The DOI matches its Crossref record; 77 of the 77 references it cites were found in a registry or an index.
Protein Design by Directed Evolution
Abstract
While nature evolved polypeptides over billions of years, protein design by evolutionary mimicry is progressing at a far more rapid pace. The mutation, selection, and amplification steps of the evolutionary cycle may be imitated in the laboratory using existing proteins, or molecules created de novo from random sequence space, as starting templates. However, the astronomically large number of possible polypeptide sequences remains an obstacle to identifying and isolating functionally interesting variants. Intelligently designed libraries and improved search techniques are consequently important for future advances. In this regard, combining experimental and computational methods holds particular promise for the creation of tailored protein receptors and catalysts for tasks unimagined by nature.
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Citations
Cites
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
Rapid evolution of a protein in vitro by DNA shuffling
Stemmer, W. P. C. (1994) · Nature · doi:10.1038/370389a0 · Cited by 1,932
Design of a Novel Globular Protein Fold with Atomic-Level Accuracy
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In Vitro Selection of Functional Nucleic Acids
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De Novo Protein Design: Fully Automated Sequence Selection
Dahiyat, B. I., & Mayo, S. L. (1997) · Science · doi:10.1126/science.278.5335.82 · Cited by 1,145
RNA-peptide fusions for the in vitro selection of peptides and proteins
Roberts, R. W., & Szostak, J. W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12297 · Cited by 1,105
In vitro selection and evolution of functional proteins by using ribosome display
Hanes, J., & Plückthun, A. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.10.4937 · Cited by 1,088
Man-made cell-like compartments for molecular evolution
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Structural Symmetry and Protein Function
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Cited by
Reetz, M. T. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201000826 · Cited by 538
Chip in a lab: microfluidics for next generation life science research
Streets, A. M., & Huang, Y. (2013) · Biomicrofluidics · doi:10.1063/1.4789751 · Cited by 180
Computational scoring and experimental evaluation of enzymes generated by neural networks
Johnson, S. R., Fu, X., Viknander, S., Goldin, C., Monaco, S., Zelezniak, A., & Yang, K. K. (2025) · Nature Biotechnology · doi:10.1038/s41587-024-02214-2 · Cited by 99
Li, T., Pantazes, R. J., & Maranas, C. D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105954 · Cited by 79
Free energy perturbation calculations of the thermodynamics of protein side-chain mutations
Steinbrecher, T., Abel, R., Clark, A., & Friesner, R. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.03.002 · Cited by 46
Metadata
- Authors
- Jäckel, C., Kast, P., & Hilvert, D.
- Venue
- Annual Review of Biophysics
- Publisher
- Annual Reviews
- Published
- 2008-06-01
- Volume
- 37
- Issue
- 1
- Pages
- 153-173
- ISSN
- 1936-122X (ISSN-L)
- 1936-1238
- OpenAlex
- W2144794655
- Cited by
- 409
- References
- 77
- FWCI
- 2.00
- Type
- journal article
- Language
- en
- Open access
- closed
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- Jäckel, C., Kast, P., & Hilvert, D. (2008). Protein Design by Directed Evolution. Annual Review of Biophysics. https://doi.org/10.1146/annurev.biophys.37.032807.125832
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
