Results 11 to 20 of about 12,774 (221)

An essential, kinetoplastid-specific GDP-Fuc:β-D-Gal α-1,2-fucosyltransferase is located in the mitochondrion of Trypanosoma brucei [PDF]

eLife, 2021
Fucose is a common component of eukaryotic cell-surface glycoconjugates, generally added by Golgi-resident fucosyltransferases. Whereas fucosylated glycoconjugates are rare in kinetoplastids, the biosynthesis of the nucleotide sugar GDP-Fuc has been ...
Ferguson, Michael A.J., Jose Carlos Paredes Franco, Ferguson, Michael Aj, Damerow, Sebastian, Guo, Hongjie, Sebastian Damerow, Ferguson, Michael A. J.; id_orcid, Maria Lucia Sempaio Guther, Beverley, Stephen, Stephen Beverley, Hongjie Guo, Angela Mehlert, Bandini, Giulia, Sempaio Güther, Maria Lucia, Michael AJ Ferguson, Paredes Franco, Jose Carlos, Mehlert, Angela, Giulia Bandini   +17 more
core   +3 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   +4 more sources

Subcellular localisation of cerebral fucosyltransferase [PDF]

FEBS Letters, 1984
GDP‐fucose : asialofetuin fucosyltransferase from sheep brain was fractionated on a sucrose gradient into two activity peaks. Using purification on Ficoll adapted from the proposed method [(1980) J. Neurochem. 35, 281‐296], double localisation of cerebral fucosyltransferase was confirmed and the subcellular active fractions identified as light ...
Broquet, P., Serres-Guillaumond, M., Baubichon-Cortay, H., Peschard, Mj, Louisot, P.   +4 more
openaire   +4 more sources

The contribution of fucosyltransferases to cancer biology [PDF]

Brazilian Journal of Biology
Abstract Fucosyltransferases are enzymes that transfer L-fucose residues from a donor substrate to target molecules. These enzymes are encoded by genes known as FUTs (FUT1 to FUT-11), along with POFUT1 and 2. Changes in FUT expression have a significant role in cancer development and malignancy.
A. O. Vasconcelos, L. M. Vieira, C. R. C. Rocha, E. I. C. Beltrão   +3 more
openaire   +4 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, Emma Scott, David Elliott, Jennifer Munkley   +3 more
openaire   +4 more sources

Suppressing α-1,6-Fucosyltransferase With a Novel Small Molecule Inhibitor Ameliorates Inflammation in Murine T-Cell-Mediated Colitis Models. [PDF]

Cell Mol Gastroenterol Hepatol
Background & Aims: Inflammatory bowel disease involves intractable intestinal inflammation often refractory to current pharmacotherapies. We investigated the therapeutic potential of a novel, orally available inhibitor targeting α -1,6-fucosyltransferase—
Asakura A, Shinzaki S, Manabe Y, Hizume K, Tsujii Y, Tashiro T, Amano T, Tani M, Otake-Kasamoto Y, Yoshihara T, Uema R, Tsujii Y, Iijima H, Kamada Y, Okuzaki D, Motooka D, Fukuda T, Kudo T, Takahashi S, Gu J, Miyoshi E, Fukase K, Hayashi Y, Takehara T.   +23 more
europepmc   +2 more sources

Utility of Bioluminescent Homogeneous Nucleotide Detection Assays in Measuring Activities of Nucleotide-Sugar Dependent Glycosyltransferases and Studying Their Inhibitors

Molecules, 2021
Traditional glycosyltransferase (GT) activity assays are not easily configured for rapid detection nor for high throughput screening because they rely on radioactive product isolation, the use of heterogeneous immunoassays or mass spectrometry.
Laurie Engel, Juliano Alves, Jacquelyn Hennek, Said A. Goueli, Hicham Zegzouti   +4 more
doaj   +1 more source

Structural Insights in Mammalian Sialyltransferases and Fucosyltransferases: We Have Come a Long Way, but It Is Still a Long Way Down

Molecules, 2021
Mammalian cell surfaces are modified with complex arrays of glycans that play major roles in health and disease. Abnormal glycosylation is a hallmark of cancer; terminal sialic acid and fucose in particular have high levels in tumor cells, with positive ...
Ravneet Kaur Grewal, Abdul Rajjak Shaikh, Suresh Gorle, Manjeet Kaur, Paula Alexendra Videira, Luigi Cavallo, Mohit Chawla   +6 more
doaj   +1 more source

Anaplasma marginale Infection of Dermacentor andersoni Primary Midgut Cell Culture Is Dependent on Fucosylated Glycans

Frontiers in Cellular and Infection Microbiology, 2022
Tick midgut is the primary infection site required by tick-borne pathogens to initiate their development for transmission. Despite the biological significance of this organ, cell cultures derived exclusively from tick midgut tissues are unavailable and ...
Rubikah Vimonish, Janaina Capelli-Peixoto, Wendell C. Johnson, Hala E. Hussein, Hala E. Hussein, Naomi S. Taus, Kelly A. Brayton, Ulrike G. Munderloh, Susan M. Noh, Susan M. Noh, Massaro W. Ueti, Massaro W. Ueti, Massaro W. Ueti   +12 more
doaj   +1 more source

Novel Insights Into N-Glycan Fucosylation and Core Xylosylation in C. reinhardtii

Frontiers in Plant Science, 2020
Chlamydomonas reinhardtii (C. reinhardtii) N-glycans carry plant typical β1,2-core xylose, α1,3-fucose residues, as well as plant atypical terminal β1,4-xylose and methylated mannoses. In a recent study, XylT1A was shown to act as core xylosyltransferase,
Anne Oltmanns, Lara Hoepfner, Martin Scholz, Karen Zinzius, Stefan Schulze, Stefan Schulze, Michael Hippler, Michael Hippler   +7 more
doaj   +1 more source