Structural characteristics of a lipid peroxidation product, trans-2-nonenal, that favour inhibition of membrane-associated phosphotyrosine phosphatase activity.

@article{HernndezHernndez2005StructuralCO,
  title={Structural characteristics of a lipid peroxidation product, trans-2-nonenal, that favour inhibition of membrane-associated phosphotyrosine phosphatase activity.},
  author={{\'A}ngel Hern{\'a}ndez-Hern{\'a}ndez and Mar{\'i}a N Garabatos and M. C. Ceballos Rodr{\'i}guez and Mar{\'i}a L Vidal and Abel L{\'o}pez-Revuelta and J Ignacio S{\'a}nchez-Gallego and Marcial Llanillo and Jes{\'u}s S{\'a}nchez-Yag{\"u}e},
  journal={Biochimica et biophysica acta},
  year={2005},
  volume={1726 3},
  pages={317-25}
}
Protein-tyrosine phosphatases (PTPs) are very susceptible to oxidation by reactive oxygen species (ROS), which induce the oxidation of catalytic cysteines, thereby inactivating these PTPs. PTPs are also inactivated by treatment with different aldehydes (such as trans-2-nonenal), produced after tissue damage by ROS. However, the molecular mechanisms behind such aldehyde-due inactivation remain unknown. Using commercially available compounds, we examined the structural characteristics of trans-2… CONTINUE READING

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