ArticleNature communications2020
Accessing unexplored regions of sequence space in directed enzyme evolution via insertion/deletion mutagenesis.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 79 citations in OpenAlex.
- High-throughput methods enabling random duplications, deletions, or nucleotide-constrained mutagenesis of entire DNA motifs.Nucleic acids research · 2026Article
- Enzyme miniaturization: Revolutionizing future biocatalysts.Biotechnology advances · 2025Review
- Indels allow antiviral proteins to evolve functional novelty inaccessible by missense mutations.Cell genomics · 2025Article
- Physics-based modeling in the new era of enzyme engineering.Nature computational science · 2025Review
- Automated Engineering Protein Dynamics via Loop Grafting: ImprovingACS catalysis · 2025Article
- Article
- Genetically-encoded temperature indicators for thermal biology.Biophysics and physicobiology · 2025Article
- Structural and energetic analysis of stabilizing indel mutations.bioRxiv : the preprint server for biology · 2024Article
- Comprehensive deletion scan of anti-CRISPR AcrIIA4 reveals essential and dispensable domains for Cas9 inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Zero-shot prediction of mutation effects with multimodal deep representation learning guides protein engineering.Cell research · 2024Article
- Comprehensive deletion scan of anti-CRISPR AcrIIA4 reveals essential and dispensable domains for Cas9 inhibition.bioRxiv : the preprint server for biology · 2024Article
- Ancestral Reconstruction and the Evolution of Protein Energy Landscapes.Annual review of biophysics · 2024Review
- Selection of a promiscuous minimalist cAMP phosphodiesterase from a library of de novo designed proteins.Nature chemistry · 2024Article
- Indels allow antiviral proteins to evolve functional novelty inaccessible by missense mutations.bioRxiv : the preprint server for biology · 2024Article
- Remote loop evolution reveals a complex biological function for chitinase enzymes beyond the active site.Nature communications · 2024Article
- Engineering Substrate Promiscuity of Nucleoside Phosphorylase Via an Insertions-Deletions Strategy.JACS Au · 2024Article
- Identification of Various InDel-II Variants of the White Spot Syndrome Virus Isolated from Frozen Shrimp and Bivalves Obtained in the Korean Commercial Market.Animals : an open access journal from MDPI · 2023Article
- Deciphering Evolutionary Trajectories of Lactate Dehydrogenases Provides New Insights into Allostery.Molecular biology and evolution · 2023Article
- Ultrahigh-Throughput Enzyme Engineering and Discovery inChemical reviews · 2023Review
- Structural Dynamics Predominantly Determine the Adaptability of Proteins to Amino Acid Deletions.International journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
Abstract
Insertions and deletions (InDels) are frequently observed in natural protein evolution, yet their potential remains untapped in laboratory evolution. Here we introduce a transposon-based mutagenesis approach (TRIAD) to generate libraries of random variants with short in-frame InDels, and screen TRIAD libraries to evolve a promiscuous arylesterase activity in a phosphotriesterase. The evolution exhibits features that differ from previous point mutagenesis campaigns: while the average activity of TRIAD variants is more compromised, a larger proportion has successfully adapted for the activity. Different functional profiles emerge: (i) both strong and weak trade-off between activities are observed; (ii) trade-off is more severe (20- to 35-fold increased k
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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.