Amongst the lysosomal cysteine cathepsin family of proteases, cathepsin S (CTSS) holds
particular interest due to distinctive properties including a normal restricted expression …

Lysosomes and lysosomal hydrolases, including the cathepsins, have been shown to
change their properties with aging brain a long time ago, although their function was not …

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 …

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

Antigen presentation by both classical MHC class II molecules and the non-classical MHC
class I-like molecule CD1D requires their entry into the endosomal/lysosomal compartment …

The subclass of cysteine proteases termed lysosomal cathepsins has long been thought to
be primarily involved in end-stage protein breakdown within lysosomal compartments …