Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway.
about
A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-IcA novel carbohydrate-deficient glycoprotein syndrome characterized by a deficiency in glucosylation of the dolichol-linked oligosaccharideSTT3, a highly conserved protein required for yeast oligosaccharyl transferase activity in vivoThe essential OST2 gene encodes the 16-kD subunit of the yeast oligosaccharyltransferase, a highly conserved protein expressed in diverse eukaryotic organismsPkh1 and Pkh2 differentially phosphorylate and activate Ypk1 and Ykr2 and define protein kinase modules required for maintenance of cell wall integrity.Saccharomyces cerevisiae sec59 cells are deficient in dolichol kinase activityFunctional characterization of Ost3p. Loss of the 34-kD subunit of the Saccharomyces cerevisiae oligosaccharyltransferase results in biased underglycosylation of acceptor substrates.New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus.Suppression of Rft1 expression does not impair the transbilayer movement of Man5GlcNAc2-P-P-dolichol in sealed microsomes from yeast.Stepwise assembly of the lipid-linked oligosaccharide in the endoplasmic reticulum of Saccharomyces cerevisiae: identification of the ALG9 gene encoding a putative mannosyl transferaseA specific screen for oligosaccharyltransferase mutations identifies the 9 kDa OST5 protein required for optimal activity in vivo and in vitroAnalysis and metabolic engineering of lipid-linked oligosaccharides in glycosylation-deficient CHO cellsYeast glycosylation mutants are sensitive to aminoglycosides.Protein glycosylation in yeast: transcript heterogeneity of the ALG7 gene.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.A mutation that prevents glucosylation of the lipid-linked oligosaccharide precursor leads to underglycosylation of secreted yeast invertaseProcessing pathway for protease B of Saccharomyces cerevisiae.Retention of glucose units added by the UDP-GLC:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum.A cell-based reglucosylation assay demonstrates the role of GT1 in the quality control of a maturing glycoproteinUridine diphosphate-glucose transport into the endoplasmic reticulum of Saccharomyces cerevisiae: in vivo and in vitro evidence.The role of glucosidase I (Cwh41p) in the biosynthesis of cell wall beta-1,6-glucan is indirectIsolation of glucose-containing high-mannose glycoprotein core oligosaccharides.Evidence that the synthesis of glucosylphosphodolichol in yeast involves a 35-kDa membrane protein.A Saccharomyces cerevisiae mutant unable to convert glucose to glucose-6-phosphate accumulates excessive glucose in the endoplasmic reticulum due to core oligosaccharide trimming.CDG Therapies: From Bench to Bedside.Identification of the gene encoding the alpha1,3-mannosyltransferase (ALG3) in Arabidopsis and characterization of downstream n-glycan processing.
P2860
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P2860
Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway.
description
1984 nî lūn-bûn
@nan
1984 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1984 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1984年の論文
@ja
1984年論文
@yue
1984年論文
@zh-hant
1984年論文
@zh-hk
1984年論文
@zh-mo
1984年論文
@zh-tw
1984年论文
@wuu
name
Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway.
@ast
Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway.
@en
Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway.
@nl
type
label
Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway.
@ast
Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway.
@en
Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway.
@nl
prefLabel
Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway.
@ast
Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway.
@en
Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway.
@nl
P2093
P1476
Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway.
@en
P2093
P304
P407
P577
1984-01-01T00:00:00Z