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Titlebook: Lectins; Innate immune defens Preetham Elumalai,Sreeja Lakshmi Book 2021 The Editor(s) (if applicable) and The Author(s), under exclusive l

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發(fā)表于 2025-3-21 18:29:02 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書目名稱Lectins
副標(biāo)題Innate immune defens
編輯Preetham Elumalai,Sreeja Lakshmi
視頻videohttp://file.papertrans.cn/584/583393/583393.mp4
概述Examines interactions between Lectin-carbohydrate interactions in the pathophysiology of various disorders.Considers the role of Immune responses by various Lectin types.Examines potential new targets
圖書封面Titlebook: Lectins; Innate immune defens Preetham Elumalai,Sreeja Lakshmi Book 2021 The Editor(s) (if applicable) and The Author(s), under exclusive l
描述.This book reviews the relationship between receptors, carbohydrate moieties, and pathogenic surfaces and lectins’ pathophysiology of immune responses and examines the mechanisms of action of the molecules for the treatment potentials. Increasing evidence has suggested that lectin-carbohydrate interactions perform important roles in various regulations of immune responses, but much remains to be learned about.?.these crucial properties and their interplay with other molecules. In addition, a better understanding of the structural and functional properties of lectin and the activated immune response will be of critical importance for the development of new diagnostic tools and therapeutic strategies. These key areas are the focus of this book, which documents the latest research findings in the field. Evidence is provided for the various lectin types from animal and plant as well as microbial or marine lectins, and this wide range of molecular knowledge directs us to variousdiseases, including infectious diseases and cancer. In presenting state-of-the-art knowledge on the interactions between lectin and its interactions,the book will help to pave the way for the development of novel
出版日期Book 2021
關(guān)鍵詞lectins; mannan-binding lectin; pentraxins; calnexin; carbohydrate recognition domain; innate immune resp
版次1
doihttps://doi.org/10.1007/978-981-16-7462-4
isbn_softcover978-981-16-7464-8
isbn_ebook978-981-16-7462-4
copyrightThe Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Nature Singapor
The information of publication is updating

書目名稱Lectins影響因子(影響力)




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發(fā)表于 2025-3-21 22:20:21 | 只看該作者
Overview of Lectins, process. Various evidences regarding their toxicity profile may be found throughout history, and it was once considered that lectins were only connected with poisonous components. However, recent research demonstrates that lectin science has advanced significantly, and their usage in studies of gly
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,Molecular Basis of Lectin–Carbohydrate Interaction,en conducted from the past two decades. That information shows that it has unique interaction with the small molecules which are predominantly hydrophobic in nature. Also the recent reports show that surface lectins are easier to be expressed with many cells, which as a result are used as recognitio
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發(fā)表于 2025-3-22 13:49:56 | 只看該作者
Animal Lectin,coconjugates in specific animal cells. It controls protein levels in the blood, modulates cell adhesion to glycoprotein production, and binds soluble extracellular and intracellular glycoproteins. Carbohydrates seen in pathogens that are not recognized by immune system host cells are identified by l
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Regulation of Immune Responses by Lectins,e, lactose, N.acetyl glucosamine, and N-acetyl galactosamine with specificity. They perform this function with or without the support of divalent cations. Moreover, some lectins can bind erythrocytes and result in agglutination, and, hence called “phytohaemagglutinin.” Lectins are structurally diver
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發(fā)表于 2025-3-23 08:04:56 | 只看該作者
,Lectin–Carbohydrate Interactions in Pathogenesis,athogenesis is the interaction between the host and pathogen. Lectins are glycan-binding proteins present in all form of organisms, which has important role in cell–cell recognition. In this chapter, a general overview of some pathogen lectin involved in the recognition of the host cell surface glyc
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