Tau pathology modulates Pin1 post-translational modifications and may be relevant as biomarker.

@article{Ando2013TauPM,
  title={Tau pathology modulates Pin1 post-translational modifications and may be relevant as biomarker.},
  author={Kuni{\'e} Ando and Pierre Dourlen and A V Sambo and Alexis Bretteville and Karim B{\'e}larbi and Val{\'e}rie Vingtdeux and Sabiha Eddarkaoui and Herv{\'e} Drobecq and Antoine Ghestem and S{\'e}verine B{\'e}gard and Emmanuelle Demey-Thomas and Patricia Melnyk and Caroline Smet and Guy Lippens and C. A. Maurage and Marie-Laure Caillet-Boudin and Yann Verdier and Jo{\"e}lle Vinh and Isabelle Landrieu and M Galas and David M. Blum and Malika Hamdane and Nicolas Sergeant and Luc Bu{\'e}e},
  journal={Neurobiology of aging},
  year={2013},
  volume={34 3},
  pages={757-69}
}
A prerequisite to dephosphorylation at Ser-Pro or Thr-Pro motifs is the isomerization of the imidic peptide bond preceding the proline. The peptidyl-prolyl cis/trans isomerase named Pin1 catalyzes this mechanism. Through isomerization, Pin1 regulates the function of a growing number of targets including the microtubule-associated tau protein and is supposed… CONTINUE READING