2017
Neuronal Death After Hemorrhagic Stroke In Vitro and In Vivo Shares Features of Ferroptosis and Necroptosis
Zille M, Karuppagounder SS, Chen Y, Gough PJ, Bertin J, Finger J, Milner TA, Jonas EA, Ratan RR. Neuronal Death After Hemorrhagic Stroke In Vitro and In Vivo Shares Features of Ferroptosis and Necroptosis. Stroke 2017, 48: 1033-1043. PMID: 28250197, PMCID: PMC5613764, DOI: 10.1161/strokeaha.116.015609.Peer-Reviewed Original ResearchConceptsCell death mechanismsCaspase-dependent apoptosisDeath mechanismsMolecular markersChemical inhibitorsCell death pathwaysNecroptotic cell deathSecondary injuryNecroptotic signalingDeath pathwaysNecrotic phenotypeIntracerebral hemorrhageCell deathMRNA synthesisNecroptosisIntracerebral hemorrhage (ICH) resultsShare featuresFerroptosisHemin-induced toxicityFerroptosis inhibitorsAutophagyCultured neuronsApoptosisHemorrhage resultsNeuronal necrosis
2014
Mitochondrial membrane protein Bcl-xL, a regulator of adult neuronal growth and synaptic plasticity: multiple functions beyond apoptosis
Park HA, Jonas EA. Mitochondrial membrane protein Bcl-xL, a regulator of adult neuronal growth and synaptic plasticity: multiple functions beyond apoptosis. Neural Regeneration Research 2014, 9: 1706-1707. PMID: 25422630, PMCID: PMC4238157, DOI: 10.4103/1673-5374.143413.Peer-Reviewed Original Research
2012
Multipolar functions of BCL-2 proteins link energetics to apoptosis
Hardwick JM, Chen YB, Jonas EA. Multipolar functions of BCL-2 proteins link energetics to apoptosis. Trends In Cell Biology 2012, 22: 318-328. PMID: 22560661, PMCID: PMC3499971, DOI: 10.1016/j.tcb.2012.03.005.Peer-Reviewed Original ResearchConceptsBcl-2 proteinClassical apoptotic cell deathBcl-2 family proteinsSub-mitochondrial localizationApoptotic cell deathFamily proteinsClassical apoptosisBiochemical activityApoptosis regulatorCritical crosstalkCell survivalCell deathProteinApoptosisProfound effectCellsMultipolar functionsRegulatorCrosstalkLocalizationCurrent assumptionsDeath
2005
The Role of the Mitochondrial Apoptosis Induced Channel MAC in Cytochrome c Release
Martinez-Caballero S, Dejean LM, Jonas EA, Kinnally KW. The Role of the Mitochondrial Apoptosis Induced Channel MAC in Cytochrome c Release. Journal Of Bioenergetics And Biomembranes 2005, 37: 155-164. PMID: 16167172, DOI: 10.1007/s10863-005-6570-z.Peer-Reviewed Original ResearchConceptsMitochondrial apoptosis-induced channelBcl-2 family proteinsMitochondrial outer membraneCytochrome cOuter membrane integrityCytochrome c releaseHigh-conductance channelPermeability transition poreIntermembrane spaceFamily proteinsCommitment stepOuter membraneC releaseProapoptotic factorsTransition poreSingle-channel behaviorMAC formationMembrane integrityCrucial eventEarly apoptosisApoptosisMolecular compositionRelease channelMAC activityMitochondriaOligomeric Bax Is a Component of the Putative Cytochrome c Release Channel MAC, Mitochondrial Apoptosis-induced Channel
Dejean LM, Martinez-Caballero S, Guo L, Hughes C, Teijido O, Ducret T, Ichas F, Korsmeyer SJ, Antonsson B, Jonas EA, Kinnally KW. Oligomeric Bax Is a Component of the Putative Cytochrome c Release Channel MAC, Mitochondrial Apoptosis-induced Channel. Molecular Biology Of The Cell 2005, 16: 2424-2432. PMID: 15772159, PMCID: PMC1087246, DOI: 10.1091/mbc.e04-12-1111.Peer-Reviewed Original ResearchConceptsMitochondrial apoptosis-induced channelOligomeric BaxBcl-2 family proteinsHeLa cellsBcl-2-overexpressing cellsCytochrome cChannel activityMAC activityIntrinsic apoptotic pathwayApoptotic cellsFamily proteinsIntrinsic apoptosisApoptotic pathwaySingle-channel behaviorMitochondriaBaxBax antibodiesMean conductanceBakUntreated cellsRelease channelProteinApoptosisCellsTranslocation