Results 171 to 180 of about 5,149 (183)

α6-Fucosyltransferase (FUT8)

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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Requirement of Fut8 for the expression of vascular endothelial growth factor receptor-2: a new mechanism for the emphysema-like changes observed in Fut8-deficient mice

Journal of Biochemistry, 2009
alpha1,6-Fucosylation plays key roles in many biological functions, as evidenced by the study of alpha1,6-fucosyltransferase (Fut8) knockout (Fut8(-/-)) mice. Phenotypically, Fut8(-/-) mice exhibit emphysema-like changes in the lung, and severe growth retardation.
Xiangchun, Wang, Tomohiko, Fukuda, Wenzhe, Li, Cong-Xiao, Gao, Akihiro, Kondo, Akio, Matsumoto, Eiji, Miyoshi, Naoyuki, Taniguchi, Jianguo, Gu   +8 more
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FUT8 Promotes Melanoma Invasion and Metastasis

Cancer Discovery, 2017
Abstract FUT8-mediated core fucosylation of L1CAM drives melanoma metastasis.
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Donor substrate binding and enzymatic mechanism of human core α1,6-fucosyltransferase (FUT8)

Biochimica et Biophysica Acta (BBA) - General Subjects, 2012
Fucosylation is essential for various biological processes including tumorigenesis, inflammation, cell-cell recognition and host-pathogen interactions. Biosynthesis of fucosylated glycans is accomplished by fucosyltransferases. The enzymatic product of core α1,6-fucosyltransferase (FUT8) plays a major role in a plethora of pathological conditions, e.g.
Miriam P, Kötzler, Simon, Blank, Frank I, Bantleon, Edzard, Spillner, Bernd, Meyer   +4 more
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FUT8-mediated core fucosylation stabilizes TMEM67 to promote ciliogenesis

Journal of Cell Biology
Glycosylation of membrane proteins plays an essential role in diverse biological processes. However, it remains unknown whether this posttranslational modification occurs on ciliary membrane proteins. Herein, by mass spectrometry–based proteomic analysis, we demonstrate that multiple membrane proteins localized in the ciliary transition zone undergo ...
Difei Wang, Qingchao Li, Zhenqi Yu, Junkui Zhao, Mingzheng Hu, Xiaoshan Geng, Xinzhe Liu, Siyang Zhao, Ting Song, Min Liu, Dengwen Li, Huijie Zhao, Jun Zhou   +12 more
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Mapping of the α-1,6-fucosyltransferase gene, FUT8, to human chromosome 14q24.3

Cytogenetic and Genome Research, 1999
α-1,6-Fucosyltransferase (α1,6FucT) is involved in the biosynthesis of asparagine-linked glycoprotein oligosaccharides. In this study, we isolated a genomic clone for the human α1,6FucT gene (FUT8) and mapped it by fluorescence in situ hybridization to chromosome 14q24.3.
Y, Yamaguchi, J, Fujii, S, Inoue, N, Uozumi, S, Yanagidani, Y, Ikeda, M, Egashira, O, Miyoshi, N, Niikawa, N, Taniguchi   +9 more
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Significance of FUT8 in Pancreatic Cancer and Others

2023
Caixia Liang, Wanli Song, Jianguo Gu
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FUT8 Assay

2009
Hideyuki Ihara, Hiroaki Korekane, Akio Matsumoto, Naoyuki Taniguchi   +3 more
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Fucosyltransferase 8 (FUT8) Polymorphism, Thr267Lys, Is Associated With Pulmonary Emphysem

Chest, 2011
Miki Yamada, Takeo Ishii, Shinobu Ikeda, Kozui Kida, Masaaki Muramatsu, Motoji Sawabe   +5 more
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FUT8

2016
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