• Publications
  • Influence
Precision mapping of the human O‐GalNAc glycoproteome through SimpleCell technology
A genetic engineering approach using human cell lines to simplify O‐glycosylation (SimpleCells) that enables proteome‐wide discovery of O-glycan sites using ‘bottom‐up’ ETD‐based mass spectrometric analysis and an improved NetOGlyc4.0 model for prediction of O‐ Glycoproteins. Expand
Glycosyltransferase activity of Fringe modulates Notch–Delta interactions
Evidence is presented that Fringe acts in the Golgi as a glycosyltransferase enzyme that modifies the epidermal growth factor modules of Notch and alters the ability of notch to bind its ligand Delta, and it is suggested that cell-type-specific modification of Glycosylation may provide a general mechanism to regulate ligand–receptor interactions in vivo. Expand
Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family.
An overview of the GalNAc-T gene family in animals is presented and a classification of the genes into subfamilies, which appear to be conserved in evolution structurally as well as functionally are proposed. Expand
Molecular genetic basis of the histo-blood group ABO system
A critical single-base deletion was found in the 0 gene, which results in an entirely different, inactive protein incapable of modifying the H antigen, and this work presents a molecular basis for the ABO genotypes. Expand
Polypeptide GalNAc-transferase T3 and Familial Tumoral Calcinosis
It is demonstrated that the secretion of the phosphaturic factor fibroblast growth factor 23 (FGF23) requires O-glycosylation, and that GalNAc-T3 selectively directs O- GlyCosylation in a subtilisin-like proprotein convertase recognition sequence motif, which blocks processing of FGF23. Expand
Pathogenesis of shigella diarrhea. XI. Isolation of a shigella toxin- binding glycolipid from rabbit jejunum and HeLa cells and its identification as globotriaosylceramide
These studies show an identical carbohydrate- specific glycolipid receptor for shigella toxin in gut and in HeLa cells and the possibility that the pilus and toxin B subunit contain homologous sequences. Expand
Intestinal metaplasia of human stomach displays distinct patterns of mucin (MUC1, MUC2, MUC5AC, and MUC6) expression.
The mucin expression profile in the different types of intestinalMetaplasia allows the identification of two patterns: one defined by decreased levels of expression of "gastric" mucins and expression of MUC2 intestinal mucin, which corresponds to type I intestinal metaplasia, and the other defined by coexpression of "Gastric mucins" (MUC1, MUC5AC, and MUC6). Expand
Mining the O-glycoproteome using zinc-finger nuclease–glycoengineered SimpleCell lines
Zinc-finger nuclease gene targeting is applied to truncate the O-glycan elongation pathway in human cells, generating stable 'SimpleCell' lines with homogenous O- glycosylation and should facilitate analyses of important functions of protein gly cosylation. Expand
Control of O-Glycan Branch Formation
  • Tilo Schwientek, Mitsuharu Nomoto, +5 authors H. Clausen
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 19 February 1999
The results confirm the predicted existence of a β1,6GlcNAc-transferase that functions in both core 2 and core 4O-glycan branch formation and are important for understanding the mechanisms leading to specific changes in core 2 branching during cell development and malignant transformation. Expand
Immunohistochemical Study of the Expression of MUC6 Mucin and Co-expression of Other Secreted Mucins (MUC5AC and MUC2) in Human Gastric Carcinomas
It is observed that MUC6 is a good marker of mucopeptic cell differentiation and is expressed in 30% of gastric carcinomas, independent of the clinicopathological features of the cases, and it is found that co-expression and co-localization of mucins in gastrics carcinomas is independent of histomorphology and staging. Expand