The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
In the light of directed evolution: Pathways of adaptive protein evolution
Open accessAbstract
Directed evolution is a widely-used engineering strategy for improving the stabilities or biochemical functions of proteins by repeated rounds of mutation and selection. These experiments offer empirical lessons about how proteins evolve in the face of clearly-defined laboratory selection pressures. Directed evolution has revealed that single amino acid mutations can enhance properties such as catalytic activity or stability and that adaptation can often occur through pathways consisting of sequential beneficial mutations. When there are no single mutations that improve a particular protein property experiments always find a wealth of mutations that are neutral with respect to the laboratory-defined measure of fitness. These neutral mutations can open new adaptive pathways by at least 2 different mechanisms. Functionally-neutral mutations can enhance a protein's stability, thereby increasing its tolerance for subsequent functionally beneficial but destabilizing mutations. They can also lead to changes in “promiscuous” functions that are not currently under selective pressure, but can subsequently become the starting points for the adaptive evolution of new functions. These lessons about the coupling between adaptive and neutral protein evolution in the laboratory offer insight into the evolution of proteins in nature.
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Deep mutational scanning: a new style of protein science
Fowler, D. M., & Fields, S. (2014) · Nature Methods · doi:10.1038/nmeth.3027 · Cited by 1,287
Exploring protein fitness landscapes by directed evolution
Romero, P. A., & Arnold, F. H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2805 · Cited by 1,161
Self-citationStability effects of mutations and protein evolvability
Tokuriki, N., & Tawfik, D. S. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.08.003 · Cited by 834
Artificial Metalloenzymes: Reaction Scope and Optimization Strategies
Schwizer, F., Okamoto, Y., Heinisch, T., Gu, Y., Pellizzoni, M. M., Lebrun, V., Reuter, R., Köhler, V., Lewis, J. C., & Ward, T. R. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00014 · Cited by 831
Metadata
- Authors
- Bloom, J. D., & Arnold, F. H.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2009-06-16
- Volume
- 106
- Issue
- supplement_1
- Pages
- 9995-10000
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2047849624
- Cited by
- 468
- References
- 61
- FWCI
- 22.81
- Type
- journal article
- Language
- en
- Open access
- green
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