PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22740701-5 2012 In the crystal structure of the complex of beta4Gal-T1 with I-antigen analog pentasaccharide, the beta1-6-branched GlcNAc moiety is bound to the sugar acceptor binding site of the beta4Gal-T1 molecule in a way similar to the crystal structures described previously; however, the extended linear tetrasaccharide moiety does not interact with the previously found extended sugar binding site on the beta4Gal-T1 molecule. pentasaccharide 77-92 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 98-105 4091823-7 1985 carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts. pentasaccharide 15-30 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 38-46 4091823-7 1985 carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts. pentasaccharide 15-30 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 69-77 15033940-3 2004 Using core-alpha1, 3-fucosyltransferase (EC 2.4.1.214) and beta1,2-xylosyltransferase (EC 2.4.2.38) recombinantly expressed in Pichia pastoris and suitable glycosidases, glycoforms containing either only fucose (MMF), only xylose (MMX), both (MMXF), or neither (MM) linked to the common pentasaccharide core were generated. pentasaccharide 287-302 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 59-66 22578491-3 2012 The use of a combination of a linear tetrasaccharide and a branched pentasaccharide as glycosyl donors led to the preparation of beta(1,3) linear octa- to hexadecasaccharides and branched nona- to heptadecasaccharides in good total yields. pentasaccharide 68-83 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 129-137 18558690-6 2008 The observation that 1-thio-linked mannosides are not well tolerated by the catalytic site of dGMII led to the synthesis of a pentasaccharide containing the alpha(1,6)-linked Man of the natural substrate and the beta(1,2)-linked GlcNAc moiety proposed to be accommodated by the extended binding site of the enzyme. pentasaccharide 126-141 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 212-220 17924631-4 2007 The combined methods are used in conjunction with more traditional NMR structural data to determine the solution structure of a pentasaccharide, GalNAc6S(beta1-4)GlcA(beta1-3)GalNAc4S(beta1-4)GlcA(beta1-3)GalNAc4S-ol, derived by enzymatic hydrolysis of chondroitin sulfate. pentasaccharide 128-143 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 154-161 17924631-4 2007 The combined methods are used in conjunction with more traditional NMR structural data to determine the solution structure of a pentasaccharide, GalNAc6S(beta1-4)GlcA(beta1-3)GalNAc4S(beta1-4)GlcA(beta1-3)GalNAc4S-ol, derived by enzymatic hydrolysis of chondroitin sulfate. pentasaccharide 128-143 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 167-174 17924631-4 2007 The combined methods are used in conjunction with more traditional NMR structural data to determine the solution structure of a pentasaccharide, GalNAc6S(beta1-4)GlcA(beta1-3)GalNAc4S(beta1-4)GlcA(beta1-3)GalNAc4S-ol, derived by enzymatic hydrolysis of chondroitin sulfate. pentasaccharide 128-143 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 184-191 17924631-4 2007 The combined methods are used in conjunction with more traditional NMR structural data to determine the solution structure of a pentasaccharide, GalNAc6S(beta1-4)GlcA(beta1-3)GalNAc4S(beta1-4)GlcA(beta1-3)GalNAc4S-ol, derived by enzymatic hydrolysis of chondroitin sulfate. pentasaccharide 128-143 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 197-204 7982953-7 1994 Addition of a xylose residue in beta 1-2 linkage to the core pentasaccharide improves the inhibitory activity. pentasaccharide 61-76 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 32-40