A UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase is essential for viability in Drosophila melanogaster.
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Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2Mucin-type O-glycosylation during developmentControl of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene familyMultiple members of the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase family are essential for viability in DrosophilaGlycobiology on the fly: developmental and mechanistic insights from DrosophilaInitiation of protein O glycosylation by the polypeptide GalNAcT-1 in vascular biology and humoral immunity.Conservation of peptide acceptor preferences between Drosophila and mammalian polypeptide-GalNAc transferase ortholog pairs.Functional characterization and expression analysis of members of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family from Drosophila melanogaster.Characterization of a UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase with an unusual lectin domain from the platyhelminth parasite Echinococcus granulosusIdentification of common and unique peptide substrate preferences for the UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases T1 and T2 derived from oriented random peptide substrates.The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation.Low density lipoprotein receptor class A repeats are O-glycosylated in linker regionsAn O-glycosyltransferase promotes cell adhesion during development by influencing secretion of an extracellular matrix integrin ligand.The role of mucin-type O-glycans in eukaryotic developmentLarge molecule bioanalysis using Q-TOF without predigestion and its data processing challenges.Two protein N-acetylgalactosaminyl transferases regulate synaptic plasticity by activity-dependent regulation of integrin signalingDissecting the biological role of mucin-type O-glycosylation using RNA interference in Drosophila cell culture.Emerging paradigms for the initiation of mucin-type protein O-glycosylation by the polypeptide GalNAc transferase family of glycosyltransferases.Expression and characterization of the first snail-derived UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase.Glycosylation of α-dystroglycan: O-mannosylation influences the subsequent addition of GalNAc by UDP-GalNAc polypeptide N-acetylgalactosaminyltransferases.The cellular microenvironment and cell adhesion: a role for O-glycosylation.O-glycosylation modulates integrin and FGF signalling by influencing the secretion of basement membrane components.Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family.The diversity of O-linked glycans expressed during Drosophila melanogaster development reflects stage- and tissue-specific requirements for cell signalingA mucin-type O-glycosyltransferase modulates cell adhesion during Drosophila developmentRecent insights into the biological roles of mucin-type O-glycosylationThe beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1.Simple sugars to complex disease--mucin-type O-glycans in cancer.Mucin-Type O-Glycosylation in Invertebrates.Biological roles of glycans.Biological and biochemical properties of two Xenopus laevis N-acetylgalactosaminyltransferases with contrasting roles in embryogenesis.An inhibitor of O-glycosylation induces apoptosis in NIH3T3 cells and developing mouse embryonic mandibular tissues.Requirement for a core 1 galactosyltransferase in the Drosophila nervous system.Mucin core O-glycosylation is modulated by neighboring residue glycosylation status. Kinetic modeling of the site-specific glycosylation of the apo-porcine submaxillary mucin tandem repeat by UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferasesProteoglycan UDP-galactose:beta-xylose beta 1,4-galactosyltransferase I is essential for viability in Drosophila melanogaster.A UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase is required for epithelial tube formation.Site-specific O-glycosylation of members of the low-density lipoprotein receptor superfamily enhances ligand interactions.Rescue of Drosophila Melanogaster l(2)35Aa lethality is only mediated by polypeptide GalNAc-transferase pgant35A, but not by the evolutionary conserved human ortholog GalNAc-transferase-T11.A molecular switch orchestrates enzyme specificity and secretory granule morphology
P2860
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P2860
A UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase is essential for viability in Drosophila melanogaster.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
A UDP-GalNAc:polypeptide N-ace ...... ty in Drosophila melanogaster.
@en
A UDP-GalNAc:polypeptide N-ace ...... ty in Drosophila melanogaster.
@nl
type
label
A UDP-GalNAc:polypeptide N-ace ...... ty in Drosophila melanogaster.
@en
A UDP-GalNAc:polypeptide N-ace ...... ty in Drosophila melanogaster.
@nl
prefLabel
A UDP-GalNAc:polypeptide N-ace ...... ty in Drosophila melanogaster.
@en
A UDP-GalNAc:polypeptide N-ace ...... ty in Drosophila melanogaster.
@nl
P2860
P356
P1476
A UDP-GalNAc:polypeptide N-ace ...... ty in Drosophila melanogaster.
@en
P2093
Duy T Tran
Kelly G Ten Hagen
P2860
P304
22616-22622
P356
10.1074/JBC.M201807200
P407
P577
2002-03-29T00:00:00Z