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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 MGAT3 Antikörper (69) und MGAT3 Kits (12) und viele weitere Produktgruppen zu diesem Protein an.
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The MGAT3 and bisected complex N-glycans retard mouse mammary tumor progression; identification of key galectins that promote mammary tumor progression in mice is not straightforward because the galectin genes are expressed; and high levels of MGAT3.
data suggest that Fut8(-/-) mice adapted to oxidative stress, both ex vivo and in vivo, by inducing various genes including GnT-III, which may compensate for the loss of core fucose functions
Mgat3 glycogene expression and GnT-III-mediated glycosylation, specifically on E-cadherin, is a novel and major component of the Epithelial-Mesenchymal-Transition and the reverted process, Mesenchymal-Epithelial-Transition mechanism.
Roles of N-acetylglucosaminyltransferase III in epithelial-to-mesenchymal transition induced by transforming growth factor beta1 (TGF-beta1) in epithelial cell lines
GnT-III expression may be precisely regulated by the interplay of E-cadherin-catenin complex-mediated cell-cell adhesion and Wnt/beta-catenin signaling
upregulation of GnT-III in AD brains may represent an adaptive response to protect them from additional beta-amyloid production
mice homozygous for the Mgat3T37 mutation that express truncated GlcNAc-TIII from two mutant alleles suffer neurological and other consequences
beta1,4-N-acetylglucosaminyltransferase III inhibits the function of alpha5beta1 integrin
An E-cadherin-dependent pathway plays a critical role in regulation of GnT-III expression; changes in GnT-III expression presumably contribute to intracellular signaling transduction during tissue development and homeostasis.
Novel insights into the epigenetic regulation of MGAT3/bisecting GlcNAc and demonstrate the importance of N-glycosylation in cancer progression.
Data suggest that GNT-III expression regulates levels/activation of the heavily glycosylated Notch receptor involved in normal and malignant cell development; suppression of GNT-III in epithelial ovarian carcinoma cell lines results in down-regulation of Notch signaling that is more potent than pharmacologic blockage of Notch activation.
MGAT3 expressed in cells stimulates lipid droplet growth. These findings provide additional evidence that MGAT3 likely functions as a triacylglycerol synthase in cells.
Core-fucosylated tetra-antennary structures were decreased in quantity likely as a result of hypomethylated MGAT3 gene promoter followed by increased expression of this gene
High expression of alpha2,6-sialylation on the cell surface could affect the anti-migratory role of GnT-III, which provides an insight into the mechanistic roles of GnT-III in tumor metastasis.
Mgat3 plays an important role in early spontaneous miscarriage in humans.
MGAT3 protein and gene expression in in uveal and cutaneous melanoma cells
HS5 cells had significantly enhanced levels of bisecting N-glycans (catalyzed by MGAT3 whereas HS27a cells had enhanced levels of Galbeta1,4GlcNAc.
functional characterization of N-acetylglucosaminyltransferases III and V in human melanoma cells
GnT-III determines E-cadherin-mediated tumor suppression, and GnT-V regulates E-cadherin-mediated tumor invasion.
MGAT3 mRNA biomarker may characterize subgroups of Alzheimer's disease patients with different disease progression.
the modulation of glycosyltransferases MGAT3 and MGAT5 by synthetic N-acetyl-D-glucosamine-calixarene correlated with the improvement of NK cell effector functions and the augmentation of tumor cells sensitivity to NK cell-mediated cytotoxicity.
down-regulation of hydrogen peroxide-induced PKC delta activation in cells transfected with this enzyme
An N-glycosylation site on the beta-propeller domain of the integrin alpha5 subunit plays key roles in both its function and site-specific modification by beta1,4-N-acetylglucosaminyltransferase III.
MGAT3 and MGAT5 competitively modified E-cadherin N-glycans.
There are believed to be over 100 different glycosyltransferases involved in the synthesis of protein-bound and lipid-bound oligosaccharides. The enzyme encoded by this gene transfers a GlcNAc residue to the beta-linked mannose of the trimannosyl core of N-linked oligosaccharides and produces a bisecting GlcNAc. Multiple alternatively spliced variants, encoding the same protein, have been identified.
, mannosyl (beta-1,4-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase
, beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like
, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III
, glcNAc-T III
, GlcNAc-T III
, N-acetylglucosaminyltransferase III
, mannoside acetyl glucosaminyltransferase 3