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Glycoproteomics is a rapidly growing field which seeks to identify and characterise glycosylation events at a proteome scale. Over the last few years considerable effort has been made in developing new technologies, enrichment systems, and analysis strategies to enhance the quality of glycoproteomic studies. Within this review we discuss the recent developments in glycoproteomics and the current state of the art approaches for analysing glycosylated substrates. We highlight key improvements in mass spectrometry instrumentation coupled with the advancements in enrichment approaches for key classes of glycosylation including mucin-O-glycosylation, O-GlcNAc glycosylation and N-linked glycosylation which now allow the identification/quantification of hundreds to thousands of glycosylation sites within individual experiments. Finally, we summarise the emerging trends within glycoproteomics to illustrate how the field is moving away from studies simply focused on identifying glycosylated substrates to studying specific mechanisms and disease states.
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http://dx.doi.org/10.1016/j.sbi.2020.10.028 | DOI Listing |
Planta
September 2025
Plant Sciences and Agro-Technology Division, CSIR-Indian Institute of Integrative Medicine, Canal Road, Jammu, 180001, India.
The Fabaceae-specific review highlights the structural, functional, and phylogenetic diversity of UGTs, revealing clade-specific glycosylation mechanisms and novel sugar conjugations that contribute to legume adaptability. These insights offer promising avenues for metabolic engineering and stress-resilient crop development. UDP-glycosyltransferases (UGTs) are the biocatalysts modifying small molecules through glycosylation to enhance their solubility, stability, and bioactivity.
View Article and Find Full Text PDFBrain
September 2025
Institute of Neuroscience, Kunming Medical University, Kunming 650500, Yunnan Province, China.
The hippocampus (HC), a central hub for memory and cognition, exhibits unique metabolic resilience during aging despite widespread brain glucose hypometabolism. Here, we report that aged humans and macaques paradoxically display elevated HC glucose uptake (18F-FDG PET SUVR) alongside strengthened connectivity to sensory-motor and limbic networks-an adaptive rewiring revealed by graph-theoretical metabolic network analysis. Integrated multi-omics profiling identified STT3A (oligosaccharyltransferase) and ALG5 (dolichyl-phosphate β-glucosyltransferase) as key regulators of age-related HC adaptation, with their upregulation in aged macaque hippocampi driving N-glycosylation-dependent metabolic reprogramming.
View Article and Find Full Text PDFInt J Biol Macromol
September 2025
Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan.
Sodium-glucose cotransporter 2 (SGLT2) inhibitors are antidiabetic drugs developed using phlorizin, a natural glucoside, as the lead compound. Chemical glycosylation requires multi-step reactions involving protection and deprotection steps, posing challenges in terms of regioselectivity and environmental burden due to the use of hazardous reagents and harsh conditions. In contrast, enzymatic glycosylation using UDP-glucosyltransferases (UGTs) enables regio- and stereoselective glycosylation under mild conditions without protection and deprotection steps.
View Article and Find Full Text PDFOrg Biomol Chem
September 2025
Department of Medicinal Chemistry, Institute of Medical Sciences, Banaras Hindu University, Varanasi-221005, India.
The stereoselective formation of glycosidic bonds remains a key challenge in carbohydrate chemistry, with far-reaching implications for glycoscience, drug development, and materials research. We report a novel method for glycosylation of glycal-derived substrates mediated by Ru(II) catalysis. Glycosylation selectivity is modulated by the presence or absence of external nucleophiles in the reaction medium.
View Article and Find Full Text PDFJ Biol Chem
August 2025
Institute of Plant Biotechnology and Cell Biology, Department of Biotechnology and Food Sciences, BOKU University; Vienna, Austria. Electronic address:
N-glycosylation is essential for protein folding in the endoplasmic reticulum (ER). Glycan attachment facilitates the binding of newly synthesised polypeptides to calnexin and calreticulin, two ER-resident lectins that act as chaperones and promote folding. The regulatory mechanism underlying this process is dictated by the glycan composition, and this study has elucidated the function of mannose trimming in the release of misfolded glycoprotein from ER quality control and subsequent transfer to ER-associated degradation (ERAD) in plants.
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