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Titlebook: Extracellular Matrix Protocols; Charles H. Streuli,Michael E. Grant Book 20001st edition Springer Science+Business Media New York 2000

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發(fā)表于 2025-3-21 19:30:40 | 只看該作者 |倒序瀏覽 |閱讀模式
書目名稱Extracellular Matrix Protocols
編輯Charles H. Streuli,Michael E. Grant
視頻videohttp://file.papertrans.cn/320/319933/319933.mp4
概述Includes supplementary material:
叢書名稱Methods in Molecular Biology
圖書封面Titlebook: Extracellular Matrix Protocols;  Charles H. Streuli,Michael E. Grant Book 20001st edition Springer Science+Business Media New York 2000
描述It is now widely accepted that much of the dynamic function of cells and tissues is regulated from outside the cell by the extracellular matrix. In ad- tion to its conventional role in providing a scaffold for building tissues, the extracellular matrix acts as a directional highway for cellular movement and provides instructional information for promoting survival, proliferation, and differentiation. Indeed, the extracellular matrix is beginning to take a starring role in the choreography of cell and tissue function. The diverse roles of the extracellular matrix are reflected in its highly complicated structure, consisting of an ever increasing number of components. Yet the mechanisms of extracellular matrix assembly and how they influences cell behavior are only just beginning to be understood. In order to solve these problems new methodologies are, of necessity, being developed. Many of these technologies are highly sophisticated and are currently available only in a ha- ful of laboratories. However, we believe that they can readily be transported and established by other researchers. Thus, the purpose of Extracellular Matrix Protocols is to present some of these complicated tech
出版日期Book 20001st edition
版次1
doihttps://doi.org/10.1385/1592590632
isbn_ebook978-1-59259-063-6Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightSpringer Science+Business Media New York 2000
The information of publication is updating

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Quantitative Determination of Collagen Crosslinkse stabilized to provide mechanical strength by a series of intermolecular crosslinks. These links are formed by oxidative deamination of the ε-amino group of the single lysine in the amino and carboxy-telopeptides by lysyl oxidase. The aldehyde thus formed reacts with an ε-amino group of a lysine at
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