Results 21 to 30 of about 28,592 (236)

Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation. [PDF]

open access: yesJ Biol Chem, 2018
Limb-girdle muscular dystrophy type 2a arises from mutations in the Ca2+-activated intracellular cysteine protease calpain-3. This calpain isoform is abundant in skeletal muscle and differs from the main isoforms, calpain-1 and -2, in being a homodimer and having two short insertion sequences.
Ye Q, Campbell RL, Davies PL.
europepmc   +4 more sources

Galectin-3 secretion and tyrosine phosphorylation is dependent on the calpain small subunit, Calpain 4 [PDF]

open access: yesBiochemical and Biophysical Research Communications, 2011
Cell adhesion and migration are important events that occur during embryonic development, immune surveillance, wound healing and in tumor metastasis. It is a multi-step process that involves both mechanical and biochemical signaling that results in cell protrusion, adhesion, contraction and retraction.
Shalini, Menon   +2 more
openaire   +2 more sources

A single c.1715G>C calpain 3 gene variant causes dominant calpainopathy with loss of calpain 3 expression and activity [PDF]

open access: yesHuman Mutation, 2020
AbstractRecessively inherited limb girdle muscular dystrophy (LGMD) type 2A is the most common LGMD worldwide. Here, we report the first single missense variant in CAPN3 causing dominantly inherited calpainopathy. A 43‐year‐old proband, his father and two sons were heterozygous for a c.1715G>C p.(Arg572Pro) variant in CAPN3.
John Vissing   +6 more
openaire   +4 more sources

An eccentric calpain, CAPN3/p94/calpain-3

open access: yesBiochimie, 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

Astragaloside IV Alleviates Brain Injury Induced by Hypoxia via the Calpain-1 Signaling Pathway

open access: yesNeural Plasticity, 2022
Long-term hypoxia can induce oxidative stress and apoptosis in hippocampal neurons that can lead to brain injury diseases. Astragaloside IV (AS-IV) is widely used in the antiapoptotic therapy of brain injury diseases.
Yan Meng   +8 more
doaj   +1 more source

Homodimerization of calpain 3 penta-EF-hand domain [PDF]

open access: yesBiochemical Journal, 2005
Calpains 1 and 2 are heterodimeric proteases in which large (relative molecular mass Mr 80000) and small (Mr 28000) subunits are linked through their respective PEF (penta-EF-hand) domains. The skeletal muscle-specific calpain 3 is believed not to form a heterodimer with the small subunit but might homodimerize through its PEF domain.
Ravikiran, Ravulapalli   +3 more
openaire   +2 more sources

Calpain Inhibitor Calpeptin Alleviates Ischemia/Reperfusion-Induced Acute Kidney Injury via Suppressing AIM2 Inflammasome and Upregulating Klotho Protein

open access: yesFrontiers in Medicine, 2022
Renal ischemia/reperfusion injury is a major contributor of acute kidney injury (AKI), leading to renal cell necrosis, apoptosis, and inflammation. Calpains, a family of Ca2+-dependent cysteine proteases, play a pivotal role in the pathogenesis of renal ...
Yong Wu   +6 more
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]

open access: yes, 2001
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

Inhibition of human mu-calpain by conformationally constrained calpastatin peptides [PDF]

open access: yes, 2008
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

Identification of calpain cleavage sites in the G1 cyclin-dependent kinase inhibitor p19(INK4d) [PDF]

open access: yes, 2006
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

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