Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol.
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Deficiency of Dol-P-Man synthase subunit DPM3 bridges the congenital disorders of glycosylation with the dystroglycanopathiesSaccharomyces cerevisiae CWH43 is involved in the remodeling of the lipid moiety of GPI anchors to ceramidesHetero-oligomeric interactions between early glycosyltransferases of the dolichol cycle.Membrane topology of the Alg14 endoplasmic reticulum UDP-GlcNAc transferase subunit.An evolving view of the eukaryotic oligosaccharyltransferase.Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional alpha1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis.The expanding horizons of asparagine-linked glycosylation.Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems.Architecture and biosynthesis of the Saccharomyces cerevisiae cell wall.Alg13p, the catalytic subunit of the endoplasmic reticulum UDP-GlcNAc glycosyltransferase, is a target for proteasomal degradation.AglC and AglK are involved in biosynthesis and attachment of diacetylated glucuronic acid to the N-glycan in Methanococcus voltaeN-linked protein glycosylation in the endoplasmic reticulum.Alg14 organizes the formation of a multiglycosyltransferase complex involved in initiation of lipid-linked oligosaccharide biosynthesis.Biochemical characterization, membrane association and identification of amino acids essential for the function of Alg11 from Saccharomyces cerevisiae, an alpha1,2-mannosyltransferase catalysing two sequential glycosylation steps in the formation ofGeneration and degradation of free asparagine-linked glycans.Glycosyltransferase mechanisms: impact of a 5-fluoro substituent in acceptor and donor substrates on catalysis.Interaction between the C termini of Alg13 and Alg14 mediates formation of the active UDP-N-acetylglucosamine transferase complex.Asparagine-Linked Glycans of Cryptosporidium parvum Contain a Single Long Arm, Are Barely Processed in the Endoplasmic Reticulum (ER) or Golgi, and Show a Strong Bias for Sites with Threonine.
P2860
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P248
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P2860
Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol.
description
2005 nî lūn-bûn
@nan
2005 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Biosynthesis of lipid-linked o ...... tion of GlcNAc(2)-PP-dolichol.
@ast
Biosynthesis of lipid-linked o ...... tion of GlcNAc(2)-PP-dolichol.
@en
Biosynthesis of lipid-linked o ...... tion of GlcNAc(2)-PP-dolichol.
@nl
type
label
Biosynthesis of lipid-linked o ...... tion of GlcNAc(2)-PP-dolichol.
@ast
Biosynthesis of lipid-linked o ...... tion of GlcNAc(2)-PP-dolichol.
@en
Biosynthesis of lipid-linked o ...... tion of GlcNAc(2)-PP-dolichol.
@nl
prefLabel
Biosynthesis of lipid-linked o ...... tion of GlcNAc(2)-PP-dolichol.
@ast
Biosynthesis of lipid-linked o ...... tion of GlcNAc(2)-PP-dolichol.
@en
Biosynthesis of lipid-linked o ...... tion of GlcNAc(2)-PP-dolichol.
@nl
P2093
P2860
P356
P1476
Biosynthesis of lipid-linked o ...... tion of GlcNAc(2)-PP-dolichol.
@en
P2093
Claude A Jakob
Ludwig Lehle
Markus Schwarz
Tanja Bickel
P2860
P304
P356
10.1074/JBC.M506358200
P407
P50
P577
2005-10-14T00:00:00Z