Explore: Cathepsins

inhibitory activity towards human cathepsins L, B, H, and K. Several inhibitors have reached clinical trials, targeting cathepsins K and S as promising therapeutics

vesicles, cathepsin K, along with reactive oxygen species generated by TRAP, further degrades the bone extracellular matrix. Several other cathepsins are expressed

polyadenylation signals exist for this gene. Cathepsin S is a member of the peptidase C1 family of cysteine cathepsins, a lysosomal cysteine protease that may

usually referred to as cysteine cathepsins—that is, the cysteine protease members of the group of proteases known as cathepsins (which includes cysteine, serine

by cathepsins (primarily cathepsin L) in endolysosomes. Hydroxychloroquine inhibits the action of cathepsin L in endolysosomes, but because cathepsin L

Cathepsin L2 (EC 3.4.22.43, also known as cathepsin V or cathepsin U) is a protein encoded in humans by the CTSV gene. The protein is a human cysteine

of papain and a number of other cathepsins including cathepsins, B, H, K, L, and S. The translated prepro-cathepsin C is processed into the mature form

Cathepsin B belongs to a family of lysosomal cysteine proteases known as the cysteine cathepsins and plays an important role in intracellular proteolysis

Cathepsin A is an enzyme that is classified both as a cathepsin and a carboxypeptidase. In humans, it is encoded by the CTSA gene. The enzyme is also

non-pepsin proteinase, cathepsin D-like acid proteinase, cathepsin E-like acid proteinase, cathepsin D-type proteinase) is an enzyme. Cathepsin E is a protease