The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Design of functional metalloproteins
Open accessAbstract
Metalloproteins catalyse some of the most complex and important processes in nature, such as photosynthesis and water oxidation. An ultimate test of our knowledge of how metalloproteins work is to design new metalloproteins. Doing so not only can reveal hidden structural features that may be missing from studies of native metalloproteins and their variants, but also can result in new metalloenzymes for biotechnological and pharmaceutical applications. Although it is much more challenging to design metalloproteins than non-metalloproteins, much progress has been made in this area, particularly in functional design, owing to recent advances in areas such as computational and structural biology.
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Cites
A General Method for Site-specific Incorporation of Unnatural Amino Acids into Proteins
Noren, C. J., Anthony-Cahill, S. J., Griffith, M. C., & Schultz, P. G. (1989) · Science · doi:10.1126/science.2649980 · Cited by 1,019 · cited 1×
“A promising and versatile technique is the use of custom evolved transfer-RNA synthetase molecules for in vitro and in vivo translation of new residues through recognition of the amber stop codo”
Cited by
Nanomaterials with enzyme-like characteristics (nanozymes): next-generation artificial enzymes
Wei, H., & Wang, E. (2013) · Chemical Society Reviews · doi:10.1039/c3cs35486e · Cited by 3,779
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
Jo, S., Cheng, X., Islam, S. M., Huang, L., Rui, H., Zhu, A., Lee, H. S., Qi, Y., Han, W., Vanommeslaeghe, K., et al. (2014) · Advances in Protein Chemistry and Structural Biology · doi:10.1016/bs.apcsb.2014.06.002 · Cited by 363
Hydrolytic catalysis and structural stabilization in a designed metalloprotein
Zastrow, M. L., Peacock, A. F. A., Stuckey, J. A., & Pecoraro, V. L. (2012) · Nature Chemistry · doi:10.1038/nchem.1201 · Cited by 355
Crittenden, C. M., Novelli, E. T., Mehaffey, M. R., Xu, G. N., Giles, D. H., Fies, W. A., Dalby, K. N., Webb, L. J., & Brodbelt, J. S. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.0c00066 · Cited by 24
Metadata
- Authors
- Lu, Y., Yeung, N., Sieracki, N., & Marshall, N. M.
- Venue
- Nature
- Published
- 2009-08-12
- Volume
- 460
- Issue
- 7257
- Pages
- 855-862
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2034971743
- Cited by
- 704
- References
- 1
- FWCI
- 16.56
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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