Background With the increasing resistance of malaria parasites to available drugs, there is an urgent demand to develop new anti-malarial drugs. Calpain inhibitor, ALLN, is proposed to inhibit parasite proliferation by suppressing haemoglobin degradation.
Soh Byoung +9 more
doaj +2 more sources
Protective effect of cannabinoid type 2 receptor agonist (JWH-133) against hepatotoxicity induced by Prangos ferulacea Lindl. extract. [PDF]
Abstract This study investigated Prangos ferulacea (PF)‐induced hepatotoxicity, its potential association with endoplasmic reticulum (ER) stress and proinflammatory cytokines, and the effect of the cannabinoid type 2 receptor agonist JWH‐133. Rats (n = 37) were divided into four groups: control–sham group (CSG, n = 9), PF extract group (PG, n = 9), PF ...
Çelik M +7 more
europepmc +2 more sources
Role of Calpain in Apoptosis [PDF]
Apoptosis, a form of programmed cell death that occurs under physiologicalas well as pathological conditions, is characterized by morphological and biochemicalfeatures.
Hamid Reza Momeni
doaj +1 more source
Cystatins as calpain inhibitors: Engineered chicken cystatin- and stefin B-kininogen domain 2 hybrids support a cystatin-like mode of interaction with the catalytic subunit of μ-calpain [PDF]
Within the cystatin superfamily, only kininogen domain 2 (KD2) is able to inhibit μ- and m-calpain. In an attempt to elucidate the structural requirements of cystatins for calpain inhibition, we constructed recombinant hybrids of human stefin B (an ...
Gross, Stefan +9 more
core +1 more source
Proteomic investigation of the class IA phosphoinositide 3-kinase signalling pathway [PDF]
PhDClass IA phosphoinositide 3-kinases (PI3Ks) are a family of enzymes with key roles in the regulation of signalling pathways, many of which are mediated through Akt.
Beltran, Luisa
core +4 more sources
Calpains are calcium-activated neutral proteases involved in the regulation of key signaling pathways. Junctophilin-2 (JP2) is a Calpain-specific proteolytic target and essential structural protein inside Ca2+ release units required for excitation ...
Gunnar Weninger +9 more
doaj +1 more source
Identification of calpain cleavage sites in the G1 cyclin-dependent kinase inhibitor p19(INK4d) [PDF]
Calpains are a large family of Ca2+-dependent cysteine proteases that are ubiquitously distributed across most cell types and vertebrate species. Calpains play a role in cell differentiation, apoptosis, cytoskeletal remodeling, signal transduction and ...
Popp, Oliver +15 more
core +1 more source
Inhibition of human mu-calpain by conformationally constrained calpastatin peptides [PDF]
Pfizer J, Assfalg-Machleidt I, Machleidt W, Schaschke N. Inhibition of human mu-calpain by conformationally constrained calpastatin peptides. BIOLOGICAL CHEMISTRY.
Machleidt, Werner +3 more
core +1 more source
Proteolysis of insulin-like growth factor binding proteins (IGFBPs) by calpain [PDF]
Calpains are non-lysosomal, Ca2+-dependent cysteine proteases, which are ubiquitously distributed across cell types and vertebrate species. The rules that govern calpain specificity have not yet been determined.
Mann, Karlheinz +12 more
core +1 more source
GPS-CCD: a novel computational program for the prediction of calpain cleavage sites. [PDF]
As one of the most essential post-translational modifications (PTMs) of proteins, proteolysis, especially calpain-mediated cleavage, plays an important role in many biological processes, including cell death/apoptosis, cytoskeletal remodeling, and the ...
Zexian Liu +5 more
doaj +1 more source

