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Understanding O-GlcNAc transferase (OGT): Every amino acid matters. [PDF]

J Biol Chem
Xu N, Zhao Y, Chi W, Yuan Y, Li J.
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N-Acetylglucosaminyltransferase Ⅲ Antagonizes the Effect of N-Acetylglucosaminyltransferase Ⅴ on α3β1 Integrin-mediated Cell Migration

N-Acetylglucosaminyltransferase Ⅲ Antagonizes the Effect of N-Acetylglucosaminyltransferase Ⅴ on α3β1 Integrin-mediated Cell Migration
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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, B, Bergmann, E, Ossikovski, R D, Walter   +3 more
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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, Suguru Oguri, Aruto Yoshida, Makoto Takeuchi   +3 more
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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
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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
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α4-N-Acetylglucosaminyltransferase

2002
α4-N-Acetylglucosaminyltransferase (α4GnT) is a glycosyltransferase that mediates transfer of GlcNAc with α1,4-linkage from UDP-GlcNAc to βGal residues preferentially present in O-glycans, forming GlcNAcα1-4Galβ-R (Nakayama et al. 1999). In the human, glycoproteins having GlcNAcα1-4Galβ-R at nonreducing terminals are exclusively limited to the mucins ...
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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
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N-Acetylglucosaminyltransferase-V

2002
N-Acetylglucosaminyltransferase-V (GnT-V, GnT-V or Mgat5) catalyzes the transfer of GlcNAc from UDP-GlcNAc to the OH-6 position of the α-linked Man residue in GlcNAcβ1-2Manα1-6Manβ1-4GlcNAc. This acceptor sequence is found in N-glycan intermediates at the medial Golgi stage of glycoprotein production (Fig. 1).
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