ArticleScience (New York, N.Y.)2016
Engineering extrinsic disorder to control protein activity in living cells.
Article in Science (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
140 citing papers in PubMed.
- Protein Surface Site Determines the Evolutionary Accessibility of Allosteric Regulation.bioRxiv : the preprint server for biology · 2026Article
- Design and optimization of a kinase-controlled allosteric switch.Nature methods · 2026Article
- Multimodal control of Cas13d activity through domain insertion at an allosteric hotspot.Nature communications · 2026Article
- High-throughput engineering of ligand-activated splicing ribozyme through domain insertion.bioRxiv : the preprint server for biology · 2026Article
- Allosteric Biosensors Unravel GTPase-Effector Feedback.bioRxiv : the preprint server for biology · 2026Article
- Optimized optogenetic anti-CRISPR for endogenous gene regulation in Drosophila.Nucleic acids research · 2026Article
- A familiar newcomer to the thermogenetic toolset.Nature chemical biology · 2026Article
- Modular engineering of thermoresponsive allosteric proteins.Nature chemical biology · 2026Article
- Optogenetic Tools for Spatiotemporal Interrogation of Cytoskeletal Dynamics.Bioconjugate chemistry · 2026Review
- Phage-assisted evolution of allosteric protein switches.Nature communications · 2026Article
- Engineered interfaces in Rac1 and Cdc42 biosensors enhance sensitivity and reduce cell perturbation.Molecular biology of the cell · 2026Article
- Optogenetic Translocation to Subcellular Compartments through Regulation of Protein Avidity.ACS synthetic biology · 2026Article
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Paths to stability - actin regulation of adherens junction mechanics.Journal of cell science · 2025Review
- Intelligent molecular logic computing toolkits: nucleic acid-based construction, functionality, and enhanced biosensing applications.Chemical science · 2025Review
- The Evolving Landscape of Protein Allostery: From Computational and Experimental Perspectives.Journal of molecular biology · 2025Review
- Optogenetic enzymes: A deep dive into design and impact.Current opinion in structural biology · 2025Review
- Photoswitchable intein for light control of covalent protein binding and cleavage.Nature communications · 2025Article
- Rational engineering of allosteric protein switches by in silico prediction of domain insertion sites.Nature methods · 2025Article
- Machine learning-trained protein domain insertion for the design of switchable proteins.Nature methods · 2025Article
80 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
7 authors.
Funding
Abstract
Optogenetic and chemogenetic control of proteins has revealed otherwise inaccessible facets of signaling dynamics. Here, we use light- or ligand-sensitive domains to modulate the structural disorder of diverse proteins, thereby generating robust allosteric switches. Sensory domains were inserted into nonconserved, surface-exposed loops that were tight and identified computationally as allosterically coupled to active sites. Allosteric switches introduced into motility signaling proteins (kinases, guanosine triphosphatases, and guanine exchange factors) controlled conversion between conformations closely resembling natural active and inactive states, as well as modulated the morphodynamics of living cells. Our results illustrate a broadly applicable approach to design physiological 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.