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Titlebook: Collagen; Methods and Protocol Irit Sagi,Nikolaos A. Afratis Book 2019 Springer Science+Business Media, LLC, part of Springer Nature 2019 E

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發(fā)表于 2025-3-21 19:40:50 | 只看該作者 |倒序瀏覽 |閱讀模式
書目名稱Collagen
副標(biāo)題Methods and Protocol
編輯Irit Sagi,Nikolaos A. Afratis
視頻videohttp://file.papertrans.cn/230/229494/229494.mp4
概述Includes cutting-edge techniques.Provides step-by-step detail essential for reproducible results.Contains key implementation advice from the experts
叢書名稱Methods in Molecular Biology
圖書封面Titlebook: Collagen; Methods and Protocol Irit Sagi,Nikolaos A. Afratis Book 2019 Springer Science+Business Media, LLC, part of Springer Nature 2019 E
描述This detailed volume compiles state-of-the-art protocols that will serve as recipes for scientists researching collagen, an abundant protein with great importance to health and disease, as well as in applications like food, cosmetics, pharmaceuticals, cosmetic surgery, artificial skin, and glue. Beginning with a section on in vitro models for the characterization of collagen formation, the book continues by highlighting large-scale analysis of collagen with mass spectrometry in order to elucidate the proteomics, degradomics, interactomes, and cross-linking of collagen, high resolution imaging approaches for collagen by the use of scanning electron microscopy and multiphoton imaging, as well as the role of collagen during physiological and pathological conditions. Written for the highly successful .Methods in Molecular Biology. series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls.?.Authoritative and practical, .Collagen: Methods and Protocols. is an ideal guide to high quality and repeatable protocols in this vi
出版日期Book 2019
關(guān)鍵詞Extracellular matrix; Connective tissue; Pathology; Collagenous matrix; Fibroblasts
版次1
doihttps://doi.org/10.1007/978-1-4939-9095-5
isbn_ebook978-1-4939-9095-5Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightSpringer Science+Business Media, LLC, part of Springer Nature 2019
The information of publication is updating

書目名稱Collagen影響因子(影響力)




書目名稱Collagen影響因子(影響力)學(xué)科排名




書目名稱Collagen網(wǎng)絡(luò)公開度




書目名稱Collagen網(wǎng)絡(luò)公開度學(xué)科排名




書目名稱Collagen被引頻次




書目名稱Collagen被引頻次學(xué)科排名




書目名稱Collagen年度引用




書目名稱Collagen年度引用學(xué)科排名




書目名稱Collagen讀者反饋




書目名稱Collagen讀者反饋學(xué)科排名




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Production and Characterization of Chemically Cross-Linked Collagen Scaffoldsntation. Herein, we describe techniques to produce cross-linked with glutaraldehyde (GTA; amine terminal cross-linker), 4-arm polyethylene glycol succinimidyl glutarate (4SP; amine terminal cross-linker), diphenyl phosphoryl azide (DPPA; carboxyl terminal cross-linker), and 1-ethyl-3-(3-dimethylamin
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Investigation of Triple-Helix Collagen Hydroxylation by Solid-State NMR Spectroscopydentifying features on an atomic length scale in tissues and protein samples without extensive extraction or purification. Hydroxylation is a key posttranslational modification of collagen that gives rise to distinctive signals in the ssNMR spectrum of collagen proteins. Here we outline the type of
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Measurement of Collagen Cross-Links from Tissue Samples by Mass Spectrometrych as fibrosis or cancer. One of the key contributors in the establishment of a fibrotic state is the abnormal deposition of extracellular matrix and cross-linked proteins, in particular collagen, leading to tissue stiffening and disruption of organ function. The precise and sensitive measurement of
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Mass Spectrometry-Based Proteomics to Define Intracellular Collagen Interactomess that enable robust and accurate determination of collagen interactomes via mass spectrometry-based proteomics. Using collagen type-I as an example, protocols for working with large, repetitive, and GC-rich collagen genes are described, followed by strategies for engineering cells that stably and i
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In Situ Detection of Degraded and Denatured Collagen via Triple Helical Hybridization: New Tool in H arthritis, and fibrosis). Here we describe histological staining of such collagens using fluorescent collagen hybridizing peptide that can specifically bind to collagen strands by folding into triple helix. The method can report the amount of denatured collagen and/or collagen remodeling activity i
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