The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Exploring protein fitness landscapes by directed evolution
Open accessAbstract
Directed evolution circumvents our profound ignorance of how a protein's sequence encodes its function by using iterative rounds of random mutation and artificial selection to discover new and useful proteins. Proteins can be tunedto adapt to new functions or environments by simple adaptive walks involving small numbers of mutations. Directed evolution studies have shown how rapidly some proteins can evolve under strong selection pressures and, because the entire 'fossil record' of evolutionary intermediates is available for detailed study, they have provided new insight into the relationship between sequence and function. Directed evolution has also shown how mutations that are functionally neutral can set the stage for further adaptation.
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Cites
No free lunch theorems for optimization
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Self-Sustained Replication of an RNA Enzyme
Lincoln, T. A., & Joyce, G. F. (2009) · Science · doi:10.1126/science.1167856 · Cited by 670
Robustness–epistasis link shapes the fitness landscape of a randomly drifting protein
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Estimating the prevalence of protein sequences adopting functional enzyme folds
Axe, D. D. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.06.058 · Cited by 86
Cited by
Unified rational protein engineering with sequence-based deep representation learning
Alley, E. C., Khimulya, G., Biswas, S., AlQuraishi, M., & Church, G. M. (2019) · Nature Methods · doi:10.1038/s41592-019-0598-1 · Cited by 1,131
Machine-learning-guided directed evolution for protein engineering
Yang, K. K., Wu, Z., & Arnold, F. H. (2019) · Nature Methods · doi:10.1038/s41592-019-0496-6 · Cited by 1,130
Self-citationLow-N protein engineering with data-efficient deep learning
Biswas, S., Khimulya, G., Alley, E. C., Esvelt, K. M., & Church, G. M. (2021) · Nature Methods · doi:10.1038/s41592-021-01100-y · Cited by 422
A Comprehensive Biophysical Description of Pairwise Epistasis throughout an Entire Protein Domain
Olson, C. A., Wu, N. C., & Sun, R. (2014) · Current Biology · doi:10.1016/j.cub.2014.09.072 · Cited by 408
Rives, A., Meier, J., Sercu, T., Goyal, S., Lin, Z., Liu, J., Guo, D., Ott, M., Zitnick, C. L., Ma, J., et al. (2019) · doi:10.1101/622803 · Cited by 3,280
“…iteratively querying a model of the mutational fitness landscape could help efficiently guide the introduction of mutations to enhance protein function (Romero & Arnold, 2009), inform protein design using a combination of activating mutants (Hu et al., 2018), and make rational substitutions to…”
Background
Metadata
- Authors
- Romero, P. A., & Arnold, F. H.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2009-12
- Volume
- 10
- Issue
- 12
- Pages
- 866-876
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2118265845
- Cited by
- 1,161
- References
- 5
- FWCI
- 3.55
- Type
- journal article
- Language
- en
- Open access
- bronze
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