The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak/Bax if Mcl-1 is neutralized.
By M. V. van Delft, A. Wei, K. Mason, C. Vandenberg, Lin Chen, P. Czabotar, Simon N. Willis, C. Scott, C. Day, Suzanne Cory and 3 more. Cancer Cell, 2006
1,255 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/898aed0b5d0b02a5a2421aa2a23cd96efc899526
How researchers see this paper
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In Molecular Biology
- Guido Kroemer
- Douglas R. Green
- L. Galluzzi
- Jerry M. Adams
- Simone Fulda
- Suzanne Cory
- F. Llambi
- J. Chipuk
In Oncology
- Guido Kroemer
- Jerry M. Adams
- L. Galluzzi
- Simone Fulda
- Suzanne Cory
- Douglas R. Green
- P. Czabotar
- Stephen W. Fesik
Citations in the corpus
- How do BCL-2 proteins induce mitochondrial outer membrane permeabilization? (2008, positive): “Thiscombination is necessary because ABT-737 can release BIM from BCL-2, BCL-xL and BCL-w and forces a BIM‐MCL-1 interaction to preserve survival [19,33,40, 41 ].”
- BCL-2 family antagonists for cancer therapy (2008, background): “In the case of BH3I-1, HA14-1, compound 6, antimycin A and chelerythrine, cell-death activity on mouse embryonic fibroblasts (MEFs) has been shown to be independent of BAX and BAK, which suggests that the weak binding affinity of all these compounds to the BCL-2 family of proteins is not related to ”
- Mitochondrial apoptosis: killing cancer using the enemy within (2015, background): “Indeed, the gene encoding BCL-2 was first identified at a chromosomal translocation breakpoint that places BCL-2 under immunoglobulin heavy chain enhancer transcriptional control, leading to constitutively high BCL-2 expression (Tsujimoto et al, 1984).”
- ROLE OF BNIP3 AND NIX IN CELL DEATH, AUTOPHAGY, AND MITOPHAGY (2009, neutral): “67 requires BAX or BAK to induce mitochondrial depolarization (unpublished results) and cell death”
- BCL-2 inhibition targets oxidative phosphorylation and selectively eradicates quiescent human leukemia stem cells (2013, background): “Knocking down BCL-XL (the other known target of ABT-263) (van Delft et al., 2006) by specific shRNA did not have a significant effect on the OXPHOS of primary leukemic cells (Figure S4F).”
- The BCL-2 Family Reunion (2010, background): “Overexpression of MCL-1 has been shown to be a potent mechanism of resistance to ABT737 and ABT-263, and agents that promote degradation of MCL-1 work synergistically to promote apoptosis (van Delft et al., 2006).”
- Targeting mitochondria for cancer therapy (2010, background): “Notably, BH3-only proteins released from interactions with BCL-2, BCL-X L and BCL-W by ABT-737 can still interact with another anti-apoptotic protein from the BCL-2 family that is not antagonized by ABT-737, namely MCL1 (Ref”
- The Bcl-2 apoptotic switch in cancer development and therapy (2007, background): “Studies with the BH3 mimetic drug ABT-737 (see below) are also consistent with this model (Konopleva et al., 2006; van Delft et al., 2006; Willis et al., 2007).”
- ABT-263: a potent and orally bioavailable Bcl-2 family inhibitor. (2008, background): “in a cellular context and is consistent with previous observations with ABT-737 (7, 11, 13, 14, 26).”
- Functional and physical interaction between Bcl‐XL and a BH3‐like domain in Beclin‐1 (2007, background): “This can be explained by the selectivity of ABT737, which binds to Bcl-2 and Bcl-XL but not to Mcl-1, and hence has a Bad-like profile (Oltersdorf et al, 2005, Van Delft et al, 2006).”