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Daily variation of rat brain fucosyltransferase
Biochemical and Biophysical Research Communications, 1981Abstract Glycoprotein fucosyltransferase activity was investigated in rat brain during 24 h periods. Up to 50 % variations were detected without correlations with either lights on or off, while acetylcholinesterase located in same membrane fractions showed no level variations.
Pierre Louisot, P. Broquet, Monique Leon
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2002
GDP-L-FucN-acetyl-β-D-glucosaminide α1-6fucosyltransferase (FUT8) catalyzes the transfer of fucose from GDP-Fuc to N-linked-type complex glycoproteins, as shown in Fig. 1. The enzymatic products, α1,6-fucosylated (core fucosylated) N-glycans, are commonly observed in many glycoproteins, and are especially abundant in brain tissue. It is well known that
Eiji Miyoshi, Naoyuki Taniguchi
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GDP-L-FucN-acetyl-β-D-glucosaminide α1-6fucosyltransferase (FUT8) catalyzes the transfer of fucose from GDP-Fuc to N-linked-type complex glycoproteins, as shown in Fig. 1. The enzymatic products, α1,6-fucosylated (core fucosylated) N-glycans, are commonly observed in many glycoproteins, and are especially abundant in brain tissue. It is well known that
Eiji Miyoshi, Naoyuki Taniguchi
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Stachybotrydial, a potent inhibitor of fucosyltransferase and sialyltransferase
Biochemical and Biophysical Research Communications, 2005Elevated expression of fucosylated glycoconjugates and fucosyltransferases (Fuc-Ts) is found in various tumor cells and has been correlated with aspects of tumor progression such as cell adhesion and metastasis. Thus, fucosyltransferase inhibitors are potentially useful as anti-tumor agents. In the present study, three known spirocyclic drimanes (1, 2,
Chien-Chih Chen +3 more
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Inhibition of fucosyltransferase V by a GDP–Azasugar
Bioorganic & Medicinal Chemistry Letters, 2001AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
Matthias Schuster, Siegfried Blechert
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Plasma α1,3-Fucosyltransferase Deficiency in Schizophrenia
Experimental and Clinical Immunogenetics, 1999Levels of plasma α1,3-fucosyltransferase (α1,3FT) were assayed in 44 patients with schizophrenia and in 50 healthy controls. Significantly reduced enzyme activities were observed in patients (p < 0.05) and 4 unrelated patients were found, for the first time in Japan, to be deficient in the enzyme activity. Two point mutations in the coding region of
Susumu Tanaka +4 more
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Fucosyltransferase-9 Knockout Mouse
2009Stage-specific embryonic antigen-1 (SSEA-1), an antigenic epitope of which was defined as a Lewis x [Lex: Galβ1–4(Fucα1–3)GlcNAc-] carbohydrate structure, is widely expressed on the surface of mammalian cells, and is considered to be involved in cell-cell interactions during embryogenesis, differentiation, and neurodevelopmental processes.
Hisashi Narimatsu, Takashi Kudo
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Fucosylation of Complex Glycosphingolipids by Recombinant Fucosyltransferase-VII
Biochemical and Biophysical Research Communications, 1997Fucosyltransferase VII (FucT-VII) is one of five known alpha 1-->3fucosyltransferases capable of transferring fucose to the C-3 position of N-acetylglucosamine residues found in lactosamine based glycans. Previous studies have indicated that FucT-VII has a very restricted specificity, capable of fucosylating only terminally alpha 2-->3sialylated ...
Eric H. Holmes, Mark R. Stroud
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Roles of Fucosyltransferases in Cancer Phenotypes
2016Fucosylation is one of the most important types of glycosylation in carcinogenesis. Fucosylation is linked to certain processes in cell-cell interaction and dynamic regulation of growth factor receptor signaling on cell surface, and changes in fucosylation result in differences of biological phenotype in cancer cells.
Eiji Miyoshi +4 more
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α3-Fucosyltransferase-V (FUT5)
2002Fuc-TVI (FUT6) was cloned as a fourth member of the human α1→3/4 fucosyltransferase gene family by Weston et al. in 1992. The enzyme shared 85% and 89% amino acid sequence identity with previously cloned Fuc-TIII (FUT3) and Fuc-TV (FUT5), respectively, and the FUT6 gene encoding the enzyme was shown to be located on chromosome 19, where the genes for ...
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Production of human fucosyltransferases in Trichoderma reesei
2022Glycosylation is the most complex posttranslational modification specific to eukaryotes and also some bacteria. . One of the bottlenecks limiting progress in the glycobiology research is the non-availability and/or high price of glycan-modifying enzymes, such as fucosyltransferases, due to the imperfections of existing production systems.
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