Apoptosis Initiated When BH3 Ligands Engage Multiple Bcl-2 Homologs, Not Bax or Bak
By Simon N. Willis, J. Fletcher, T. Kaufmann, M. F. V. Delft, Lin Chen, P. Czabotar, Helen Ierino, Erinna F. Lee, W. Fairlie, P. Bouillet and 4 more. Science, 2007
1,236 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/8049ef99ed491acffcd2f1a781a55a29d36953bc
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Citations in the corpus
- Control of mitochondrial apoptosis by the Bcl-2 family (2009, background): “By contrast, however, a combined knockout of Bid and Bim results in relatively minor defects in apoptosis (Willis et al., 2007), but it is likely that additional factors other than Bid and Bim can act as activators.”
- Neuronal Cell Death. (2018, neutral): “The ability of Puma, Bim, and Bid to bind with high affinity to all anti-apoptotic Bcl-2 proteins may provide an explanation for their relatively high potency in terms of inducing apoptosis compared with other BH3-only proteins (729).”
- Cellular Stress Responses: Cell Survival and Cell Death (2010, background): “In contrast, the indirect activation model proposes that BH3-only proteins activate Bax and Bak in an indirect manner by binding to the multiple anti-apoptotic Bcl-2 proteins that inhibit Bax and Bak, which in turn leads to the release of Bax and Bak [33, 34].”
- How do BCL-2 proteins induce mitochondrial outer membrane permeabilization? (2008, neutral): “However, if the direct activators are limited to BID and BIM, as suggested [ 17 ,32], why are bid/; bim/ cells”
- Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax. (2008, background): “Experiments using soluble protein domains and peptides have failed to demonstrate productive interactions between BH3-only proteins and Bax (Willis et al., 2007), whereas in other studies, membrane permeabilization in cells, isolated mitochondria, or liposomes by full-length Bax usually depends…”