Of asparagine-linked oligosaccharides

Figure 47-4. Structures of the major types of asparagine-linked oligosaccharides. The boxed area encloses the pentasaccharide core common to all N-linked glycoproteins. (Reproduced, with permission, from Kornfeld R, Kornfeld S Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 1985 54 631.)...

Kornfeld R, Kornfeld S Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 1985 54 631. 

Watson, E., Bhide, A., Kenney, W. C., and Lin, F.-K., High-performance anion-exchange chromatography of asparagine-linked oligosaccharides, Anal. Bio-chem., 205, 90, 1992. 

Kornfeld, R. and Kornfeld, S. (1985) Assembly of asparagine linked oligosaccharides. Annual Review of Biochemistry 54, 631-664. 

Komfeld, R. Komfeld, S., Assembly of Asparagine-Linked Oligosaccharides. Annu. Rev. Biochem. 1985, 54, 631-664. 

Takahashi N, Hitotsuya H, Hanzawa H, Arata Y, Kurihara Y, Structural study of asparagine-linked oligosaccharide moiety of taste-modifying protein, miraculin,... 

Table 10. Calculated dihedral angles of asparagine linked oligosaccharides [130, 125]...

Taverna, F. A., Wang, L. Y., MacDonald, J. F., and Hampson, D. R. (1994). A transmembrane model for an ionotropic glutamate receptor predicted on the basis of the location of asparagine-linked oligosaccharides./. Biol. Chem. 269, 14159-14164. 

R. Kornfeld and S. Kornfeld, Assembly of asparagines-linked oligosaccharides, Anna. Rev. Biochem. 54 (1985), 631-664. 

Dennis, J. W. and Laferte, S. (1985). Recognition of asparagine-linked oligosaccharides on murine tumor cells by natural killer cells. Cancer Res. 45, 6034-6040. 

R. Komfeld and S. Komfeld, Assembly of asparagine-linked oligosaccharides, Anna. Rev Biochem. 54 631 (1985). 

Methyl a-1,3- and Q -l,6-C-mannobiosides 159 and 160, as well as the branched C-tri-mannose analog 161 of the common core stmcture of asparagine-linked oligosaccharides have also been synthesized using the same sulfone 156 and, for the C-trimer, the monosaccharide dialdehyde 165 ( Scheme 32 and Scheme 33) [78,79,80]. 

Direct comparison of the lateral mobility of chimeric proteins, where the GPI anchor is replaced with a transmembrane domain, demonstrates little change in their mobility [126,127]. Removal of asparagine-linked oligosaccharides has a greater effect on the lateral movement of the transmembrane protein H-2L[128] than removal of its cytoplasmic tail [129]. Moreover, the lateral mobility of the sperm protein PH-20 changes during development [124]. 

Cummings, R., and Kornfeld, S. (1982). Fractionation of Asparagin-linked Oligosaccharides by Serial Lectin-agarose Affinity Chromatography, ./ Biol. Chem. 257 11235-11240. 

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