Results 11 to 20 of about 155,076 (257)
Frontiers in Cell and Developmental Biology, 2022 Glycosylation is a ubiquitous and universal cellular process in all domains of life. In eukaryotes, many glycosylation pathways occur simultaneously onto proteins and lipids for generating a complex diversity of glycan structures.
Zoé Durin +7 more
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Studying Lactoferrin N-Glycosylation [PDF]
International Journal of Molecular Sciences, 2017 Lactoferrin is a multifunctional glycoprotein found in the milk of most mammals. In addition to its well-known role of binding iron, lactoferrin carries many important biological functions, including the promotion of cell proliferation and differentiation, and as an anti-bacterial, anti-viral, and anti-parasitic protein.
Sercan Karav +4 more
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GlypNirO: An automated workflow for quantitative N- and O-linked glycoproteomic data analysis
Beilstein Journal of Organic Chemistry, 2020 Mass spectrometry glycoproteomics is rapidly maturing, allowing unprecedented insights into the diversity and functions of protein glycosylation. However, quantitative glycoproteomics remains challenging.
Toan K. Phung +2 more
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Stereoselective N-Glycosylation by Staudinger Ligation [PDF]
Organic Letters, 2004 AbstractFor Abstract see ChemInform Abstract in Full Text.
Yi, He +3 more
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Unraveling the Mechanism of Protein N-Glycosylation [PDF]
Journal of Biological Chemistry, 2005 Asparagine-linked glycosylation is the most ubiquitous protein co-translational modification in the endoplasmic reticulum (ER). The enzyme that catalyzes this process is called oligosaccharyl transferase (OT). It catalyzes the transfer of an oligosaccharyl moiety (Glc3Man9GlcNAc2) from the dolichol-linked pyrophosphate donor to the side chain of Asn ...
Lennarz, WJ, Yan, A
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Comparison of Fc N-Glycosylation of Pharmaceutical Products of Intravenous Immunoglobulin G. [PDF]
PLoS ONE, 2015 Intravenous immunoglobulin (IVIg) products from different pharmaceutical companies vary in composition, in part because of the selected blood donors and production process.
Willem Jan R Fokkink +5 more
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The Impact of N-Glycosylation on the Functions of Polysialyltransferases [PDF]
Journal of Biological Chemistry, 2001 Poly-alpha-2,8-sialic acid (polysialic acid) is a post-translational modification of the neural cell adhesion molecule (NCAM) and an important regulator of neuronal cell-cell interactions. The synthesis of polysialic acid depends on the two polysialyltransferases ST8SiaII and ST8SiaIV.
M, Mühlenhoff +4 more
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Extracellular Domain N-Glycosylation Controls Human Thrombopoietin Receptor Cell Surface Levels
Frontiers in Endocrinology, 2011 The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation and hematopoietic stem cell renewal.
Roxana I. Albu +1 more
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Proteome-wide analysis of single-nucleotide variations in the N-glycosylation sequon of human genes. [PDF]
PLoS ONE, 2012 N-linked glycosylation is one of the most frequent post-translational modifications of proteins with a profound impact on their biological function.
Raja Mazumder +4 more
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N-glycosylation is required for secretion and enzymatic activity of human hyaluronidase1
FEBS Open Bio, 2014 Hyaluronidase1 (HYAL1) is a hydrolytic enzyme that degrades hyaluronic acid (HA) and has three predicted N-glycosylation sites at Asn99, Asn216, and Asn350. In this report, we show the functional significance of N-glycosylation on HYAL1 functions.
Yuki Goto +5 more
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