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• W2050952262 abstract "Three papers in this issue of Neurology 1-3⇓⇓ and one that appeared 3 months ago4 report patients with newly discovered diseases of protein glycosylation. Glycosylation is a post-translational modification of proteins to form glycoproteins, which serve crucial roles in function such as mediating cell adhesion and signaling, as well as being the backbone of basal lamina.5 Glycosylation takes place in the Golgi apparatus by the sequential attachment and removal of oligosaccharide moieties or glycans (including mannose, galactose, fucose, N-acetylglucosamine, N-acetyl galactosamine, and sialic acid). Glycoproteins have been classified as N-linked or O-linked.5 In N-linked glycoproteins the glycan moiety is linked, via N-acetylglucosamine, to the amide group of an asparagine residue of the protein.6 In the most abundant form of O-linked glycoproteins the glycan is linked, via N-acetylgalactosamine to the hydroxyl group of either serine or threonine of the protein.5 Recently, however, other types of O-glycosylation have been described in mammals, including O-mannosylation, in which the glycan moiety is linked, via mannose, to the hydroxyl group of either serine or threonine.7 O-mannosyl types of glycoproteins are of particular importance for skeletal muscle because a key sarcolemmal glycoprotein, α-dystroglycan, important in the pathogenesis of many muscular dystrophies, belongs in this category.8A disturbed glycosylation profile of proteins may be a result of nonspecific cellular pathology, but in the past 3 years many diseases have been discovered to be caused by a primary genetic defect that disrupts the normal glycosylation pattern of proteins. Glycosylation defects may occur as a result of a deficient …" @default.
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• W2050952262 date "2002-12-10" @default.
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• W2050952262 title "Sweetening the pot in muscle: Genetic defects of protein glycosylation causing muscle disease" @default.
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• W2050952262 doi "https://doi.org/10.1212/01.wnl.0000041160.67746.f6" @default.
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