Protein Tyrosine Phosphatases

Methods and Protocols

AvDamien Thévenin,Jörg P. Müller

Häftad, Engelska, 2024

Del i serien Methods in Molecular Biology

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Beskrivning

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.

Produktinformation

Utgivningsdatum:2024-12-28
Mått:178 x 254 x 19 mm
Vikt:626 g
Format:Häftad
Språk:Engelska
Serie:Methods in Molecular Biology
Antal sidor:318
Upplaga:2
Förlag:Springer-Verlag New York Inc.
ISBN:9781071635711

Utforska kategorier

Biokemi inom Naturvetenskap och teknik
Cellbiologi inom Naturvetenskap och teknik

Innehållsförteckning

Induction of Translational Readthrough on Protein Tyrosine Phosphatases Targeted by Premature Termination Codon Mutations in Human Disease.- Understanding Pseudophosphatase Function through Biochemical Interactions.- CRISPR/Cas9-Mediated Modification of PTP Expression.- Osteoclast Methods in Protein Phosphatase Research.- OT-I TCR Transgenic Mice to Study the Role of PTPN22 in Anti-Cancer Immunity.- Protein-Tyrosine Phosphatases Studied in Zebrafish.- Examining Phosphatases through Immunofluorescent Microscopy.- Identification of Protein Tyrosine Phosphatase (PTP) Substrates.- Kinase-Catalyzed Biotinylation to Identify Phosphatase Substrates (K-BIPS).- Systems-Level Analysis of the Effects of RPTPs on Cellular Signaling Networks.- Detection of Protein Tyrosine Phosphatase Interacting Partners by Mass Spectrometry.- Detecting PTP Protein-Protein Interactions by Fluorescent Immunoprecipitation Analysis (FIPA).- Identifying Transmembrane Interactions in Receptor Protein Tyrosine Phosphatase Homodimerization and Heterodimerization.- Preparation of Oxidized and Reduced PTP4A1 for Structural and Functional Studies.- Measuring the Reversible Oxidation of Protein Tyrosine Phosphatases using a Modified Cysteinyl-Labeling Assay.- Identification and Optimization of Protein Tyrosine Phosphatase Inhibitors via Fragment Ligation.- Targeting Non-Conserved and Pathogenic Cysteines of Protein Tyrosine Phosphatases with Small Molecules.- In Vitro Phosphatase Assays for the Eya2 Tyrosine Phosphatase.- High Throughput Discovery and Characterization of Covalent Inhibitors for Protein Tyrosine Phosphatases.