Protein NMR Studies of Substrate Binding to Human Blood Group A and B Glycosyltransferases
Author:
Affiliation:
1. Institute of Chemistry; University of Lübeck; Ratzeburger Allee 160 23562 Lübeck Germany
2. Department of Biochemistry and Microbiology; University of Victoria; P. O. Box 3800 STN CSC Victoria BC V8W 3P6 Canada
Publisher
Wiley
Subject
Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/cbic.201700025/fullpdf
Reference59 articles.
1. ABO(H) Blood Group A and B Glycosyltransferases Recognize Substrate via Specific Conformational Changes
2. The structural basis for specificity in human ABO(H) blood group biosynthesis
3. Glycosyltransferases: Structures, Functions, and Mechanisms
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1. Glycan structures and their interactions with proteins. A NMR view;Current Opinion in Structural Biology;2020-06
2. Fragment Growing to Design Optimized Inhibitors for Human Blood Group B Galactosyltransferase (GTB);ChemMedChem;2019-07-08
3. Insights into Allosteric Control of Human Blood Group A and B Glycosyltransferases from Dynamic NMR;ChemistryOpen;2019-06
4. Substrate Binding Drives Active-Site Closing of Human Blood Group B Galactosyltransferase as Revealed by Hot-Spot Labeling and NMR Spectroscopy Experiments;ChemBioChem;2018-04-14
5. Complete assignment of Ala, Ile, Leu, Met and Val methyl groups of human blood group A and B glycosyltransferases using lanthanide-induced pseudocontact shifts and methyl–methyl NOESY;Journal of Biomolecular NMR;2018-04
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