@article{SchmitzBeckmannDudicetal.2014,
  author    = {Janina Schmitz and Anna-Madeleine Beckmann and Adela Dudic and Tianwei Li and Robert Sellier and Ulrike Bartz and Michael G{\"u}tschow},
  title     = {3-Cyano-3-aza-β-amino Acid Derivatives as Inhibitors of Human Cysteine Cathepsins},
  series   = {ACS Medicinal Chemistry Letters},
  volume    = {5},
  number    = {10},
  publisher = {ACS Publications},
  issn      = {1948-5875},
  doi       = {10.1021/ml500238q},
  url       = {https://nbn-resolving.org/urn:nbn:de:hbz:1044-opus-13258},
  pages     = {1076 -- 1081},
  year      = {2014},
  abstract  = {Nitrile-type inhibitors are known to interact with cysteine proteases in a covalent-reversible manner. The chemotype of 3-cyano-3-aza-β-amino acid derivatives was designed in which the N-cyano group is centrally arranged in the molecule to allow for interactions with the nonprimed and primed binding regions of the target enzymes. These compounds were evaluated as inhibitors of the human cysteine cathepsins K, S, B, and L. They exhibited slow-binding behavior and were found to be exceptionally potent, in particular toward cathepsin K, with second-order rate constants up to 52 900 × 103 M–1 s–1.},
  language  = {en}
}