Kinetic basis for the donor nucleotide-sugar specificity of beta1, 4-N-acetylglucosaminyltransferase III.

Kinetic basis for the donor nucleotide-sugar specificity of beta1, 4-N-acetylglucosaminyltransferase III.

Item
http://www.wikidata.org/entity/Q33919694
Pompe disease results in a Golgi-based glycosylation deficit in human induced pluripotent stem cell-derived cardiomyocytes.Enzymatic glycosylation of multivalent scaffolds.The action of N-acetylglucosaminyltransferase-V is prevented by the bisecting GlcNAc residue at the catalytic step.Reaction mechanism and substrate specificity for nucleotide sugar of mammalian alpha1,6-fucosyltransferase--a large-scale preparation and characterization of recombinant human FUT8.UDP-GlcNAc concentration is an important factor in the biosynthesis of beta1,6-branched oligosaccharides: regulation based on the kinetic properties of N-acetylglucosaminyltransferase V.Down-regulation of the alpha-Gal epitope expression in N-glycans of swine endothelial cells by transfection with the N-acetylglucosaminyltransferase III gene. Modulation of the biosynthesis of terminal structures by a bisecting GlcNAc.A catalytically inactive beta 1,4-N-acetylglucosaminyltransferase III (GnT-III) behaves as a dominant negative GnT-III inhibitor.UDP-4-Keto-6-Deoxyglucose, a Transient Antifungal Metabolite, Weakens the Fungal Cell Wall Partly by Inhibition of UDP-Galactopyranose Mutase.Dynamic control of oligosaccharide modification in the mammary gland: linking recombinant human erythropoietin functional analysis of transgenic mouse milk-derived hEPO.Kinetic properties and substrate specificities of two recombinant human N-acetylglucosaminyltransferase-IV isozymes.Two N-terminally truncated variants of human β-galactoside α2,6 sialyltransferase I with distinct properties for in vitro protein glycosylation.
P2860

Kinetic basis for the donor nucleotide-sugar specificity of beta1, 4-N-acetylglucosaminyltransferase III.

Item
http://www.wikidata.org/entity/Q33919694
description
2000 nî lūn-bûn
@nan
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Kinetic basis for the donor nu ...... ylglucosaminyltransferase III.
@ast
Kinetic basis for the donor nu ...... ylglucosaminyltransferase III.
@en
type
label
Kinetic basis for the donor nu ...... ylglucosaminyltransferase III.
@ast
Kinetic basis for the donor nu ...... ylglucosaminyltransferase III.
@en
prefLabel
Kinetic basis for the donor nu ...... ylglucosaminyltransferase III.
@ast
Kinetic basis for the donor nu ...... ylglucosaminyltransferase III.
@en
P1433
P1476
P2093
P304
P31
P356
P433
P478
P577
P698
P356
P1433
P1476
Kinetic basis for the donor nu ...... ylglucosaminyltransferase III.
@en
P2093
P304
P31
P356
10.1093/OXFORDJOURNALS.JBCHEM.A022793
P433
P478
P577
P698