Human μ-calpain: Simple isolation from erythrocytes and characterization of autolysis fragments [PDF]
, 2001 Heterodimeric μ-calpain, consisting of the large (80 kDa) and the small (30 kDa) subunit, was isolated and purified from human erythrocytes by a highly reproducible four-step purification procedure.
Crawford C. +13 more
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GPS-CCD: a novel computational program for the prediction of calpain cleavage sites. [PDF]
PLoS ONE, 2011 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
Frontiers in Molecular Biosciences, 2023 Objectives: The goal of our bioinformatics study was to comprehensively analyze the association between the whole calpain family members and the progression and prognosis of hepatocellular carcinoma (HCC).Methods: The data were collected from The Cancer ...
Dongjun Dai +13 more
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Augmented generation of protein fragments during wakefulness as the molecular cause of sleep: A hypothesis [PDF]
, 2012 Despite extensive understanding of sleep regulation, the molecular-level cause and function of sleep are unknown. I suggest that they originate in individual neurons and stem from increased production of protein fragments during wakefulness.
Varshavsky, Alexander
core +1 more source
An eccentric calpain, CAPN3/p94/calpain-3
Biochimie, 2016 Calpains are Ca(2+)-regulated proteolytic enzymes that are involved in a variety of biological phenomena. Calpains process substrates by limited proteolysis to modulate various protein functions in the cell, and are thus called "modulator proteases." CAPN3, previously called p94 or calpain-3, has unique features that are not found in any of the other ...
Ono, Yasuko +4 more
openaire +2 more sources
Characterization of the definitive classical calpain family of vertebrates using phylogenetic, evolutionary and expression analyses [PDF]
, 2014 Peer reviewedPublisher ...
Benton MJ +4 more
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Cell Discovery, 2023 Calpains are a class of non-lysosomal cysteine proteases that exert their regulatory functions via limited proteolysis of their substrates. Similar to the lysosomal and proteasomal systems, calpain dysregulation is implicated in the pathogenesis of ...
Jaiprakash Sharma +9 more
doaj +1 more source
Activation of calpain-1 in human carotid artery atherosclerotic lesions
BMC Cardiovascular Disorders, 2009 Background In a previous study, we observed that oxidized low-density lipoprotein-induced death of endothelial cells was calpain-1-dependent. The purpose of the present paper was to study the possible activation of calpain in human carotid plaques, and ...
Pedro Luis M +7 more
doaj +1 more source
Inhibition of calpain prevents manganese-induced cell injury and alpha-synuclein oligomerization in organotypic brain slice cultures. [PDF]
PLoS ONE, 2015 Overexposure to manganese has been known to promote alpha-synuclein oligomerization and enhance cellular toxicity. However, the exact mechanism of Mn-induced alpha-synuclein oligomerization is unclear.
Bin Xu +5 more
doaj +1 more source
Reduction of myocardial infarction by postischemic administration of the calpain inhibitor A-705253 in comparison to the Na(+)/H(+) exchange inhibitor Cariporide (R) in isolated perfused rabbit hearts [PDF]
, 2008 The calpain inhibitor A-705253 and the Na(+)/H(+) exchange inhibitor Cariporide (R) were studied in isolated perfused rabbit hearts subjected to 60 min occlusion of the ramus interventricularis of the left coronary artery (below the origin of the first ...
Bardenheuer H. +19 more
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