The general view on cysteine cathepsins, which were long believed to be primarily involved
in intracellular protein turnover, has dramatically changed in last 10 to 15 years. The …

Since the discovery of the key role of cathepsin K in bone resorption, cysteine cathepsins
have been investigated by pharmaceutical companies as drug targets. The first clinical …

Thirteen papain-like cysteine proteases (cathepsins) are coded in the human genome from
which two represent pseudogenes. Initially it was believed that lysosomal cysteine …

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 (11 in humans) are mostly located in the acidic compartments of cells.
They have been known for decades to be involved in intracellular protein degradation as …

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 …

Human cysteine proteases of the papain family have been recognized as potential drug
targets for musculoskeletal diseases. Most of the interest is focused on cathepsins S and K …

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 …

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 are a family of lysosomal proteases that are often upregulated in
various human cancers, and have been implicated in distinct tumorigenic processes such as …