cathepsin O and cathepsin X (both misleading, having been used forother enzymes)
Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency.
Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification.
Structure and design of potent and selective cathepsin k inhibitors.
Crystal structure of human osteoclast cathepsin K complex with E-64.
Crystal structure of human cathepsin K complexed with a potent inhibitor.
inhibitor designe (X-ray crystallography, MS, NMR, kinetic studies)
Design of potent and selective human cathepsin K inhibitors that span the active site.
Autocatalytic activation of human cathepsin K.
Use of x-ray co-crystal structures and molecular modeling to design potent and selective non-peptide inhibitors of cathepsin k.
The crystal structure of human procathepsin K.
Crystal structure of wild-type human procathepsin K.
Inhibition of cathepsin K by nitric oxide donors: evidence for the formation of mixed disulfides and a sulfenic acid.
Preparation of active recombinant cathepsin K expressed in bacteria as inclusion body.
This enzyme belongs to the peptidase family-C1. The literature [4] & [5] reported that the active-site triad of this enzyme comprises Cys25, His162, Asn182. Moreover, this cysteine residue play a catalytic role as nucleophile, which attack the substrate to form a covalent bond with it (see [4] & [5]).