Targeted Inactivation of Dipeptidyl Peptidase 9 Enzymatic Activity Causes Mouse Neonate Lethality

@inproceedings{Gall2013TargetedIO,
  title={Targeted Inactivation of Dipeptidyl Peptidase 9 Enzymatic Activity Causes Mouse Neonate Lethality},
  author={Margaret G. Gall and Yiqian Chen and Ana J{\'u}lia Vieira de Ribeiro and Hui Zhang and Charles G. Bailey and Derek S. Spielman and Denise Ming Tse Yu and Mark D Gorrell},
  booktitle={PloS one},
  year={2013}
}
Dipeptidyl Peptidase (DPP) 4 and related dipeptidyl peptidases are emerging as current and potential therapeutic targets. DPP9 is an intracellular protease that is regulated by redox status and by SUMO1. DPP9 can influence antigen processing, epidermal growth factor (EGF)-mediated signaling and tumor biology. We made the first gene knock-in (gki) mouse with a serine to alanine point mutation at the DPP9 active site (S729A). Weaned heterozygote DPP9 (wt/S729A) pups from 110 intercrosses were… CONTINUE READING
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Structure-Activity Relationship Studies on Isoindoline Inhibitors of Dipeptidyl Peptidases 8 and 9 (DPP8, DPP9): Is DPP8-Selectivity an Attainable Goal

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