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Results 1 - 10 of 27 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.144malfunction detailed glycomic analysis of the effect of GnT-III overexpression in WM266-4-GnT-III metastatic melanoma cells, overview. Overexpression of GnT-III in melanoma leads to modification of a broad range of N-glycan types by the introduction of the bisecting GlcNAc residue with highly branched complex structures among them. The presence of these unusual complex N-glycans results in stronger interactions of cellular glycoproteins with the PHA-L. Elevated activity of GnT-III in cancer cells does not necessarily lead to a total abrogation of the formation of highly branched glycans. The modification of pre-existing N-glycans by the introduction of bisecting GlcNAc can modulate their capacity to interact with carbohydrate-binding proteins such as plant lectins 759316
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.144malfunction downregulated N-acetylglucosaminyltransferase III is involved in attenuating trophoblast migration and invasion under hypoxia-reoxygenation condition. Excessive oxidative stress can decrease GnT-III expression in trophoblast and the decreased expression of GnT-III may be involved in the development of preeclampsia. Clinical characteristics of preeclampsia group comparedwith normal pregnancy group, overview 759591
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.144malfunction knockdown of GnT-III by siRNA causes no alteration in expression levels of E-cadherin mRNA and protein, but induces alterations on E-cadherin cellular localization in MCF-7/AZ cells. GnT-III knockdown cells reveal a membrane de-localization of E-cadherin leading to its cytoplasmic accumulation and cause modifications of E-cadherin N-glycans catalyzed by GnT-III and GnT-V 703956
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.144malfunction suppression of GnT-III in epithelial ovarian carcinoma (EOC) cell lines and primary tumor-derived cells results in an inhibition of Notch signaling that is more potent than pharmacologic blockage of Notch activation via gamma-secretase inhibition. The inhibition results from the redirection of the Notch receptor to the lysosome, a distinct mechanism 759483
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.144metabolism existence of a bi-directional cross-talk between E-cadherin and two major N-glycan processing enzymes, N-acetylglucosaminyltransferase-III or -V (GnT-III or GnT-V). Molecular mechanisms underlying E-cadherin regulation in gastric cancer, overview 721738
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.144metabolism GnT-III is considered to be a key glycosyltransferase in the N-glycan biosynthetic pathway because the introduction of the bisecting GlcNAc residue suppresses further processing and elongation of the N-glycans catalyzed by GnT-V. So, in the tumor context, GnT-III and GnT-V have generally a dual role where GnT-III acts as metastases suppressors whereas GnT-V is associated with increased malignancy and metastasis 759591
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.144metabolism interplay between GnT-III and sialyltransferases in the expression of their enzymatic products and also their functions in tumor metastasis. Interplay between GnT-III and ST6GAL1 in regulating cell migration 736507
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.144metabolism N-acetylglucosaminyltransferase-III-mediated glycosylation, specifically on E-cadherin, is a major component of the Epithelial-Mesenchymal-Transition /Mesenchymal-Epithelial-Transition mechanism signature 723551
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.144more GnT-III overexpression does not affect cell morphology 721738
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.144more usage of MALDI-TOF and ESIion-trap-MS/MS together with HILIC-HPLC of 2-AA labeled N-glycans to study the N-glycome of membrane-attached and secreted proteins. Characterization of N-glycan epitopes on membrane and secreted proteins using plant lectins, several plant lectins are used in lectin blot assay, overview 759316
Results 1 - 10 of 27 > >>