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- W2903198249 endingPage "169" @default.
- W2903198249 startingPage "149" @default.
- W2903198249 abstract "N-linked oligosaccharides attached to proteins act as tags for glycoprotein quality control, ensuring their appropriate foldingFolding and trafficking in cells. Interactions with a variety of intracellular lectinsLectin lectins determine glycoprotein fates. Monoglucosylated glycoforms are the hallmarks of incompletely folded glycoproteins in the protein quality-control system, in which glucosidase II and UDP-glucose/glycoprotein glucosyltransferase are, respectively, responsible for glucose trimming and attachment. In this review, we summarize a recently emerging view of the structural basis of the functional mechanisms of these key enzymes as well as substrate N-linked oligosaccharides exhibiting flexible structures, as revealed by applying a series of biophysical techniques including small-angle X-ray scattering, X-ray crystallography, high-speed atomic force microscopyAtomic force microscopy (AFM) atomic force microscopy , electron microscopyElectron microscopy (EM) electron microscopy , and computational simulation in conjunction with NMR spectroscopy." @default.
- W2903198249 created "2018-12-11" @default.
- W2903198249 creator A5047494990 @default.
- W2903198249 creator A5052214706 @default.
- W2903198249 date "2018-01-01" @default.
- W2903198249 modified "2023-09-25" @default.
- W2903198249 title "Structural Aspects of ER Glycoprotein Quality-Control System Mediated by Glucose Tagging" @default.
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