ArticleNature communications2020
Development of light-responsive protein binding in the monobody non-immunoglobulin scaffold.
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 32 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
32 citing papers in PubMed.
- 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
- Optogenetics for Investigating and Targeting Hallmark Traits of Cancer.Biomolecules · 2026Review
- Conditionally Activatable Antibody Platforms: Mechanisms, Modalities, and Clinical Translation Potential.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- Utilizing Engineered Monobodies for the Electrochemical Quantification of Lysozyme.Analytical chemistry · 2025Article
- A Photoswitchable HaloTag for Spatiotemporal Control of Fluorescence in Living Cells.Angewandte Chemie (International ed. in English) · 2025Article
- Optogenetic engineering for precision cancer immunotherapy.Trends in pharmacological sciences · 2025Review
- Design of a light and CaProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Field-domain rapid-scan EPR at 240GHz for studies of protein functional dynamics at room temperature.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2024Article
- Rapid and reversible dissolution of biomolecular condensates using light-controlled recruitment of a solubility tag.Nature communications · 2024Article
- HOPS-Dependent Endosomal Escape Demands Protein Unfolding.ACS central science · 2024Article
- Synthetic Biology Meets CaCells · 2024Review
- Rapid and reversible dissolution of biomolecular condensates using light-controlled recruitment of a solubility tag.bioRxiv : the preprint server for biology · 2024Article
- Chimeric Protein Switch Biosensors.Advances in biochemical engineering/biotechnology · 2024Review
- Design rules for efficient endosomal escape.bioRxiv : the preprint server for biology · 2023Article
- Light-switchable transcription factors obtained by direct screening in mammalian cells.Nature communications · 2023Article
- Allosteric inactivation of an engineered optogenetic GTPase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Regulation of IL-24/IL-20R2 complex formation using photocaged tyrosines and UV light.Frontiers in molecular biosciences · 2023Article
- LOV2-based photoactivatable CaMKII and its application to single synapses: Local Optogenetics.Biophysics and physicobiology · 2023Article
- Optophysiology: Illuminating cell physiology with optogenetics.Physiological reviews · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Monobodies are synthetic non-immunoglobulin customizable protein binders invaluable to basic and applied research, and of considerable potential as future therapeutics and diagnostic tools. The ability to reversibly control their binding activity to their targets on demand would significantly expand their applications in biotechnology, medicine, and research. Here we present, as proof-of-principle, the development of a light-controlled monobody (OptoMB) that works in vitro and in cells and whose affinity for its SH2-domain target exhibits a 330-fold shift in binding affinity upon illumination. We demonstrate that our αSH2-OptoMB can be used to purify SH2-tagged proteins directly from crude E. coli extract, achieving 99.8% purity and over 40% yield in a single purification step. By virtue of their ability to be designed to bind any protein of interest, OptoMBs have the potential to find new powerful applications as light-switchable binders of untagged proteins with the temporal and spatial precision afforded by light.
Indexed as
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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.