AbstractAutolysis of the Ca2+-dependent cysteine protease m-calpain involves cleavage of the large (80 kDa) and small (30 kDa) subunits of the enzyme, and an increase in Ca2+ sensitivity. The appearance of increased Ca2+ sensitivity was found to correlate with the cleavage of the large subunit after residue 9
Calpains are calcium-regulated neutral cysteine proteases that include ubiquitous, as well as tissue...
The hypothesis that calpain subunits dissociate in the presence of Ca2+ has been tested by methods w...
AbstractCa2+ signaling by calpains leads to controlled proteolysis during processes ranging from cyt...
AbstractAutolysis of the Ca2+-dependent cysteine protease m-calpain involves cleavage of the large (...
m-Calpain is a heterodimeric, cytosolic, thiol protease, which is activated by Ca2+-binding to EF-ha...
The calpains form a growing family of structurally related intracellular multidomain cysteine protei...
Milli- and micro-calpains are ubiquitous cytoplasmic cysteine proteases activated by calcium. They d...
AbstractThe two Ca2+-dependent cysteine proteases, μ- and m-calpain, are involved in various Ca2+-li...
In an ongoing study of the mechanisms of calpain catalysis and Ca2+-induced activation, the effects ...
AbstractSite-directed mutagenesis was used to alter putative active site residues in the large subun...
AbstractCalpain, a Ca2+-dependent cytosolic cysteine protease, proteolytically modulates specific su...
The roles of N-terminal autolysis of the large (80 kDa) and small (28 kDa) subunits in activation of...
Expression and purification of rat m-calpaln has been developed to produce 5-10 mg of pure enzyme in...
AbstractCalpain, a Ca2+-dependent biomodulator, alters the properties of substrate proteins by cleav...
Site-directed mutagenesis was used to alter putative active site residues in the large subunit of ca...
Calpains are calcium-regulated neutral cysteine proteases that include ubiquitous, as well as tissue...
The hypothesis that calpain subunits dissociate in the presence of Ca2+ has been tested by methods w...
AbstractCa2+ signaling by calpains leads to controlled proteolysis during processes ranging from cyt...
AbstractAutolysis of the Ca2+-dependent cysteine protease m-calpain involves cleavage of the large (...
m-Calpain is a heterodimeric, cytosolic, thiol protease, which is activated by Ca2+-binding to EF-ha...
The calpains form a growing family of structurally related intracellular multidomain cysteine protei...
Milli- and micro-calpains are ubiquitous cytoplasmic cysteine proteases activated by calcium. They d...
AbstractThe two Ca2+-dependent cysteine proteases, μ- and m-calpain, are involved in various Ca2+-li...
In an ongoing study of the mechanisms of calpain catalysis and Ca2+-induced activation, the effects ...
AbstractSite-directed mutagenesis was used to alter putative active site residues in the large subun...
AbstractCalpain, a Ca2+-dependent cytosolic cysteine protease, proteolytically modulates specific su...
The roles of N-terminal autolysis of the large (80 kDa) and small (28 kDa) subunits in activation of...
Expression and purification of rat m-calpaln has been developed to produce 5-10 mg of pure enzyme in...
AbstractCalpain, a Ca2+-dependent biomodulator, alters the properties of substrate proteins by cleav...
Site-directed mutagenesis was used to alter putative active site residues in the large subunit of ca...
Calpains are calcium-regulated neutral cysteine proteases that include ubiquitous, as well as tissue...
The hypothesis that calpain subunits dissociate in the presence of Ca2+ has been tested by methods w...
AbstractCa2+ signaling by calpains leads to controlled proteolysis during processes ranging from cyt...
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