The oligosaccharyltransferase subunits OST48, DAD1 and KCP2 function as ubiquitous and selective modulators of mammalian N-glycosylation

@article{Roboti2012TheOS,
  title={The oligosaccharyltransferase subunits OST48, DAD1 and KCP2 function as ubiquitous and selective modulators of mammalian N-glycosylation},
  author={Peristera Roboti and S. High},
  journal={Journal of Cell Science},
  year={2012},
  volume={125},
  pages={3474 - 3484}
}
Summary Protein N-glycosylation is an essential modification that occurs in all eukaryotes and is catalysed by the oligosaccharyltransferase (OST) in the endoplasmic reticulum. Comparative studies have clearly shown that eukaryotic STT3 proteins alone can fulfil the enzymatic requirements for N-glycosylation, yet in many cases STT3 homologues form stable complexes with a variety of non-catalytic OST subunits. Whereas some of these additional components might play a structural role, others… Expand
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TLDR
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JCB_201702159 3625..3638
Asparagine-linked glycosylation is an essential protein modification reaction critical for the folding, trafficking, and function of many proteins that enter the secretory pathway. In mostExpand
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