Prolyl isomerase, Pin1: new findings of post-translational modifications and physiological substrates in cancer, asthma and Alzheimer’s disease

@article{Takahashi2007ProlylIP,
  title={Prolyl isomerase, Pin1: new findings of post-translational modifications and physiological substrates in cancer, asthma and Alzheimer’s disease},
  author={Kyoko C Takahashi and Chiyoko Uchida and R.-W. Shin and Kuniko Shimazaki and Takafumi Uchida},
  journal={Cellular and Molecular Life Sciences},
  year={2007},
  volume={65},
  pages={359-375}
}
The peptidyl prolyl cis/trans isomerase Pin1 specifically binds phosphorylated Ser/Thr-Pro protein motifs and catalyzes the cis/trans isomerization of the peptide bond. Accumulating studies have revealed that Pin1 isomerase activity is regulated by its post-translational modifications, including phosphorylation and oxidation. Various transcription factors and regulators have been identified as substrates for Pin1. It enhances AP-1 activity via isomerization of both c-Jun and c-Fos for cellular… CONTINUE READING

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