Results 21 to 30 of about 5,149 (183)

FUT8-AS1 Inhibits the Malignancy of Melanoma Through Promoting miR-145-5p Biogenesis and Suppressing NRAS/MAPK Signaling

Frontiers in Oncology, 2021
Melanoma is the major lethal skin malignancy. However, the critical molecular drivers governing melanoma progression and prognosis are still not clear. By analyzing The Cancer Genome Atlas (TCGA) data, we identified FUT8-AS1 as a prognosis-related long ...
Xiang-jun Chen, Sha Liu, Dong-mei Han, De-zhi Han, Wei-jing Sun, Xiao-chun Zhao, Jun-qing Liang, Li Yu   +7 more
doaj   +1 more source

Loss of core fucosylation suppressed the humoral immune response in Salmonella typhimurium infected mice

Journal of Microbiology, Immunology and Infection, 2021
Background: The humoral immune response is pivotal to protect the host from Salmonella typhimurium (S. typhimurium) infection. Previously, we found that core fucosylation catalyzed by core fucosyltransferase (Fut8) could regulate the immune responses ...
Danish Zahid, Nianzhu Zhang, Hui Fang, Jianguo Gu, Ming Li, Wenzhe Li   +5 more
doaj   +1 more source

The SH3 domain in the fucosyltransferase FUT8 controls FUT8 activity and localization and is essential for core fucosylation [PDF]

Journal of Biological Chemistry, 2020
Core fucose is an N-glycan structure synthesized by α1,6-fucosyltransferase 8 (FUT8) localized to the Golgi apparatus and critically regulates the functions of various glycoproteins. However, how FUT8 activity is regulated in cells remains largely unclear.
Seita Tomida, Misaki Takata, Tetsuya Hirata, Masamichi Nagae, Miyako Nakano, Yasuhiko Kizuka   +5 more
openaire   +2 more sources

Positive association of serum FUT8 activity with renal tubulointerstitial injury in IgA nephropathy patients

Immunity, Inflammation and Disease, 2022
Background α‐1,6 Fucosyltransferase (FUT8) appears to play an essential role in the pathogenesis of renal fibrosis. However, it remained unknown whether FUT8 also contributed to renal fibrosis in immunoglobulin A nephropathy (IgAN). In the present study,
Ning Yang, Long‐kai Li, Hui He, Xia‐nan Guo, Xue‐feng Yuan, Zhi‐tong Li, Wei‐dong Wang, Biao‐jie Qin, Xiang‐ning Du, Xu Zhang, Shu‐ni Chen, Hong‐li Lin   +11 more
doaj   +1 more source

Expanding the molecular and clinical phenotypes of FUT8‐CDG [PDF]

Journal of Inherited Metabolic Disease, 2020
AbstractPathogenic variants in the Golgi localised alpha 1,6 fucosyltransferase, FUT8, cause a rare inherited metabolic disorder known as FUT8‐CDG. To date, only three affected individuals have been reported presenting with a constellation of symptoms including intrauterine growth restriction, severe delays in growth and development, other neurological
Ng B. G., Dastsooz H., Silawi M., Habibzadeh P., Jahan S. B., Fard M. A. F., Halliday B. J., Raymond K., Ruzhnikov M. R. Z., Tabatabaei Z., Taghipour-Sheshdeh A., Brimble E., Robertson S. P., Faghihi M. A., Freeze H. H.   +14 more
openaire   +3 more sources

Crystal structure of mammalian α1,6-fucosyltransferase, FUT8 [PDF]

Glycobiology, 2006
Mammalian alpha1,6-fucosyltransferase (FUT8) catalyses the transfer of a fucose residue from a donor substrate, guanosine 5'-diphosphate-beta-L-fucose to the reducing terminal N-acetylglucosamine (GlcNAc) of the core structure of an asparagine-linked oligosaccharide.
Hideyuki, Ihara, Yoshitaka, Ikeda, Sachiko, Toma, Xiangchun, Wang, Tadashi, Suzuki, Jianguo, Gu, Eiji, Miyoshi, Tomitake, Tsukihara, Koichi, Honke, Akio, Matsumoto, Atsushi, Nakagawa, Naoyuki, Taniguchi   +11 more
openaire   +2 more sources

FUT8 (fucosyltransferase 8 (alpha (1,6) fucosyltransferase)) [PDF]

Atlas of Genetics and Cytogenetics in Oncology and Haematology, 2011
Review on FUT8 (fucosyltransferase 8 (alpha (1,6) fucosyltransferase)), with data on DNA, on the protein encoded, and where the gene is implicated.
Ihara, H, Gao, CX, Ikeda, Y, Taniguchi, N   +3 more
openaire   +2 more sources

Protein glycosylation as a diagnostic and prognostic marker of chronic inflammatory gastrointestinal and liver diseases [PDF]

, 2020
Glycans are sequences of carbohydrates that are added to proteins or lipids to modulate their structure and function. Glycans modify proteins required for regulation of immune cells, and alterations have been associated with inflammatory conditions.
Callewaert, Nico, Colombel, Jean-Frederic, Dias, Ana M, Pinho, Salome S, Van Vlierberghe, Hans, Verhelst, Xavier, Vermeire, Severine   +6 more
core   +1 more source

FUT8 and Protein Core Fucosylation in Tumours: From Diagnosis to Treatment [PDF]

Journal of Cancer, 2021
Glycosylation changes are key molecular events in tumorigenesis, progression and glycosyltransferases play a vital role in the this process. FUT8 belongs to the fucosyltransferase family and is the key enzyme involved in N-glycan core fucosylation. FUT8 and/or core fucosylated proteins are frequently upregulated in liver, lung, colorectal, pancreas ...
Liao, Chengcheng, An, Jiaxing, Yi, Suqin, Tan, Zhangxue, Wang, Hui, Li, Hao, Guan, Xiaoyan, Liu, Jianguo, Wang, Qian   +8 more
openaire   +2 more sources

Progestins Related to Progesterone and Testosterone Elicit Divergent Human Endometrial Transcriptomes and Biofunctions. [PDF]

, 2020
Progestins are widely used for the treatment of gynecologic disorders and alone, or combined with an estrogen, are used as contraceptives. While their potencies, efficacies and side effects vary due to differences in structures, doses and routes of ...
Balayan, Shayna, Chen, Joseph C, Giudice, Linda C, Greenblatt, Ruth M, Houshdaran, Sahar, Irwin, Juan C, Smith-McCune, Karen, Vallvé-Juanico, Júlia, Vo, Kim Chi   +8 more
core   +2 more sources