ArticleScience signaling2023
Data-driven design of orthogonal protein-protein interactions.
Article in Science signaling, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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
6 citing papers in PubMed.
- Inference and Visualization of Complex Genotype-Phenotype Maps.Molecular biology and evolution · 2026Article
- Atypical β-strand insertion mediates the noncovalent cross-linking in amyloid aggregates.Nature communications · 2026Article
- Inference and visualization of complex genotype-phenotype maps withbioRxiv : the preprint server for biology · 2025Article
- TMEM138: From Biological Functions to Diseases.Physiological research · 2025Review
- Reactive Oxygen Species Mechanisms that Regulate Protein-Protein Interactions in Cancer.International journal of molecular sciences · 2024Review
- Integrative bioinformatics analysis to identify ferroptosis-related genes in non-obstructive azoospermia.Journal of assisted reproduction and genetics · 2024Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Engineering protein-protein interactions to generate new functions presents a challenge with great potential for many applications, ranging from therapeutics to synthetic biology. To avoid unwanted cross-talk with preexisting protein interaction networks in a cell, the specificity and selectivity of newly engineered proteins must be controlled. Here, we developed a computational strategy that mimics gene duplication and the divergence of preexisting interacting protein pairs to design new interactions. We used the bacterial PhoQ-PhoP two-component system as a model system to demonstrate the feasibility of this strategy and validated the approach with known experimental results. The designed protein pairs are predicted to exclusively interact with each other and to be insulated from potential cross-talk with their native partners. Thus, our approach enables exploration of uncharted regions of the protein sequence space and the design of new interacting protein pairs.
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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.