Structure based development of novel speci ¢ c inhibitors for cathepsin L and cathepsin S in vitro and in vivo

@inproceedings{Katunumaa1999StructureBD,
  title={Structure based development of novel speci ¢ c inhibitors for cathepsin L and cathepsin S in vitro and in vivo},
  author={N. Katunumaa and E. Murataa and H. Kakegawaa and A. Matsuia and H. Tsuzukia and H. Tsugea and D. Turkc and V. Turkc and M. Fukushimab and Y. Tadab and T. Asaob},
  year={1999}
}
  • N. Katunumaa, E. Murataa, +8 authors T. Asaob
  • Published 1999
Specific inhibitors for cathepsin L and cathepsin S have been developed with the help of computer-graphic modeling based on the stereo-structure. The common fragment, N-(Ltrans-carbamoyloxyrane-2-carbonyl)-phenylalanine-dimethylamide, is required for specific inhibition of cathepsin L. Seven novel inhibitors of the cathepsin L inhibitor Katunuma (CLIK) specifically inhibited cathepsin L at a concentration of 1037 M in vitro, while almost no inhibition of cathepsins B, C, S and K was observed… CONTINUE READING

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