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Matrix Metalloproteases

Overview of attention for book
Cover of 'Matrix Metalloproteases'

Table of Contents

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    Book Overview
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    Chapter 1 Expression and Purification of Matrix Metalloproteinases in Escherichia coli
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    Chapter 2 Expression and Purification of a Matrix Metalloprotease Transmembrane Domain in Escherichia coli
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    Chapter 3 Heterologous Expression of the Astacin Protease Meprin β in Pichia pastoris
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    Chapter 4 Structural Studies of Matrix Metalloproteinase by X-Ray Diffraction
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    Chapter 5 Mapping Lipid Bilayer Recognition Sites of Metalloproteinases and Other Prospective Peripheral Membrane Proteins
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    Chapter 6 Using Small Angle X-Ray Scattering (SAXS) to Characterize the Solution Conformation and Flexibility of Matrix Metalloproteinases (MMPs)
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    Chapter 7 Molecular Dynamics Studies of Matrix Metalloproteases
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    Chapter 8 Determining the Substrate Specificity of Matrix Metalloproteases using Fluorogenic Peptide Substrates
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    Chapter 9 Time-Resolved Analysis of Matrix Metalloproteinase Substrates in Complex Samples
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    Chapter 10 Identification of Protease Cleavage Sites by Charge-Based Enrichment of Protein N-Termini
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    Chapter 11 Mapping the Substrate Recognition Landscapes of Metalloproteases Using Comprehensive Mutagenesis
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    Chapter 12 Detection of Matrix Metalloproteinases by Zymography
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    Chapter 13 Imaging Matrix Metalloproteases in Spontaneous Colon Tumors: Validation by Correlation with Histopathology
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    Chapter 14 Virtual High-Throughput Screening for Matrix Metalloproteinase Inhibitors
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    Chapter 15 Computational Approaches to Matrix Metalloprotease Drug Design
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    Chapter 16 A Simple Adaptable Blood-Brain Barrier Cell Model for Screening Matrix Metalloproteinase Inhibitor Functionality
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    Chapter 17 Matrix Metalloproteases as Biomarkers of Disease
Attention for Chapter 10: Identification of Protease Cleavage Sites by Charge-Based Enrichment of Protein N-Termini
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Chapter title
Identification of Protease Cleavage Sites by Charge-Based Enrichment of Protein N-Termini
Chapter number 10
Book title
Matrix Metalloproteases
Published in
Methods in molecular biology, March 2017
DOI 10.1007/978-1-4939-6863-3_10
Pubmed ID
28299738
Book ISBNs
978-1-4939-6861-9, 978-1-4939-6863-3
Authors

Zon W. Lai, Oliver Schilling

Editors

Charles A. Galea

Abstract

Differential proteolytic processing, for example by matrix metalloproteases (MMPs), has been recognized as an important hallmark in numerous pathological conditions. One crucial challenge in the present studies of proteases is system-wide identification of endogenous biological substrates. In this chapter, we highlight a robust method for the identification of bioactive substrates and their sites of MMP cleavage, as well as by other proteases and peptidases, in a system-wide manner. This approach enriches for putative protein N-termini by removal of internal peptides using a charge reversal strategy. In addition, this straightforward method can be used in combination with gel-based pre-separation of proteins to allow better estimation of the molecular weight of the identified cleavage product of a given bioactive substrate.

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The data shown below were collected from the profile of 1 X user who shared this research output. Click here to find out more about how the information was compiled.
 Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 3 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 3 100%

Demographic breakdown

Readers by professional status Count As %
Unspecified 1 33%
Researcher 1 33%
Unknown 1 33%
Readers by discipline Count As %
Unspecified 1 33%
Medicine and Dentistry 1 33%
Unknown 1 33%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 21 March 2017.
All research outputs
#20,410,007
of 22,959,818 outputs
Outputs from Methods in molecular biology
#9,919
of 13,136 outputs
Outputs of similar age
#268,999
of 308,429 outputs
Outputs of similar age from Methods in molecular biology
#245
of 313 outputs
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So far Altmetric has tracked 13,136 research outputs from this source. They receive a mean Attention Score of 3.4. This one is in the 1st percentile – i.e., 1% of its peers scored the same or lower than it.
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