ArticleNucleic acids research2004
Protein evolution by codon-based random deletions.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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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Who cites it
7 citing papers in PubMed, 23 citations in OpenAlex.
- A novel framework for engineering protein loops exploring length and compositional variation.Scientific reports · 2021Article
- Accessing unexplored regions of sequence space in directed enzyme evolution via insertion/deletion mutagenesis.Nature communications · 2020Article
- Extensive libraries of gene truncation variants generated by in vitro transposition.Nucleic acids research · 2017Article
- Article
- The effect of amino acid deletions and substitutions in the longest loop of GFP.BMC chemical biology · 2007Article
- Directed evolution of protein switches and their application to the creation of ligand-binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Combinatorial codon-based amino acid substitutions.Nucleic acids research · 2004Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A method to delete in-phase codons throughout a defined target region of a gene has been developed. This approach, named the codon-based random deletion (COBARDE) method, is able to delete complete codons in a random and combinatorial mode. Robustness, automation and fine-tuning of the mutagenesis rate are essential characteristics of the method, which is based on the assembly of oligonucleotides and on the use of two transient orthogonal protecting groups during the chemical synthesis. The performance of the method for protein function evolution was demonstrated by changing the substrate specificity of TEM-1 beta-lactamase. Functional ceftazidime-resistant beta-lactamase variants containing several deleted residues inside the catalytically important omega-loop region were found. The results show that the COBARDE method is a useful new molecular tool to access previously unexplorable sequence space.
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Registered trials
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