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- W2896738812 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 eubacterial and archaebacterial organisms revealed the location of donor and acceptor substrate binding sites and provided the basis for a catalytic mechanism. Cryoelectron microscopy structures of the octameric yeast OST provided substantial insight into the organization and assembly of the multisubunit oligosaccharyltransferases. Furthermore, the cryoelectron microscopy structure of a complex consisting of a mammalian OST complex, the protein translocation channel and a translating ribosome revealed new insight into the mechanism of cotranslational glycosylation." @default.
- W2896738812 created "2018-10-26" @default.
- W2896738812 creator A5075463702 @default.
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- W2896738812 date "2018-10-31" @default.
- W2896738812 modified "2023-10-02" @default.
- W2896738812 title "Oligosaccharyltransferase structures provide novel insight into the mechanism of asparagine-linked glycosylation in prokaryotic and eukaryotic cells" @default.
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- W2896738812 doi "https://doi.org/10.1093/glycob/cwy093" @default.
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