title: Redox redux: revisiting PTPs and the control of cell signaling.
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.
authors.affiliation: Cold Spring Harbor Laboratory, New York 11724, USA. tonks@cshl.edu
authors.forename: Nicholas K
authors.initials: NK
authors.lastname: Tonks
mesh_terms: D000818:Animals; D006801:Humans; D048031:JNK Mitogen-Activated Protein Kinases / Q000378:metabolism; D008264:Macrophages / Q000201:enzymology; D010084:Oxidation-Reduction; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism*; D017382:Reactive Oxygen Species / Q000378:metabolism; D011947:Receptors, Antigen, B-Cell / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology*; D014409:Tumor Necrosis Factor-alpha / Q000378:metabolism
chemical_list: D017382:Reactive Oxygen Species; D011947:Receptors, Antigen, B-Cell; D014409:Tumor Necrosis Factor-alpha; D048031:JNK Mitogen-Activated Protein Kinases; D017027:Protein Tyrosine Phosphatases