Cathepsins encompass a family of lysosomal proteases that mediate protein degradation
and turnover. Although mainly localized in the endolysosomal compartment, cathepsins are …

Cathepsins are the most abundant lysosomal proteases that are mainly found in acidic
endo/lysosomal compartments where they play a vital role in intracellular protein …

The state of enzymes in the human body determines the normal physiology or pathology, so
all the six classes of enzymes are crucial. Proteases, the hydrolases, can be of several types …

Kidney disease is worldwide the 12th leading cause of death affecting 8–16% of the entire
population. Kidney disease encompasses acute (short-lasting episode) and chronic …

Cathepsins can be found in the extracellular space, cytoplasm, and nucleus. It was initially
suspected that the primary physiological function of the cathepsins was to break down …

Intracellular protein degradation is a universal feature of eukaryotic cells and vital for
nutrition, protein turnover, intracellular signaling, development and other major physiological …

Cathepsins were first described, as endolysosomal proteolytic enzymes in reference to the
organelles where they degrade the bulk of endogenous and exogenous substrates in a …

Helminth pathogens express papain-like cysteine peptidases, termed cathepsins, which
have important roles in virulence, including host entry, tissue migration and the suppression …

Cysteine cathepsins, as the most abundant proteases found in the lysosomes, play a vital
role in several processes—such as protein degradation, changes in cell signaling, cell …

Proteinases and their inhibitors play essential functional roles in basic biological processes
in both hosts and pathogens. Endo/lysosomal cathepsins participate in immune response in …