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his book gathers reviews and articles on the role of O-GlcNAcylation in cancer underlying the pharmacological targeting of the O-GlcNAcylation enzymes OGT and OGA as a promising anticancer strategy. Particular attention is paid to the involvement of O-GlcNAcylation in the regulation of transcription and as a link between nutrition and epigenetic dynamics or cellular energy metabolism. The role of O-GlcNAcylation in metastasis, immune responses, and resistance to chemotherapeutic agents is also discussed.

Glycosylation.

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"Glycobiology is now one of the more rapidly growing fields in the natural sciences, with broad relevance to many areas of basic research, biomedicine, and biotechnology, including the chemistry of carbohydrates, the enzymology of glycan formation and degradation, the recognition of glycans by specific proteins, roles of glycans in complex biological systems, and their analysis or manipulation by various techniques. This fourth edition textbook seeks to provide a basic overview, directed toward the advanced undergraduate or the beginning graduate-level student of molecular and cellular biology and biomedicine"--

Glycoproteins. --- Glycomics. --- Glycosylation.

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O-linked N-acetylglucosamine (O-GlcNAc) is a prevalent post-translational modification of numerous intracellular proteins. This modification has recently emerged as a key regulator of various important biological processes, including gene transcription, stress response, metabolic homeostasis, and immune regulation. Given the critical role of O-GlcNAc in normal physiology, increasing evidence has now demonstrated that deregulation of O-GlcNAc is closely associated with the development and progression of various diseases, including neurodegeneration, cardiovascular disease, and cancer. This book provides a comprehensive overview of the current progress and understanding of this modification in biology, and likely provides new research directions in the future.

Medicine --- Biology --- Cytology. --- Biomedical Research. --- Cell Biology. --- Research. --- Glucosamine. --- Glycosylation.

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Post-translational modifications (PTMs) are widely employed by all living organisms to control the enzymatic activity, localization or stability of proteins on a much shorter time scale than the transcriptional control. In eukarya, global analyses consistently reveal that proteins are very extensively phosphorylated, acetylated and ubiquitylated. Glycosylation and methylation are also very common, and myriad other PTMs, most with a proven regulatory potential, are being discovered continuously. The emergent picture is that PTM sites on a single protein are not independent; modification of one residue often affects (positively or negatively) modification of other sites on the same protein. The best example of this complex behavior is the histone “bar-code” with very extensive cross-talk between phosphorylation, acetylation and methylation sites. Traditionally it was believed that large networks of PTMs exist only in complex eukaryal cells, which exploit them for coordination and fine-tuning of various cellular functions. PTMs have also been detected in bacteria, but the early examples focused on a few important regulatory events, based mainly on protein phosphorylation. The global importance (and abundance) of PTMs in bacterial physiology was systematically underestimated. In recent years, global studies have reported large datasets of phosphorylated, acetylated and glycosylated proteins in bacteria. Other modifications of bacterial proteins have been recently described: pupylation, methylation, sirtuin acetylation, lipidation, carboxylation and bacillithiolation. As the landscape of PTMs in bacterial cells is rapidly expanding, primarily due to advances of detection methods in mass spectrometry, our research field is adapting to comprehend the potential impact of these modifications on the cellular physiology. The field of protein phosphorylation, especially of the Ser/Thr/Tyr type, has been profoundly transformed. We have become aware that bacterial kinases phosphorylate many protein substrates and thus constitute regulatory nodes with potential for signal integration. They also engage in cross-talk and eukaryal-like mutual activation cascades. The regulatory potential of protein acetylation and glycosylation in bacteria is also rapidly emerging, and the cross-talk between acetylation and phosphorylation has been documented. This topic deals with the complexity of the PTM landscape in bacteria, and focus in particular on the physiological roles that PTMs play and methods to study them. The topic is associated to the 1st International Conference on Post-Translational Modifications in Bacteria (September 9-10, 2014, Göttingen, Germany).

Infection --- Phosphorylation --- Hydroxylation --- Protein Kinases --- S-thiolation --- Proteomics --- Bacteria --- Dehydration --- N-glycosylation --- antimicrobial peptides

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This eBook is a collection of articles from a Frontiers Research Topic. Frontiers Research Topics are very popular trademarks of the Frontiers Journals Series: they are collections of at least ten articles, all centered on a particular subject. With their unique mix of varied contributions from Original Research to Review Articles, Frontiers Research Topics unify the most influential researchers, the latest key findings and historical advances in a hot research area! Find out more on how to host your own Frontiers Research Topic or contribute to one as an author by contacting the Frontiers Editorial Office: frontiersin.org/about/contact

Medicine --- Dietetics & nutrition --- prebiotic --- dietary fiber --- gut microbiota --- bovine milk oligosaccharides --- human milk oligosaccharides --- enzymatic glycosylation --- non-digestible carbohydrates --- cross feeding