about
MPDU1 mutations underlie a novel human congenital disorder of glycosylation, designated type IfCongenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferaseNogo-B receptor is necessary for cellular dolichol biosynthesis and protein N-glycosylationIn vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylationIdentification and functional analysis of a defect in the human ALG9 gene: definition of congenital disorder of glycosylation type IL.A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised.Cell wall assembly in Saccharomyces cerevisiaeDeficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type IeDeficiency of Dol-P-Man synthase subunit DPM3 bridges the congenital disorders of glycosylation with the dystroglycanopathiesPhotocross-linking of nascent chains to the STT3 subunit of the oligosaccharyltransferase complexAcetamido sugar biosynthesis in the EuryarchaeaHuman RFT1 deficiency leads to a disorder of N-linked glycosylationDiatom-Specific Oligosaccharide and Polysaccharide Structures Help to Unravel Biosynthetic Capabilities in DiatomsN-linked sugar-regulated protein folding and quality control in the ERThe potential of sarcospan in adhesion complex replacement therapeutics for the treatment of muscular dystrophyCore Steps of Membrane-Bound Peptidoglycan Biosynthesis: Recent Advances, Insight and OpportunitiesInsights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural analysis of covalent reaction intermediatesStructure-guided identification of a new catalytic motif of oligosaccharyltransferaseSolution Structure of Alg13: The Sugar Donor Subunit of a Yeast N-Acetylglucosamine TransferaseCrystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylationStructure and mechanism of an active lipid-linked oligosaccharide flippaseStructure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysisFree-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p).The CWH8 gene encodes a dolichyl pyrophosphate phosphatase with a luminally oriented active site in the endoplasmic reticulum of Saccharomyces cerevisiae.Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases.Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation.Mammalian PIG-X and yeast Pbn1p are the essential components of glycosylphosphatidylinositol-mannosyltransferase I.Cell growth-dependent coordination of lipid signaling and glycosylation is mediated by interactions between Sac1p and Dpm1p.Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol.ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis.The oligosaccharyltransferase complex from Saccharomyces cerevisiae. Isolation of the OST6 gene, its synthetic interaction with OST3, and analysis of the native complex.Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulumThe activity of a putative polyisoprenol-linked sugar translocase (Wzx) involved in Escherichia coli O antigen assembly is independent of the chemical structure of the O repeatCommon origin and evolution of glycosyltransferases using Dol-P-monosaccharides as donor substrateArchaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modificationsTwo distinct but interchangeable mechanisms for flipping of lipid-linked oligosaccharidesPurification and characterization of the bacterial UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecAThe Fusarium oxysporum gnt2, encoding a putative N-acetylglucosamine transferase, is involved in cell wall architecture and virulenceIdentification and characterization of a cDNA encoding a dolichyl pyrophosphate phosphatase located in the endoplasmic reticulum of mammalian cellsThe ins(ide) and out(side) of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum
P2860
Q24291964-18A27CFD-B148-4EBC-864D-A0BF9E296866Q24296242-0C4E1B34-3188-4FBA-8B42-8A5A9953A023Q24302402-B4B44C95-F24F-4088-AA56-E48F381CAE79Q24530464-F938D191-AB56-4D08-ACC5-C76D12D76ECBQ24533520-7873EBC6-012D-4468-BBF3-2B4106538183Q24535941-B3FDEF5F-5180-4BC7-A2CA-7471D1E98FECQ24549234-00ECE634-4BB2-4862-9079-BB7F60AEE385Q24621090-CA21289D-D4A7-4FC0-9E31-F12E208CC6B8Q24651944-7C2D37C7-35B4-44F9-B867-827032915001Q24652203-D25638E0-77C7-473D-867D-D7F5533D05D3Q24655253-A928A64E-3628-49AC-9120-1883E5B364E5Q24655471-D7DEEE36-C9BA-4307-897A-EE617B78CB96Q26782262-02520B42-0E8D-4F7E-ABA1-1D6914B98506Q26827318-BA98EDA3-8C4B-4E6B-AE66-74982234B4EBQ26827638-EB6B2DF1-D220-43EC-B2C4-3D1ECC46239DQ27025371-464FC52E-4682-4AF2-9F26-86C3127002F7Q27641969-C69B3F87-5D27-4044-9670-1DFDBF6CD5FCQ27649167-3F4C32CC-6CFA-4614-A9B8-5B662BDB4033Q27650802-BAFD3233-1C8C-4FC4-AC37-5B6DCF97C94AQ27680366-E68BD05A-F22C-43B9-BC7F-C6A169353159Q27701786-C96D9DEC-325C-455F-8B43-D0C04A1B26B9Q27703283-C9CBDD34-CD29-42FA-8A1C-5E9EEC424B81Q27931323-2913206F-F8BF-4CFC-B16A-ACE3BAC9175FQ27931459-F8622AE5-EFEF-42C2-8FB2-526A1EAAC1DFQ27932071-7F3034A8-7293-4D40-8732-401F10A6CC98Q27932621-2E3BC136-6E0B-4A0D-99D2-44EC952F55AEQ27933583-7B5DB310-A981-46D2-971A-2B0AE917CB68Q27934953-0B2DA642-CABF-47E0-9BF9-DBD934E3AEB0Q27935145-F5F62C7B-FBFF-4901-A2D2-BCBB7A203A99Q27935927-3A3BBFBA-97D1-4703-A8AA-6FFFDD552756Q27937029-7E2C7E1A-6197-481A-A276-9B3D0FA997E9Q27939524-E49FAC09-75ED-40E3-965C-57B8B5D448A6Q28138737-766EC82F-920B-4ECA-8F7D-04911D6238D5Q28219347-EADB56B9-7ADB-44D3-BC9D-FD9E34428960Q28264353-C6B9619F-BF39-4137-810D-389E2D5C3E52Q28484954-2F160628-C41B-4FA2-AC27-8B9B0A13DE09Q28485419-82240D6C-856F-4543-A79A-14840089255DQ28538545-A86060B3-E182-43B7-A4ED-BB661FD1D319Q28588980-DEDCCEFA-7230-456F-AF14-550AEA17D3B2Q28610119-A4B0C0CD-0546-4B2D-A47D-F603FE2FC0CD
P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The dolichol pathway of N-linked glycosylation.
@ast
The dolichol pathway of N-linked glycosylation.
@en
The dolichol pathway of N-linked glycosylation.
@nl
type
label
The dolichol pathway of N-linked glycosylation.
@ast
The dolichol pathway of N-linked glycosylation.
@en
The dolichol pathway of N-linked glycosylation.
@nl
prefLabel
The dolichol pathway of N-linked glycosylation.
@ast
The dolichol pathway of N-linked glycosylation.
@en
The dolichol pathway of N-linked glycosylation.
@nl
P1476
The dolichol pathway of N-linked glycosylation.
@en
P304
P356
10.1016/S0304-4165(98)00127-5
P407
P577
1999-01-01T00:00:00Z