ArticleChemical science2017
Designing brighter near-infrared fluorescent proteins: insights from structural and biochemical studies.
Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed, 59 citations in OpenAlex.
- An ultralow-background far-red light-responsive optogenetic tool based on an engineered biliverdin-binding domain.Nature methods · 2026Article
- Bright monomeric fluorescent protein elite-niRFP704 for two-channel near-infrared STED nanoscopy.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mechanisms of Red-Shifted Absorption in Biliverdin-Binding Proteins.Biochemistry · 2026Article
- 3D-PAULM: Integrated Photoacoustic Tomography and Ultrasound Localization Microscopy for Multiparametric Brain and Tumor Imaging.bioRxiv : the preprint server for biology · 2026Article
- Synthetic multicolor antigen-stabilizable nanobody platform for intersectional labeling and functional imaging.Nature methods · 2026Article
- Synthetic multicolor antigen-stabilizable nanobody platform for intersectional labelling and functional imaging.bioRxiv : the preprint server for biology · 2025Article
- Unravelling molecular dynamics in living cells: Fluorescent protein biosensors for cell biology.Journal of microscopy · 2025Review
- Dual-Cys bacteriophytochromes: intermediates in cyanobacterial phytochrome evolution?The FEBS journal · 2025Article
- Blue-shift photoconversion of near-infrared fluorescent proteins for labeling and tracking in living cells and organisms.Nature communications · 2023Article
- Development of bright red-shifted miRFP704nano using structural analysis of miRFPnano proteins.Protein science : a publication of the Protein Society · 2023Article
- Gas and light: triggers of c-di-GMP-mediated regulation.FEMS microbiology reviews · 2023Review
- Practical Guidance for Developing Small-Molecule Optical Probes for In Vivo Imaging.Molecular imaging and biology · 2023Review
- Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- A genetically encoded far-red fluorescent calcium ion biosensor derived from a biliverdin-binding protein.Protein science : a publication of the Protein Society · 2022Article
- Impact of Double Covalent Binding of BV in NIR FPs on Their Spectral and Physicochemical Properties.International journal of molecular sciences · 2022Article
- Transition Metals Induce Quenching of Monomeric Near-Infrared Fluorescent Proteins.Biochemistry · 2022Article
- Biliverdin incorporation into the cyanobacteriochrome SPI1085g3 fromFrontiers in microbiology · 2022Article
- Influence of the Environment on Shaping the Absorption of Monomeric Infrared Fluorescent Proteins.The journal of physical chemistry. B · 2021Article
- Real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome.Communications chemistry · 2021Article
- A far-red cyanobacteriochrome lineage specific for verdins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 5 countries.
Funding
Abstract
Brighter near-infrared (NIR) fluorescent proteins (FPs) are required for multicolor microscopy and deep-tissue imaging. Here, we present structural and biochemical analyses of three monomeric, spectrally distinct phytochrome-based NIR FPs, termed miRFPs. The miRFPs are closely related and differ by only a few amino acids, which define their molecular brightness, brightness in mammalian cells, and spectral properties. We have identified the residues responsible for the spectral red-shift, revealed a new chromophore bound simultaneously to two cysteine residues in the PAS and GAF domains in blue-shifted NIR FPs, and uncovered the importance of amino acid residues in the N-terminus of NIR FPs for their molecular and cellular brightness. The novel chromophore covalently links the N-terminus of NIR FPs with their C-terminal GAF domain, forming a topologically closed knot in the structure, and also contributes to the increased brightness. Based on our studies, we suggest a strategy to develop spectrally distinct NIR FPs with enhanced brightness.
Identifiers
What OpenQuestion holds
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.