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Properties of the caspases

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1998
Caspases comprise a structurally related group of cysteine proteases that share a dominant primary specificity for cleaving peptide bonds following Asp residues. Present in the cytosol of all animals, the caspases participate in proteolytic pathways required for executing programmed cell death, or apoptosis.
H R, Stennicke, G S, Salvesen
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Caspases and apoptosis

Essays in Biochemistry, 2002
The ability of metazoan cells to undergo programmed cell death is vital to both the precise development and long-term survival of the mature adult. Cell deaths that result from engagement of this programme end in apoptosis, the ordered dismantling of the cell that results in its 'silent' demise, in which packaged cell fragments are removed by ...
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Death without caspases, caspases without death

Trends in Cell Biology, 2004
Apoptosis is a conserved cell-death process displaying characteristic morphological and molecular changes including activation of caspase proteases. Recent work challenges the accepted roles of these proteases. New investigations in mice and the nematode Caenorhabditis elegans suggest that there could be caspase-independent pathways leading to cell ...
Mary C, Abraham, Shai, Shaham
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Caspase cascades and caspase targets

2000
Apoptosis is an evolutionarily conserved form of cell suicide. Cells that die by apoptosis are disassembled in a stereotypical manner resulting in a characteristic ‘apoptotic morphology’. It was this characteristic, uniform morphology displayed by cells during apoptosis which led to the assumption that cells contain a similar execution machinery ...
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Caspases and Their Substrates

Cold Spring Harbor Perspectives in Biology, 2022
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Caspase Family

2012
Boucher, Dave, Denault, Jean-Bernard
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Caspase-8 and Caspase-10

2013
Bram J. van Raam, Guy S. Salvesen
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Caspase-4 and Caspase-5

2013
Junjun Gao, James A. Wells
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