Redox redux: revisiting PTPs and the control of cell signaling

Tonks, N. K. (June 2005) Redox redux: revisiting PTPs and the control of cell signaling. Cell, 121 (5). pp. 667-70. ISSN 0092-8674 (Print)

URL: https://www.ncbi.nlm.nih.gov/pubmed/15935753
DOI: 10.1016/j.cell.2005.05.016

Abstract

The architecture of the active site of members of the protein tyrosine phosphatase (PTP) superfamily renders these enzymes sensitive to reversible oxidation and inactivation. The importance of reversible oxidation of PTP superfamily members in controlling the signal output following an extracellular stimulus is discussed.

Item Type: Paper
Uncontrolled Keywords: Animals Humans JNK Mitogen Activated Protein Kinases metabolism Macrophages enzymology Oxidation Reduction Protein Tyrosine Phosphatase metabolism PTP Reactive Oxygen Species metabolism Receptors Antigen B-Cell metabolism Signal Transduction physiology Tumor Necrosis Factor alpha metabolism TNF
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein tyrosine phosphatase
CSHL Authors:
Communities: CSHL labs > Tonks lab
Depositing User: CSHL Librarian
Date: 3 June 2005
Date Deposited: 05 Jan 2012 15:50
Last Modified: 21 Feb 2017 20:42
Related URLs:
URI: http://repository.cshl.edu/id/eprint/22723

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