The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
Protein disulfide engineering
Abstract
Improving the stability of proteins is an important goal in many biomedical and industrial applications. A logical approach is to emulate stabilizing molecular interactions found in nature. Disulfide bonds are covalent interactions that provide substantial stability to many proteins and conform to well‐defined geometric conformations, thus making them appealing candidates in protein engineering efforts. Disulfide engineering is the directed design of novel disulfide bonds into target proteins. This important biotechnological tool has achieved considerable success in a wide range of applications, yet the rules that govern the stabilizing effects of disulfide bonds are not fully characterized. Contrary to expectations, many designed disulfide bonds have resulted in decreased stability of the modified protein. We review progress in disulfide engineering, with an emphasis on the issue of stability and computational methods that facilitate engineering efforts.
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Cited by
Nick Pace, C., Scholtz, J. M., & Grimsley, G. R. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.05.006 · Cited by 386
Review: Engineering of thermostable enzymes for industrial applications
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FoldX as Protein Engineering Tool: Better Than Random Based Approaches?
Buß, O., Rudat, J., & Ochsenreither, K. (2018) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2018.01.002 · Cited by 284
CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae
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Metadata
- Authors
- Dombkowski, A. A., Sultana, K. Z., & Craig, D. B.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2013-11-26
- Volume
- 588
- Issue
- 2
- Pages
- 206-212
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2019519304
- Cited by
- 282
- References
- 55
- FWCI
- 4.03
- Type
- journal article
- Language
- en
- Open access
- closed
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