ArticleNature communications2013
Far-red light photoactivatable near-infrared fluorescent proteins engineered from a bacterial phytochrome.
Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 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
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
60 citing papers in PubMed, 115 citations in OpenAlex.
- Mechanisms of Red-Shifted Absorption in Biliverdin-Binding Proteins.Biochemistry · 2026Article
- Genetically Encoded Near-Infrared Fluorescent Proteins for Viral Imaging and Detection: A Mini-Review.Current microbiology · 2026Review
- Next-generation bacteriophage therapeutic systems: CRISPR-based engineering, near-infrared bioimaging, and precision strategies for treating multidrug-resistant and extensively drug-resistant bacterial infections.Frontiers in microbiology · 2026Review
- The near-infrared bacteriophytochrome-derived fluorescent protein PENELOPE enables RESOLFT superresolution microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Serial-femtosecond crystallography reveals how a phytochrome variant couples chromophore and protein structural changes.Science advances · 2025Article
- Nonlinear optical properties of photosensory core modules of monomeric and dimeric bacterial phytochromes.Protein science : a publication of the Protein Society · 2025Article
- Bacteria-Based Living Probes: Preparation and the Applications in Bioimaging and Diagnosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Review
- Blue-shift photoconversion of near-infrared fluorescent proteins for labeling and tracking in living cells and organisms.Nature communications · 2023Article
- Current Trends of Bacterial and Fungal Optoproteins for Novel Optical Applications.International journal of molecular sciences · 2023Review
- Photodegradable by Yellow-Orange Light degFusionRed Optogenetic Module with Autocatalytically Formed Chromophore.International journal of molecular sciences · 2023Article
- 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
- Dual-expression system for blue fluorescent protein optimization.Scientific reports · 2022Article
- Use of red, far-red, and near-infrared light in imaging of yeasts and filamentous fungi.Applied microbiology and biotechnology · 2022Review
- Single-domain near-infrared protein provides a scaffold for antigen-dependent fluorescent nanobodies.Nature methods · 2022Article
- Transition Metals Induce Quenching of Monomeric Near-Infrared Fluorescent Proteins.Biochemistry · 2022Article
- Improved fluorescent phytochromes for in situ imaging.Scientific reports · 2022Article
- Rapid directed molecular evolution of fluorescent proteins in mammalian cells.Protein science : a publication of the Protein Society · 2022Article
- Enhanced small green fluorescent proteins as a multisensing platform for biosensor development.Frontiers in bioengineering and biotechnology · 2022Article
- Single-component near-infrared optogenetic systems for gene transcription regulation.Nature communications · 2021Article
- Advances in engineering near-infrared luminescent materials.iScience · 2021Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The ability to modulate the fluorescence of optical probes can be used to enhance signal-to-noise ratios for imaging within highly autofluorescent environments, such as intact tissues and living organisms. Here, we report two bacteriophytochrome-based photoactivatable near-infrared fluorescent proteins, named PAiRFP1 and PAiRFP2. PAiRFPs utilize haem-derived biliverdin, ubiquitous in mammalian tissues, as the chromophore. Initially weakly fluorescent PAiRFPs undergo photoconversion into a highly fluorescent state with excitation/emission at 690/717 nm following a brief irradiation with far-red light. After photoactivation, PAiRFPs slowly revert back to initial state, enabling multiple photoactivation-relaxation cycles. Low-temperature optical spectroscopy reveals several intermediates involved in PAiRFP photocycles, which all differ from that of the bacteriophytochrome precursor. PAiRFPs can be photoactivated in a spatially selective manner in mouse tissues, and optical modulation of their fluorescence allows for substantial contrast enhancement, making PAiRFPs advantageous over permanently fluorescent probes for in vivo imaging conditions of high autofluorescence and low signal levels.
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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.