Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae.
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Rooting the tree of life by transition analysesSolution Structure of Alg13: The Sugar Donor Subunit of a Yeast N-Acetylglucosamine TransferaseAlg14 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.Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol.Hetero-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.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.Demonstration of an oligosaccharide-diphosphodolichol diphosphatase activity whose subcellular localization is different than those of dolichyl-phosphate-dependent enzymes of the dolichol cycleA case of fatal Type I congenital disorders of glycosylation (CDG I) associated with low dehydrodolichol diphosphate synthase (DHDDS) activityThe multiple evolutionary origins of the eukaryotic N-glycosylation pathway.Alg14 organizes the formation of a multiglycosyltransferase complex involved in initiation of lipid-linked oligosaccharide biosynthesis.Suggestive evidence for Darwinian Selection against asparagine-linked glycans of Plasmodium falciparum and Toxoplasma gondii.Acceptor substrate selectivity and kinetic mechanism of Bacillus subtilis TagA.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.Novel exopolysaccharides produced by Lactococcus lactis subsp. lactis, and the diversity of epsE genes in the exopolysaccharide biosynthesis gene clusters.
P2860
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P248
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P2860
Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae.
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2005年の論文
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2005年論文
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2005年論文
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2005年論文
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2005年論文
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2005年論文
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name
Two proteins homologous to the ...... s in Saccharomyces cerevisiae.
@ast
Two proteins homologous to the ...... s in Saccharomyces cerevisiae.
@en
Two proteins homologous to the ...... s in Saccharomyces cerevisiae.
@nl
type
label
Two proteins homologous to the ...... s in Saccharomyces cerevisiae.
@ast
Two proteins homologous to the ...... s in Saccharomyces cerevisiae.
@en
Two proteins homologous to the ...... s in Saccharomyces cerevisiae.
@nl
prefLabel
Two proteins homologous to the ...... s in Saccharomyces cerevisiae.
@ast
Two proteins homologous to the ...... s in Saccharomyces cerevisiae.
@en
Two proteins homologous to the ...... s in Saccharomyces cerevisiae.
@nl
P2093
P3181
P356
P1476
Two proteins homologous to the ...... s in Saccharomyces cerevisiae.
@en
P2093
Alain Barbat
Isabelle Chantret
Julia Dancourt
Stuart E H Moore
P304
P3181
P356
10.1074/JBC.M413941200
P407
P577
2005-03-11T00:00:00Z