The DOI matches its Crossref record; 121 of the 121 references it cites were found in a registry or an index.
FoldX as Protein Engineering Tool: Better Than Random Based Approaches?
Open accessAbstract
Improving protein stability is an important goal for basic research as well as for clinical and industrial applications but no commonly accepted and widely used strategy for efficient engineering is known. Beside random approaches like error prone PCR or physical techniques to stabilize proteins, e.g. by immobilization, in silico approaches are gaining more attention to apply target-oriented mutagenesis. In this review different algorithms for the prediction of beneficial mutation sites to enhance protein stability are summarized and the advantages and disadvantages of FoldX are highlighted. The question whether the prediction of mutation sites by the algorithm FoldX is more accurate than random based approaches is addressed.
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Cites
The FoldX web server: an online force field
Schymkowitz, J., Borg, J., Stricher, F., Nys, R., Rousseau, F., & Serrano, L. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki387 · Cited by 2,759
Enzyme immobilisation in biocatalysis: why, what and how
Sheldon, R. A., & van Pelt, S. (2013) · Chem. Soc. Rev. · doi:10.1039/c3cs60075k · Cited by 2,675
Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability
Vieille, C., & Zeikus, G. J. (2001) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.65.1.1-43.2001 · Cited by 2,123
Leaver-Fay (2011) · doi:10.1016/b978-0-12-381270-4.00019-6 · Cited by 1,904
Biocatalytic Asymmetric Synthesis of Chiral Amines from Ketones Applied to Sitagliptin Manufacture
Savile, C. K., Janey, J. M., Mundorff, E. C., Moore, J. C., Tam, S., Jarvis, W. R., Colbeck, J. C., Krebber, A., Fleitz, F. J., Brands, J., et al. (2010) · Science · doi:10.1126/science.1188934 · Cited by 1,756
Guerois, R., Nielsen, J. E., & Serrano, L. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00442-4 · Cited by 1,728 · cited 1×
“The force fi eld algorithm, which was originally created by Guerois et al. became popular as webtool in 2005 by Schymkowitz et al. and was re fi ned to the currently last version FoldX 4.0 [82 – 84].”
MethodInfluentialPrediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
Fernandez-Escamilla, A.-M., Rousseau, F., Schymkowitz, J., & Serrano, L. (2004) · Nature Biotechnology · doi:10.1038/nbt1012 · Cited by 1,658
The Rosetta All-Atom Energy Function for Macromolecular Modeling and Design
Alford, R. F., Leaver-Fay, A., Jeliazkov, J. R., O’Meara, M. J., DiMaio, F. P., Park, H., Shapovalov, M. V., Renfrew, P. D., Mulligan, V. K., Kappel, K., et al. (2017) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.7b00125 · Cited by 1,532
Glucose Biosensors: An Overview of Use in Clinical Practice
Yoo, E.-H., & Lee, S.-Y. (2010) · Sensors · doi:10.3390/s100504558 · Cited by 1,137
The challenge of enzyme cost in the production of lignocellulosic biofuels
Klein‐Marcuschamer, D., Oleskowicz‐Popiel, P., Simmons, B. A., & Blanch, H. W. (2012) · Biotechnology and Bioengineering · doi:10.1002/bit.24370 · Cited by 998
Cited by
Transfer learning to leverage larger datasets for improved prediction of protein stability changes
Dieckhaus, H., Brocidiacono, M., Randolph, N. Z., & Kuhlman, B. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2314853121 · Cited by 205
RosettaDDGPrediction for high‐throughput mutational scans: From stability to binding
(2022) · doi:10.1002/pro.4527 · Cited by 90
DIP/Dpr interactions and the evolutionary design of specificity in protein families
Sergeeva, A. P., Katsamba, P. S., Cosmanescu, F., Brewer, J. J., Ahlsen, G., Mannepalli, S., Shapiro, L., & Honig, B. (2020) · Nature Communications · doi:10.1038/s41467-020-15981-8 · Cited by 38
A3D 2.0 update for the prediction and optimization of protein solubility
Pujols, J., Iglesias, V., Santos, J., Kuriata, A., Kmiecik, S., & Ventura, S. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-1859-2_3 · Cited by 19
Ramon, A., Ni, M., Predeina, O., Gaffey, R., Kunz, P., Onuoha, S., & Sormanni, P. (2025) · mAbs · doi:10.1080/19420862.2024.2442750 · Cited by 13
Metadata
- Authors
- Buß, O., Rudat, J., & Ochsenreither, K.
- Venue
- Computational and Structural Biotechnology Journal
- Published
- 2018
- Volume
- 16
- Pages
- 25-33
- ISSN
- 2001-0370 (ISSN-L)
- OpenAlex
- W2788217325
- Cited by
- 284
- References
- 121
- FWCI
- 6.12
- Type
- journal article
- Language
- en
- Open access
- gold
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- Buß, O., Rudat, J., & Ochsenreither, K. (2018). FoldX as Protein Engineering Tool: Better Than Random Based Approaches? Computational and Structural Biotechnology Journal. https://doi.org/10.1016/j.csbj.2018.01.002
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