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Titlebook: Glycobiology of Innate Immunology; Cheorl-Ho Kim Book 2022 The Editor(s) (if applicable) and The Author(s), under exclusive license to Spr

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发表于 2025-3-21 17:55:46 | 显示全部楼层 |阅读模式
书目名称Glycobiology of Innate Immunology
编辑Cheorl-Ho Kim
视频video
概述Presents the latest research results in the field.Covers all aspects of glycan-mediated signaling and its regulations.Examines various glycan interactions during infection and inflammation
图书封面Titlebook: Glycobiology of Innate Immunology;  Cheorl-Ho Kim Book 2022 The Editor(s) (if applicable) and The Author(s), under exclusive license to Spr
描述.This book presents the latest knowledge and the most recent research results on glycobiology of innate immunology. Innate immunity is the crucial part of the immunological defense system that exerts their distinct functions through binding to certain functional glycoproteins. They play a role in various human diseases and also function against microbial invaders and self-associated molecular patterns. Co-regulated expression of glycan-binding is associated with many biological components such as cellular oncotransformation, phenotype change, neuronal or embryonic development, regulation of cell division, cell–cell interaction, cell attachment, adhesion, and motility, and intracellular signaling via protein–carbohydrate or carbohydrate–carbohydrate interactions..This book opens by providing the key background on glycans in innate immunity and its mechanisms behind the Dendritic cell interactions during infection and inflammation are examined in depth, and the concluding chapteris devoted to signaling tumor immunotherapy. Up-to-date information is then presented on all aspects of glycan structure-recognizing signaling. The book should assist in the further development of new strateg
出版日期Book 2022
关键词Glycobiology; innate immunology; Glycans; dendritic cell; Glycan regulation; trafficking; Glycan structure
版次1
doihttps://doi.org/10.1007/978-981-16-9081-5
isbn_softcover978-981-16-9083-9
isbn_ebook978-981-16-9081-5
copyrightThe Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Nature Singapor
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发表于 2025-3-21 21:17:53 | 显示全部楼层
Book 2022ractions during infection and inflammation are examined in depth, and the concluding chapteris devoted to signaling tumor immunotherapy. Up-to-date information is then presented on all aspects of glycan structure-recognizing signaling. The book should assist in the further development of new strateg
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https://doi.org/10.1007/978-3-658-22368-7ion of complement pathways. Oligosaccharide structures of cell surface and soluble glycans encode complex information. Like the stepwise recognition, cellular information is being decoded by carbohydrate-binding molecules, and these carbohydrates regulate the interaction between cells and cells or i
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Bt Cotton and the Legitimation of Democracy,cs was discovered, for example, Siglec-2 (or CD22) present on B cells. Siglec-1, known as sialoadhesin present on macrophage surfaces, was found. The Ig-like domains of such lectins are different from those of other known C-type lectins or Ca.-dependent lectins. Among them, I-type lectins are named
发表于 2025-3-22 22:54:50 | 显示全部楼层
https://doi.org/10.1007/978-3-8349-4113-8ostatic regulation, recognizing self-antigens to allow tolerance from the tissue environment. Therefore, one question is how the nature of the recognized antigens takes the balance between immunity and tolerance. CLRs expressed on DCs substantially recognize and bind glycosylated self-antigens and p
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Semantiken der Ungleichheitslegitimationlian galectins, encoded by the LGALS genes, are known. Galectins are lectins with carbohydrate-binding capacity. Among them, Galectins-1, -2, -3, -4, -7, -8, -9, -10, -12, and -13 are found in human. They bind glycosylated receptors. Many galectin types recognize their ligands in either bivalent or
发表于 2025-3-23 08:02:25 | 显示全部楼层
https://doi.org/10.1007/978-3-658-16036-4immune DC-SIGN receptor is also called CD209 and discovered over two decades ago. It recognizes a broad ligand structure of pathogen-derived patterns and self-glycoproteins. DC-SIGN functions for intercellular adhesion, antigen uptake, and signaling, crucial for DCs, although most studies on DC-SIGN
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