ArticleNature communications2015
Design of protein switches based on an ensemble model of allostery.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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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
38 citing papers in PubMed.
- Dynamic view of an allosteric intermediate in a positively cooperative dimer.bioRxiv : the preprint server for biology · 2026Article
- Mechanistic Insight into Conformational Control of Enzyme Activity by Genetically Encoded Metal-Responsive Switches.Chembiochem : a European journal of chemical biology · 2026Article
- Artificial allosteric protein switches with machine-learning-designed receptors.Nature biotechnology · 2026Article
- Advances in uncovering the mechanisms of macromolecular conformational entropy.Nature chemical biology · 2025Review
- Precise Engineering and Efficient Biosynthesis of Robust and High-Activity Human Haemoglobin for Artificial Oxygen Carriers.Microbial biotechnology · 2025Article
- Post-translational digital data encoding into the genomes of mammalian cell populations.bioRxiv : the preprint server for biology · 2024Article
- Plug-and-play protein biosensors using aptamer-regulated in vitro transcription.Nature communications · 2024Article
- Allosteric inactivation of an engineered optogenetic GTPase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Intrinsically disordered proteins: Ensembles at the limits of Anfinsen's dogma.Biophysics reviews · 2022Review
- Development and assessment of novel machine learning models to predict medication non-adherence risks in type 2 diabetics.Frontiers in public health · 2022Article
- Structure-based design of a photoswitchable affibody scaffold.Protein science : a publication of the Protein Society · 2021Article
- Article
- Discovery and mechanism of a pH-dependent dual-binding-site switch in the interaction of a pair of protein modules.Science advances · 2020Article
- Nanosecond-Timescale Dynamics and Conformational Heterogeneity in Human GCK Regulation and Disease.Biophysical journal · 2020Article
- Targeted insertional mutagenesis libraries for deep domain insertion profiling.Nucleic acids research · 2020Article
- A Time-Dependent Quantum Approach to Allostery and a Comparison With Light-Harvesting in Photosynthetic Phenomenon.Frontiers in molecular biosciences · 2020Article
- De novo design of bioactive protein switches.Nature · 2019Article
- Plant Synthetic Biology: Quantifying the "Known Unknowns" and Discovering the "Unknown Unknowns".Plant physiology · 2019Review
- Domain insertion permissibility-guided engineering of allostery in ion channels.Nature communications · 2019Article
- Converting a Periplasmic Binding Protein into a Synthetic Biosensing Switch through Domain Insertion.BioMed research international · 2019Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Switchable proteins that can be regulated through exogenous or endogenous inputs have a broad range of biotechnological and biomedical applications. Here we describe the design of switchable enzymes based on an ensemble allosteric model. First, we insert an enzyme domain into an effector-binding domain such that both domains remain functionally intact. Second, we induce the fusion to behave as a switch through the introduction of conditional conformational flexibility designed to increase the conformational entropy of the enzyme domain in a temperature- or pH-dependent fashion. We confirm the switching behaviour in vitro and in vivo. Structural and thermodynamic studies support the hypothesis that switching result from an increase in conformational entropy of the enzyme domain in the absence of effector. These results support the ensemble model of allostery and embody a strategy for the design of protein switches.
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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.