BCL-2, BCL-XL Sequester BH3 Domain-Only Molecules Preventing BAX- and BAK-Mediated Mitochondrial Apoptosis
Emily H. Cheng,Michael C. Wei,Solly Weiler,Richard A. Flavell,Tak W. Mak,Tullia Lindsten,Stanley J. Korsmeyer +6 more
TL;DR: In mammals, BH3 domain-only molecules activate multidomain proapoptotic members to trigger a mitochondrial pathway, which both releases cytochrome c to activate caspases and initiates caspase-independent mitochondrial dysfunction.
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About: This article is published in Molecular Cell. The article was published on 01 Sep 2001. and is currently open access. The article focuses on the topics: Mitochondrial apoptosis-induced channel & Bcl-2-associated X protein.
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Citations
Upgrading the BCL-2 network.
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Inhibition of neuronal apoptosis in vitro and in vivo using TAT-mediated protein transduction.
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PECAM-1 functions as a specific and potent inhibitor of mitochondrial-dependent apoptosis.
Cunji Gao,Weiyong Sun,Melpo Christofidou-Solomidou,Motoshi Sawada,Debra K. Newman,Carmen Bergom,Steven M. Albelda,Shigemi Matsuyama,Peter J. Newman +8 more
TL;DR: In this article, platelet endothelial cell adhesion molecule-1 (PECAM-1), a homophilic-binding member of the immunoreceptor tyrosine-based inhibitory motif (ITIM) family of inhibitory receptors, functions prominently to inhibit apoptosis in naturally occurring vascular cells subjected to apoptotic stimuli.
138
Apoptosis induction by Bid requires unconventional ubiquitination and degradation of its N-terminal fragment
TL;DR: It is concluded that unconventional ubiquitination and proteasome-dependent degradation of tBid-N is required to unleash the proapoptotic activity of t Bcl-2 homology 3 (BH3) domain in the cleaved complex.
Microglia-derived TNFα induces apoptosis in neural precursor cells via transcriptional activation of the Bcl-2 family member Puma.
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137
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Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade
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Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death
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Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors
TL;DR: The purification of a cytosolic protein that induces cytochrome c release from mitochondria in response to caspase-8, the apical caspases activated by cell surface death receptors such as Fas and TNF is reported.
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Apaf-1, a Human Protein Homologous to C. elegans CED-4, Participates in Cytochrome c–Dependent Activation of Caspase-3
TL;DR: The purification and cDNA cloning of Apaf-1, a novel 130 kd protein from HeLa cell cytosol that participates in the cytochrome c-dependent activation of caspase-3, leading to apoptosis is reported here.
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