Results 21 to 30 of about 25,344,123 (207)
Molecular Aspects of Medicine, 2020 It is well known that numerous cancer-related changes occur in glycans that are attached to glycoproteins, glycolipids and proteoglycans on the cell surface and these changes in structure and the expression of the glycans are largely regulated by ...
N. Taniguchi +7 more
semanticscholar +1 more source
The nonidentity of porcine N-acetylglucosaminyltransferases I and II.
Journal of Biological Chemistry, 1981 R L Hill
exaly +2 more sources
Fringe controls naïve CD4(+)T cells differentiation through modulating notch signaling in asthmatic rat models. [PDF]
PLoS ONE, 2012 The ability of Notch signaling to regulate T helper cell development and differentiation has been widely accepted. Fringe, O-fucose-β1,3-N-acetylglucosaminyltransferases modulate Notch receptor expression and promote the Notch signaling pathway through ...
Wen Gu, Weiguo Xu, Tao Ding, Xuejun Guo
doaj +1 more source
GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal domain
eLife, 2015 Mouse GnT1IP-L, and membrane-bound GnT1IP-S (MGAT4D) expressed in cultured cells inhibit MGAT1, the N-acetylglucosaminyltransferase that initiates the synthesis of hybrid and complex N-glycans.
Hung-Hsiang Huang +5 more
doaj +1 more source
Identification and functional characterization of a highly divergent N-acetylglucosaminyltransferase I (TbGnTI) in Trypanosoma brucei [PDF]
, 2014 Trypanosoma brucei expresses a diverse repertoire of N-glycans, ranging from oligomannose and paucimannose structures to exceptionally large complex N-glycans.
Damerow, Manuela +5 more
core +1 more source
Minimal catalytic domain of N-acetylglucosaminyltransferase V [PDF]
Glycobiology, 2000 UDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T ...
Korczak B. +4 more
openaire +3 more sources
6″-Azido-6″-deoxy-UDP-N-acetylglucosamine as a glycosyltransferase substrate [PDF]
, 2011 6 ''-Azido-6 ''-deoxy-UDP-N-acetylglucosamine (UDP-6Az-GlcNAc) is a potential alternate substrate for N-acetylglucosaminyltransferases. This compound could be used to generate various glycoconjugates bearing an azide functionality that could in turn be ...
Mayer, Alain +9 more
core +1 more source
Substrate Engagement and Catalytic Mechanisms of N-Acetylglucosaminyltransferase V [PDF]
ACS Catalysis, 2020 α-Mannoside β-1,6-N-acetylglucosaminyltransferase V (MGAT5) is a mammalian glycosyltransferase involved in complex N-glycan formation, which strongly drives cancer when overexpressed. Despite intense interest, the catalytic mechanism of MGAT5 is not known in detail, precluding therapeutic exploitation.
John F. Darby +8 more
openaire +5 more sources
Angewandte Chemie, EarlyView.A glycan having a hydrazide tag enables chemoenzymatic synthesis of HS oligosaccharides. The hydrazide can, under mild acidic conditions, react with an aldehyde‐containing resin to give an immobilized hydrazone that is stable under neutral conditions, allowing washing. The product can be released by transiminolysis using aqueous hydroxylamine to give a
Francesco Palmieri +4 more
wiley +2 more sources
Biochimie, 2014 An important role in cancer pathogenesis is attributed to N-glycans with "bisecting" N-acetylglucosamine and beta1-6 branches but the exact mechanisms still remain to be elucidated. Two structures are formed by Golgi beta-1,4-mannosyl-glycoprotein 4-beta-
M. Bubka +4 more
semanticscholar +1 more source