• Title of article

    Redox regulation of protein-tyrosine phosphatases

  • Author/Authors

    den Hertog، نويسنده , , Jeroen and Groen، نويسنده , , Arnoud and van der Wijk، نويسنده , , Thea، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2005
  • Pages
    5
  • From page
    11
  • To page
    15
  • Abstract
    The protein-tyrosine phosphatases (PTPs) form a large family of signaling proteins with essential functions in embryonic development and adult physiology. The PTPs are characterized by an absolutely conserved catalytic site cysteine with a low pKa due to its microenvironment, making it vulnerable to oxidation. PTPs are differentially oxidized and inactivated in vitro and in living cells. Many cellular stimuli induce a shift in the cellular redox state towards oxidation and evidence is accumulating that at least part of the cellular responses to these stimuli are due to specific, transient inactivation of PTPs, indicating that PTPs are important sensors of the cellular redox state.
  • Keywords
    conformational change , dimerization , regulation , redox , Oxidation , Protein-tyrosine phosphatase
  • Journal title
    Archives of Biochemistry and Biophysics
  • Serial Year
    2005
  • Journal title
    Archives of Biochemistry and Biophysics
  • Record number

    1626796