Toxic proteins released from mitochondria in cell death
By X. Saelens, N. Festjens, L. Walle, Maria van Gurp, G. van Loo, Peter Vandenabeele. Oncogene, 2004
1,098 citations recorded by the source corpus.
Subfields: Epidemiology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/aa4f03455355156c23710f7fadf499624722f7e2
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Citations in the corpus
- Apoptosis and Molecular Targeting Therapy in Cancer (2014, background): “Two of these naturally occurring IAP-antagonists, SMAC (Diablo) and HtrA2 (Omi), are sequestered inside mitochondria, becoming released into the cytosol during apoptosis [51].”
- Caspase-mediated cleavage of Beclin-1 inactivates Beclin-1-induced autophagy and enhances apoptosis by promoting the release of proapoptotic factors from mitochondria (2010, background): “pathway by death-receptor triggering, or via the intrinsic pathway when mitochondrial pro-death factors, such as cytochrome c (cyt c) and HtrA2 (high-temperature requirement protein-A2)/Omi, are released.(10) Apoptotic signaling leads to activation of caspases (casps), which specifically cleave nati”
- Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy (2006, background): “…of cytochrome c into the cytosol directly triggers caspase-3 activation through formation of the cytochrome c/Apaf-1/caspase-9-containing apoptosome complex, Smac/DIABLO and Omi/HtrA2 indirectly promote caspase activation through antagonizing the inhibitory effects to IAPs (Saelens et al., 2004).”
- Mitochondrial Ceramide and the Induction of Apoptosis (2005, background): “…is often an increase in the permeability of the mitochondrial outer membrane that leads to the release of intermembrane space proteins, including cytochrome c, procaspases, apoptosis-inducing factor (AIF), heat shock proteins, Smac/Diablo, and endonuclease G (for review see Saelens et al., 2004).”