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Glycosylation

About: Glycosylation is a research topic. Over the lifetime, 18900 publications have been published within this topic receiving 719461 citations.


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01 Aug 1999
TL;DR: General principles - historical background and overview saccharide structure and nomenclature evolution of glycan diversity protein-glycan Interactions exploring the biological roles of glycans biosynthesis, metabolism, and function.
Abstract: General principles - historical background and overview saccharide structure and nomenclature evolution of glycan diversity protein-glycan Interactions exploring the biological roles of glycans biosynthesis, metabolism, and function - monosaccharide metabolism N-glycans O-glycans glycosphingolipids glycophospholipid anchors proteoglycans and glycosaminoglycans other classes of golgi-derived glycans nuclear and cytoplasmic glycosylation the O-GlcNAc modification sialic acids structures common to different types of glycans glycosyltransferases degradation and turnover of glycans glycosylation in "model" organisms glycobiology of plant cells bacterial polysaccharides proteins that recognize glycans - discovery and classification of animal lectins P-type lectins I-type lectins C-type lectins selectins S-type lectins (galectins) microbial glycan-binding proteins glycosaminoglycan-binding proteins plant lectins glycans in genetic disorders and disease - genetic disorders of glycosylation in cultured cells naturally occurring genetic disorders of glycosylation in animals determining glycan function using genetically modified mice glycosylation changes in ontogeny and cell activation glycosylation changes in cancer glycobiology of protozoal and helminthic parasites acquired glycosylation changes in human disease methods and applications - structural analysis and sequencing of glycans chemical and enzymatic synthesis of glycans natural and synthetic inhibitors of glycosylation glycobiology in biotechnology and medicine.

3,001 citations

Journal ArticleDOI
08 Sep 2006-Cell
TL;DR: This review discusses the increasingly sophisticated molecular mechanisms being discovered by which mammalian glycosylation governs physiology and contributes to disease.

2,376 citations

Journal ArticleDOI
Ari Helenius1, Markus Aebi
TL;DR: From a process involved in cell wall synthesis in archaea and some bacteria, N-linked glycosylation has evolved into the most common covalent protein modification in eukaryotic cells.
Abstract: From a process involved in cell wall synthesis in archaea and some bacteria, N-linked glycosylation has evolved into the most common covalent protein modification in eukaryotic cells. The sugars are added to nascent proteins as a core oligosaccharide unit, which is then extensively modified by removal and addition of sugar residues in the endoplasmic reticulum (ER) and the Golgi complex. It has become evident that the modifications that take place in the ER reflect a spectrum of functions related to glycoprotein folding, quality control, sorting, degradation, and secretion. The glycans not only promote folding directly by stabilizing polypeptide structures but also indirectly by serving as recognition "tags" that allow glycoproteins to interact with a variety of lectins, glycosidases, and glycosyltranferases. Some of these (such as glucosidases I and II, calnexin, and calreticulin) have a central role in folding and retention, while others (such as alpha-mannosidases and EDEM) target unsalvageable glycoproteins for ER-associated degradation. Each residue in the core oligosaccharide and each step in the modification program have significance for the fate of newly synthesized glycoproteins.

1,945 citations

Journal ArticleDOI
TL;DR: The roles of glycans are highlighted by the fact that alterations in glycosylation regulate the development and progression of cancer, serving as important biomarkers and providing a set of specific targets for therapeutic intervention.
Abstract: Despite recent progress in understanding the cancer genome, there is still a relative delay in understanding the full aspects of the glycome and glycoproteome of cancer. Glycobiology has been instrumental in relevant discoveries in various biological and medical fields, and has contributed to the deciphering of several human diseases. Glycans are involved in fundamental molecular and cell biology processes occurring in cancer, such as cell signalling and communication, tumour cell dissociation and invasion, cell-matrix interactions, tumour angiogenesis, immune modulation and metastasis formation. The roles of glycans in cancer have been highlighted by the fact that alterations in glycosylation regulate the development and progression of cancer, serving as important biomarkers and providing a set of specific targets for therapeutic intervention. This Review discusses the role of glycans in fundamental mechanisms controlling cancer development and progression, and their applications in oncology.

1,920 citations

Journal ArticleDOI
TL;DR: RAGE is a new member of the immunoglobulin superfamily of cell surface molecules and shares significant homology with MUC 18, NCAM, and the cytoplasmic domain of CD20 and could potentially mediate cellular effects of this class of glycosylated proteins.

1,507 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023795
20221,426
2021728
2020727
2019602
2018590