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 prodomains of several cysteine proteases of the papain family have been shown to be
potent inhibitors of their parent enzymes. An increased interest in cysteine proteases …

Based on recent information about the anti‐substrate binding mode of the propeptide portion
of procathepsin B and the well established substrate‐like binding of epoxysuccinyl …

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The design and synthesis of dipeptidyl disulfides and dipeptidyl benzoylhydrazones as
selective inhibitors of the cysteine protease Cathepsin S are described. These inhibitors …

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-(L …

A cDNA clone encoding the human cysteine protease cathepsin L was expressed at high
levels in Escherichia coli in a T7 expression system. The insoluble recombinant enzyme was …

Cathepsin S, a lysosomal cysteine protease of the papain superfamily, has been implicated
in the preparation of MHC class II αβ-heterodimers for antigen presentation to CD4+ T …

The mini-chain of human cathepsin H has been identified as the major structural element
determining the proteases substrate specificity. A genetically engineered mutant of human …

A series of Nα-2-benzoxazolyl-α-amino acid-(arylaminoethyl) amides were identified as
potent, selective, and noncovalent inhibitors of cathepsin S. Structure–activity relationships …