ArticleNature communications2020
Optogenetic control of protein binding using light-switchable nanobodies.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 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
93 citing papers in PubMed, 150 citations in OpenAlex.
- Beyond ER-Golgi trafficking: unconventional protein secretion as a new design frontier for synthetic secretion switches in mammalian cells.Communications biology · 2026Review
- Intracellular protein binders for imaging, control and future therapeutics.Nature biomedical engineering · 2026Review
- Design and optimization of a kinase-controlled allosteric switch.Nature methods · 2026Article
- Engineering viral protease-operated nanobodies for programmable and orthogonal control of protein function.Nature communications · 2026Article
- Quantum transduction from electron spin state to a signaling state in a wild-type LOV photoreceptor.bioRxiv : the preprint server for biology · 2026Article
- Technologies to measure and modulate protein subcellular localization.Nature reviews. Molecular cell biology · 2026Review
- Multimodal control of Cas13d activity through domain insertion at an allosteric hotspot.Nature communications · 2026Article
- Design principles for optogenetic-based targeted protein degradation.Synthetic and systems biotechnology · 2026Review
- Tissue rigidity phase transition shapes morphogen gradients.Nature cell biology · 2026Article
- An engineered streptavidin condensate platform for chemically inducible control of endogenous proteins in mammalian cells.bioRxiv : the preprint server for biology · 2026Article
- Three cryo-EM structures of complement C3d-bound αScience advances · 2026Article
- Optimized optogenetic anti-CRISPR for endogenous gene regulation in Drosophila.Nucleic acids research · 2026Article
- Optogenetic Translocation to Subcellular Compartments through Regulation of Protein Avidity.ACS synthetic biology · 2026Article
- Optogenetics for Investigating and Targeting Hallmark Traits of Cancer.Biomolecules · 2026Review
- An engineered nanobody inhibitor for molecular-to-circuit control of opioid receptor function.bioRxiv : the preprint server for biology · 2026Article
- Optogenetic BlueGENEs engineered into a human safe harbor locus.Nucleic acids research · 2026Article
- Adhesion-driven rigidity transition decoupled from density-driven jamming triggers epithelial organization in embryonic tissues.Nature physics · 2026Article
- Optogenetic engineering of synthetic and natural receptors: design principles, functional mechanisms and biomedical applications.Regenerative biomaterials · 2026Review
- Conditionally Activatable Antibody Platforms: Mechanisms, Modalities, and Clinical Translation Potential.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- A Photoswitchable HaloTag for Spatiotemporal Control of Fluorescence in Living Cells.Angewandte Chemie (International ed. in English) · 2025Article
33 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
9 authors at 1 institution in 1 country.
Funding
Abstract
A growing number of optogenetic tools have been developed to reversibly control binding between two engineered protein domains. In contrast, relatively few tools confer light-switchable binding to a generic target protein of interest. Such a capability would offer substantial advantages, enabling photoswitchable binding to endogenous target proteins in cells or light-based protein purification in vitro. Here, we report the development of opto-nanobodies (OptoNBs), a versatile class of chimeric photoswitchable proteins whose binding to proteins of interest can be enhanced or inhibited upon blue light illumination. We find that OptoNBs are suitable for a range of applications including reversibly binding to endogenous intracellular targets, modulating signaling pathway activity, and controlling binding to purified protein targets in vitro. This work represents a step towards programmable photoswitchable regulation of a wide variety of target proteins.
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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.