2025
S-Nitrosylation of CRTC1 in Alzheimer’s disease impairs CREB-dependent gene expression induced by neuronal activity
Zhang X, Vlkolinsky R, Wu C, Dolatabadi N, Scott H, Prikhodko O, Zhang A, Blanco M, Lang N, Piña-Crespo J, Nakamura T, Roberto M, Lipton S. S-Nitrosylation of CRTC1 in Alzheimer’s disease impairs CREB-dependent gene expression induced by neuronal activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2025, 122: e2418179122. PMID: 40014571, PMCID: PMC11892585, DOI: 10.1073/pnas.2418179122.Peer-Reviewed Original ResearchConceptsActivity-dependent gene expressionGene expressionAlzheimer's diseaseCREB-dependent gene expressionS-nitrosylationNitric oxide (NO)-related speciesTargets of S-nitrosylationNeuronal activity-dependent gene expressionPathogenesis of ADDecreased neurite lengthIncreased neuronal cell deathNeuronal cell deathSynaptic plasticityTranscriptional pathwaysCell deathCRISPR/Cas9 techniqueTranscription coactivator 1AD modelLong-term memory formationIncreased S-nitrosylationLong-term potentiationTherapeutic targetExpressionNeurite lengthCerebrocortical neurons
2023
S-Nitrosylation-mediated dysfunction of TCA cycle enzymes in synucleinopathy studied in postmortem human brains and hiPSC-derived neurons
Doulias P, Yang H, Andreyev A, Dolatabadi N, Scott H, K Raspur C, Patel P, Nakamura T, Tannenbaum S, Ischiropoulos H, Lipton S. S-Nitrosylation-mediated dysfunction of TCA cycle enzymes in synucleinopathy studied in postmortem human brains and hiPSC-derived neurons. Cell Chemical Biology 2023, 30: 965-975.e6. PMID: 37478858, PMCID: PMC10530441, DOI: 10.1016/j.chembiol.2023.06.018.Peer-Reviewed Original ResearchConceptsTCA cycleLewy body dementiaAberrant S-nitrosylationMitochondrial metabolic dysfunctionTricarboxylic acid cyclePluripotent stem cellsMitochondrial energy metabolismParkinson's diseaseHiPSC-derived neuronsTCA enzymesMetabolic flux experimentsS-nitrosylationAcid cycleCell deathNeuronal cell deathΑ-ketoglutaratePostmortem human brainEnergy metabolismStem cellsLBD brainsDendritic lengthBioenergetic failureMetabolic dysfunctionSynaptic integrityPathophysiological relevanceApoptotic cell death in disease—Current understanding of the NCCD 2023
Vitale I, Pietrocola F, Guilbaud E, Aaronson S, Abrams J, Adam D, Agostini M, Agostinis P, Alnemri E, Altucci L, Amelio I, Andrews D, Aqeilan R, Arama E, Baehrecke E, Balachandran S, Bano D, Barlev N, Bartek J, Bazan N, Becker C, Bernassola F, Bertrand M, Bianchi M, Blagosklonny M, Blander J, Blandino G, Blomgren K, Borner C, Bortner C, Bove P, Boya P, Brenner C, Broz P, Brunner T, Damgaard R, Calin G, Campanella M, Candi E, Carbone M, Carmona-Gutierrez D, Cecconi F, Chan F, Chen G, Chen Q, Chen Y, Cheng E, Chipuk J, Cidlowski J, Ciechanover A, Ciliberto G, Conrad M, Cubillos-Ruiz J, Czabotar P, D’Angiolella V, Daugaard M, Dawson T, Dawson V, De Maria R, De Strooper B, Debatin K, Deberardinis R, Degterev A, Del Sal G, Deshmukh M, Di Virgilio F, Diederich M, Dixon S, Dynlacht B, El-Deiry W, Elrod J, Engeland K, Fimia G, Galassi C, Ganini C, Garcia-Saez A, Garg A, Garrido C, Gavathiotis E, Gerlic M, Ghosh S, Green D, Greene L, Gronemeyer H, Häcker G, HajnĂłczky G, Hardwick J, Haupt Y, He S, Heery D, Hengartner M, Hetz C, Hildeman D, Ichijo H, Inoue S, Jäättelä M, Janic A, Joseph B, Jost P, Kanneganti T, Karin M, Kashkar H, Kaufmann T, Kelly G, Kepp O, Kimchi A, Kitsis R, Klionsky D, Kluck R, Krysko D, Kulms D, Kumar S, Lavandero S, Lavrik I, Lemasters J, Liccardi G, Linkermann A, Lipton S, Lockshin R, LĂłpez-OtĂn