Results 181 to 190 of about 59,835 (238)
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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
exaly +3 more sources
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
exaly +3 more sources
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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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
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Trends in Biochemical Sciences, 1983
Calpain is a Ca2(+)-dependent cysteine endopeptidase and calpastatin is a calpain-specific endogenous inhibitor protein. Both calpain and calpastatin are very widely distributed in various animal tissues and cells. Low (microM) Ca2(+)-requiring calpain I and high (mM) Ca2(+)-requiring calpain II are known to exist. Calpain consists of one heavy (80 kDa)
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Calpain is a Ca2(+)-dependent cysteine endopeptidase and calpastatin is a calpain-specific endogenous inhibitor protein. Both calpain and calpastatin are very widely distributed in various animal tissues and cells. Low (microM) Ca2(+)-requiring calpain I and high (mM) Ca2(+)-requiring calpain II are known to exist. Calpain consists of one heavy (80 kDa)
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Biochemical and Biophysical Research Communications, 2004
Calpains are calcium-modulated proteases which respond to Ca2+ signals by removing limited portions of protein substrates, thereby irreversibly modifying their function(s). Members of this protease family are present in a variety of organisms ranging from mammals to plants; some of them are ubiquitously expressed, while others are tissue specific ...
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Calpains are calcium-modulated proteases which respond to Ca2+ signals by removing limited portions of protein substrates, thereby irreversibly modifying their function(s). Members of this protease family are present in a variety of organisms ranging from mammals to plants; some of them are ubiquitously expressed, while others are tissue specific ...
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Journal of Neurochemistry, 1988
Abstract: Anti‐chicken muscle calpain (calcium‐activated neutral protease) antibody (ACAb) was found to be absorbed by purified human brain myelin when titrated by enzyme‐linked immunosorbent assay, suggesting the close association of the protease with myelin.
K, Yanagisawa +5 more
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Abstract: Anti‐chicken muscle calpain (calcium‐activated neutral protease) antibody (ACAb) was found to be absorbed by purified human brain myelin when titrated by enzyme‐linked immunosorbent assay, suggesting the close association of the protease with myelin.
K, Yanagisawa +5 more
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