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- W2935851821 abstract "Abstract The biological activity of the glycoprotein hormone erythropoietin (EPO) is dependent mainly on the structure of its N‐linked glycans. We aimed to readily attach defined N ‐glycans to EPO through copper‐catalyzed azide alkyne cycloaddition. EPO variants with an alkyne‐bearing non‐natural amino acid (Plk) at the N ‐glycosylation sites 24, 38, and 83 were obtained by amber suppression followed by protein purification and refolding. Click conjugation of the alkynyl EPOs with biantennary N ‐glycan azides provided biologically active site‐specifically modified EPO glycoconjugates." @default.
- W2935851821 created "2019-04-25" @default.
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- W2935851821 date "2019-07-09" @default.
- W2935851821 modified "2023-09-23" @default.
- W2935851821 title "Synthesis of Erythropoietins Site‐Specifically Conjugated with Complex‐Type<i>N</i>‐Glycans" @default.
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- W2935851821 doi "https://doi.org/10.1002/cbic.201900023" @default.
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