Glucosaminylglycan biosynthesis: what we can learn from the X-ray crystal structures of glycosyltransferases GlcAT1 and EXTL2.
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T. Darden | L. Pedersen | L. Pedersen | M. Negishi | Jian Dong | J. Dong
[1] S. Walker,et al. Remarkable structural similarities between diverse glycosyltransferases. , 2002, Chemistry & biology.
[2] G. J. Swaminathan,et al. Structural Basis of Ordered Binding of Donor and Acceptor Substrates to the Retaining Glycosyltransferase, α-1,3-Galactosyltransferase* , 2002, The Journal of Biological Chemistry.
[3] J. Magdalou,et al. The Donor Substrate Specificity of the Human β1,3-Glucuronosyltransferase I toward UDP-Glucuronic Acid Is Determined by Two Crucial Histidine and Arginine Residues* , 2002, The Journal of Biological Chemistry.
[4] T. Darden,et al. Crystal Structure of β1,3-Glucuronyltransferase I in Complex with Active Donor Substrate UDP-GlcUA* , 2002, The Journal of Biological Chemistry.
[5] B. Ramakrishnan,et al. Structure-based design of beta 1,4-galactosyltransferase I (beta 4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: point mutation broadens beta 4Gal-T1 donor specificity. , 2002, The Journal of biological chemistry.
[6] S. Selleck,et al. Order out of chaos: assembly of ligand binding sites in heparan sulfate. , 2002, Annual review of biochemistry.
[7] G. J. Swaminathan,et al. Structure of UDP Complex of UDP-galactose:β-Galactoside-α-1,3-galactosyltransferase at 1.53-Å Resolution Reveals a Conformational Change in the Catalytically Important C Terminus* , 2001, The Journal of Biological Chemistry.
[8] G J Davies,et al. Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: a comparison with related NDP-sugar glycosyltransferases. , 2001, Journal of molecular biology.
[9] H. Kitagawa,et al. Molecular Cloning and Expression of a Human Chondroitin Synthase* , 2001, The Journal of Biological Chemistry.
[10] B Henrissat,et al. Glycoside hydrolases and glycosyltransferases: families and functional modules. , 2001, Current opinion in structural biology.
[11] C. Breton,et al. Structural and functional features of glycosyltransferases. , 2001, Biochimie.
[12] O Hindsgaul,et al. Bovine α1,3‐galactosyltransferase catalytic domain structure and its relationship with ABO histo‐blood group and glycosphingolipid glycosyltransferases , 2001, The EMBO journal.
[13] G. Davies. Sweet secrets of synthesis , 2001, Nature Structural Biology.
[14] Stephen G. Withers,et al. Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs , 2001, Nature Structural Biology.
[15] T. Darden,et al. Heparan/Chondroitin Sulfate Biosynthesis , 2000, The Journal of Biological Chemistry.
[16] H. Kitagawa,et al. Recent advances in the study of the biosynthesis and functions of sulfated glycosaminoglycans. , 2000, Current opinion in structural biology.
[17] J. Rini,et al. Glycosyltransferase structure and mechanism. , 2000, Current opinion in structural biology.
[18] O Habuchi,et al. Diversity and functions of glycosaminoglycan sulfotransferases. , 2000, Biochimica et biophysica acta.
[19] Christian Cambillau,et al. Crystal structures of the bovine β4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose , 1999, The EMBO journal.
[20] H. Kitagawa,et al. The Tumor Suppressor EXT-like Gene EXTL2 Encodes an α1, 4-N-Acetylhexosaminyltransferase That TransfersN-Acetylgalactosamine and N-Acetylglucosamine to the Common Glycosaminoglycan-Protein Linkage Region , 1999, The Journal of Biological Chemistry.
[21] C. McCormick,et al. The Putative Tumor Suppressors EXT1 and EXT2 Are Glycosyltransferases Required for the Biosynthesis of Heparan Sulfate* , 1998, The Journal of Biological Chemistry.
[22] L. Kjellén,et al. Regulated Diversity of Heparan Sulfate* , 1998, The Journal of Biological Chemistry.
[23] M. Palcic,et al. Sequential Interchange of Four Amino Acids from Blood Group B to Blood Group A Glycosyltransferase Boosts Catalytic Activity and Progressively Modifies Substrate Recognition in Human Recombinant Enzymes* , 1997, The Journal of Biological Chemistry.