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Protein Terminal Profiling

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Cover of 'Protein Terminal Profiling'

Table of Contents

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    Book Overview
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    Chapter 1 [14C]-Acetyl-Coenzyme A-Based In Vitro N-Terminal Acetylation Assay
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    Chapter 2 DTNB-Based Quantification of In Vitro Enzymatic N-Terminal Acetyltransferase Activity
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    Chapter 3 SILProNAQ: A Convenient Approach for Proteome-Wide Analysis of Protein N-Termini and N-Terminal Acetylation Quantitation
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    Chapter 4 Profiling of Protein N-Termini and Their Modifications in Complex Samples
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    Chapter 5 Protease Substrate Profiling by N-Terminal COFRADIC
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    Chapter 6 Doublet N-Terminal Oriented Proteomics for N-Terminomics and Proteolytic Processing Identification
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    Chapter 7 Multidimensional Analysis of Protease Substrates and Their Cellular Origins in Mixed Secretomes from Multiple Cell Types
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    Chapter 8 System-Wide Profiling of Protein Amino Termini from Formalin-Fixed, Paraffin-Embedded Tissue Specimens for the Identification of Novel Substrates
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    Chapter 9 Identification of Carboxypeptidase Substrates by C-Terminal COFRADIC
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    Chapter 10 ProC-TEL: Profiling of Protein C-Termini by Enzymatic Labeling
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    Chapter 11 Determining Protease Substrates Within a Complex Protein Background Using the PROtein TOpography and Migration Analysis Platform (PROTOMAP)
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    Chapter 12 Multiplexed Protease Specificity Profiling Using Isobaric Labeling
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    Chapter 13 FPPS: Fast Profiling of Protease Specificity
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    Chapter 14 Profiling of Protease Cleavage Sites by Proteome-Derived Peptide Libraries and Quantitative Proteomics
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    Chapter 15 Prediction of Proteases Involved in Peptide Generation
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    Chapter 16 Live-Cell Imaging of Protease Activity: Assays to Screen Therapeutic Approaches
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    Chapter 17 Protein Translocation Assays to Probe Protease Function and Screen for Inhibitors
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    Chapter 18 Simultaneous Detection of Metalloprotease Activities in Complex Biological Samples Using the PrAMA (Proteolytic Activity Matrix Assay) Method
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    Chapter 19 Synthesis and Application of Activity-Based Probes for Proteases
Attention for Chapter 13: FPPS: Fast Profiling of Protease Specificity
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Chapter title
FPPS: Fast Profiling of Protease Specificity
Chapter number 13
Book title
Protein Terminal Profiling
Published in
Methods in molecular biology, March 2017
DOI 10.1007/978-1-4939-6850-3_13
Pubmed ID
Book ISBNs
978-1-4939-6849-7, 978-1-4939-6850-3
Authors

Matej Vizovišek, Robert Vidmar, Marko Fonović

Editors

Oliver Schilling

Abstract

Profiling of protease specificity is crucial for characterization of these important enzymes that play numerous roles in health and disease. In the past, several proteomic methods have been developed that enable profiling of protease specificities. Although able to identify thousands of protease cleavage events, these degradomics approaches are often time consuming and methodologically challenging, which limits their application to specialized proteomic groups or the laboratories that initially introduced them. The FPPS approach described here (i.e., fast proteomic profiling of protease specificity) is simple and straightforward and produces reliable results comparable to other more elaborate procedures. It employs labeling the novel N-termini generated by the protease under investigation and subsequent peptide fractionation on SAX-C18 Stage Tips. The procedure can be performed in 2 days, does not require peptide enrichment steps, and can thus be implemented in any proteomic laboratory.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 5 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 5 100%

Demographic breakdown

Readers by professional status Count As %
Unspecified 1 20%
Lecturer > Senior Lecturer 1 20%
Student > Ph. D. Student 1 20%
Student > Master 1 20%
Researcher 1 20%
Other 1 20%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 3 60%
Chemical Engineering 1 20%
Unspecified 1 20%
Computer Science 1 20%