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Titlebook: Glycovirology; Methods and Protocol Yasuo Suzuki Book 2022 The Editor(s) (if applicable) and The Author(s), under exclusive license to Spri

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發(fā)表于 2025-3-21 16:57:10 | 只看該作者 |倒序瀏覽 |閱讀模式
書目名稱Glycovirology
副標(biāo)題Methods and Protocol
編輯Yasuo Suzuki
視頻videohttp://file.papertrans.cn/388/387121/387121.mp4
概述Includes cutting-edge methods and protocols.Provides step-by-step detail essential for reproducible results.Contains key notes and implementation advice from the experts
叢書名稱Methods in Molecular Biology
圖書封面Titlebook: Glycovirology; Methods and Protocol Yasuo Suzuki Book 2022 The Editor(s) (if applicable) and The Author(s), under exclusive license to Spri
描述.This volume details applications in molecular biological techniques and focuses on applications to determine the involvement of glycans in virus interactions. Chapters guide readers through glycan analysis, glycan distribution analysis, glycan and lectin microarray, preparation of recombinant viral domain protein, reverse genetics and receptor binding, virus-host interactions and receptor binding, and sialidase: assays and inhibitors.?Written in the successful?.Methods in Molecular Biology.?series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible protocols, and notes on troubleshooting and avoiding known pitfalls...?Authoritative and cutting-edge,?.Glycovirology: Methods and Protocols?.aims?to be?an essential resource for researchers who wish to learn more about glycovirology...?.
出版日期Book 2022
關(guān)鍵詞Glycans; Viral diseases; Host cells; Host-virus interactions; Enzymology; Carbohydrate chemistry
版次1
doihttps://doi.org/10.1007/978-1-0716-2635-1
isbn_softcover978-1-0716-2637-5
isbn_ebook978-1-0716-2635-1Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightThe Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Science+Busines
The information of publication is updating

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Preparation of Glycan Arrays Using Glycopeptides Derived From Biomaterials, only because commercially available, structure-defined glycans are limited, but also because such interactions, if any, between viruses and isolated glycans are relatively weak, and thus, difficult to detect by conventional methods, e.g., enzyme-linked immune-sorbent assay. We describe a practical
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發(fā)表于 2025-3-22 13:58:28 | 只看該作者
Glycan Profiling of Viral Glycoproteins with the Lectin Microarray,at glycoform of the viral glycoproteins is closely related to their immunogenicity as vaccine antigens. Although mass spectrometric approach is a gold standard for the glycoproteomic analysis of viral glycoproteins, lectin microarray (LMA) is regarded as an alternative method for analyzing glycan at
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發(fā)表于 2025-3-22 18:29:12 | 只看該作者
Preparation of Recombinant PA Endonuclease Domain Protein of Influenza A Virus and Its Application influenza A virus drugs such as glycoconjugates. To test this activity, purified viral PA endonuclease domain protein is necessary. Here, we describe a method for the expression and purification of recombinant influenza A virus PA endonuclease domain protein, and a PA endonuclease assay to test glyc
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發(fā)表于 2025-3-22 23:10:35 | 只看該作者
Receptor-Binding Specificity of Influenza Viruses,hment is mediated by the viral surface glycoprotein hemagglutinin (HA). Influenza A viruses have a wide host range, meaning they are able to infect many mammal and bird species. Influenza pandemics have been caused by viruses that contain genes from avian influenza viruses. Therefore, the infection
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發(fā)表于 2025-3-23 03:24:53 | 只看該作者
Functional Analysis of Sulfatide in Influenza A Virus Infection and Replication,tract, trachea, kidney, and central nervous system. Influenza A virus binds not only to glycoconjugates terminally containing sialic acid as a viral binding receptor but also to sulfatide not containing sialic acid. On the surface of infected cells, the envelope glycoprotein hemagglutinin of influen
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發(fā)表于 2025-3-23 09:07:25 | 只看該作者
Quantification of Receptor Association, Dissociation, and NA-Dependent Motility of Influenza A Partinylated synthetic sialoglycans or sialoglycoproteins (biotinylated or Fc-tagged) were immobilized on the tip of biosensors (coated with streptavidin or protein A) that were subsequently dipped into IAV particle solutions in 96-well plates. Association and/or dissociation of IAV particles was record
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