The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Fluorinated amino acids in protein design and engineering
Abstract
Selective incorporation of unnatural amino acids into proteins is a powerful tool for illuminating the principles of protein design. In particular, fluorinated amino acids have recently emerged as valuable building blocks for designing hyperstable protein folds, as well as directing highly specific protein-protein interactions. We review the collagen mimetic and coiled coil peptide systems that exemplify generalizable paradigms for future design. The unique electronic and phase properties of fluorocarbons are discussed, and protein synthesis using unnatural amino acids is briefly reviewed.
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Cites
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Wang, L., Brock, A., Herberich, B., & Schultz, P. G. (2001) · Science · doi:10.1126/science.1060077 · Cited by 1,499
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
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Facile Catalyst Separation Without Water: Fluorous Biphase Hydroformylation of Olefins
Horváth, I. T., & Rábai, J. (1994) · Science · doi:10.1126/science.266.5182.72 · Cited by 1,416
Coiled coils: new structures and new functions
LUPAS, A. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10052-9 · Cited by 1,183
Synthesis of Native Proteins by Chemical Ligation
Dawson, P. E., & Kent, S. B. H. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.923 · Cited by 1,082
Yan, L. Z., & Dawson, P. E. (2001) · Journal of the American Chemical Society · doi:10.1021/ja003265m · Cited by 661
Code for collagen's stability deciphered
Holmgren, S. K., Taylor, K. M., Bretscher, L. E., & Raines, R. T. (1998) · Nature · doi:10.1038/33573 · Cited by 498
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Conformational Stability of Collagen Relies on a Stereoelectronic Effect
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Cited by
Fluorine in Medicinal Chemistry and Chemical Biology
(2009) · Wiley eBooks · doi:10.1002/9781444312096 · Cited by 1,731
The Design of Coiled-Coil Structures and Assemblies
Woolfson, D. N. (2005) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(05)70004-8 · Cited by 585
Protein Design: Toward Functional Metalloenzymes
Yu, F., Cangelosi, V. M., Zastrow, M. L., Tegoni, M., Plegaria, J. S., Tebo, A. G., Mocny, C. S., Ruckthong, L., Qayyum, H., & Pecoraro, V. L. (2014) · Chemical Reviews · doi:10.1021/cr400458x · Cited by 441
Posttranslational mutagenesis: A chemical strategy for exploring protein side-chain diversity
Wright, T. H., Bower, B. J., Chalker, J. M., Bernardes, G. J. L., Wiewiora, R., Ng, W.-L., Raj, R., Faulkner, S., Vallée, M. R. J., Phanumartwiwath, A., et al. (2016) · Science · doi:10.1126/science.aag1465 · Cited by 317
Metadata
- Authors
- Yoder, N. C., & Kumar, K.
- Venue
- Chemical Society Reviews
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2002-09-13
- Volume
- 31
- Issue
- 6
- Pages
- 335-341
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W2330772790
- Cited by
- 317
- References
- 27
- FWCI
- 3.56
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
