Suppression of Rft1 Expression Does Not Impair the Transbilayer Movement of Man5GlcNAc2-P-P-Dolichol in Sealed Microsomes from Yeast
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference40 articles.
1. Transmembrane organization of protein glycosylation. Mature oligosaccharide-lipid is located on the luminal side of microsomes from Chinese hamster ovary cells.
2. Glycoprotein biosynthesis in yeast
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4. Roles of N-Linked Glycans in the Endoplasmic Reticulum
5. The Unfolded Protein Response Regulates Multiple Aspects of Secretory and Membrane Protein Biogenesis and Endoplasmic Reticulum Quality Control
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1. Molecular characterization of Rft1, an ER membrane protein associated with congenital disorder of glycosylation RFT1-CDG;Journal of Biological Chemistry;2024-08
2. Rft1 catalyzes lipid-linked oligosaccharide translocation across the ER membrane;Nature Communications;2024-06-17
3. Molecular characterization of Rft1, an ER membrane protein associated with congenital disorder of glycosylation RFT1-CDG;2024-04-03
4. Structural and mechanistic studies of the N-glycosylation machinery: from lipid-linked oligosaccharide biosynthesis to glycan transfer;Glycobiology;2023-07-03
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