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- W4296167811 endingPage "102788" @default.
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- W4296167811 abstract "Proteins continue to represent a large fraction of the therapeutics market, reaching over a hundred billion dollars in market size globally. One key feature of protein modification that can affect both structure and function is the addition of glycosylation following protein folding, leading to regulatory requirements for the accurate assessment of protein attributes, including glycan structures. The non-template-driven, innately heterogeneous N-glycosylation process thus requires accurate detection to robustly generate protein therapies. A challenge exists in the timely detection of protein glycosylation without labor-intensive manipulation. In this article, we discuss progress toward N-glycoprotein control, focusing on novel control strategies and the advancement of rapid, high-throughput analysis methods." @default.
- W4296167811 created "2022-09-18" @default.
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- W4296167811 date "2022-12-01" @default.
- W4296167811 modified "2023-10-16" @default.
- W4296167811 title "Progress toward rapid, at-line N-glycosylation detection and control for recombinant protein expression" @default.
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- W4296167811 doi "https://doi.org/10.1016/j.copbio.2022.102788" @default.
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