Characterization of a UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase That Displays Glycopeptide N-Acetylgalactosaminyltransferase Activity
Open Access
- 1 September 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (39) , 27867-27874
- https://doi.org/10.1074/jbc.274.39.27867
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Dipeptidyl aminotransferase activity and in vitroO-glycosylation of MUCSAC mucin motif peptides by human gastric microsomal preparationsChemical Biology & Drug Design, 2009
- Cloning of a Human UDP-N-Acetyl-α-d-Galactosamine:PolypeptideN-Acetylgalactosaminyltransferase That Complements Other GalNAc-Transferases in Complete O-Glycosylation of the MUC1 Tandem RepeatJournal of Biological Chemistry, 1998
- Cloning and Expression of a Novel, Tissue Specifically Expressed Member of the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase FamilyJournal of Biological Chemistry, 1998
- cDNA Cloning and Expression of a Family of UDP-N-acetyl-dgalactosamine:PolypeptideN-Acetylgalactosaminyltransferase Sequence Homologs fromCaenorhabditis elegansJournal of Biological Chemistry, 1998
- Determination of the Site-specific O-Glycosylation Pattern of the Porcine Submaxillary Mucin Tandem Repeat GlycopeptideJournal of Biological Chemistry, 1997
- Human Mucin Gene MUC5B, the 10.7-kb Large Central Exon Encodes Various Alternate Subdomains Resulting in a Super-repeatJournal of Biological Chemistry, 1997
- Cloning and Expression of Mouse UDP-GalNAc:PolypeptideN-Acetylgalactosaminyltransferase-T3Biochemical and Biophysical Research Communications, 1996
- cDNA Cloning and Expression of a Novel Human UDP- -acetyl-α-D-galactosamineJournal of Biological Chemistry, 1996
- UDP-N-acetyl-α-D-galactosamine:polypeptide N-AcetylgalactosaminyltransferasePublished by Elsevier ,1995
- Why are proteins O-glycosylated?Trends in Biochemical Sciences, 1990