ArticleAIChE journal. American Institute of Chemical Engineers2020
Directed evolution methods for overcoming trade-offs between protein activity and stability.
Article in AIChE journal. American Institute of Chemical Engineers, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Multidimensional maturation of antibody variable domains with machine-learning assistance.mAbs · 2026Article
- Rapid screening of staphylokinase protein variants using an unpurified cell-free expression system.FEBS open bio · 2026Article
- Application of the YebF secretion pathway inRSC chemical biology · 2026Article
- How far can you go? Extrapolating values of catalytic activity from known protein landscapes in natural and directed evolution.Chemical Society reviews · 2026Review
- Accurate protein stability prediction for small domains using mega-scale experiments.bioRxiv : the preprint server for biology · 2026Article
- Beyond Resistance Genes: Silencing Susceptibility.International journal of molecular sciences · 2026Review
- Precise, minimally evolved adenine base editors generated through mutation reversion analysis.Nature biotechnology · 2026Article
- Computational redesign of a thermostable T7 RNA polymerase.Protein engineering, design & selection : PEDS · 2026Article
- Family-Specialized Transformer for L-cystathionine gamma-lyase Engineering and Its Structural Interpretation.Computational and structural biotechnology journal · 2026Article
- Computational redesign of a thermostable T7 RNA polymerase.bioRxiv : the preprint server for biology · 2025Article
- Directed evolution of a beta-lactamase samples a wide variety of conformational states.Protein science : a publication of the Protein Society · 2025Article
- Reshaping of a Glycoside Hydrolase Active Site through Expression-Compensated Droplet-Based Microfluidic Screening Provides Useful Tools for Glycomics.ACS central science · 2025Article
- Optimization of synthetic human VProtein science : a publication of the Protein Society · 2025Article
- Directed Evolution of a Modular Polyketide Synthase Thioesterase for Generation of a Hybrid Macrocyclic Ring System.ACS catalysis · 2025Article
- Computational Stabilization of a Non-Heme Iron Enzyme Enables Efficient Evolution of New Function.Angewandte Chemie (International ed. in English) · 2025Article
- Targeting Efficient Features of Urate Oxidase to Increase Its Solubility.Applied biochemistry and biotechnology · 2024Article
- Computational stabilization of a non-heme iron enzyme enables efficient evolution of new function.bioRxiv : the preprint server for biology · 2024Article
- Simultaneous enhancement of multiple functional properties using evolution-informed protein design.Nature communications · 2024Article
- Biosynthetic production of anticoagulant heparin polysaccharides through metabolic and sulfotransferases engineering strategies.Nature communications · 2024Article
- Viral Receptor-Binding Protein Evolves New Function through Mutations That Cause Trimer Instability and Functional Heterogeneity.Molecular biology and evolution · 2024Article
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3 authors.
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Abstract
Engineered proteins are being widely developed and employed in applications ranging from enzyme catalysts to therapeutic antibodies. Directed evolution, an iterative experimental process composed of mutagenesis and library screening, is a powerful technique for enhancing existing protein activities and generating entirely new ones not observed in nature. However, the process of accumulating mutations for enhanced protein activity requires chemical and structural changes that are often destabilizing, and low protein stability is a significant barrier to achieving large enhancements in activity during multiple rounds of directed evolution. Here we highlight advances in understanding the origins of protein activity/stability trade-offs for two important classes of proteins (enzymes and antibodies) as well as innovative experimental and computational methods for overcoming such trade-offs. These advances hold great potential for improving the generation of highly active and stable proteins that are needed to address key challenges related to human health, energy and the environment.
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