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- W2134884592 endingPage "1103" @default.
- W2134884592 startingPage "1091" @default.
- W2134884592 abstract "The synthesis of many of the proteins that are translocated into the endoplasmic reticulum is accompanied by the co-translational attachment of preformed oligosaccharide chains to certain Asn residues. These glycans can play a variety of roles in the mature proteins, including the one of stabilizing the protein and protecting the polypeptide backbone from the action of proteases. In addition, they can have a crucial function during the process of polypeptide folding, when aggregation with other proteins would hamper the acquisition of the native conformation. Their influence on protein folding can be direct, or mediated by interactions with endoplasmic reticulum-located molecular chaperones. The elucidation of the mechanisms that govern glycoprotein folding in the plant endoplasmic reticulum should contribute to the understanding of how much plant cells rely on glycan chains to achieve the efficient folding of many proteins under diverse environmental conditions. In addition, a better knowledge of the level of conservation of the in vivo folding mechanisms will be important for the exploitation of plant cells in the production of heterologous glycoproteins." @default.
- W2134884592 created "2016-06-24" @default.
- W2134884592 creator A5042666141 @default.
- W2134884592 creator A5050104338 @default.
- W2134884592 creator A5079390587 @default.
- W2134884592 date "1998-07-01" @default.
- W2134884592 modified "2023-10-06" @default.
- W2134884592 title "Effects of N-glycosylation on the folding and structure of plant proteins" @default.
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