Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family-Reference-Cited by-同舟云学术

Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family

Published:2015-11-26 Issue:4 Volume:26 Page:360-376
ISSN:0959-6658
Container-title:Glycobiology
language:en
Short-container-title:Glycobiology

Author:

Revoredo Leslie,Wang Shengjun,Bennett Eric Paul,Clausen Henrik,Moremen Kelley W,Jarvis Donald L,Ten Hagen Kelly G,Tabak Lawrence A,Gerken Thomas A

Publisher

Oxford University Press (OUP)

Subject

Biochemistry

Link

http://academic.oup.com/glycob/article-pdf/26/4/360/17486001/cwv108.pdf

Reference61 articles.

1. NMR Characterization of Immunoglobulin G Fc Glycan Motion on Enzymatic Sialylation

2. A novel human UDP-N-acetyl-D-galactosamine:polypeptideN-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates

3. 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 Repeat

4. Control of mucin-type O-glycosylation: A classification of the polypeptide GalNAc-transferase gene family

5. UDP-N-Acetyl-d-Galactosamine: Polypeptide N-Acetylgalactosaminyltransferase-6 as a New Immunohistochemical Breast Cancer Marker

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