Results 141 to 150 of about 25,344,123 (207)
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Substrate Preference and Interplay of Fucosyltransferase 8 and N-Acetylglucosaminyltransferases

Journal of the American Chemical Society, 2017
Tsui-Ling Hsu   +2 more
exaly   +2 more sources

Systematic Synthesis of Bisubstrate-Type Inhibitors ofN-Acetylglucosaminyltransferases

Chemistry - A European Journal, 2006
Naoyuki Taniguchi   +2 more
exaly   +2 more sources

Synthesis of a Bisubstrate-Type Inhibitor ofN-Acetylglucosaminyltransferases

Angewandte Chemie - International Edition, 2004
Naoyuki Taniguchi   +2 more
exaly   +2 more sources

N-Acetylglucosaminyltransferase-IV

2002
Complex-type Asn-linked oligosaccharides do not always have the same number of branches, although there are normally from two to five. Each branch is formed by a specific N-acetylglucosaminyltransferase (GnT). N-Acetylglucosaminyltransferase-IV (GnT-IV) is essential in producing multiantennary sugar chains cooperatively with GnT-V.
Mari T. Minowa   +3 more
openaire   +1 more source

N-acetylglucosaminyltransferase from ascaris suum

International Journal for Parasitology, 1991
The occurrence of N-acetylglucosaminyltransferase, the initial step in the synthesis of the carbohydrate moiety of N-linked glycoproteins, is demonstrated in the microsomal fraction of the nematode Ascaris suum. Phosphatidylglycerol stimulated enzyme activity three- to six-fold without affecting the Km values of either substrates, uridinediphospho-N ...
Z, Kyossev   +3 more
openaire   +2 more sources

N-Acetylglucosaminyltransferase-VI

2002
The biological roles of asparagine-linked oligosaccharides (N-glycans) on glycoproteins are thought to take place through the interaction of terminal glycan structures and their receptors. The diversity and avidity of the terminal structures, however, are regulated by the core structure of N-glycans (Schachter 1991).
Koichi Honke, Naoyuki Taniguchi
openaire   +1 more source

N-Acetylglucosaminyltransferase-III

2002
N-Acetylglucosaminyltransferase-III (β-1,4-mannosyl-glycoprotein β1,4-N-acetylglu- cosaminyltransferase: EC 2.4.1.144) catalyzes the formation of a unique structure, bisecting GlcNAc, and is involved in the biosynthesis of complex and hybrid types of N-glycans.
Yoshitaka Ikeda, Naoyuki Taniguchi
openaire   +1 more source

N-Acetylglucosaminyltransferase-I

2002
Structural analyses of sugars on secreted glycoproteins performed about 30 years ago revealed bi-, tri-, and tetraantennary N-glycans in which GlcNAc residues linked to a conserved trimannosyl core initiated each antenna. These same structures were lectin binding sites on red cell glycoproteins (Kornfeld and Kornfeld 1970), prompting the search for the
openaire   +1 more source

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