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Titlebook: Matrix Metalloproteinase Protocols; Ian M. Clark Book 20011st edition Humana Press 2001

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书目名称Matrix Metalloproteinase Protocols
编辑Ian M. Clark
视频video
概述Includes supplementary material:
丛书名称Methods in Molecular Biology
图书封面Titlebook: Matrix Metalloproteinase Protocols;  Ian M. Clark Book 20011st edition Humana Press 2001
描述Research in the matrix metalloproteinase field began with the demonstration by Gross and Lapière, in 1962, that resorbing tadpole tail expressed an enzyme that could degrade collagen gels. These humble beginnings have led us to the elucidation of around twenty distinct vertebrate MMPs, along with a variety of homologs from such diverse organisms as sea urchin, plants, nematode worm, and bacteria. This, coupled with four known specific inhibitors of MMPs, the TIMPs, gives a complex picture. Part I of Matrix Metalloproteinase Protocols provides the reader with a selective overview of the MMP arena, and a chance to come to grips with where the field has been, where it is, and where it is going. I hope that this complements all of the methodology that comes later. Part II presents the reader with a diverse set of methods for the expression and purification of MMPs and TIMPs, bringing together the long and often hard-earned experience of a number of researchers. Part III allows the reader to detect MMPs and TIMPs at both the protein and mRNA level, whereas Part IV gives the ability to assay MMP and TIMP activities in a wide variety of circumstances.
出版日期Book 20011st edition
版次1
doihttps://doi.org/10.1385/1592590462
isbn_ebook978-1-59259-046-9Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightHumana Press 2001
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The Matrix Metalloproteinase (MMP) and Tissue Inhibitor of Metalloproteinase (TIMP) Genesssue Inhibitors of Metalloproteinases (TIMPs), which consist of four family members (.). Whereas all four TIMPs can inhibit all MMPs in vitro, preferential TIMP-MMP interactions and tissue-restricted TIMP expression suggest that each TIMP has a specific function (.).
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Models for Gain-of-Function and Loss-of-Function of MMPss and their inhibitors. A number of mouse strains with ectopic expression of normal and mutant proteins have also been made. These transgenic mice are giving us new insights into the processes of development and pathogenesis.
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Expression of Recombinant Matrix Metalloproteinases in ,enase-1, collagenase-3, neutrophil collagenase, and membrane type-1 MMP (.–.). The expression of a truncated form of human stromelysin-1 (SL-1) will be used to illustrate the methods utilized for the expression of a matrix metalloproteinase in . and for its extraction, refolding, and purification
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MMPs and TIMPsagments of resorbing tadpole tail were cultured on reconstituted collagen gels. A collagenolytic enzyme was recovered from the culture medium which could attack native collagen fibrils. Within a short time these studies were extended to show a similar activity in a wide variety of tissues, that the
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Strategies for Cloning New MMPs and TIMPsciated with normal mammalian development and growth, and in the degradative processes accompanying diseases such as rheumatoid arthritis, pulmonary emphysema or tumor cell invasion and metastasis (.). Because of the importance of these proteins in both normal and pathological conditions, over the la
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Structural Studies on MMPs andTIMPs Wolfram Bode and Klaus Maskosogenous protein inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). Disruption of this balance results in serious diseases such as arthritis and tumor growth and metastasis. Knowledge of the tertiary structures of the proteins involved is crucial for understanding their functional prope
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