ArticleNature biotechnology2026
Artificial allosteric protein switches with machine-learning-designed receptors.
Article in Nature biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 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
6 citing papers in PubMed.
- The Allosteric Revolution: From Static Structures to Conformational Ensembles and Next-Generation Therapeutics.Journal of molecular biology · 2026Review
- Liquid-Liquid Phase Separation-Enhanced Multienzyme Catalysis: Mechanisms and Applications.ChemSusChem · 2026Review
- Systematic discovery of circular permutations across the protein universe using CIRPIN.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Genetically encoded tools for tracking metabolites in live cells.Biochemical Society transactions · 2026Review
- WormSORT: A detection-based multiple object tracking model for individual silkworms in breeding environments.PLoS computational biology · 2026Article
- Review
Corrections and comments
- Erratum issued
Authors and funding
20 authors.
Funding
Abstract
Protein allostery underlies most information and energy processing in biology and the development of artificial allosteric proteins is a key objective of synthetic biology and biotechnology. We show that machine-learning-engineered minimal ligand-binding domains act as efficient receptors in single-component allosteric switches, despite lacking global conformational change. Such colorimetric, luminescent and electrochemical biosensors of small molecules, peptides and proteins can be compiled into intramolecular YES and AND logic gates. Furthermore, we report fully synthetic allosteric switches composed of artificial receptor and reporter domains. Hydrogen/deuterium exchange mass spectrometry and
Identifiers
41986695What 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.