The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index.
Redox-based reagents for chemoselective methionine bioconjugation
Open accessAbstract
Targeting proteins at the other sulfur: As the only amino acid with a thiol (SH) group, cysteine is easily targeted for site-selective protein modifications. Hydrophobic methionine also has sulfur in its side chain, but its capping methyl group has hindered analogous targeting efforts. Lin et al. introduce a complementary protocol to tether new substituents exclusively to methionine, even in the presence of cysteine. They used an oxaziridine group as an oxidant to form sulfimide (S=N) linkages. The approach allowed antibody-drug conjugation and chemoproteomic screening for reactive methionine surface residues. Science , this issue p. 597
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Metadata
- Authors
- Lin, S., Yang, X., Jia, S., Weeks, A. M., Hornsby, M., Lee, P. S., Nichiporuk, R. V., Iavarone, A. T., Wells, J. A., Toste, F. D., & Chang, C. J.
- Venue
- Science
- Published
- 2017-02-10
- Volume
- 355
- Issue
- 6325
- Pages
- 597-602
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2593943479
- Cited by
- 513
- References
- 56
- FWCI
- 17.58
- Type
- journal article
- Language
- en
- Open access
- green
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- Lin, S., Yang, X., Jia, S., Weeks, A. M., Hornsby, M., Lee, P. S., Nichiporuk, R. V., Iavarone, A. T., Wells, J. A., Toste, F. D., & Chang, C. J. (2017). Redox-based reagents for chemoselective methionine bioconjugation. Science. https://doi.org/10.1126/science.aal3316
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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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