C, Luedde T, MacFarlane M, Madeo F, Malorni W, Manic G, Mantovani R, Marchi S, Marine J, Martin S, Martinou J, Mastroberardino P, Medema J, Mehlen P, Meier P, Melino G, Melino S, Miao E, Moll U, Muñoz-Pinedo C, Murphy D, Niklison-Chirou M, Novelli F, Núñez G, Oberst A, Ofengeim D, Opferman J, Oren M, Pagano M, Panaretakis T, Pasparakis M, Penninger J, Pentimalli F, Pereira D, Pervaiz S, Peter M, Pinton P, Porta G, Prehn J, Puthalakath H, Rabinovich G, Rajalingam K, Ravichandran K, Rehm M, Ricci J, Rizzuto R, Robinson N, Rodrigues C, Rotblat B, Rothlin C, Rubinsztein D, Rudel T, Rufini A, Ryan K, Sarosiek K, Sawa A, Sayan E, Schroder K, Scorrano L, Sesti F, Shao F, Shi Y, Sica G, Silke J, Simon H, Sistigu A, Stephanou A, Stockwell B, Strapazzon F, Strasser A, Sun L, Sun E, Sun Q, Szabadkai G, Tait S, Tang D, Tavernarakis N, Troy C, Turk B, Urbano N, Vandenabeele P, Vanden Berghe T, Vander Heiden M, Vanderluit J, Verkhratsky A, Villunger A, von Karstedt S, Voss A, Vousden K, Vucic D, Vuri D, Wagner E, Walczak H, Wallach D, Wang R, Wang Y, Weber A, Wood W, Yamazaki T, Yang H, Zakeri Z, Zawacka-Pankau J, Zhang L, Zhang H, Zhivotovsky B, Zhou W, Piacentini M, Kroemer G, Galluzzi L. Apoptotic cell death in disease—Current understanding of the NCCD 2023. Cell Death & Differentiation 2023, 30: 1097-1154. PMID: 37100955, PMCID: PMC10130819, DOI: 10.1038/s41418-023-01153-w.Peer-Reviewed Original ResearchConceptsRegulated cell deathCell deathAdult tissue homeostasisMultiple human disordersApoptotic cell deathOrganismal developmentOrganismal homeostasisMolecular machineryContext of diseaseApoptotic apparatusMammalian systemsCaspase familyTissue homeostasisGenetic strategiesHuman disordersNomenclature CommitteeApoptosisHomeostasisMachineryOncogenesisProteaseCell lossActivationFamilyDeath
2014
Essential versus accessory aspects of cell death: recommendations of the NCCD 2015
Galluzzi L, Bravo-San Pedro JM, Vitale I, Aaronson SA, Abrams JM, Adam D, Alnemri ES, Altucci L, Andrews D, Annicchiarico-Petruzzelli M, Baehrecke EH, Bazan NG, Bertrand MJ, Bianchi K, Blagosklonny MV, Blomgren K, Borner C, Bredesen DE, Brenner C, Campanella M, Candi E, Cecconi F, Chan FK, Chandel NS, Cheng EH, Chipuk JE, Cidlowski JA, Ciechanover A, Dawson TM, Dawson VL, De Laurenzi V, De Maria R, Debatin KM, Di Daniele N, Dixit VM, Dynlacht BD, El-Deiry WS, Fimia GM, Flavell RA, Fulda S, Garrido C, Gougeon ML, Green DR, Gronemeyer H, Hajnoczky G, Hardwick JM, Hengartner MO, Ichijo H, Joseph B, Jost PJ, Kaufmann T, Kepp O, Klionsky DJ, Knight RA, Kumar S, Lemasters JJ, Levine B, Linkermann A, Lipton SA, Lockshin RA, LĂłpez-OtĂn C, Lugli E, Madeo F, Malorni W, Marine JC, Martin SJ, Martinou JC, Medema JP, Meier P, Melino S, Mizushima N, Moll U, Muñoz-Pinedo C, Nuñez G, Oberst A, Panaretakis T, Penninger JM, Peter ME, Piacentini M, Pinton P, Prehn JH, Puthalakath H, Rabinovich GA, Ravichandran KS, Rizzuto R, Rodrigues CM, Rubinsztein DC, Rudel T, Shi Y, Simon HU, Stockwell BR, Szabadkai G, Tait SW, Tang HL, Tavernarakis N, Tsujimoto Y, Vanden Berghe T, Vandenabeele P, Villunger A, Wagner EF, Walczak H, White E, Wood WG, Yuan J, Zakeri Z, Zhivotovsky B, Melino G, Kroemer G. Essential versus accessory aspects of cell death: recommendations of the NCCD 2015. Cell Death & Differentiation 2014, 22: 58-73. PMID: 25236395, PMCID: PMC4262782, DOI: 10.1038/cdd.2014.137.Peer-Reviewed Original ResearchConceptsRegulated cell deathAccidental cell deathCell deathCellular demiseCourse of apoptosisAdaptive responseExecutioner caspasesMammalian systemsLethal signalPhysiologic programGenetic interventionsNomenclature CommitteeBiochemical phenomenaCytoprotective effectsMechanical stimuliCaspasesTransductionBiochemical correlatesApoptosisCytoprotectionDeathCellsActivationResponseVariantsConcept of Excitotoxicity via Glutamate Receptors
