T
Tilo Schwientek
Researcher at University of Cologne
Publications - 38
Citations - 2606
Tilo Schwientek is an academic researcher from University of Cologne. The author has contributed to research in topics: Glycosylation & Gene. The author has an hindex of 22, co-authored 38 publications receiving 2497 citations. Previous affiliations of Tilo Schwientek include University of Copenhagen & Umeå University.
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Journal ArticleDOI
Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions.
TL;DR: Emerging evidence indicates that formation of many glycosidic linkages is covered by large homologous glycosyltransferase gene families, and that the existence of multiple enzyme isoforms provides a degree of redundancy as well as a higher level of regulation of the glycoforms synthesized.
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Chemoenzymatically synthesized multimeric Tn/STn MUC1 glycopeptides elicit cancer-specific anti-MUC1 antibody responses and override tolerance.
Anne Louise Sørensen,Celso A. Reis,Celso A. Reis,Mads Agervig Tarp,Ulla Mandel,Kavitha Ramachandran,Vasanthi Sankaranarayanan,Tilo Schwientek,Ros Graham,Joyce Taylor-Papadimitriou,Michael A. Hollingsworth,Joy Burchell,Henrik Clausen +12 more
TL;DR: Chemoenzymatic synthesis of extended MUC1 TR glycopeptides with cancer-associated O-glycosylation using a panel of recombinant human glycosyltransferases is developed and a MAb with similar specificity as the elicited immune response was generated and shown to have the same remarkable cancer specificity.
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Cloning and Expression of a Proteoglycan UDP-Galactose:β-Xylose β1,4-Galactosyltransferase I A SEVENTH MEMBER OF THE HUMAN β4-GALACTOSYLTRANSFERASE GENE FAMILY
Raquel Almeida,Steven B. Levery,Ulla Mandel,Hans Kresse,Tilo Schwientek,Eric P. Bennett,Henrik Clausen +6 more
TL;DR: Molecular cloning of β4Gal-T7 should facilitate general studies of its pathogenic role in progeroid syndromes and connective tissue disorders with affected proteoglycan biosynthesis.
Journal ArticleDOI
The relative activities of the C2GnT1 and ST3Gal-I glycosyltransferases determine O-glycan structure and expression of a tumor-associated epitope on MUC1.
Martin Dalziel,Caroline A. Whitehouse,Ian McFarlane,Inka Brockhausen,Stephen Gschmeissner,Tilo Schwientek,Henrik Clausen,Joy Burchell,Joyce Taylor-Papadimitriou +8 more
TL;DR: Even when C2GnT1 is expressed, the O-glycans added to MUC1 become core 1-dominated structures, provided expression of ST3Gal-I is increased as it is in breast cancer, which indicates a switch to core 2 structures.
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Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine : polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals - One subfamily composed of l(2)35Aa is essential in Drosophila
Tilo Schwientek,Eric P. Bennett,Carlos Flores,John Thacker,Martin Hollmann,Celso A. Reis,Jane Behrens,Ulla Mandel,Birgit Keck,Mireille A. Schäfer,Kim F. Haselmann,Roman A. Zubarev,Peter Roepstorff,Joy Burchell,Joyce Taylor-Papadimitriou,Michael A. Hollingsworth,Henrik Clausen +16 more
TL;DR: The finding that subfamilies of GalNAc-transferases with distinct catalytic functions are evolutionarily conserved stresses that GalNAC-transferase isoforms may serve unique biological functions rather than providing functional redundancy, and this is further supported by the lethal phenotype of l(2)35Aa.