Results 161 to 170 of about 90,413 (210)
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Deficiency in caspase-9 or caspase-3 induces compensatory caspase activation
Nature Medicine, 2000Dysregulation of apoptosis contributes to the pathogenesis of many human diseases. As effectors of the apoptotic machinery, caspases are considered potential therapeutic targets. Using an established in vivo model of Fas-mediated apoptosis, we demonstrate here that elimination of certain caspases was compensated in vivo by the activation of other ...
T S, Zheng +7 more
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Regulation of NF-κB signaling by caspases and MALT1 paracaspase [PDF]
Cell Research, 2010 Caspases are intracellular proteases that are best known for their function in apoptosis signaling. It has become evident that many caspases also function in other signaling pathways that propagate cell proliferation and inflammation, but studies on the ...
Rudi Beyaert +2 more
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Apoptosis, 2009
Developmental and tissue homeostasis is a delicate balance between cell proliferation and cell death. The activation of caspases, a conserved family of cysteine proteases, is a main event in the initiation and execution of programmed cell death. While caspases have been characterized from many organisms, comparatively little is known about insect ...
Dawn M, Cooper +2 more
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Developmental and tissue homeostasis is a delicate balance between cell proliferation and cell death. The activation of caspases, a conserved family of cysteine proteases, is a main event in the initiation and execution of programmed cell death. While caspases have been characterized from many organisms, comparatively little is known about insect ...
Dawn M, Cooper +2 more
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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 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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Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2008
Caspases belong to a family of highly conserved aspartate-specific cysteine proteases and are members of the interleukin-1beta-converting enzyme family, present in multicellular organisms. The caspase gene family consists of 15 mammalian members that are grouped into two major sub-families, namely inflammatory caspases and apoptotic caspases.
Indrajit, Chowdhury +2 more
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Caspases belong to a family of highly conserved aspartate-specific cysteine proteases and are members of the interleukin-1beta-converting enzyme family, present in multicellular organisms. The caspase gene family consists of 15 mammalian members that are grouped into two major sub-families, namely inflammatory caspases and apoptotic caspases.
Indrajit, Chowdhury +2 more
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The International Journal of Biochemistry & Cell Biology, 2000
Caspase-9 is a member of caspase family of cysteine proteases that have been implicated in apoptosis and cytokine processing. When cells receive apoptotic stimuli, mitochondria releases cytochrome c which then binds to Apaf-1, the mammalian Ced-4 homologue, together with dATP.
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Caspase-9 is a member of caspase family of cysteine proteases that have been implicated in apoptosis and cytokine processing. When cells receive apoptotic stimuli, mitochondria releases cytochrome c which then binds to Apaf-1, the mammalian Ced-4 homologue, together with dATP.
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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 ...
A H, Stegh, M E, Peter
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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 ...
A H, Stegh, M E, Peter
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Current Research in Translational Medicine
Recent studies prove that the three well-established cell death pathways-pyroptosis, apoptosis, and necroptosis-are not isolated but rather engage in extensive crosstalk. PANoptosis, a newly identified pathway of inflammatory regulated cell death (RCD), integrates characteristics of apoptosis, pyroptosis, and necroptosis.
Kaiyuan Song, Yongbin Wu, Sipin Tan
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Recent studies prove that the three well-established cell death pathways-pyroptosis, apoptosis, and necroptosis-are not isolated but rather engage in extensive crosstalk. PANoptosis, a newly identified pathway of inflammatory regulated cell death (RCD), integrates characteristics of apoptosis, pyroptosis, and necroptosis.
Kaiyuan Song, Yongbin Wu, Sipin Tan
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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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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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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 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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