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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-II

2002
The synthesis of complex N-glycans can be divided into three distinct stages. The first stage occurs primarily in the cytoplasm and rough endoplasmic reticulum, and involves the synthesis of Glc3Man9GlcNAc2-pyrophosphate-dolichol. The second stage begins with the transfer of GlcP3Man9GlcNAc2 from Glc3Man9GlcNAc2-pyrophosphate- dolichol to an Asn ...
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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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An enzyme-linked immunosorbent assay for N-acetylglucosaminyltransferase-V

Analytical Biochemistry, 1990
The development of an enzyme-linked immunosorbent assay (ELISA) for uridine 5'-diphospho-N-acetyl-glucosamine: alpha mannoside beta 1----6 N-acetylglucosaminyltransferase (GnT-V) is reported. The assay quantitates the enzymatic conversion of the specific synthetic GnT-V acceptor GlcNAc beta 1----2Man alpha 1----6Man beta-R (5) to the product GlcNAc ...
S C, Crawley   +4 more
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β3-N-Acetylglucosaminyltransferase (Fringe)

2002
Fringe provides a clear example of the role that carbohydrate modifications can play in regulating signal transduction events. Fringe was originally identified for its role in dorsal/ventral boundary formation during Drosophila wing development (Irvine and Wieschaus 1994).
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β3-N-Acetylglucosaminyltransferase (iGnT)

2002
β3-N-Acetylglucosaminyrtransferase, i-extension enzyme (iGnT), is a glycosyltransferase that catalyzes the transfer of GlcNAc from UDP-GlcNAc to Gal in the Galβ1-4Glc(NAc) structure with β1,3-linkage. In N-glycans, the addition of β1,3- linked GlcNAc is usually followed by galactosylation by β1,4-galactosyltransferase I, the predominant member of the ...
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β6-N-Acetylglucosaminyltransferase (IGnT)

2002
I-branching β6-N-acetylglucosaminyltransferase (IGnT) is a glycosyltransferase that catalyzes the transfer of GlcNAc from UDP-GlcNAc to β1,4-linked Gal residue in a linear poly-N-acetyllactosamine, ±Galβ1-4GlcNAcβ1-3Galβ1-4Glc(NAc)-R, forming ±Galβ1-4GlcNAcβ1-3(GlcNAcβ1-6)Galβ1-4Glc(NAc)-R.
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Chemical Modification of N-acetylglucosaminyltransferases.

Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica
The essential groups of three N-acetylglucosaminyltransferases (GnTs) of rat kidney were studied by using chemical modification and substrate protection methods. It was found that the amino and indolyl groups were the common essential groups of GnT-III, GnT-IV and GnT-V.
Hua-Bei, Guo, An-Li, Jiang, Hui-Li, Chen
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Structure and function of N-acetylglucosaminyltransferase V (GnT-V)

Biochimica et Biophysica Acta (BBA) - General Subjects
The β1,6-GlcNAc branch in N-glycans, produced by a glycosyltransferase N-acetylglucosaminyltransferase V (GnT-V or MGAT5), is associated with cancer and autoimmune diseases.Here, we summarize the structure and activity regulation of GnT-V. We also describe the roles of the β1,6-GlcNAc branch on glycoproteins in cells and the phenotypes of Mgat5 ...
Reina F, Osuka   +2 more
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E-cadherin and adherens-junctions stability in gastric carcinoma: functional implications of glycosyltransferases involving N-glycan branching biosynthesis, N-acetylglucosaminyltransferases III and V.

Biochimica et Biophysica Acta, 2013
S. Pinho   +13 more
semanticscholar   +1 more source

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