Enhancement of therapeutic protein in vivo activities through glycoengineering

Author:

Elliott Steve,Lorenzini Tony,Asher Sheilah,Aoki Ken,Brankow David,Buck Lynette,Busse Leigh,Chang David,Fuller Janis,Grant James,Hernday Natasha,Hokum Martha,Hu Sylvia,Knudten Andrew,Levin Nancy,Komorowski Renee,Martin Frank,Navarro Rachell,Osslund Timothy,Rogers Gary,Rogers Norma,Trail Geri,Egrie Joan

Publisher

Springer Science and Business Media LLC

Subject

Biomedical Engineering,Molecular Medicine,Applied Microbiology and Biotechnology,Bioengineering,Biotechnology

Reference44 articles.

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2. Sytkowski, A.J., Lunn, E.D., Risinger, M.A. & Davis, K.L. An erythropoietin fusion protein comprised of identical repeating domains exhibits enhanced biological properties. J. Biol. Chem. 274, 24773–24778 (1999).

3. Sytkowski, A.J., Lunn, E.D., Davis, K.L., Feldman, L. & Siekman, S. Human erythropoietin dimers with markedly enhanced in vivo activity. Proc. Natl. Acad. Sci. USA 95, 1184–1188 (1998).

4. Dalle, B. et al. Dimeric erythropoietin fusion protein with enhanced erythropoietic activity in vitro and in vivo. Blood 97, 3776–3782 (2001).

5. Furuhashi, M. et al. Fusing the carboxy-terminal peptide of the chorionic gonadotropin (CG) β-subunit to the common α-subunit: retention of O-linked glycosylation and enhanced in vivo bioactivity of chimeric human CG. Mol. Endocrinol. 9, 54–63 (1995).

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