Cishan Li
University of Maryland, Baltimore
7 Papers
27 Citations
Cishan Li is an academic researcher from University of Maryland, Baltimore. The author has contributed to research in topics: Glycan & Glycosylation. The author has an hindex of 7, co-authored 7 publications.
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Papers
A combined method for producing homogeneous glycoproteins with eukaryotic N-glycosylation
Flavio Schwarz,Wei Huang,Cishan Li,Benjamin L. Schulz,Christian Lizak,Alessandro Palumbo,Shin Numao,Dario Neri,Markus Aebi,Lai-Xi Wang +9 more
TL;DR: A novel method for producing homogeneous eukaryotic N-glycoproteins by engineering and functional transfer of the C. jejuni glycosylation machinery in E. coli to express Glycosylated proteins with the key GlcNAc-Asn linkage is described.
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Glycosynthases Enable a Highly Efficient Chemoenzymatic Synthesis of N-Glycoproteins Carrying Intact Natural N-Glycans
TL;DR: In this article, two endo-beta-N-acetylglucosaminidases from Arthrobacter protophormiae (Endo-A) and Mucor hiemalis (endo-M) were used to construct homogeneous N-glycoproteins carrying natural Nglycans.
Expression, Glycoform Characterization, and Antibody-binding of HIV-1 V3 Glycopeptide Domain Fused with Human IgG1-Fc
TL;DR: The expression and characterization of glycosylated, full-size V3 domain derived from HIV-1(Bal) strain as an IgG1-Fc fusion protein, including its binding to two broadly HIV-neutralizing antibodies 2G12 and 447-52D is reported.
20
Chemoenzymatic synthesis of N-linked neoglycoproteins through a chitinase-catalyzed transglycosylation.
Cishan Li,Wei Huang,Lai-Xi Wang +2 more
TL;DR: Although the yield needs to be optimized, the chitinase-catalyzed transglycosylation provides a potentially useful tool for the synthesis of neoglycoproteins carrying novel N-linked oligosaccharides.
9
Chemoenzymatic Synthesis and Fcγ Receptor Binding of Homogeneous Glycoforms of Antibody Fc Domain. Presence of a Bisecting Sugar Moiety Enhances the Affinity of Fc to FcγIIIa Receptor
TL;DR: The chemoenzymatic synthesis and Fcγ receptor binding of an array of homogeneous IgG-Fc glycoforms provide a useful tool for elucidating how a fine Fc N-glycan structure precisely affects the function of the Fc domain.