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Titlebook: Matrix Metalloproteinase Inhibitors in Cancer Therapy; Neil J. Clendeninn,Krzysztof Appelt Book 2001 Springer Science+Business Media New Y

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書(shū)目名稱Matrix Metalloproteinase Inhibitors in Cancer Therapy
編輯Neil J. Clendeninn,Krzysztof Appelt
視頻videohttp://file.papertrans.cn/628/627757/627757.mp4
概述Includes supplementary material:
叢書(shū)名稱Cancer Drug Discovery and Development
圖書(shū)封面Titlebook: Matrix Metalloproteinase Inhibitors in Cancer Therapy;  Neil J. Clendeninn,Krzysztof Appelt Book 2001 Springer Science+Business Media New Y
描述Cutting-edge investigators review the current status of the entire field, from the biology of MMPs through the current clinical studies. The authors include many leading scientists from pharmaceutical companies who present all the latest concepts and results on the preferred design strategies for MMP inhibitors, their molecular mechanisms, and their substrates. In addition, they fully describe their personal research on specific MMP inhibitors, detailing vanguard design strategies, their in vitro activity, the outcome of animal model studies and, where available, their toxicology, safety, efficacy in human clinical trials. .Comprehensive and state-of-the-art, Matrix Metalloproteinase Inhibitors in Cancer Therapy offers basic and clinical investigators alike a richly informative summary of all the latest research on these powerful new drugs, and their high promise as emerging cancer therapeutics..
出版日期Book 2001
關(guān)鍵詞cancer; cancer therapy; clinical trial; oncology; research; toxicology
版次1
doihttps://doi.org/10.1007/978-1-59259-011-7
isbn_softcover978-1-61737-123-3
isbn_ebook978-1-59259-011-7Series ISSN 2196-9906 Series E-ISSN 2196-9914
issn_series 2196-9906
copyrightSpringer Science+Business Media New York 2001
The information of publication is updating

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https://doi.org/10.1007/978-1-59259-011-7cancer; cancer therapy; clinical trial; oncology; research; toxicology
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Cancer Drug Discovery and Developmenthttp://image.papertrans.cn/m/image/627757.jpg
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Research on MMP Inhibitors with Unusual Scaffolds,groups, each as a ligand for the active-site zinc atom of metalloproteases. Several of these inhibitors have been crystallized in complexes with the catalytic domains of various matrix metalloproteinases (MMPs).
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Mark D. Sternlicht PhD,Lisa M. Coussens PhD,Thiennu H. Vu MD, PhD,Zena Werb PhDtion of flows relevant to aircraft, ships, and missiles. Fifty-five papers and 20 brief communications were presented at the Symposium, which was held at the California State University at Long Beach from 21 to 24 January 1985. A panel discussion was chaired by A. M. O. Smith and includeq state- men
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