Cysteine cathepsin protease activity is frequently dysregulated in the context of neoplastic
transformation. Increased activity and aberrant localization of proteases within the tumour …

It is more than 50years since the lysosome was discovered. Since then its hydrolytic
machinery, including proteases and other hydrolases, has been fairly well identified and …

Proteolytic enzymes are crucial for a variety of biological processes in organisms ranging
from lower (virus, bacteria, and parasite) to the higher organisms (mammals). Proteases …

During the past 15 years, the methylotrophic yeast Pichia pastoris has developed into a
highly successful system for the production of a variety of heterologous proteins. The …

Cathepsins were originally identified as proteases that act in the lysosome. Recent work has
uncovered nontraditional roles for cathepsins in the extracellular space as well as in the …

The methylotrophic yeast Pichia pastoris is now one of the standard tools used in molecular
biology for the generation of recombinant protein. P. pastoris has demonstrated its most …

The large family of peptide-bond-cleaving hydrolases, the peptidases () proteases, EC 3.4),
can be categorized as endopeptidases () proteinases, EC 3.4. 21-99) and exopeptidases …

Lysosomal cysteine proteases were believed to be mainly involved in intracellular protein
degradation. Under special conditions they have been found outside lysosomes resulting in …

Proteases can be categorized based on their substrate specificities or mechanisms of
catalysis. Enzymes cleaving within a polypeptide chain are named endopeptidases, and …

Proteolytic enzymes are synthesized as inactive precursors, or “zymogens,” to prevent
unwanted protein degradation, and to enable spatial and temporal regulation of proteolytic …