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 …

For a long time, cysteine cathepsins were considered primarily as proteases crucial for
nonspecific bulk proteolysis in the endolysosomal system. However, this view has …

Cysteine cathepsins are highly upregulated in a wide variety of cancers by mechanisms
ranging from gene amplification to post-transcriptional modification. Their localization within …

OBJECTIVES: Contemporary adhesives lose their bond strength to dentin regardless of the
bonding system used. This loss relates to the hydrolysis of collagen matrix of the hybrid …

Background Cysteine cathepsins are normally found in the lysosomes where they are
involved in intracellular protein turnover. Their ability to degrade the components of the …

Cysteine cathepsins belong to the papain-like family C1 of clan CA cysteine peptidases.
These enzymes are ubiquitously expressed and exert their proteolytic activity mainly, but not …

Cysteine cathepsins are key regulators of the innate and adaptive arms of the immune
system. Their expression, activity, and subcellular localization are associated with the …

Cysteine cathepsins have been for a long time considered to execute mainly nonspecific
bulk proteolysis in the endolysosomal system. However, this view has been changing …

Biomedical research often focuses on properties that differentiate between diseased and
healthy tissue; one of the current focuses is elevated expression and altered localisation of …

Heparan sulfate proteoglycans are ubiquitously found at the cell surface and extracellular
matrix in all the animal species. This review will focus on the structural characteristics of the …