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Protein Tyrosine Phosphatases

Methods and Protocols

  • Book
  • © 2024
  • Latest edition

Overview

Editors:
  1. Damien Thévenin

    1. Department of Chemistry, Lehigh University, Bethlehem, USA

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  2. Jörg P. Müller

    1. Center for Molecular Biomedicine, University Hospital, Friedrich Schiller University Jena, Jena, Germany

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    You can also search for this editor in PubMed   Google Scholar

  • Includes cutting-edge methods and protocols
  • Provides step-by-step detail essential for reproducible results
  • Contains key notes and implementation advice from the experts

Part of the book series: Methods in Molecular Biology (MIMB, volume 2743)

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About this book

This second edition volume expands on the previous edition with discussions on the latest advancements in protein tyrosine phosphatases (PTP) research used to investigate these essential enzymes and new inhibitors. The new techniques covered in the chapters of this book include studying enzymes in vitro, in cells, and in animal models through proteomics, genomics, and structural biology. Furthermore, new advances in pharmacology and drug design have contributed to the developing novel therapeutics that target PTPs.  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.

Cutting-edge and comprehensive, Protein Tyrosine Phosphatases: Methods and Protocols, Second Edition is a valuable resource for both experienced and novel researchers in this field, and will lead to discoveries and accelerated progress in the field of PTP, signal transduction, and drug development.

 

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Table of contents (19 protocols)

  1. Front Matter

    Pages i-xi
    Download chapter PDF

  2. Induction of Translational Readthrough on Protein Tyrosine Phosphatases Targeted by Premature Termination Codon Mutations in Human Disease

    • Leire Torices, Caroline E. Nunes-Xavier, Janire Mingo, Sandra Luna, Asier Erramuzpe, Jesús M. Cortés et al.
    Pages 1-19

  3. Understanding Pseudophosphatase Function Through Biochemical Interactions

    • Shantá D. Hinton
    Pages 21-41

  4. CRISPR/Cas9-Mediated Modification of PTP Expression

    • Carolin Lossius, Anne Kresinsky, Laura Quiet, Jörg P. Müller
    Pages 43-56

  5. Osteoclast Methods in Protein Phosphatase Research

    • Nina Reuven, Maayan Barnea-Zohar, Ari Elson
    Pages 57-79

  6. OT-I TCR Transgenic Mice to Study the Role of PTPN22 in Anti-cancer Immunity

    • Rebecca J. Brownlie, Rose Zamoyska, Robert J. Salmond
    Pages 81-92

  7. Protein Tyrosine Phosphatase Studies in Zebrafish

    • Daniëlle T. J. Woutersen, Jisca Majolée, Jeroen den Hertog
    Pages 93-110

  8. Examining Phosphatases Through Immunofluorescent Microscopy

    • Caroline N. Smith, Jessica S. Blackburn
    Pages 111-122

  9. Identification of Protein Tyrosine Phosphatase (PTP) Substrates

    • Sravan Perla, Bin Qiu, Sam Dorry, Jae-Sung Yi, Anton M. Bennett
    Pages 123-133

  10. Kinase-Catalyzed Biotinylation to Identify Phosphatase Substrates (K-BIPS)

    • Hannah J. Bremer, Mary Kay H. Pflum
    Pages 135-152

  11. System-Level Analysis of the Effects of RPTPs on Cellular Signaling Networks

    • Jacqueline Gerritsen, Sophie Rizzo, Damien Thévenin, Forest M. White
    Pages 153-163

  12. Detection of Protein Tyrosine Phosphatase Interacting Partners by Mass Spectrometry

    • Martina Samiotaki, George Panayotou, Panagiotis Chandris
    Pages 165-180

  13. Detecting PTP Protein–Protein Interactions by Fluorescent Immunoprecipitation Analysis (FIPA)

    • Natalia Kruglova, Alexander Filatov
    Pages 181-194

  14. Identifying Transmembrane Interactions in Receptor Protein Tyrosine Phosphatase Homodimerization and Heterodimerization

    • Sophie Rizzo, Damien Thévenin
    Pages 195-209

  15. Preparation of Oxidized and Reduced PTP4A1 for Structural and Functional Studies

    • Ganesan Senthil Kumar
    Pages 211-222

  16. Measuring the Reversible Oxidation of Protein Tyrosine Phosphatases Using a Modified Cysteinyl-Labeling Assay

    • Avinash D. Londhe, Benoit Boivin
    Pages 223-237

  17. Identification and Optimization of Protein Tyrosine Phosphatase Inhibitors Via Fragment Ligation

    • Markus Tiemann, Jörg Rademann
    Pages 239-270

  18. Targeting Nonconserved and Pathogenic Cysteines of Protein Tyrosine Phosphatases with Small Molecules

    • Anthony C. Bishop, Anna Serbina
    Pages 271-283

  19. In Vitro Phosphatase Assays for the Eya2 Tyrosine Phosphatase

    • Christopher Alderman, Aaron Krueger, John Rossi, Heide L. Ford, Rui Zhao
    Pages 285-300

  20. High-Throughput Discovery and Characterization of Covalent Inhibitors for Protein Tyrosine Phosphatases

    • Zihan Qu, Aaron D. Krabill, Zhong-Yin Zhang
    Pages 301-316
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Editors and Affiliations

  • Department of Chemistry, Lehigh University, Bethlehem, USA

    Damien Thévenin

  • Center for Molecular Biomedicine, University Hospital, Friedrich Schiller University Jena, Jena, Germany

    Jörg P. Müller

Bibliographic Information

  • Book Title: Protein Tyrosine Phosphatases

  • Book Subtitle: Methods and Protocols

  • Editors: Damien Thévenin, Jörg P. Müller

  • Series Title: Methods in Molecular Biology

  • DOI: https://doi.org/10.1007/978-1-0716-3569-8

  • Publisher: Humana New York, NY

  • eBook Packages: Springer Protocols

  • Copyright Information: The Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature 2024

  • Hardcover ISBN: 978-1-0716-3568-1Published: 27 December 2023

  • Softcover ISBN: 978-1-0716-3571-1Due: 09 January 2025

  • eBook ISBN: 978-1-0716-3569-8Published: 26 December 2023

  • Series ISSN: 1064-3745

  • Series E-ISSN: 1940-6029

  • Edition Number: 2

  • Number of Pages: XI, 318

  • Number of Illustrations: 88 b/w illustrations, 47 illustrations in colour

  • Topics: Chemistry/Food Science, general, Cell Biology

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