Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis

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tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome cPreprint

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Bid Induces the Oligomerization and Insertion of Bax into the Outer Mitochondrial Membrane

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Loss of OPA1 Perturbates the Mitochondrial Inner Membrane Structure and Integrity, Leading to Cytochrome c Release and Apoptosis

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Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c

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OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L

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Mitochondrial Rhomboid PARL Regulates Cytochrome c Release during Apoptosis via OPA1-Dependent Cristae Remodeling

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Bax Is Present as a High Molecular Weight Oligomer/Complex in the Mitochondrial Membrane of Apoptotic Cells

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Regulation of OPA1 processing and mitochondrial fusion by m -AAA protease isoenzymes and OMA1

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Bax Crystal Structures Reveal How BH3 Domains Activate Bax and Nucleate Its Oligomerization to Induce Apoptosis

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Membrane Binding by tBid Initiates an Ordered Series of Events Culminating in Membrane Permeabilization by Bax

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Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells

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Bax and Bak Coalesce into Novel Mitochondria-Associated Clusters during Apoptosis

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BID, BIM, and PUMA Are Essential for Activation of the BAX- and BAK-Dependent Cell Death Program

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Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis

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Stress‐induced OMA1 activation and autocatalytic turnover regulate OPA1‐dependent mitochondrial dynamics

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Opa1-Mediated Cristae Opening Is Bax/Bak and BH3 Dependent, Required for Apoptosis, and Independent of Bak Oligomerization

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Loss of mitochondrial protease OMA1 alters processing of the GTPase OPA1 and causes obesity and defective thermogenesis in mice

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Release of OPA1 during Apoptosis Participates in the Rapid and Complete Release of Cytochrome c and Subsequent Mitochondrial Fragmentation

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Bax-type Apoptotic Proteins Porate Pure Lipid Bilayers through a Mechanism Sensitive to Intrinsic Monolayer Curvature

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Oligomeric Bax Is a Component of the Putative Cytochrome c Release Channel MAC, Mitochondrial Apoptosis-induced Channel

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YME1L controls the accumulation of respiratory chain subunits and is required for apoptotic resistance, cristae morphogenesis, and cell proliferation

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tBid interaction with cardiolipin primarily orchestrates mitochondrial dysfunctions and subsequently activates Bax and Bak

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Mitochondrial Outer Membrane Proteins Assist Bid in Bax-mediated Lipidic Pore Formation

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Assembly of the Mitochondrial Apoptosis-induced Channel, MAC

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tBid Elicits a Conformational Alteration in Membrane-bound Bcl-2 Such That It Inhibits Bax Pore Formation

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Mitochondria as multifaceted regulators of cell death

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Neuronal Cell Death

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Oxidative stress and diabetic retinopathy: Molecular mechanisms, pathogenetic role and therapeutic implications

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Bid Induces the Oligomerization and Insertion of Bax into the Outer Mitochondrial Membrane

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Bax directly induces release of cytochrome c from isolated mitochondria

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