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
Link To Document :
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