Glycosylation in cellular mechanisms of health and disease.

By K. Ohtsubo, J. Marth. Cell, 2006

2,668 citations recorded by the source corpus.

Glycosylation produces an abundant, diverse, and highly regulated repertoire of cellular glycans that are frequently attached to proteins and lipids. The past decade of research on glycan function has revealed that the enzymes responsible for glycosylation-the glycosyltransferases and glycosidases-are essential in the development and physiology of living organisms. Glycans participate in many key biological processes including cell adhesion, molecular trafficking and clearance, receptor activation, signal transduction, and endocytosis. This review discusses the increasingly sophisticated molecular mechanisms being discovered by which mammalian glycosylation governs physiology and contributes to disease.

Subfields: Immunology, Molecular Biology, Organic Chemistry

View Paper: https://www.semanticscholar.org/paper/a07c491cd59621cabc8fe3ec0e7b22f056a69aae

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Citations in the corpus

Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins (2007, background): “These sugar chains are often covalently attached to underlying proteins or lipids, and form various structures that are cell-type specific and developmentally regulated, typically changing in response to environmental cue”
Post-translational modifications in proteins: resources, tools and prediction methods (2021, background): “This enzymatic process, which is catalyzed by a glycosyltransferase enzyme, usually occurs in the side chain of residues such as Trp, Ala, Arg, Asn, Asp, Ile, Lys, Ser, Thr, Val, Glu, Pro, Tyr, Cys and Gly (6); however, it occurs more frequently on Ser, Thr, Asn and Trp residues in proteins and lipo”
Protein Glycosylation in Cancer (2015, background): “Given the significant role glycans play in the molecular composition of a glycoprotein, alterations in glycosylation can significantly impact overall glycoprotein charge and conformation and therefore readily alter its biological activity (4, 17).”
Sialic acids in the brain: gangliosides and polysialic acid in nervous system development, stability, disease, and regeneration. (2014, background): “Advances in the biochemistry, cell biology, and genetics of glycobiology have provided the means to relate glycan structures to physiology and pathology (351).”
CHARMM-GUI Glycan Modeler for modeling and simulation of carbohydrates and glycoconjugates (2019, background): “Carbohydrate moieties, also referred to as glycans, are one of the most abundant cell components (Ohtsubo and Marth 2006).”
The sweet and sour of cancer: glycans as novel therapeutic targets (2005, background): “significant modification under distinct physiological or pathological conditions [7, 23].”
Death-receptor O-glycosylation controls tumor-cell sensitivity to the proapoptotic ligand Apo2L/TRAIL (2007, background): “O-glycan biosynthesis involves generation and transport of nucleotide-sugar donors to the endoplasmic reticulum and Golgi apparatus, as well as activity of glycosyltransferases and glycosidase”
Protein-glycan interactions in the control of innate and adaptive immune responses (2008, background): “In addition, several carbohydrate structures, such as Tn (GalNAc-α-Ser/Thr, CD175), sialyl Tn (N-acetylneuraminic acid-α6-GalNAc-α-Ser/Thr, CD175s), Thomsen-Friedenreich disaccharide (Gal-β(1-3)-GalNAc, CD176) and (sialylated) Lewis antigens (CD15s) are highly upregulated in malignant cells and have”
A systematic approach to protein glycosylation analysis: a path through the maze. (2010, background): “The modification of the basic glycan structures by intricate dynamics between glycoenzymes (glycosyltransferases, glycosylhydrolases) allows for the generation of cell type–specific glycan expression patterns, which in multicellular organisms are also subject to striking changes—for example, during ”