Engineering inhibitors highly selective for the S1 sites of Ser190 trypsin-like serine protease drug targets.

@article{Katz2001EngineeringIH,
  title={Engineering inhibitors highly selective for the S1 sites of Ser190 trypsin-like serine protease drug targets.},
  author={Bradley A. Katz and Paul A. Sprengeler and Christine Luong and Erik Verner and Kyle C Elrod and Michelle L. Kirtley and James W. Janc and Jeffrey R Spencer and James Guy Breitenbucher and Hon C. Hui and D P Mcgee and Darin Allen and Arnold Martelli and Richard L Mackman},
  journal={Chemistry & biology},
  year={2001},
  volume={8 11},
  pages={1107-21}
}
BACKGROUND Involved or implicated in a wide spectrum of diseases, trypsin-like serine proteases comprise well studied drug targets and anti-targets that can be subdivided into two major classes. In one class there is a serine at position 190 at the S1 site, as in urokinase type plasminogen activator (urokinase or uPA) and factor VIIa, and in the other there is an alanine at 190, as in tissue type plasminogen activator (tPA) and factor Xa. A hydrogen bond unique to Ser190 protease-arylamidine… CONTINUE READING
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