ArticlePLoS biology2006
Structure-guided recombination creates an artificial family of cytochromes P450.
Article in PLoS biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
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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.
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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
40 citing papers in PubMed, 150 citations in OpenAlex.
- Thermostable ancestors enabled evolutionary diversification of promiscuous chemical defence enzymes.The EMBO journal · 2026Article
- Advancing genetic engineering with active learning: theory, implementations and potential opportunities.Briefings in bioinformatics · 2025Review
- Development of a high throughput cytochrome P450 ligand-binding assay.The Journal of biological chemistry · 2024Article
- Context-dependent design of induced-fit enzymes using deep learning generates well-expressed, thermally stable and active enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Self-driving laboratories to autonomously navigate the protein fitness landscape.Nature chemical engineering · 2024Article
- Consequences of Genetic Recombination on Protein Folding Stability.Journal of molecular evolution · 2023Article
- Recombination of Single Beneficial Substitutions Obtained from Protein Engineering by Computer-Assisted Recombination (CompassR).Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Directed evolution methods for overcoming trade-offs between protein activity and stability.AIChE journal. American Institute of Chemical Engineers · 2020Article
- Computer-Assisted Recombination (CompassR) Teaches us How to Recombine Beneficial Substitutions from Directed Evolution Campaigns.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Deciphering protein evolution and fitness landscapes with latent space models.Nature communications · 2019Article
- A Continuing Career in Biocatalysis: Frances H. Arnold.ACS catalysis · 2019Article
- A machine learning approach for reliable prediction of amino acid interactions and its application in the directed evolution of enantioselective enzymes.Scientific reports · 2018Article
- In Vivo Selection of a Computationally Designed SCHEMA AAV Library Yields a Novel Variant for Infection of Adult Neural Stem Cells in the SVZ.Molecular therapy : the journal of the American Society of Gene Therapy · 2018Article
- Structure-guided SCHEMA recombination generates diverse chimeric channelrhodopsins.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Recent Structural Insights into Cytochrome P450 Function.Trends in pharmacological sciences · 2016Review
- Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Chemical Society reviews · 2015Review
- Peroxygenase reactions catalyzed by cytochromes P450.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Review
- SCHEMA computational design of virus capsid chimeras: calibrating how genome packaging, protection, and transduction correlate with calculated structural disruption.ACS synthetic biology · 2013Article
- Structural evidence: a single charged residue affects substrate binding in cytochrome P450 BM-3.Biochemistry · 2013Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Creating artificial protein families affords new opportunities to explore the determinants of structure and biological function free from many of the constraints of natural selection. We have created an artificial family comprising 3,000 P450 heme proteins that correctly fold and incorporate a heme cofactor by recombining three cytochromes P450 at seven crossover locations chosen to minimize structural disruption. Members of this protein family differ from any known sequence at an average of 72 and by as many as 109 amino acids. Most (>73%) of the properly folded chimeric P450 heme proteins are catalytically active peroxygenases; some are more thermostable than the parent proteins. A multiple sequence alignment of 955 chimeras, including both folded and not, is a valuable resource for sequence-structure-function studies. Logistic regression analysis of the multiple sequence alignment identifies key structural contributions to cytochrome P450 heme incorporation and peroxygenase activity and suggests possible structural differences between parents CYP102A1 and CYP102A2.
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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.