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ProteomicsCovalent Inhibition of Pro-Apoptotic BAX
BCL-2-associated X protein (BAX) is a promising therapeutic target for activating or restraining apoptosis in diseases of pathologic cell survival or cell death, respectively. In response to cellular stress, BAX transforms from a quiescent cytosolic monomer into a toxic oligomer that permeabilizes t...
ORGANISM(S): Homo sapiens (Human) 
2024-01-19 | PXD040917 | Pride
Bax  hdx-ms  hydrogen/deuterium exchange mass spectrometry  covalent inhibitor 
ProteomicsInhibition of Oligomeric BAX by an Anti-Apoptotic Dimer
BAX is a pro-apoptotic BCL-2 protein that resides in the cytosol as a monomer until triggered by cellular stress to transform into an oligomer that permeabilizes the mitochondria and induces apoptosis. We previously reported the generation of a full-length BAX oligomer (BAXO) that recapitulates pro-...
ORGANISM(S): Homo sapiens (Human) 
2025-11-21 | PXD049315 | Pride
Bcl-w  bax  bcl-w dimer  bax oligomer  hdx-ms  hydrogen/deuterium exchange mass spectrometry  apoptotic regulation 
UnknownAllosteric sensitization of proapoptotic BAX.
Not available
S-EPMC5675120 | biostudies-literature
UnknownCovalent inhibition of pro-apoptotic BAX.
Not available
S-EPMC11252247 | biostudies-literature
UnknownEltrombopag directly inhibits BAX and prevents cell death.
Not available
S-EPMC7892824 | biostudies-literature
UnknownHomogeneous Oligomers of Pro-apoptotic BAX Reveal Structural Determinants of Mitochondrial Membrane Permeabilization.
Not available
S-EPMC7472837 | biostudies-literature
UnknownConformational Heterogeneity in the Activation Mechanism of Bax.
Not available
S-EPMC5558158 | biostudies-literature
UnknownMitochondrial residence of the apoptosis inducer BAX is more important than BAX oligomerization in promoting membrane permeabilization.
Not available
S-EPMC7008371 | biostudies-literature
UnknownMolecular details of Bax activation, oligomerization, and membrane insertion.
Not available
S-EPMC2825459 | biostudies-literature
UnknownBax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis.
Not available
S-EPMC1150878 | biostudies-literature
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