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Stability effects of mutations and protein evolvability
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Citations
Cites
Guerois, R., Nielsen, J. E., & Serrano, L. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00442-4 · Cited by 1,728
Robustness–epistasis link shapes the fitness landscape of a randomly drifting protein
Bershtein, S., Segal, M., Bekerman, R., Tokuriki, N., & Tawfik, D. S. (2006) · Nature · doi:10.1038/nature05385 · Cited by 414 · cited 3×
“This result is in agreement with in vitro measurements of fitness losses, and the threshold model, by which, once the margin of stability is compromised, mutations cause immediate fitness losses [2,4].”
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Enzyme promiscuity: A mechanistic and evolutionary perspective
Tawfik, O. K. A. D. S. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-030409-143718 · Cited by 1,355
Mutation effects predicted from sequence co-variation
Hopf, T. A., Ingraham, J. B., Poelwijk, F. J., Schärfe, C. P. I., Springer, M., Sander, C., & Marks, D. S. (2017) · Nature Biotechnology · doi:10.1038/nbt.3769 · Cited by 775
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
Mega-scale experimental analysis of protein folding stability in biology and design
Tsuboyama, K., Dauparas, J., Chen, J., Laine, E., Mohseni Behbahani, Y., Weinstein, J. J., Mangan, N. M., Ovchinnikov, S., & Rocklin, G. J. (2023) · Nature · doi:10.1038/s41586-023-06328-6 · Cited by 350
Ferreiro, D. U., Komives, E. A., & Wolynes, P. G. (2014) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583514000092 · Cited by 314
The Causes and Consequences of Genetic Interactions (Epistasis)
Domingo, J., Baeza-Centurion, P., & Lehner, B. (2019) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-083118-014857 · Cited by 242
Porebski, B. T., & Buckle, A. M. (2016) · Protein Engineering Design and Selection · doi:10.1093/protein/gzw015 · Cited by 215
Lessons from the lysozyme of phage T4
Baase, W. A., Liu, L., Tronrud, D. E., & Matthews, B. W. (2010) · Protein Science · doi:10.1002/pro.344 · Cited by 199
The Role of Conformational Dynamics and Allostery in Modulating Protein Evolution
Campitelli, P., Modi, T., Kumar, S., & Ozkan, S. B. (2020) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-052118-115517 · Cited by 190
AlphaFold2 Can Predict Single-Mutation Effects
McBride, J. M., Polev, K., Abdirasulov, A., Reinharz, V., Grzybowski, B. A., & Tlusty, T. (2023) · Physical Review Letters · doi:10.1103/physrevlett.131.218401 · Cited by 87
Xu, Y., Liu, D., & Gong, H. (2024) · Nature Computational Science · doi:10.1038/s43588-024-00716-2 · Cited by 41
Accurate protein stability predictions from homology models
Valanciute, A., Nygaard, L., Zschach, H., Maglegaard Jepsen, M., Lindorff-Larsen, K., & Stein, A. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.11.048 · Cited by 33
RNA language models predict mutations that improve RNA function
Shulgina, Y., Trinidad, M. I., Langeberg, C. J., Nisonoff, H., Chithrananda, S., Skopintsev, P., Nissley, A. J., Patel, J., Boger, R. S., Shi, H., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54812-y · Cited by 32
Lv, X., Chen, J., Lu, Y., Chen, Z., Xiao, N., & Yang, Y. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c00064 · Cited by 26
ESM ‐scan—A tool to guide amino acid substitutions
Totaro, M. G., Vide, U., Zausinger, R., Winkler, A., & Oberdorfer, G. (2024) · Protein Science · doi:10.1002/pro.5221 · Cited by 19
Heterologous expression of naturally evolved putative de novo proteins with chaperones
Eicholt, L. A., Aubel, M., Berk, K., Bornberg‐Bauer, E., & Lange, A. (2022) · Protein Science · doi:10.1002/pro.4371 · Cited by 18
Chaperoning the Mononegavirales: Current Knowledge and Future Directions
Latorre, V., Mattenberger, F., & Geller, R. (2018) · Viruses · doi:10.3390/v10120699 · Cited by 14
Komp, E., Alanzi, H. N., Francis, R., Vuong, C., Roberts, L., Mosallanejad, A., & Beck, D. A. C. (2023) · Scientific Data · doi:10.1038/s41597-023-02553-w · Cited by 7
Hacisuleyman, A., Gul, A., & Erman, B. (2025) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26795 · Cited by 1
Metadata
- Authors
- Tokuriki, N., & Tawfik, D. S.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2009-10
- Volume
- 19
- Issue
- 5
- Pages
- 596-604
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2145317354
- Cited by
- 834
- References
- 2
- FWCI
- 15.15
- Type
- journal article
- Language
- en
- Open access
- closed
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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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.