Piña-Crespo J, Sanz-Blasco S, Lipton S. Concept of Excitotoxicity via Glutamate Receptors. 2014, 1015-1038. DOI: 10.1007/978-1-4614-5836-4_125.Peer-Reviewed Original ResearchDownstream intracellular signaling cascadesIntracellular signaling cascadesGlutamate receptorsPattern of expressionUncovering genesNeuroprotective therapiesIntracellular effectorsSignaling cascadesCell injuryMolecular mechanismsSecond messengerGlutamate receptor overactivationMolecular biologyDisease statesCell deathNeuropsychiatric diseasesNitric oxideInositol phospholipidsAmino acidsCell surfaceConcept of excitotoxicityPotential neuroprotective therapiesExcitatory amino acidsGlutamate-mediated neurotoxicityNerve cell injury
2011
Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012
Galluzzi L, Vitale I, Abrams J, Alnemri E, Baehrecke E, Blagosklonny M, Dawson T, Dawson V, El-Deiry W, Fulda S, Gottlieb E, Green D, Hengartner M, Kepp O, Knight R, Kumar S, Lipton S, Lu X, Madeo F, Malorni W, Mehlen P, Nuñez G, Peter M, Piacentini M, Rubinsztein D, Shi Y, Simon H, Vandenabeele P, White E, Yuan J, Zhivotovsky B, Melino G, Kroemer G. Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012. Cell Death & Differentiation 2011, 19: 107-120. PMID: 21760595, PMCID: PMC3252826, DOI: 10.1038/cdd.2011.96.Peer-Reviewed Original ResearchConceptsCell death subroutinesCell death modalitiesCell deathDeath modalitiesMitotic catastropheMolecular definitionCell death morphologyAutophagic cell deathUtility of expressionNomenclature CommitteeExtrinsic apoptosisDeath morphologyRegulated necrosisIntrinsic apoptosisGenetic explorationFunctional classificationApoptosisBiochemical featuresVivo settingsSubstantial progressExpressionDeathRole of the Mitochondrial Fission Protein Drp1 in Synaptic Damage and Neurodegeneration
Nakamura T, Cho D, Lipton S. Role of the Mitochondrial Fission Protein Drp1 in Synaptic Damage and Neurodegeneration. 2011, 215-234. DOI: 10.1007/978-94-007-1291-1_8.Peer-Reviewed Original ResearchMitochondrial fission protein Drp1Fission protein Drp1Mitochondrial fissionProtein Drp1Dynamin-related protein 1Abnormal mitochondrial morphologyMitochondrial fusionDrp1 activityPosttranslational modificationsMitochondrial morphologyMitochondrial structureCell deathDrp1Protein 1Recent insightsNeurodegenerative diseasesSynaptic damageNeuronal cell injuryNeurodegenerative conditionsFissionMitofusinsDynaminGTPasesFusionOPA1
2009
Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes
Galluzzi L, Aaronson SA, Abrams J, Alnemri ES, Andrews DW, Baehrecke EH, Bazan NG, Blagosklonny MV, Blomgren K, Borner C, Bredesen DE, Brenner C, Castedo M, Cidlowski JA, Ciechanover A, Cohen GM, De Laurenzi V, De Maria R, Deshmukh M, Dynlacht BD, El-Deiry WS, Flavell RA, Fulda S, Garrido C, Golstein P, Gougeon ML, Green DR, Gronemeyer H, Hajnóczky G, Hardwick JM, Hengartner MO, Ichijo H, Jäättelä M, Kepp O, Kimchi A, Klionsky DJ, Knight RA, Kornbluth S, Kumar S, Levine B, Lipton SA, Lugli E, Madeo F, Malorni W, Marine J, Martin SJ, Medema JP, Mehlen P, Melino G, Moll UM, Morselli E, Nagata S, Nicholson DW, Nicotera P, Nuñez G, Oren M, Penninger J, Pervaiz S, Peter ME, Piacentini M, Prehn JH, Puthalakath H, Rabinovich GA, Rizzuto R, Rodrigues CM, Rubinsztein DC, Rudel T, Scorrano L, Simon HU, Steller H, Tschopp J, Tsujimoto Y, Vandenabeele P, Vitale I, Vousden KH, Youle RJ, Yuan J, Zhivotovsky B, Kroemer G. Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes. Cell Death & Differentiation 2009, 16: 1093-1107. PMID: 19373242, DOI: 10.1038/cdd.2009.44.Peer-Reviewed Original ResearchConceptsCell deathNumerous human diseasesDead cellsHigher eukaryotesModel organismsCellular demisePhysiological processesHuman diseasesInterpretation of assaysNovel therapeutic strategiesPathological scenariosCell culturesBiomedical researchCellsEukaryotesAssaysTherapeutic strategiesTremendous implicationsOrganismsDeregulationCascadeDozens of methodsDeathDepth investigation
2007
Molecular mechanisms of nitrosative stress-mediated protein misfolding in neurodegenerative diseases
Nakamura T, Lipton S. Molecular mechanisms of nitrosative stress-mediated protein misfolding in neurodegenerative diseases. Cellular And Molecular Life Sciences 2007, 64: 1609-1620. PMID: 17453143, PMCID: PMC11136414, DOI: 10.1007/s00018-007-6525-0.Peer-Reviewed Original ResearchConceptsUbiquitin-proteasome systemNormal protein degradationProtein disulfide isomeraseMolecular chaperonesSpecific chaperonesGlucose-regulated protein 78Proper foldingProtein misfoldingAberrant proteinsProtein foldingUPS proteinsProtein degradationMolecular mechanismsShock proteinsConformational changesExcessive reactive oxygenCell deathNeuronal cell deathProteinChaperonesProtein 78Reactive oxygenMisfoldingNitrogen speciesNitrosative stressS-Nitrosylation and uncompetitive/fast off-rate (UFO) drug therapy in neurodegenerative disorders of protein misfolding
Nakamura T, Lipton S. S-Nitrosylation and uncompetitive/fast off-rate (UFO) drug therapy in neurodegenerative disorders of protein misfolding. Cell Death & Differentiation 2007, 14: 1305-1314. PMID: 17431424, DOI: 10.1038/sj.cdd.4402138.Peer-Reviewed Original ResearchConceptsS-nitrosylationProtein functionProtein misfoldingCell deathNeuronal cell deathProper protein foldingProtein disulfide isomeraseCysteine thiol groupsHeat shock proteinsExcessive NMDA receptor activityGlucose-regulated protein 78Neurodegenerative disordersProtein foldingExcitotoxic damageFree radical nitric oxideConformational changesMisfoldingForm of neurotoxicityRadical nitric oxideN-methyl-D-aspartate receptorsNitric oxideExcessive activityProteinProtein 78Chronic neurodegenerative disorders
2006
Mitochondrial fission is an upstream and required event for bax foci formation in response to nitric oxide in cortical neurons
Yuan H, Gerencser A, Liot G, Lipton S, Ellisman M, Perkins G, Bossy-Wetzel E. Mitochondrial fission is an upstream and required event for bax foci formation in response to nitric oxide in cortical neurons. Cell Death & Differentiation 2006, 14: 462-471. PMID: 17053808, DOI: 10.1038/sj.cdd.4402046.Peer-Reviewed Original ResearchConceptsMitochondrial fissionNitric oxideFoci formationCortical neuronsMitochondrial fission machineryBcl-2 familyNitrosative stressAntiapoptotic Bcl-xLNeuronal cell deathFission machineryMitofusin 1Puncta formationBioenergetic crisisBax accumulationMitochondrial inhibitorsNeuronal demiseBcl-xLCell deathMitochondrial dysfunctionMitochondriaNeurodegenerative disordersNO donorNeuronsScission siteFissionHIV-1 coreceptors CCR5 and CXCR4 both mediate neuronal cell death but CCR5 paradoxically can also contribute to protection
