ArticleJournal of the American Chemical Society2021
Climbing Up and Down Binding Landscapes through Deep Mutational Scanning of Three Homologous Protein-Protein Complexes.
Article in Journal of the American Chemical Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 35 citations in OpenAlex.
- Machine-learning prediction of affinity and epistasis in the bovine pancreatic trypsin inhibitor-chymotrypsin complex.Protein science : a publication of the Protein Society · 2026Article
- MutPPI+: a multimodal framework for predicting mutation effects on protein-protein interactions via mutation-path-based data augmentation.Briefings in bioinformatics · 2026Article
- Structural ontogeny of protein-protein interactions.Science (New York, N.Y.) · 2026Article
- ProBASS-a language model with sequence and structural features for predicting the effect of mutations on binding affinity.Bioinformatics (Oxford, England) · 2025Article
- Understanding epistatic networks in the B1 β-lactamases through coevolutionary statistical modeling and deep mutational scanning.Nature communications · 2024Article
- Computational screening of the effects of mutations on protein-protein off-rates and dissociation mechanisms by τRAMD.Communications biology · 2024Article
- Deciphering GB1's Single Mutational Landscape: Insights from MuMi Analysis.The journal of physical chemistry. B · 2024Article
- Optimization of a deep mutational scanning workflow to improve quantification of mutation effects on protein-protein interactions.BMC genomics · 2024Article
- Cold Spot SCANNER: Colab Notebook for predicting cold spots in protein-protein interfaces.BMC bioinformatics · 2024Article
- A Nexus between Genetic and Non-Genetic Mechanisms Guides KRAS Inhibitor Resistance in Lung Cancer.Biomolecules · 2023Article
- Combining deep mutational scanning to heatmap of HLA class II binding of immunogenic sequences to preserve functionality and mitigate predicted immunogenicity.Frontiers in immunology · 2023Article
- Cold spots are universal in protein-protein interactions.Protein science : a publication of the Protein Society · 2022Article
- Mechanisms of protein evolution.Protein science : a publication of the Protein Society · 2022Review
- Quantifying the binding landscapes of protein-protein interactions.Communications chemistry · 2021Article
- Computational design and experimental optimization of protein binders with prospects for biomedical applications.Protein engineering, design & selection : PEDS · 2021Review
- Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Protein-protein interactions (PPIs) have evolved to display binding affinities that can support their function. As such, cognate and noncognate PPIs could be highly similar structurally but exhibit huge differences in binding affinities. To understand this phenomenon, we study three homologous protease-inhibitor PPIs that span 9 orders of magnitude in binding affinity. Using state-of-the-art methodology that combines protein randomization, affinity sorting, deep sequencing, and data normalization, we report quantitative binding landscapes consisting of ΔΔ
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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.