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Osborne MJ, Rahardjo AK, Volpon L, et al. . Biomol NMR Assign. 2021;15(2):323-328doi: 10.1007/s12104-021-10024-9.
Osborne, M. J., Rahardjo, A. K., Volpon, L., & Borden, K. L. B. (2021). . Biomolecular NMR assignments, 15(2), 323-328. https://doi.org/10.1007/s12104-021-10024-9
Osborne, Michael J, et al. "." Biomolecular NMR assignments vol. 15,2 (2021): 323-328. doi: https://doi.org/10.1007/s12104-021-10024-9
Osborne MJ, Rahardjo AK, Volpon L, Borden KLB. . Biomol NMR Assign. 2021 Oct;15(2):323-328. doi: 10.1007/s12104-021-10024-9. Epub 2021 Apr 18. PMID: 33870481; PMCID: PMC8549657.
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Biomol NMR Assign. 2021 Oct;15(2):323-328. doi: 10.1007/s12104-021-10024-9. Epub 2021 Apr 18.

[No title available]

Biomolecular NMR assignments

Michael J Osborne, Amanda K Rahardjo, Laurent Volpon, Katherine L B Borden

Affiliations

  1. Department of Pathology and Cell Biology, Institute of Research in Immunology and Cancer (IRIC), Université de Montréal, Pavillion Marcelle-Coutu, Chemin Polytechnique, Montreal, QC, Canada.
  2. Department of Pathology and Cell Biology, Institute of Research in Immunology and Cancer (IRIC), Université de Montréal, Pavillion Marcelle-Coutu, Chemin Polytechnique, Montreal, QC, Canada. [email protected].

PMID: 33870481 PMCID: PMC8549657 DOI: 10.1007/s12104-021-10024-9

Abstract

The human UDP-glucuronosyltransferase (UGT) family of enzymes catalyze the covalent addition of glucuronic acid to a wide range of compounds, generally rendering them inactive. Although important for clearance of environmental toxins and metabolites, UGT activation can lead to inappropriate glucuronidation of therapeutics underlying drug resistance. Indeed, 50% of medications are glucuronidated. To better understand this mode of resistance, we studied the UGT2B7 enzyme associated with glucuronidation of cancer drugs such as Tamoxifen and Sorafenib. We report

© 2021. The Author(s), under exclusive licence to Springer Nature B.V.

Keywords: Backbone resonance assignment; Drug resistance; Glucuronidation; UGT

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