Results 21 to 30 of about 90,413 (210)
Caspases and their substrates [PDF]
Cell Death & Differentiation, 2017 Protease biology is intimately linked to the functional consequences of substrate cleavage events. Human caspases are a family of 12 fate-determining cysteine proteases that are best known for driving cell death, either apoptosis or pyroptosis. More recently, caspases have been shown to be involved in other cellular remodeling events as well including ...
Olivier Julien, James A Wells
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Metalloporphyrins inactivate caspase-3 and -8 [PDF]
, 2005 Activation of caspases represents one of the earliest biochemical indicators for apoptotic cell death. Therefore, measurement of caspase activity is a widely used and generally accepted method to determine apoptosis in a wide range of in vivo and in ...
Blumenthal, Signe B. +8 more
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Cell Death & Differentiation, 2000 Caspases, a group of cysteine proteases, constitute the effector arm of the cell death machinery. There are seven caspases known in Drosophila, three of which contain long amino-terminal prodomains. Although, compared to mammalian caspases, much less is known about the biology of Drosophila caspases, many studies have shown that caspases are essential ...
S, Kumar, J, Doumanis
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Caspases: an ancient cellular sword of Damocles. [PDF]
, 2020 Caspases are a family of cysteine proteases homologous to the Caenorhabditis elegans programmed cell death gene product CED-3. Caspases and their distant relatives, meta- and paracaspases, have been found in phylogenetically distant nonmetazoan groups ...
Boyce, M, Yuan, J, Degterev, A
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The Calotropis Gigantea Methanolic Extract Induces Apoptosis in Human Breast Carcinoma Cells [PDF]
Iranian Journal of Medical Sciences, 2019 Background: Calotropis gigantea (family: Asclepiadaceae) has been known to contain cardiac glycosides. The C. gigantea extracts have been reported as cytotoxic to a few cancer cell lines. The present study was designed to examine the effect of Calotropis
Kiran R. Kharat, Arun S. Kharat
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Cell Death & Differentiation, 1999 Caspases are the key effector molecules of the physiological death process known as apoptosis, although some are involved in activation of cytokines, rather than cell death. They exist in most of our cells as inactive precursors (zymogens) that kill the cell once activated. Caspases can be controlled in two ways.
P G, Ekert, J, Silke, D L, Vaux
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Domain structure of zebrafish caspases. [PDF]
, 2018 Caspases are presented based on the classical classification of caspases as inflammatory, initiator, or executioner. The catalytic CASc domain is indicated in yellow, with large and small subunits in orange.
Cory J. Donelson (5264564) +3 more
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Molecules, 2022 Leaves of Olea europaea are a by-product of the olive oil industry and a dietary supplement with acknowledged antioxidant and anti-inflammatory activity but underestimated photoprotective potential. We investigated the protective effects of the LC-PDA-MS/
Paulina Machała +5 more
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Caspases in developmental cell death [PDF]
, 1999 Caspases are a family of evolutionarily conserved cysteine proteases that constitute the effector arm of the apoptotic machinery. Studies in Caenorhabditis elegans, Drosophila melanogaster, and mouse point to evolutionarily conserved caspase function in ...
Shearwin-Whyatt, L., Kumar, S.
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Inhibitor of apoptosis proteins as E3 ligases for ubiquitin and NEDD8
Biomolecular Concepts, 2013 The inhibitors of apoptosis proteins (IAPs) are endogenous inhibitors for apoptosis. Apoptosis is carried out by caspases, which are the family of cystein proteases. IAPs regulate caspases through two conserved regions, the baculovirus IAP repeats (BIRs)
Kamada Shinji
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