Initial glycosylation of proteins with acetylgalactosaminylserine linkages.
about
Goblet cells and mucins: role in innate defense in enteric infectionsFunctional contributions of carbohydrate on AIDS virus glycoproteinUse of a mutant cell line to study the kinetics and function of O-linked glycosylation of low density lipoprotein receptorsSimian immunodeficiency virus from the sooty mangabey and rhesus macaque is modified with O-linked carbohydrate.Gp120 on HIV-1 Virions Lacks O-Linked Carbohydrate.Subcellular localization of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary glandMicroRNA-214 suppresses growth and invasiveness of cervical cancer cells by targeting UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 7.Cytochemical localization of terminal N-acetyl-D-galactosamine residues in cellular compartments of intestinal goblet cells: implications for the topology of O-glycosylationSite of addition of N-acetyl-galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59A computational and experimental study of O-glycosylation. Catalysis by human UDP-GalNAc polypeptide:GalNAc transferase-T2Processing, surface expression, and immunogenicity of carboxy-terminally truncated mutants of G protein of human respiratory syncytial virusDNA sequence of the gene for pseudorabies virus gp50, a glycoprotein without N-linked glycosylation.Post-translational glycosylation of coronavirus glycoprotein E1: inhibition by monensin.Amino acid distributions around O-linked glycosylation sites.Two enzymes involved in the synthesis of O-linked oligosaccharides are localized on membranes of different densities in mouse lymphoma BW5147 cells.Early O-glycosidic glycosylation of proglucagon in pancreatic islets: an unusual type of prohormonal modification.Temporal aspects of O-glycosylation of glycoprotein C from herpes simplex virus type-1.Quantitative aspects of mucus glycoprotein biosynthesis in rat gastric mucosa.Biosynthesis of GlyCAM-1, a mucin-like ligand for L-selectin.
P2860
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P2860
Initial glycosylation of proteins with acetylgalactosaminylserine linkages.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on June 1979
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Initial glycosylation of proteins with acetylgalactosaminylserine linkages.
@en
Initial glycosylation of proteins with acetylgalactosaminylserine linkages.
@nl
type
label
Initial glycosylation of proteins with acetylgalactosaminylserine linkages.
@en
Initial glycosylation of proteins with acetylgalactosaminylserine linkages.
@nl
prefLabel
Initial glycosylation of proteins with acetylgalactosaminylserine linkages.
@en
Initial glycosylation of proteins with acetylgalactosaminylserine linkages.
@nl
P2860
P356
P1476
Initial glycosylation of proteins with acetylgalactosaminylserine linkages.
@en
P2093
P2860
P304
P356
10.1073/PNAS.76.6.2694
P407
P577
1979-06-01T00:00:00Z