Kaul M, Ma Q, Medders K, Desai M, Lipton S. HIV-1 coreceptors CCR5 and CXCR4 both mediate neuronal cell death but CCR5 paradoxically can also contribute to protection. Cell Death & Differentiation 2006, 14: 296-305. PMID: 16841089, DOI: 10.1038/sj.cdd.4402006.Peer-Reviewed Original ResearchConceptsHuman immunodeficiency virus-1Neuronal cell deathStromal cell-derived factor-1HIV-1 envelope glycoprotein gp120Cell-derived factor-1Cell deathHIV-1 coreceptor CCR5Chemokine receptor CCR5Immunodeficiency virus-1Brain-derived cellsEnvelope glycoprotein gp120Intracellular free Ca2Gp120 neurotoxicityCCR5 ligandsHIV coreceptorsP38 mitogen-activated protein kinaseCCR5 agonistsNeuroprotective pathwaysReceptor CCR5Heterologous desensitizationCoreceptor CCR5CXCR4 agonistCCR5Glial culturesGlycoprotein gp120
2000
Functional role and therapeutic implications of neuronal caspase-1 and -3 in a mouse model of traumatic spinal cord injury
Li M, Ona V, Chen M, Kaul M, Tenneti L, Zhang X, Stieg P, Lipton S, Friedlander R. Functional role and therapeutic implications of neuronal caspase-1 and -3 in a mouse model of traumatic spinal cord injury. Neuroscience 2000, 99: 333-342. PMID: 10938439, DOI: 10.1016/s0306-4522(00)00173-1.Peer-Reviewed Original ResearchConceptsSpinal cord injuryCord injuryCaspase-1Acute central nervous system insultLesion sizeCentral nervous system insultsTraumatic spinal cord injuryVehicle-treated miceSham-operated miceNervous system insultsCaspase-3Spinal cord samplesNon-neuronal cellsN-benzyloxycarbonyl-ValCaspase-1 activityCaspase-3 expressionCell deathNeurological dysfunctionCord samplesMotor functionTissue injuryMouse modelTherapeutic implicationsTransgenic miceTissue damageRole of p38 Mitogen-Activated Protein Kinase in Axotomy-Induced Apoptosis of Rat Retinal Ganglion Cells
Kikuchi M, Tenneti L, Lipton S. Role of p38 Mitogen-Activated Protein Kinase in Axotomy-Induced Apoptosis of Rat Retinal Ganglion Cells. Journal Of Neuroscience 2000, 20: 5037-5044. PMID: 10864961, PMCID: PMC6772303, DOI: 10.1523/jneurosci.20-13-05037.2000.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisAxonal TransportAxotomyCell NucleusCell SurvivalDizocilpine MaleateEnzyme InhibitorsFluorescent DyesImidazolesKineticsMaleMitogen-Activated Protein KinasesNeuroprotective AgentsOptic Nervep38 Mitogen-Activated Protein KinasesPhosphorylationPyridinesRatsRats, Long-EvansRetinal Ganglion CellsSignal TransductionStilbamidinesTime FactorsConceptsRetinal ganglion cellsProtein kinaseP38 Mitogen-Activated Protein KinaseMitogen-Activated Protein KinaseMAP kinase activationIntracellular signal transductionRole of p38P38 MAP kinase activationApoptotic cell deathDose-dependent mannerP38 MAP kinase inhibitorMAP kinase inhibitorRGC apoptosisOptic nerveGanglion cellsSignal transductionNMDA receptorsAxotomy-induced apoptosisApoptotic signalingKinase activationP38 inhibitorRat retinal ganglion cellsCell deathCell typesOptic nerve traumaAntiapoptotic role of the p38 mitogen-activated protein kinase–myocyte enhancer factor 2 transcription factor pathway during neuronal differentiation
Okamoto S, Krainc D, Sherman K, Lipton S. Antiapoptotic role of the p38 mitogen-activated protein kinase–myocyte enhancer factor 2 transcription factor pathway during neuronal differentiation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 7561-7566. PMID: 10852968, PMCID: PMC16585, DOI: 10.1073/pnas.130502697.Peer-Reviewed Original ResearchConceptsMyocyte enhancer factor 2Mitogen-activated protein kinase p38alphaNeuronal differentiationDominant-negative p38alphaProtein kinase p38alphaDominant-negative formTranscription factor pathwaysMADS familyMEF2 familyMEF2 pathwayCell divisionTranscription factorsMyogenic phenotypeExpression patternsMyogenic factorsAntiapoptotic roleCell deathMammalian cerebral cortexP38alphaApoptotic deathNegative formPrecursor cellsFactor 2Factor pathwayApoptosis
