Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Miriam P. Kötzler"'
Autor:
Hong-Ming Chen, Lawrence P. McIntosh, Kyle Robinson, Stephen G. Withers, Mark Okon, Miriam P. Kötzler
Publikováno v:
Journal of the American Chemical Society. 140:8268-8276
Understanding the detailed mechanisms of enzyme-catalyzed hydrolysis of the glycosidic bond is fundamentally important, not only to the design of tailored cost-efficient, stable and specific catalysts but also to the development of specific glycosida
Publikováno v:
Protein Science. 26:1555-1563
Xylanases are important polysaccharide-cleaving catalysts for the pulp and paper, animal feeds and biofuels industries. They have also proved to be valuable model systems for understanding enzymatic catalysis, with one of the best studied being the G
Autor:
Stephen G. Withers, Miriam P. Kötzler
Publikováno v:
Journal of Biological Chemistry. 291:429-434
Proteolytic processing of human host cell factor 1 (HCF-1) to its mature form was recently shown, unexpectedly, to occur in a UDP-GlcNAc-dependent fashion within the transferase active site of O-GlcNAc-transferase (OGT) (Lazarus, M. B., Jiang, J., Ka
Autor:
Eric Samain, Rafi Chapanian, Miriam P. Kötzler, Jayachandran N. Kizhakkedathu, Stephen G. Withers, David H. Kwan, Alisdair B. Boraston, Iren Constantinescu, Melanie A. Higgins
Publikováno v:
Journal of the American Chemical Society. 137:5695-5705
Blood transfusions are critically important in many medical procedures, but the presence of antigens on red blood cells (RBCs, erythrocytes) means that careful blood-typing must be carried out prior to transfusion to avoid adverse and sometimes fatal
Publikováno v:
Protein science : a publication of the Protein Society. 26(8)
Xylanases are important polysaccharide‐cleaving catalysts for the pulp and paper, animal feeds and biofuels industries. They have also proved to be valuable model systems for understanding enzymatic catalysis, with one of the best studied being the
Autor:
Edzard Spillner, Simon Blank, Miriam P. Kötzler, Frank I. Bantleon, Martin Wienke, Bernd Meyer
Publikováno v:
ACS Chemical Biology. 8:1830-1840
α1,6-Core-fucosyltransferase (FUT8) is a vital enzyme in mammalian physiological and pathophysiological processes such as tumorigenesis and progress of, among others, non-small cell lung cancer and colon carcinoma. It was also shown that therapeutic
Autor:
Dirk Alpers, Henning N. Behnken, Bernd Meyer, Frank I. Bantleon, Edzard Spillner, Simon Blank, Miriam P. Kötzler
Publikováno v:
Insect Biochemistry and Molecular Biology. 42:116-125
Glycans of glycoproteins are often associated with IgE mediated allergic immune responses. Hymenoptera venoms, e.g., carry α1,3-fucosyl residues linked to the proximal GlcNAc of glycoproteins. This epitope, formed selectively by α1,3-fucosyltransfe
Autor:
Yi Jin, Jianbing Jiang, Miriam P. Kötzler, Hong-Ming Chen, David H. Kwan, Stephen G. Withers, Herman S. Overkleeft, Gideon J. Davies
Publikováno v:
FEBS letters, 590(4), 461-468
Covalent, mechanism-based inhibitors of glycosidases are valuable probe molecules for visualising enzyme activities in complex systems. We here describe the chemoenzymatic synthesis of 6-phospho-cyclophellitol and evaluate its behaviour as a mechanis
Publikováno v:
Glycobiology. 25(8)
A facile enzymatic synthesis of the methylumbelliferyl β-glycoside of the type 2 A blood group tetrasaccharide in good yields is reported. Using this compound, we developed highly sensitive fluorescence-based high-throughput assays for both endo-β-
Publikováno v:
eLS
Glycosidases catalyse the hydrolysis of glycosidic linkages, thereby degrading oligosaccharides and glycoconjugates, the structurally most diverse class of biopolymers. These efficient and highly specific catalysts play important roles in biological