Results 151 to 160 of about 13,321 (212)

Fucosylation in Urological Cancers [PDF]

International Journal of Molecular Sciences, 2021
Fucosylation is an oligosaccharide modification that plays an important role in immune response and malignancy, and specific fucosyltransferases (FUTs) catalyze the three types of fucosylations: core-type, Lewis type, and H type. FUTs regulate cancer proliferation, invasiveness, and resistance to chemotherapy by modifying the glycosylation of signaling
Hirotsugu Uemura, Mamoru Hashimoto, Norio Nonomura   +2 more
exaly   +3 more sources

The role of FUT8‐catalyzed core fucosylation in Alzheimer's amyloid‐β oligomer‐induced activation of human microglia

Glia, 2023
Fucosylation, especially core fucosylation of N‐glycans catalyzed by α1‐6 fucosyltransferase (fucosyltransferase 8 or FUT8), plays an important role in regulating the peripheral immune system and inflammation.
Jacopo Di Lucente, Izumi Maezawa
exaly   +3 more sources

Roles of core fucosylation modification in immune system and diseases

Cell Insight
Core fucosylation, catalyzed by α1,6-fucosyltransferase (FUT8), is an important N-glycosylation modification process that attaches a fucose residue via an α1,6-linkage to the core N-acetylglucosamine of N-glycans in mammals.
Xiao-Lian Zhang, Qiu Pan
exaly   +2 more sources

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A metabolic inhibitor blocks cellular fucosylation and enables production of afucosylated antibodies

Proceedings of the National Academy of Sciences of the United States of America
Significance The monosaccharide fucose is a common constituent of glycoproteins from multicellular organisms. Fucosylation modulates the functions of various proteins, thereby exerting control over a range of physiological processes.
David Vočadlo, , Wesley Zandberg
exaly   +2 more sources

A Redox‐Controlled Substrate Engineering Strategy for Site‐Specific Enzymatic Fucosylation

Angewandte Chemie - International Edition, 2022
Fucosylation is one of the most common modifications of oligo-N-acetyllactosamine (oligo-LacNAc) glycans. However, none of the known fucosyltransferases (FucTs) could install the a1,3-linked fucose to the oligo-LacNAc substrates in a site-specific manner.
Chang-Cheng Liu, Hongzhi Cao
exaly   +2 more sources

"Two Birds One Stone" Strategy for the Site-Specific Analysis of Core Fucosylation and O-GlcNAcylation.

Journal of the American Chemical Society, 2023
Core fucosylation and O-GlcNAcylation are the two most famous protein glycosylation modifications that regulate diverse physiological and pathological processes in living organisms.
Yawen Luo, Yuqiu Wang, Yinping Tian, Hu Zhou, Liuqing Wen   +4 more
semanticscholar   +1 more source

Aberrant fucosylation sustains the NOTCH and EGFR/NF-κB pathways and has a prognostic value in human intrahepatic cholangiocarcinoma

Hepatology, 2023
Background and Aims: Intrahepatic cholangiocarcinoma (iCCA) is a lethal malignancy, with increasing incidence worldwide and limited therapeutic options. Aberrant protein glycosylation is a hallmark of cancer. Here, we thoroughly investigated the possible
Cindy Ament, Sara Steinmann, K. Evert, G. Pes, S. Ribback, Isabella Gigante, Elena Pizzuto, J. Banales, P. Rodrigues, P. Olaizola, Haichuan Wang, G. Giannelli, Xin Chen, M. Evert, D. Calvisi   +14 more
semanticscholar   +1 more source