Cysteine cathepsin protease activity is frequently dysregulated in the context of neoplastic
transformation. Increased activity and aberrant localization of proteases within the tumour …

Stimulus-cleavable nanoscale drug delivery systems are receiving significant attention
owing to their capability of achieving exquisite control over drug release via the exposure to …

Reactive oxygen, nitrogen, and sulfur species, referred to as ROS, RNS, and RSS,
respectively, are produced during normal cell function and in response to various stimuli. An …

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

Subtilases are members of the clan (or superfamily) of subtilisin‐like serine proteases. Over
200 subtilases are presently known, more than 170 of which with their complete amino acid …

The large family of peptide-bond-cleaving hydrolases, the peptidases () proteases, EC 3.4),
can be categorized as endopeptidases () proteinases, EC 3.4. 21-99) and exopeptidases …

Cysteine proteases play numerous indispensable roles in the biology of parasitic organisms.
Aside from previously known general catabolic functions and protein processing, cysteine …

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

Replication of the genomic RNA of severe acute respiratory syndrome coronavirus (SARS-
CoV) is mediated by replicase polyproteins that are processed by two viral proteases …

▪ Abstract Cysteine proteases have traditionally been viewed as lysosomal mediators of
terminal protein degradation. However, recent findings refute this limited view and suggest a …