Results 41 to 50 of about 17,134 (208)
A new superfamily of protein-O-fucosyltransferases, 2-fucosyltransferases, and 6-fucosyltransferases: phylogeny and identification of conserved peptide motifs [PDF]
The presence of three conserved peptide motifs shared by alpha2-fucosyltransferases, alpha6-fucosyltransferases, the protein-O-fucosyltransferase family 1 (POFUT1) and a newly identified protein-O-fucosyltransferase family 2 (POFUT2), together with evidence that the present genes encoding for these enzymes have originated from a common ancestor by ...
Ivan, Martinez-Duncker +4 more
openaire +2 more sources
Identification of the Plasticity-Relevant Fucose-α(1−2)-Galactose Proteome from the Mouse Olfactory Bulb [PDF]
Fucose-α(1−2)-galactose [Fucα(1−2)Gal] sugars have been implicated in the molecular mechanisms that underlie neuronal development, learning, and memory. However, an understanding of their precise roles has been hampered by a lack of information regarding
Domino, Steven E. +5 more
core +4 more sources
Fucosyltransferase 2 inhibitors: Identification via docking and STD-NMR studies.
Fucosyltransferase 2 (FUT2) catalyzes the biosynthesis of A, B, and H antigens and other important glycans, such as (Sialyl Lewisx) sLex, and (Sialyl Lewisy) sLey.
Humaira Zafar +3 more
doaj +1 more source
Human α1,3/4 Fucosyltransferases [PDF]
residues, in addition to a free Cys residue that lies near the binding site for GDP-fucose (Holmes, E. H.,
Eric H. Holmes +9 more
openaire +3 more sources
Fucosyllactoses (FL), including 2′‐fucosyllactose (2′‐FL) and 3‐fucosyllactose (3‐FL), have garnered considerable interest for their value in newborn formula and pharmaceuticals.
Mengli Li +5 more
doaj +1 more source
Over half of all proteins are glycosylated, and alterations in glycosylation have been observed in numerous physiological and pathological processes.
Gordan Lauc +25 more
doaj +1 more source
Structural basis for substrate specificity and catalysis of α1,6-fucosyltransferase
Core-fucosylation of the N-glycan core is an essential biological modification and the α1,6- fucosyltransferase FUT8 is the only enzyme in humans that catalyses this modification through the addition of an α-1,6-linked fucose to N-glycans.
Ana García-García +6 more
doaj +1 more source
Fucosyltransferase 1 Mediates Angiogenesis in Rheumatoid Arthritis [PDF]
Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/108009/1/art38648 ...
Amin +45 more
core +1 more source
Cellular adaptations to change often involve post-translational modifications of nuclear and cytoplasmic proteins. An example found in protists and plants is the modification of serine and threonine residues of dozens to hundreds of nucleocytoplasmic ...
Megna Tiwari +11 more
doaj +1 more source
α-1,6-Fucosyltransferase Is Essential for Myogenesis in Zebrafish
Glycosylation is an important mechanism regulating various biological processes, including intercellular signaling and adhesion. α-1,6-fucosyltransferase (Fut8) belongs to a family of enzymes that determine the terminal structure of glycans.
Nozomi Hayashiji +7 more
doaj +1 more source

