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Folding of glycoproteins

Calnexin Chaperone, Fectin Folding of glycoproteins clxA... [Pg.328]

Helenius A, Trombetta ES, Hebert DN et al (1997) Calnexin, calreticulin and the folding of glycoproteins. Trends Cell Biol 7 193-200... [Pg.333]

Shental-Bechor, D., Levy, Y. Folding of glycoproteins Toward understanding the biophysics of the glycosylation code. Curr. Opin. Struct. Biol. 2009,19, 524-33. [Pg.279]

Studies with simian viral hemagglutinin neuraminidase and yeast acid phosphatase suggest that AT-glycans are needed for proper folding of glycoproteins... [Pg.169]

Oligosaccharide side chains may assist in the proper folding of glycoproteins, help protect the mature proteins from proteolysis, participate in cell-cell adhesion, and function as antigens. [Pg.680]

Glucosidase inhibitors, particularly castanospermine (CST), have proven to be useful tools to study the in vivo effects of blocking the interactions of calnexin and calreticulin with glycoproteins. Most studies support the view that these molecules function to promote the correct folding of glycoproteins. For example, treatment... [Pg.2092]

In addition to their involvement in the folding of glycoproteins, calnexin and calreticulin participate in the retention of non-native glycoproteins within the ER... [Pg.2093]

Some membrane proteins are covalently linked to complex arrays of carbohydrate. For example, in gly-cophorin, a glycoprotein of the erythrocyte plasma membrane, 60% of the mass consists of complex oligosaccharide units covalently attached to specific amino acid residues. Ser, Thr, and Asn residues are the most common points of attachment (see Fig. 7-31). At the other end of the scale is rhodopsin of the rod cell plasma membrane, which contains just one hexasac-charide. The sugar moieties of surface glycoproteins influence the folding of the proteins, as well as their sta-... [Pg.371]


See other pages where Folding of glycoproteins is mentioned: [Pg.266]    [Pg.1777]    [Pg.1778]    [Pg.263]    [Pg.267]    [Pg.339]    [Pg.1245]    [Pg.2101]    [Pg.266]    [Pg.1777]    [Pg.1778]    [Pg.263]    [Pg.267]    [Pg.339]    [Pg.1245]    [Pg.2101]    [Pg.508]    [Pg.526]    [Pg.636]    [Pg.113]    [Pg.48]    [Pg.448]    [Pg.449]    [Pg.145]    [Pg.145]    [Pg.117]    [Pg.492]    [Pg.206]    [Pg.250]    [Pg.486]    [Pg.1721]    [Pg.376]    [Pg.369]    [Pg.369]    [Pg.353]    [Pg.27]    [Pg.155]    [Pg.267]    [Pg.117]    [Pg.186]    [Pg.304]    [Pg.315]    [Pg.580]    [Pg.1942]    [Pg.63]    [Pg.11]    [Pg.338]    [Pg.193]    [Pg.422]   
See also in sourсe #XX -- [ Pg.267 , Pg.268 , Pg.269 ]




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Glycoproteins folding

Of glycoproteins

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