The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Pyrrolysyl-tRNA synthetase: An ordinary enzyme but an outstanding genetic code expansion tool
Open accessAbstract
The genetic incorporation of the 22nd proteinogenic amino acid, pyrolysine (Pyl) at amber codon is achieved by the action of pyrrolysyl-tRNA synthetase (PylRS) together with its cognate tRNAPyl. Unlike most aminoacyl-tRNA synthetases, PylRS displays high substrate side chain promiscuity, low selectivity toward its substrate α-amine, and low selectivity toward the anticodon of tRNAPyl. These unique but ordinary features of PylRS as an aminoacyl-tRNA synthetase allow the Pyl incorporation machinery to be easily engineered for the genetic incorporation of more than 100 non-canonical amino acids (NCAAs) or α-hydroxy acids into proteins at amber codon and the reassignment of other codons such as ochre UAA, opal UGA, and four-base AGGA codons to code NCAAs.
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Cites
Adding New Chemistries to the Genetic Code
Liu, C. C., & Schultz, P. G. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.105824 · Cited by 1,725
Universal rules and idiosyncratic features in tRNA identity
Giege, R., Sissler, M., & Florentz, C. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.22.5017 · Cited by 769
Pyrrolysine and Selenocysteine Use Dissimilar Decoding Strategies
Zhang, Y., Baranov, P. V., Atkins, J. F., & Gladyshev, V. N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501458200 · Cited by 135
Cited by
Bell, E. L., Finnigan, W., France, S. P., Green, A. P., Hayes, M. A., Hepworth, L. J., Lovelock, S. L., Niikura, H., Osuna, S., Romero, E., et al. (2021) · Nature Reviews Methods Primers · doi:10.1038/s43586-021-00044-z · Cited by 685
Bioorthogonal Chemistry and Its Applications
Bird, R. E., Lemmel, S. A., Yu, X., & Zhou, Q. A. (2021) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.1c00461 · Cited by 409
Diels-Alder reaction–triggered bioorthogonal protein decaging in living cells
Li, J., Jia, S., & Chen, P. R. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1656 · Cited by 277
Continuous directed evolution of aminoacyl-tRNA synthetases
Bryson, D. I., Fan, C., Guo, L.-T., Miller, C., Söll, D., & Liu, D. R. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2474 · Cited by 264
Labeling and Single-Molecule Methods To Monitor G Protein-Coupled Receptor Dynamics
Tian, H., Fürstenberg, A., & Huber, T. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00084 · Cited by 114
Metadata
- Authors
- Wan, W., Tharp, J. M., & Liu, W. R.
- Venue
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Publisher
- Elsevier BV
- Published
- 2014-06
- Volume
- 1844
- Issue
- 6
- Pages
- 1059-1070
- ISSN
- 1570-9639 (ISSN-L)
- OpenAlex
- W2029672674
- Cited by
- 396
- References
- 3
- FWCI
- 10.71
- Type
- journal article
- Language
- en
- Open access
- green
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- Wan, W., Tharp, J. M., & Liu, W. R. (2014). Pyrrolysyl-tRNA synthetase: An ordinary enzyme but an outstanding genetic code expansion tool. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. https://doi.org/10.1016/j.bbapap.2014.03.002
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