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There are believed to be over 100 different glycosyltransferases involved in the synthesis of protein-bound and lipid-bound oligosaccharides. Zusätzlich bieten wir Ihnen Mannosyl (Alpha-1,3-)-Glycoprotein beta-1,2-N-Acetylglucosaminyltransferase Antikörper (97) und Mannosyl (Alpha-1,3-)-Glycoprotein beta-1,2-N-Acetylglucosaminyltransferase Kits (13) und viele weitere Produktgruppen zu diesem Protein an.
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In this study we showed that the activation of Wnt/beta-catenin pathway culminates in the upregulation of MGAT1 enzyme both at transcriptional and post-transcriptional levels. We also showed that overexpression of the beta-catenin gene (CTNNB1) increased the promoter activity of MGAT1.
The presence of the rs4285184 polymorphism of the MGAT1 gene increased the risk for developing body fat associated with obesity in the Mexican population.
MGAT1 is downregulated in peripheral blood mononuclear cells of galactosaemia patients.
The authors show here that the luminal domain of GnT1IP-L contains its MGAT1 inhibitory activity.
UDP-galactose (SLC35A2) and UDP-N-acetylglucosamine (SLC35A3) Transporters Form Glycosylation-related Complexes with Mannoside Acetylglucosaminyltransferases (Mgats).
The IL2RA and IL7RA variants had univariate association in MS and T1D, whereas the MGAT1 and CTLA-4 variants associated with only MS or T1D, respectively.
analysis of suppression of cancer progression by MGAT1 shRNA knockdown
Genetic variants downstream MGAT1 seem to influence susceptibility to obesity. Moreover, these genetic variants affect the levels of serum unsaturated fatty acids and Delta desaturase indices, variables previously shown to correlate with obesity.
Activity of HuGnTI in plants is limited by a combination of reduced protein stability, alternative protein targeting and possibly to some extend to lower enzymatic performance of the catalytic domain in the plant biochemical environment.
The analysis enabled us to identify a new candidate gene, MGAT1, associated with weight in women.
Findings indicated that cysteine 121 has a structural role in maintaining active site geometry of hGnT1, rather than a catalytic role, and illustrates for the first time the potential utility of E. coli as an expression system for hGnT1.
MGAT1 is required to regulate ERK1/2 signaling during spermatogenesis, potentially via different mechanisms.
The MGAT1 interacts with DGAT2, which serves to synergistically increase the TAG biosynthesis and LD expansion, leading to enhancement of lipid accumulation in the liver and fat.
this study shows that loss of O-GlcNAc transferase blocks T cell progenitor renewal, malignant transformation and peripheral T cell clonal expansion
Inhibition of hepatic Mogat1 improves hepatic metabolic abnormalities without attenuating liver inflammation and injury.
Data from transgenic mice suggest that a lack of complex N- and O-glycans impairs early embryo development and viability in vivo leading to delayed implantation and embryo loss; Mgat1 and C1galt1 are required for embryo development and implantation.
the MGAT1 pathway induced by hepatic PPARgamma is critically important in the development of hepatic steatosis during diet-induced obesity
essential for spermatogenesis
Mgat1 mutant oocytes had an altered zona pellucida (ZP) that was thinner than the control ZP, and they did not possess complex N-glycans
analysis of developmental and nutritional regulation of monoacylglycerol lipase and monoacylglycerol acyltransferase
MGAT1-dependent N-glycosylation shapes the synaptomatrix carbohydrate environment and endogenous lectin localization within this domain, to modulate retention of trans-synaptic signaling ligands driving synaptic scaffold recruitment during synaptogenesis.
show that knockdown of Mgat1 in the central nervous system (CNS) of wild-type flies decreases locomotor activity and life span.
beta1,2-N-acetylglucosaminyltransferase I-dependent N-glycans are required for locomotory activity, life span, and brain development in Drosophila
N-acetylglucosaminyltransferase I activity in the oviduct may contribute to the induction of glycosylation and thereby contributing to the provision of the optimal microenvironment for fertilization and early development of the embryos.
There are believed to be over 100 different glycosyltransferases involved in the synthesis of protein-bound and lipid-bound oligosaccharides. UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I is a medial-Golgi enzyme essential for the synthesis of hybrid and complex N-glycans. The protein, encoded by a single exon, shows typical features of a type II transmembrane protein. The protein is believed to be essential for normal embryogenesis. Several variants encoding the same protein have been found for this gene.
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
, alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
, glcNAc-T I
, N-acetylglucosaminyltransferase I
, MGAT1 gene for N-acetylglucosaminyltransferase
, mannoside acetylglucosaminyltransferase 1
, alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase
, UDP-GlcNAc:a-3-D-mannoside-beta-1,2-N-acetylglucosaminyltransferase I
, mannosyl (alpha-1,3-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase
, Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase