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Enzymology
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- Protein Structure and FoldingOpen Access
The KIM-family protein-tyrosine phosphatases use distinct reversible oxidation intermediates: Intramolecular or intermolecular disulfide bond formation
Journal of Biological ChemistryVol. 292Issue 21p8786–8796Published online: April 7, 2017- Luciana E.S.F. Machado
- Tun-Li Shen
- Rebecca Page
- Wolfgang Peti
Cited in Scopus: 13The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes hematopoietic protein-tyrosine phosphatase (HePTP), striatal-enriched protein-tyrosine phosphatase (STEP), and protein-tyrosine phosphatase receptor type R (PTPRR). KIM-PTPs bind and dephosphorylate mitogen-activated protein kinases (MAPKs) and thereby critically modulate cell proliferation and differentiation. PTP activity can readily be diminished by reactive oxygen species (ROS), e.g. H2O2, which oxidize the catalytically indispensable active-site cysteine.