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Shaping the Immune Landscape in Cancer by Galectin-Driven Regulatory Pathways
(Elsevier, 2016-03-30)
Along with the discovery of tumor-driven inflammatory pathways, there has been a considerable progress over the past 10 years in understanding the mechanisms leading to cancer immunosurveillance and immunoediting. Several ...
Critical role of evolutionarily conserved glycosylation at Asn211in the intracellular trafficking and activity of sialyltransferase ST3Gal-II
(Portland Press, 2015-07)
ST3Gal-II, a type II transmembrane protein, is the main mammalian sialyltransferase responsible for GD1a and GT1b ganglioside biosynthesis in brain. It contains two putative N-glycosylation sites (Asn92 and Asn211). Whereas ...
Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals
(American Society for Cell Biology, 2009-07)
Glucosidase II (GII) plays a key role in glycoprotein biogenesis in the endoplasmic reticulum (ER). It is responsible for the sequential removal of the two innermost glucose residues from the glycan (Glc(3)Man(9)GlcNAc(2)) ...
N-glycan trimming by glucosidase II is essential for Arabidopsis development
(Springer, 2008-10)
Glucosidase II, one of the early N-glycan processing enzymes and a major player in the glycoprotein folding quality control, has been described as a soluble heterodimer composed of alpha and beta subunits. Here we present ...
The Arabidopsis Golgi-localized GDP-L-fucose transporter is required for plant development
(NATURE PUBLISHING GROUP, 2016-07)
Nucleotide sugar transport across Golgi membranes is essential for the luminal biosynthesis of glycan structures. Here we identify GDP-fucose transporter 1 (GFT1), an Arabidopsis nucleotide sugar transporter that translocates ...
Core 1 O-N-acetylgalactosamine (O-GalNAc) glycosylation in the human cell nucleus
(De Gruyter, 2020-08)
Glycosylation is a very frequent post-translational modification in proteins, and the initiation of O-N-acetylgalactosamine (O-GalNAc) glycosylation has been recently described on relevant nuclear proteins. Here we evaluated ...
When galectins recognize glycans: From biochemistry to physiology and back again
(American Chemical Society, 2011-09)
In the past decade, increasing efforts have been devoted to the study of galectins, a family of evolutionarily conserved glycan-binding proteins with multifunctional properties. Galectins function, either intracellularly ...
Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunit
(National Academy of Sciences, 2006-10)
Most eukaryotic cells show a strong preference for the transfer in vivo and in vitro of the largest dolichol-P-P-linked glycan (Glc3Man 9GlcNAc2) to protein chains over that of biosynthetic intermediates that lack the full ...