A novel series of noncovalent inhibitors of cathepsin L have been designed to mimic the
mode of autoinhibition of procathepsin L. Just like the propeptide, these peptide-based …

We report a series of noncovalent, reversible inhibitors of cathepsin L that have been
designed to explore additional binding interactions with the S′ subsites. The design was …

A small library of peptide amides was designed to profile the cathepsin L active site. Within
the cathepsin family of cysteine proteases, the first round of selection was on cathepsin L …

By screening a combinatorial pentapeptide amide collection in an inhibition assay, we
systematically evaluated the potential of 19 proteinogenic amino acids and seven …

The extension of a previously reported cathepsin K azepanone-based inhibitor template to
the design and synthesis of potent and selective inhibitors of the homologous cysteine …

Cathepsin L plays a key role in many pathophysiological conditions including rheumatoid
arthritis, tumor invasion and metastasis, bone resorption and remodeling. Here we report the …

We have determined the three dimensional structure of the complex of human cathepsin L
and E-64, an irreversible inhibitor of cysteine proteases, at 2.5 Å resolution. The overall …

Ten overlapping 15-mer peptides (peptidyl amides) spanning the proregion of rat cathepsin
B (residues 1p–60p) were constructed to identify minimal segments having inhibitory activity …

The cathepsin L propeptide (phcl-2) was expressed in Saccharomyces cerevisiae using a
human procathepsin L/α-factor fusion construct containing a stop codon at position− 1 (the C …

The substrate activity screening (SAS) method, a substrate-based fragment identification
and optimization method for the development of enzyme inhibitors, was previously applied …