ArticleProceedings of the National Academy of Sciences of the United States of America1998
A method for directed evolution and functional cloning of enzymes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Directed evolution of enzymes at the crossroads of tradition and innovation.FEBS open bio · 2026Review
- Phase diagrams for biophysical fitness landscape design.bioRxiv : the preprint server for biology · 2026Article
- T7 Phage as an Emerging Nanobiomaterial with Genetically Tunable Target Specificity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Review
- Bacteriophage Capsid Modification by Genetic and Chemical Methods.Bioconjugate chemistry · 2021Review
- New Trends in Bioremediation Technologies Toward Environment-Friendly Society: A Mini-Review.Frontiers in bioengineering and biotechnology · 2021Review
- Design of Catalytic Peptides and Proteins Through Rational and Combinatorial Approaches.Annual review of biomedical engineering · 2016Review
- Sperm navigation along helical paths in 3D chemoattractant landscapes.Nature communications · 2015Article
- Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding.Chemical science · 2015Article
- Chemical strategies for the covalent modification of filamentous phage.Frontiers in microbiology · 2014Review
- Self-made phage libraries with heterologous inserts in the Mtd of Bordetella bronchiseptica.Protein engineering, design & selection : PEDS · 2012Article
- Phage display of combinatorial peptide libraries: application to antiviral research.Molecules (Basel, Switzerland) · 2011Review
- Characterisation of a DNA polymerase highly mutated along the template binding interface.Molecular biotechnology · 2010Article
- Laboratory-directed protein evolution.Microbiology and molecular biology reviews : MMBR · 2005Review
- Efficient display of two enzymes on filamentous phage using an improved signal sequence.Molecular biotechnology · 2003Article
- Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Directed evolution of novel polymerase activities: mutation of a DNA polymerase into an efficient RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- A novel strategy for the functional cloning of enzymes using filamentous phage display: the case of nucleotidyl transferases.Nucleic acids research · 2002Article
- Continuous affinity-based selection: rapid screening and simultaneous amplification of bacterial surface-display libraries.The Biochemical journal · 2001Article
- Substrate-assisted catalysis: molecular basis and biological significance.Protein science : a publication of the Protein Society · 2000Review
- Selection for improved subtiligases by phage display.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
A general scheme is described for the in vitro evolution of protein catalysts in a biologically amplifiable system. Substrate is covalently and site specifically attached by a flexible tether to the pIII coat protein of a filamentous phage that also displays the catalyst. Intramolecular conversion of substrate to product provides a basis for selecting active catalysts from a library of mutants, either by release from or attachment to a solid support. This methodology has been developed with the enzyme staphylococcal nuclease as a model. An analysis of factors influencing the selection efficiency is presented, and it is shown that phage displaying staphylococcal nuclease can be enriched 100-fold in a single step from a library-like ensemble of phage displaying noncatalytic proteins. Additionally, this approach should allow one to functionally clone natural enzymes, based on their ability to catalyze specific reactions (e.g., glycosyl transfer, sequence-specific proteolysis or phosphorylation, polymerization, etc.) rather than their sequence- or structural homology to known enzymes.
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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.