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 …

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

Metabolite alteration has been associated with the pathogenesis of inflammatory bowel
disease (IBD), including colitis. Mannose, a natural bioactive monosaccharide that is …

Epigenetic markers are potential biomarkers for diabetes and related complications. Using a
prospective cohort from the Hong Kong Diabetes Register, we perform two independent …

Simple Summary Proteolytic enzymes, such as matrix metalloproteinases, plasminogen
activators and cathepsins, as well as non-proteolytic enzymatic partners, such as …

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

With aging, the kidney undergoes inexorable and progressive changes in structural and
functional performance. These aging‐related alterations are more obvious and serious in …

In the last few decades, heparan sulfate (HS) proteoglycans (HSPGs) have been an
intriguing subject of study for their complex structural characteristics, their finely regulated …

Human cathepsin L belongs to the cathepsin family of proteolytic enzymes with primarily an
endopeptidase activity. Although its primary functions were originally thought to be only of a …

Staphylococcus aureus (S. aureus) is the major pathogen responsible for mastitis in dairy
cows, an important threat to their health, but prevention of S. aureus infection of the …