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- W4245965461 abstract "Glycoproteins can be divided into two large classes of molecules based on the atom linking the carbohydrate to the protein. N-linked glycoprotein refers to the subset where carbohydrates are linked to protein through the amide nitrogen of an asparagine residue. O-linked glycoprotein refers to glycoproteins where the carbohydrate is linked to the protein through an oxygen atom. The fact that cell surfaces are coated with numerous glycoproteins bearing thousands of different, structurally complex carbohydrate structures caused researchers over 40 years ago to propose that these carbohydrates would play roles in communication between cells and their environment. Since then, numerous examples demonstrating that such communication exists have been uncovered. In the past few years, several specific examples showing functional roles for cell-surface oligosaccharides have been poignantly provided through the study of unusual forms of O-linked oligosaccharides, including O-fucose, O-glucose, and O-mannose. In particular, roles for these carbohydrates in both regulation of signal transduction events and in cell-surface binding events have been demonstrated. These examples have provided firm evidence that the predictions of 40 years ago were true and are now serving as paradigms for the functional relevance of many different forms of glycosylation." @default.
- W4245965461 created "2022-05-12" @default.
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- W4245965461 date "2021-01-01" @default.
- W4245965461 modified "2023-09-29" @default.
- W4245965461 title "Protein Modifications | Glycoprotein-Mediated Cell Interactions, Nonmucin-Type O-Linked" @default.
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- W4245965461 doi "https://doi.org/10.1016/b978-0-12-819460-7.00162-6" @default.
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