Results 161 to 170 of about 34,572 (205)
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Journal of Biochemistry, 2001
Recent very rapid developments in genome and EST projects have identified an increasing number of gene products homologous to those that were previously identified by other methods. Calpain is no exception. At the time this review is written, 83 genes from 23 living organisms have been identified in the database to encode amino acid sequences showing ...
H, Sorimachi, K, Suzuki
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Recent very rapid developments in genome and EST projects have identified an increasing number of gene products homologous to those that were previously identified by other methods. Calpain is no exception. At the time this review is written, 83 genes from 23 living organisms have been identified in the database to encode amino acid sequences showing ...
H, Sorimachi, K, Suzuki
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Calpain Protects the Heart from Hemodynamic Stress
Journal of Biological Chemistry, 2011 Calpains make up a family of Ca(2+)-dependent intracellular cysteine proteases that include ubiquitously expressed μ- and m-calpains. Both are heterodimers consisting of a distinct large catalytic subunit (calpain 1 for μ-calpain and calpain 2 for m ...
Manabu Taneike +2 more
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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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Nature Reviews Cancer, 2011
The calpains are a conserved family of cysteine proteinases that catalyse the controlled proteolysis of many specific substrates. Calpain activity is implicated in several fundamental physiological processes, including cytoskeletal remodelling, cellular signalling, apoptosis and cell survival. Calpain expression is altered during tumorigenesis, and the
Sarah J Storr +2 more
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The calpains are a conserved family of cysteine proteinases that catalyse the controlled proteolysis of many specific substrates. Calpain activity is implicated in several fundamental physiological processes, including cytoskeletal remodelling, cellular signalling, apoptosis and cell survival. Calpain expression is altered during tumorigenesis, and the
Sarah J Storr +2 more
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The International Journal of Biochemistry & Cell Biology, 2005
Calpains are intracellular nonlysosomal Ca(2+)-regulated cysteine proteases. They mediate regulatory cleavages of specific substrates in a large number of processes during the differentiation, life and death of the cell. The purpose of this review is to synthesize our current understanding of the participation of calpains in muscle atrophy.
Bartoli, Marc, Richard, I
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Calpains are intracellular nonlysosomal Ca(2+)-regulated cysteine proteases. They mediate regulatory cleavages of specific substrates in a large number of processes during the differentiation, life and death of the cell. The purpose of this review is to synthesize our current understanding of the participation of calpains in muscle atrophy.
Bartoli, Marc, Richard, I
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Molecular Neurobiology, 2006
Proteolysis by calpain is a unique posttranslational modification that can change integrity, localization, and activity of endogenous proteins. Two ubiquitous calpains, mu-calpain and m-calpain, are highly expressed in the central nervous system, and calpain substrates such as membrane receptors, postsynaptic density proteins, kinases, and phosphatases
Hai-Yan, Wu, David R, Lynch
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Proteolysis by calpain is a unique posttranslational modification that can change integrity, localization, and activity of endogenous proteins. Two ubiquitous calpains, mu-calpain and m-calpain, are highly expressed in the central nervous system, and calpain substrates such as membrane receptors, postsynaptic density proteins, kinases, and phosphatases
Hai-Yan, Wu, David R, Lynch
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Calpain activation in apoptosis
Journal of Cellular Physiology, 1994AbstractProgrammed cell death is an active process wherein the cell initiates a sequence of events culminating in the fragmentation of its DNA, nuclear collapse, and disintegration of the cell into small, membrane‐bound apoptotic bodies. Examination of the death program in various models has shown common themes, including a rise in cytoplasmic calcium,
M K, Squìer +3 more
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Calpains: structure and function of the calpain super family
1999Calpain (EC 3.4.22.17) is a typical cytosolic cysteine protease whose activity is regulated by calcium, an important second messenger of extra-cellular stimuli [1–4]. Since calpain is distributed ubiquitously among cells and tissues of most higher organisms, it has been predicted to play an essential role in cellular functions.
Yasuko Ono +2 more
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Calpains in the cardiovascular system
Cardiovascular Research, 2012This editorial refers to the following review articles in the issue which make up this Review Focus on Calpains in the Cardiovascular System: H. Sorimachi and Y. Ono, pp. 11–22; J. Inserte et al. pp. 23–31; M.A. Smith and R.G. Schnellmann, pp. 32–37; E. Letavernier et al. , pp. 38–45; O. Yamaguchi et al. , pp. 46–52. Although proteolytic systems have
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1996
Abstract Ca/pains (µ,- and m-) are non-Jysosoma/ cysteine proteinases present in most mammalian tissues in varying amounts and have been detected in all vertebrate species tested. Activation in vitro requires 1-100 µ,M, and 0.1-1 mM levels of Ca2• forµ,- and m-ca/pain, respectively.
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Abstract Ca/pains (µ,- and m-) are non-Jysosoma/ cysteine proteinases present in most mammalian tissues in varying amounts and have been detected in all vertebrate species tested. Activation in vitro requires 1-100 µ,M, and 0.1-1 mM levels of Ca2• forµ,- and m-ca/pain, respectively.
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