Oligosaccharyltransferase structures provide novel insight into the mechanism of asparagine-linked glycosylation in prokaryotic and eukaryotic cells.
Sign Up to like & getrecommendations! Published in 2019 at "Glycobiology"
DOI: 10.1093/glycob/cwy093
Abstract: Asparagine-linked (N-linked) glycosylation is one of the most common protein modification reactions in eukaryotic cells, occurring upon the majority of proteins that enter the secretory pathway. X-ray crystal structures of the single subunit OSTs from… read more here.
Keywords: mechanism; microscopy; linked glycosylation; glycosylation ... See more keywords
Complex N-Linked Glycosylation: A Potential Modifier of Niemann–Pick Disease, Type C1 Pathology
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DOI: 10.3390/ijms23095082
Abstract: Complex asparagine-linked glycosylation plays key roles in cellular functions, including cellular signaling, protein stability, and immune response. Previously, we characterized the appearance of a complex asparagine-linked glycosylated form of lysosome-associated membrane protein 1 (LAMP1) in… read more here.
Keywords: pathology; mice; asparagine linked; linked glycosylation ... See more keywords