Results 151 to 160 of about 34,572 (205)
Copper ionophore elicits calpain-dependent paraptosis coincident with proteotoxic stress. [PDF]
Cell Commun SignalSae-Fung A, Fadeel B.
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Glucose shields RINm5F beta cells against arsenic-induced apoptosis. [PDF]
Sci RepOrtiz-Huidobro RI +4 more
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The International Journal of Biochemistry & Cell Biology, 2002
The calcium-dependent thiol proteases, calpains, are widely expressed with ubiquitous and tissue specific isoforms. Calpains have been implicated in basic cellular processes including cell proliferation, apoptosis and differentiation. The focus of the current review is to summarize recent findings implicating calpains in cytoskeletal rearrangements and
B J, Perrin, A, Huttenlocher
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The calcium-dependent thiol proteases, calpains, are widely expressed with ubiquitous and tissue specific isoforms. Calpains have been implicated in basic cellular processes including cell proliferation, apoptosis and differentiation. The focus of the current review is to summarize recent findings implicating calpains in cytoskeletal rearrangements and
B J, Perrin, A, Huttenlocher
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Trends in Neurosciences, 1989
In recent years interest has increased concerning the characterization of the structural-functional properties and the identification of the physiological role of non-lysosomal intracellular proteinases. Among these, calpain, a calcium-dependent cysteine proteinase ubiquitously present in a variety of tissues and cells, has been most extensively ...
MELLONI, EDON, PONTREMOLI, SANDRO
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In recent years interest has increased concerning the characterization of the structural-functional properties and the identification of the physiological role of non-lysosomal intracellular proteinases. Among these, calpain, a calcium-dependent cysteine proteinase ubiquitously present in a variety of tissues and cells, has been most extensively ...
MELLONI, EDON, PONTREMOLI, SANDRO
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Effect of μ-Calpain on m-Calpain
Biochemical and Biophysical Research Communications, 2000The free Ca(2+) concentrations required for half-maximal proteolytic activity of m-calpain are in the range of 400-800 microM and are much higher than the 50-500 nM free Ca(2+) concentrations that exist in living cells. Consequently, a number of studies have attempted to find mechanisms that would lower the Ca(2+) concentration required for proteolytic
V F, Thompson, K, Lawson, D E, Goll
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Physiological Reviews, 2003
Goll, Darrel E., Valery F. Thompson, Hongqi Li, Wei Wei, and Jinyang Cong. The Calpain System. Physiol Rev 83: 731–801, 2003; 10.1152/physrev.00029.2002.—The calpain system originally comprised three molecules: two Ca2+-dependent proteases, μ-calpain and m-calpain, and a third polypeptide, calpastatin, whose only known function is to inhibit the two ...
Darrell E, Goll +4 more
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Goll, Darrel E., Valery F. Thompson, Hongqi Li, Wei Wei, and Jinyang Cong. The Calpain System. Physiol Rev 83: 731–801, 2003; 10.1152/physrev.00029.2002.—The calpain system originally comprised three molecules: two Ca2+-dependent proteases, μ-calpain and m-calpain, and a third polypeptide, calpastatin, whose only known function is to inhibit the two ...
Darrell E, Goll +4 more
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New England Journal of Medicine, 2005
Calpains are members of a large family of Ca2+-dependent proteolytic enzymes. Some are tissue-specific; others are ubiquitous.
Mayana, Zatz, Alessandra, Starling
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Calpains are members of a large family of Ca2+-dependent proteolytic enzymes. Some are tissue-specific; others are ubiquitous.
Mayana, Zatz, Alessandra, Starling
openaire +2 more sources