Results 31 to 40 of about 120,191 (200)
Non-invasive imaging of cysteine cathepsin activity in solid tumors using a 64Cu-labeled activity-based probe. [PDF]
PLoS ONE, 2011 The papain family of cysteine cathepsins are actively involved in multiple stages of tumorigenesis. Because elevated cathepsin activity can be found in many types of human cancers, they are promising biomarkers that can be used to target radiological ...
Gang Ren +11 more
doaj +1 more source
Cysteine Cathepsin Activity Regulation by Glycosaminoglycans [PDF]
BioMed Research International, 2014 Cysteine cathepsins are a group of enzymes normally found in the endolysosomes where they are primarily involved in intracellular protein turnover but also have a critical role in MHC II-mediated antigen processing and presentation. However, in a number of pathologies cysteine cathepsins were found to be heavily upregulated and secreted into ...
Marko Novinec +2 more
openaire +2 more sources
The role of the host—Neutrophil biology
Periodontology 2000, EarlyView., 2023 Abstract Neutrophilic polymorphonuclear leukocytes (neutrophils) are myeloid cells packed with lysosomal granules (hence also called granulocytes) that contain a formidable antimicrobial arsenal. They are terminally differentiated cells that play a critical role in acute and chronic inflammation, as well as in the resolution of inflammation and wound ...
Iain L. C. Chapple +4 more
wiley +1 more source
PLoS Pathogens, 2020 Over the last 2 decades, several coronaviruses (CoVs) have crossed the species barrier into humans, causing highly prevalent and severe respiratory diseases, often with fatal outcomes.
Anja Pišlar +7 more
doaj +1 more source
The Carboxypeptidase Activity of Cathepsin X is Not Controlled by Endogenous Inhibitors
Acta Chimica Slovenica, 2019 Cysteine cathepsins are peptidases with housekeeping functions that play different specific roles in different tissues. Endogenous peptidase inhibitors, such as cystatins and thyropins are the ultimate way of controlling their activity.
Urša Pečar Fonović +4 more
doaj +1 more source
Бюллетень сибирской медицины, 2020 Aim. To study the level of activity of lysosomal cysteine proteases (cathepsins H, B, L) in blood plasma and fractionated leukocytes (polymorphonuclear and mononuclear) in patients with Alzheimer’s disease in comparison with similar indicators in persons
M. G. Sorokina +3 more
doaj +1 more source
Design and Synthesis of Cysteine Protease Inhibitors
Proceedings, 2017 We have been preparing new dipeptidyl inhibitors against parasitic cysteine proteases cruzain (related to Chagas disease) and rhodesain (related to Sleeping Sickness disease), and against human cathepsins. [...]
Florenci V. Gonzalez
doaj +1 more source
Structural basis for specificity of propeptide-enzyme interaction in barley C1A cysteine peptidases. [PDF]
PLoS ONE, 2012 C1A cysteine peptidases are synthesized as inactive proenzymes. Activation takes place by proteolysis cleaving off the inhibitory propeptide. The inhibitory capacity of propeptides from barley cathepsin L and B-like peptidases towards commercial and ...
Inés Cambra +3 more
doaj +1 more source
The Multifaceted Role of the Lysosomal Protease Cathepsins in Kidney Disease
Frontiers in Cell and Developmental Biology, 2017 Kidney disease is worldwide the 12th leading cause of death affecting 8–16% of the entire population. Kidney disease encompasses acute (short-lasting episode) and chronic (developing over years) pathologies both leading to renal failure.
Pasquale Cocchiaro +14 more
doaj +1 more source
Redox-based inactivation of cysteine cathepsins by compounds containing the 4-aminophenol moiety. [PDF]
PLoS ONE, 2011 BACKGROUND: Redox cycling compounds have been reported to cause false positive inhibition of proteases in drug discovery studies. This kind of false positives can lead to unusually high hit rates in high-throughput screening campaigns and require further
Bojana Mirković +3 more
doaj +1 more source