2-nitrophenyl)-ethyl lysine and nitrodibenzylfuranyl lysine, for sequential light-activation of protein function in live cells. Nitrodibenzylfuranyl (NDBF) caging groups have a redshifted absorbance maximum and high sensitivity to light compared to the 1-(2-nitrophenyl)-ethyl group (NPE), enabling selective decaging and protein activation. We characterized the responses of these new caged amino acids by optically triggering nuclear localization and firefly luciferase activity. The ability to selectively activate distinct proteins through simple light titration makes this a useful approach with broad applications.
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Registered trials
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