Targeting the reversibly oxidized protein tyrosine phosphatase superfamily

Boivin, B., Tonks, N. K. , Yang, M. (August 2010) Targeting the reversibly oxidized protein tyrosine phosphatase superfamily. Science Signaling, 3 (137).

Abstract

Controlled production of reactive oxygen species leads to reversible oxidation of protein tyrosine phosphatases (PTPs) and has emerged as an important tier of regulation over phosphorylation-dependent signal transduction. We present a modified cysteinyl-labeling assay that detects reversible oxidation of members of each of the different PTP subclasses. Here, we describe the methods for enriching reversibly oxidized PTPs from complex protein extracts, illustrating the procedure in IMR90 fibroblasts.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > design > protein design
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > Mapping and Rendering > Structure Rendering
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase > tyrosine kinase
CSHL Authors:
Communities: CSHL labs > Tonks lab
Depositing User: CSHL Librarian
Date: 31 August 2010
Date Deposited: 27 Sep 2011 14:52
Last Modified: 21 Feb 2017 20:03
PMCID: PMC3418810
Related URLs:
URI: https://repository.cshl.edu/id/eprint/15364

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