Results 11 to 20 of about 5,149 (183)
L-Fucose treatment of FUT8-CDG
Molecular Genetics and Metabolism Reports, 2020 FUT8-CDG is a severe multisystem disorder caused by mutations in FUT8, encoding the α-1,6-fucosyltransferase. We report on dizygotic twins with FUT8-CDG presenting with dysmorphisms, failure to thrive, and respiratory abnormalities.
Julien H. Park +10 more
doaj +4 more sources
Effects of microRNAs on fucosyltransferase 8 (FUT8) expression in hepatocarcinoma cells. [PDF]
PLoS ONE, 2013 Fucosyltransferase 8 (FUT8) catalyzes the transfer of α1,6-linked fucose to the first N-acetylglucosamine in N-linked glycans (core fucosylation). Increased core fucosylation has been reported during hepatocarcinogenesis, in both cell-associated and ...
Cinzia Bernardi +3 more
doaj +5 more sources
Glycoproteomic Characterization of FUT8 Knock-Out CHO Cells Reveals Roles of FUT8 in the Glycosylation [PDF]
Frontiers in Chemistry, 2021 The α1,6-fucosyltransferase (encoded by FUT8 gene) is the key enzyme transferring fucose to the innermost GlcNAc residue on an N-glycan through an α-1,6 linkage in the mammalian cells.
Ganglong Yang +5 more
doaj +3 more sources
PLoS ONE, 2014 The core alpha1,6-fucosyltransferase (FUT8) catalyzes the transfer of a fucosyl moiety from GDP-fucose to the innermost asparagine-linked N-acetylglucosamine residue of glycoproteins.
Sylvie Juliant +7 more
doaj +5 more sources
Diagnosis and prognosis of serum Fut8 for epilepsy and refractory epilepsy in children
PLoS ONE, 2023 With adequate serum concentration of antiepileptic drugs, the epilepsy symptoms in many patients still cannot be controlled well. The alteration of glycosyltransferase has obvious influence on the pathogenesis of epilepsy.
Yunxiu Huang, Zhou Zhang, Linmu Chen
doaj +4 more sources
Fucosyltransferase 8 (FUT8) and core fucose expression in oxidative stress response.
PLoS ONE, 2023 GlycoMaple is a new tool to predict glycan structures based on the expression levels of 950 genes encoding glycan biosynthesis-related enzymes and proteins using RNA-seq data.
Yuki M Kyunai +4 more
doaj +5 more sources
Development of a FUT8 Inhibitor with Cellular Inhibitory Properties [PDF]
Angewandte Chemie International EditionCore fucosylation is catalyzed by α‐1,6‐fucosyltransferase (FUT8), which fucosylates the innermost GlcNAc of N‐glycans. Given the association of FUT8 with various diseases, including cancer, selective FUT8 inhibitors applicable to in vivo or cell‐based ...
Asakura, Akiko +13 more
core +10 more sources
FUT8 promotes breast cancer cell invasiveness by remodeling TGF-β receptor core fucosylation [PDF]
Breast Cancer Research, 2017 Background Core fucosylation (addition of fucose in α-1,6-linkage to core N-acetylglucosamine of N-glycans) catalyzed by fucosyltransferase 8 (FUT8) is critical for signaling receptors involved in many physiological and pathological processes such as ...
Cheng-Fen Tu +4 more
doaj +3 more sources
Cell & Bioscience, 2023 Background Atherosclerosis (AS) is the leading underlying cause of the majority of clinical cardiovascular events. Retention of foamy macrophages in plaques is the main factor initiating and promoting the atherosclerotic process. Our previous work showed
Xi Yang +11 more
doaj +3 more sources
FUT8 Alpha-(1,6)-Fucosyltransferase in Cancer [PDF]
International Journal of Molecular Sciences, 2021 Aberrant glycosylation is a universal feature of cancer cells that can impact all steps in tumour progression from malignant transformation to metastasis and immune evasion. One key change in tumour glycosylation is altered core fucosylation. Core fucosylation is driven by fucosyltransferase 8 (FUT8), which catalyses the addition of α1,6-fucose to the ...
Kayla Bastian +3 more
openaire +3 more sources