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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.
Henning R. Stennicke, Guy S. Salvesen
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APOPTOSIS AND CASPASES

Cardiology Clinics, 2001
The expedition into the apoptosis signaling pathway, although it has just begun, has resulted in the discovery of a significant number of remarkable signaling molecules at all levels of this novel pathway After the pinnacle of this frenetic cloning effort has been reached, however, it is important to put this pathway and its constituents into a ...
Marcus E. Peter, Alexander H. Stegh
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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 ...
Shai Shaham, Mary C. Abraham
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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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Caspase activation

Biochemical Society Symposia, 2003
Caspase activation is the 'point of no return' commitment to cell death. Synthesized as inactive zymogens, it is essential that the caspases remain inactive until the death signal is received. It is known for the downstream executioner caspases-3 and -7 that the activation event is proteolytic cleavage, and this had been assumed to apply to the ...
Kelly M, Boatright, Guy S, Salvesen
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Caspase Mechanisms

2008
The main effectors of apoptosis encompass proteases from the caspase family, which reside as latent precursors in most nucleated animal cells. The apoptotic caspases constitute a minimal two-step signaling pathway. The apical (initiator) caspases are activated within oligomeric signaling complexes in response to apoptotic stimuli.
Guy S, Salvesen, Stefan J, Riedl
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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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Caspase-12 compensates for lack of caspase-2 and caspase-3 in female germ cells

Apoptosis, 2007
Previously, we analyzed mice lacking either caspase-2 or caspase-3 and documented a role for caspase-2 in developmental and chemotherapy-induced apoptosis of oocytes. Those data also revealed dispensability of caspase-3, although we found this caspase critical for ovarian granulosa cell death.
Takai, Y.   +13 more
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Immunoreactivity to caspase-3, caspase-7, caspase-8, and caspase-9 forms is frequently lost in human prostate tumors

Human Pathology, 2012
Caspases are essential initiators and executioners of apoptosis. Changes in their expression may contribute to the development of proliferative disorders such as cancer, by altering the death-proliferation homeostatic balance. The aim of this work was to analyze the expression of a broad panel of caspases at the epithelial level in human prostate ...
Mar Royuela   +7 more
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Characterization of caspase-8L: a novel isoform of caspase-8 that behaves as an inhibitor of the caspase cascade

Blood, 2002
Caspase-8 (Fas-associating protein with death domain–like interleukin-1β– converting enzyme [FLICE]/MACH/Mch5) belongs to a family of cysteine proteases presumed to be the apex of the apoptotic signaling pathways. We recently reported the presence of a novel isoform of caspase-8, named caspase-8L, generated by the alternative splicing of human caspase ...
Takahiko Horiuchi   +5 more
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