Results 1 to 10 of about 19,439 (257)

Fucosyltransferase 1 and 2 play pivotal roles in breast cancer cells. [PDF]

open access: yesCell Death Discovery, 2019
FUT1 and FUT2 encode alpha 1, 2-fucosyltransferases which catalyze the addition of alpha 1, 2-linked fucose to glycans. Glycan products of FUT1 and FUT2, such as Globo H and Lewis Y, are highly expressed on malignant tissues, including breast cancer ...
Chang, Nai-Chuan   +9 more
core   +3 more sources

FUT8 Alpha-(1,6)-Fucosyltransferase in Cancer [PDF]

open access: yesInternational 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.
K. Bastian   +3 more
semanticscholar   +5 more sources

Intestinal Fut2 deficiency exacerbated alcohol-related liver disease by disrupting nicotinamide metabolism. [PDF]

open access: yesClin Transl Med
Loss of intestinal epithelial fucosylation exacerbates alcohol‐related liver injuries. Intestinal epithelial deletion of Fut2 disrupts nicotinamide (NAM) metabolism due to the decline in bacterial nicotinamidase (PncA). Supplemented with pncA overexpressed E.coli to restore gut PncA levels can improve liver damage in alcohol‐induced intestinal ...
Chen L   +9 more
europepmc   +2 more sources

Maternal fucosyltransferase 2 status affects the gut bifidobacterial communities of breastfed infants. [PDF]

open access: yesMicrobiome, 2015
BackgroundIndividuals with inactive alleles of the fucosyltransferase 2 gene (FUT2; termed the 'secretor' gene) are common in many populations. Some members of the genus Bifidobacterium, common infant gut commensals, are known to consume 2'-fucosylated ...
German, J Bruce   +11 more
core   +2 more sources

Fucosyltransferase 2: A Genetic Risk Factor for Intestinal Diseases

open access: yesFrontiers in Microbiology, 2022
The fucosyltransferase 2 gene (FUT2) mediates the synthesis of histoblood group antigens (HBGA) that occur in vivo from multiple organs, particularly on the surface of intestinal epithelial cells and body fluids.
Mingyang Hu   +5 more
semanticscholar   +1 more source

Improved production of 2′-fucosyllactose in engineered Saccharomyces cerevisiae expressing a putative α-1, 2-fucosyltransferase from Bacillus cereus

open access: yesMicrobial Cell Factories, 2021
Background 2′-fucosyllactose (2′-FL) is one of the most abundant oligosaccharides in human milk. It constitutes an authorized functional additive to improve infant nutrition and health in manufactured infant formulations.
Mingyuan Xu   +4 more
semanticscholar   +1 more source

Alpha-(1,6)-fucosyltransferase (FUT8) affects the survival strategy of osteosarcoma by remodeling TNF/NF-κB2 signaling

open access: yesCell Death and Disease, 2021
Glycosylation is an important modification of membrane proteins that results in functional changes in many cellular activities, from cell-cell recognition to regulatory signaling.
Shanyi Lin   +7 more
semanticscholar   +1 more source

A broadly active fucosyltransferase LmjFUT1 whose mitochondrial localization and activity are essential in parasitic Leishmania

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2021
Significance Abundant surface glycoconjugates play key roles in the infectious cycle of protozoan parasites including Leishmania. Through defining biosynthetic pathways, we identified a fucosyltransferase FUT1 localized to the parasite mitochondrion, an ...
Hongjie Guo   +7 more
semanticscholar   +1 more source

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

open access: yes, 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   +6 more
core   +1 more source

Structural basis for substrate specificity and catalysis of α1,6-fucosyltransferase

open access: yesNature Communications, 2020
Core-fucosylation is an essential biological modification by which a fucose is transferred from GDP-β-L-fucose to the innermost N-acetylglucosamine residue of N-linked glycans.
A. García-García   +6 more
semanticscholar   +1 more source

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