Study of the preferred modification sites of the quinone methide intermediate resulting from the latent trapping device of the activity probes for hydrolases.

@article{Lo2005StudyOT,
  title={Study of the preferred modification sites of the quinone methide intermediate resulting from the latent trapping device of the activity probes for hydrolases.},
  author={L C Lo and Ying-Ling Chiang and Chi-Hsien Kuo and H Liao and Yu-Ju Chen and J Lin},
  journal={Biochemical and biophysical research communications},
  year={2005},
  volume={326 1},
  pages={30-5}
}
Use of activity probes has been demonstrated to be a powerful tool in modern chemical proteomic study. Previously we have designed and synthesized a series of mechanism-based activity probes that utilized quinone methide chemistry. Here, we characterized the trend of chemical reactivity for the reactive quinone methide intermediate 3 (QM-3) resulting from the latent trapping device. In a competition assay, the labeling of PTP1B by probe 1a was blocked by externally added cysteine without… CONTINUE READING
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