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Titlebook: Matrix Metalloproteases; Methods and Protocol Charles A. Galea Book 2017 Springer Science+Business Media LLC 2017 matrix metalloprotease.X-

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发表于 2025-3-21 19:16:31 | 显示全部楼层 |阅读模式
书目名称Matrix Metalloproteases
副标题Methods and Protocol
编辑Charles A. Galea
视频videohttp://file.papertrans.cn/628/627755/627755.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.Includes supplementary materia
丛书名称Methods in Molecular Biology
图书封面Titlebook: Matrix Metalloproteases; Methods and Protocol Charles A. Galea Book 2017 Springer Science+Business Media LLC 2017 matrix metalloprotease.X-
描述.Since the identification of the first matrix metalloprotease (insterstitial collagenase or MMP-1) more than 20 closely related and evolutionarily conserved vertebrate MMPs have been discovered. Chapters in this volume detail methods and protocols on recent advances in the expression and purification of MMPs, biophysical methods such as X-ray crystallography, NMR spectroscopy and small angle X-ray scattering, computational and experimental methods for determining MMP specificity, methods for detecting MMP activity .in vitro. and .in vivo., and methods for the development and characterization of MMP-based inhibitors as potential therapeutics for the treatment of various diseases. Written in the highly 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 laboratory protocols, and tips on troubleshooting and avoiding known pitfalls... Authoritative and practical, .Matrix Metalloproteases: Methods and Protocols .aims to ensure successful results in the further study of this vital field.
出版日期Book 2017
关键词matrix metalloprotease; X-ray crystallography; NMR spectroscopy; small angle X-ray scattering; enzymes; s
版次1
doihttps://doi.org/10.1007/978-1-4939-6863-3
isbn_softcover978-1-4939-8321-6
isbn_ebook978-1-4939-6863-3Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightSpringer Science+Business Media LLC 2017
The information of publication is updating

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Time-Resolved Analysis of Matrix Metalloproteinase Substrates in Complex Samplesrates (TAILS), with the focus on MMP substrate identification and characterization in cell culture supernatants and introduce an automated procedure for the interpretation of time-resolved iTRAQ-TAILS datasets.
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Determining the Substrate Specificity of Matrix Metalloproteases using Fluorogenic Peptide Substrateic MMPs, (b) the collagen preferences of these MMPs, and (c) the relative roles of MMP domains and specific residues in efficient collagenolysis. The present chapter provides an overview of MMP FRET triple-helical substrates and describes how to construct and utilize these substrates.
circumvent
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Mapping the Substrate Recognition Landscapes of Metalloproteases Using Comprehensive Mutagenesistagenesis substrate phage display library. High-throughput sequencing of uncleaved phage at various reaction time points enables ../.. determination for every possible single amino acid substitution at each position of the substrate, providing unprecedented resolution for the interaction between a protease and its substrate.
CT-angiography
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Imaging Matrix Metalloproteases in Spontaneous Colon Tumors: Validation by Correlation with Histopatn early event in the development of colorectal lesions. Although the probe employed serves as a reporter of the activity of MMPs, our method can be applied to any fluorescent probe that targets an early molecular event in the development of colorectal tumors.
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