Results 21 to 30 of about 10,478,036 (300)
Medical Mycology, 2001 O-Glycosylation in many fungal species is initiated in the endoplasmic reticulum by protein mannosyltransferases (Pmt-proteins), which transfer mannose to serine or threonine residues, and it is completed by mannosyltransferases (Mnt-proteins) in the Golgi.
J F, Ernst, S K, Prill
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O-Glycosylation of snails [PDF]
Glycoconjugate Journal, 2012 The glycosylation abilities of snails deserve attention, because snail species serve as intermediate hosts in the developmental cycles of some human and cattle parasites. In analogy to many other host-pathogen relations, the glycosylation of snail proteins may likewise contribute to these host-parasite interactions. Here we present an overview on the O-
Stepan, Herwig +5 more
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Abnormal B cell glycosylation in autoimmunity: A new potential treatment strategy
Frontiers in Immunology, 2022 Systemic lupus erythematosus (SLE) and primary Sjögren’s syndrome (pSS) are two autoimmune diseases characterised by the production of pathogenic autoreactive antibodies. Their aetiology is poorly understood. Nevertheless, they have been shown to involve
Marie Morel +18 more
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Chemical O‐Glycosylations: An Overview [PDF]
ChemistryOpen, 2016 AbstractThe development of glycobiology relies on the sources of particular oligosaccharides in their purest forms. As the isolation of the oligosaccharide structures from natural sources is not a reliable option for providing samples with homogeneity, chemical means become pertinent.
Das, Rituparna, Mukhopadhyay, Balaram
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Nucleocytoplasmic O-glycosylation in protists [PDF]
Current Opinion in Structural Biology, 2019 O-Glycosylation is an increasingly recognized modification of intracellular proteins in all kingdoms of life, and its occurrence in protists has been investigated to understand its evolution and its roles in the virulence of unicellular pathogens. We focus here on two kinds of glycoregulation found in unicellular eukaryotes: one is a simple O-fucose ...
Christopher M, West, Hyun W, Kim
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N- and O-Glycosylation in the Murine Synaptosome [PDF]
Molecular & Cellular Proteomics, 2013 We present the first large scale study characterizing both N- and O-linked glycosylation in a site-specific manner on hundreds of proteins. We demonstrate that a lectin-affinity fractionation step using wheat germ agglutinin enriches not only peptides carrying intracellular O-GlcNAc, but also those bearing ER/Golgi-derived N- and O-linked carbohydrate ...
Trinidad, Jonathan C +3 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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mAbs, 2021 Bioconjugates are an important class of therapeutic molecules. To date, O-glycan-based metabolic glycoengineering has had limited use in this field, due to the complexities of the endogenous O-glycosylation pathway and the lack of an O-glycosylation ...
Thomas V. Murray +13 more
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A Sweet Warning: Mucin-Type O-Glycans in Cancer
Cells, 2022 Glycosylation is a common post-translational modification process of proteins. Mucin-type O-glycosylation is an O-glycosylation that starts from protein serine/threonine residues.
Yuhan Zhang +6 more
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Prediction Of O-Glycosylation Site Using Pre-Trained Language Model And Machine Learning [PDF]
International Journal of Intelligent Computing and Information Sciences, 2023 O-glycosylation is a typical type of protein post-translational modifications (PTMs), which is linked to several diseases and has significant roles in many biological processes.
Alhasan Alkuhlani +3 more
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