1999
Excitotoxins in Neuronal Apoptosis and Necrosis
Nicotera P, Lipton S. Excitotoxins in Neuronal Apoptosis and Necrosis. Cerebrovascular And Brain Metabolism Reviews 1999, 19: 583-591. PMID: 10366188, DOI: 10.1097/00004647-199906000-00001.Peer-Reviewed Original ResearchConceptsCommon histopathologic featuresLocal inflammatory reactionProgression of diseaseCell deathNeuronal injuryNeuronal lossHistopathologic featuresNeuronal demiseNeuropathologic conditionsInflammatory reactionNeurotoxic injuryNeuronal apoptosisPathologic conditionsNecrosisCell destructionPrevention of apoptosisNuclear pyknosisNeurodegenerative diseasesType of deathInjuryCell swellingGeneralized disruptionDeathApoptosisPrevalenceShakespeare in love—with NMDA receptors?
Lipton S, Nakanishi N. Shakespeare in love—with NMDA receptors? Nature Medicine 1999, 5: 270-271. PMID: 10086378, DOI: 10.1038/6481.Peer-Reviewed Original Research
1998
â– REVIEW : Excitotoxicity, Free Radicals, Necrosis, and Apoptosis
Lipton S, Nicotera P. â– REVIEW : Excitotoxicity, Free Radicals, Necrosis, and Apoptosis. The Neuroscientist 1998, 4: 345-352. DOI: 10.1177/107385849800400516.Peer-Reviewed Original ResearchNitric oxideMajor excitatory neurotransmitterCentral nervous systemFailure of neuronsFree radicalsNeuronal cell culturesActivation of proteasesNeuronal injuryAIDS dementiaNeuronal necrosisInitial insultExcitatory neurotransmitterNervous systemApoptotic death programAlzheimer's diseaseHuntington's diseaseDiseaseInsultExcitotoxicityMitochondrial membrane potentialNecrosisCell deathDeath programNeuronsApoptosisNitrate therapy may retard glaucomatous optic neuropathy, perhaps through modulation of glutamate receptors
Zurakowski D, Vorwerk C, Gorla M, Kanellopoulos A, Chaturvedi N, Grosskreutz C, Lipton S, Dreyer E. Nitrate therapy may retard glaucomatous optic neuropathy, perhaps through modulation of glutamate receptors. Vision Research 1998, 38: 1489-1494. PMID: 9667013, DOI: 10.1016/s0042-6989(98)00003-0.Peer-Reviewed Original ResearchConceptsEffects of nitroglycerinGlaucomatous optic neuropathyRetinal ganglion cellsAnginal symptomsNitroglycerin preparationsNitrate therapyGlaucomatous damageOptic neuropathyIntraocular pressureGanglion cellsGlutamate receptorsGlaucomatous blindnessNitroglycerinCell deathNeuropathyTherapySymptomsReceptorsICAM-1 dependent pathway is not involved in the development of neuronal apoptosis after transient focal cerebral ischemia
Soriano S, Wang Y, Lipton S, Dikkes P, Gutierrez-Ramos J, Hickey P. ICAM-1 dependent pathway is not involved in the development of neuronal apoptosis after transient focal cerebral ischemia. Brain Research 1998, 780: 337-341. PMID: 9507184, DOI: 10.1016/s0006-8993(97)01298-5.Peer-Reviewed Original ResearchConceptsFocal cerebral ischemiaCerebral ischemiaTerminal deoxynucleotidyltransferase-mediated dUTP-biotin nick end labeling (TUNEL) stainingICAM-1-dependent pathwayTransient focal cerebral ischemiaICAM-1-deficient miceDUTP-biotin nick end labeling stainingNick end labeling stainingICAM-1 deficiencyNeuronal cell deathEnd labeling stainingPresence of apoptosisIschemic hemisphereNontransgenic littermatesDeficient miceTemporary MCAONeuronal apoptosisBrain sectionsDependent pathwayApoptotic cellsIschemiaNecrosisCell deathMiceApoptosis
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