2025
Testosterone, 8‐Oxo‐2′‐Deoxyguanosine (8‐OHdG) and Cu/Zn Superoxide Dismutase (SOD) in Adult Shuar Males of Amazonian Ecuador: A Test for Evidence of Trade‐Offs Between Reproductive Effort and Oxidative Stress
Bribiescas R, Sancilio A, Amir D, Cepon‐Robins T, Gildner T, Liebert M, Madimenos F, Urlacher S, Snodgrass J, Sugiyama L. Testosterone, 8‐Oxo‐2′‐Deoxyguanosine (8‐OHdG) and Cu/Zn Superoxide Dismutase (SOD) in Adult Shuar Males of Amazonian Ecuador: A Test for Evidence of Trade‐Offs Between Reproductive Effort and Oxidative Stress. American Journal Of Human Biology 2025, 37: e70042. PMID: 40231632, DOI: 10.1002/ajhb.70042.Peer-Reviewed Original ResearchConceptsReproductive effortBiomarkers of oxidative stressEvidence of trade-offsCu/Zn superoxide dismutaseAssociated with biomarkers of oxidative stressSuperoxide dismutaseOxidative stressAmazonian EcuadorPopulation of adult malesMultivariate modelUrinary 8-hydroxy-2'-deoxyguanosineLow testosterone levelsMale animal modelsAssociated with biomarkersMultiple linear regression modelMeasures of oxidative stressHuman malesNo significant correlationNon-industrialized populationsAnthropometric measurementsTestosterone levelsSomatic maintenanceAdult malesAnimal modelsTrade-Offs
2024
Plasma oxidative stress marker levels related to functional brain abnormalities in first-episode drug-naive major depressive disorder
Liu Y, Zhang B, Zhou Y, Li M, Gao Y, Qin W, Xie Y, Liu W, Jing Y, Li J. Plasma oxidative stress marker levels related to functional brain abnormalities in first-episode drug-naive major depressive disorder. Psychiatry Research 2024, 333: 115742. PMID: 38232568, DOI: 10.1016/j.psychres.2024.115742.Peer-Reviewed Original ResearchMeSH KeywordsBrainBrain MappingDepressive Disorder, MajorGyrus CinguliHumansMagnetic Resonance ImagingSuperoxide DismutaseConceptsMajor depressive disorderMajor depressive disorder patientsAmplitude of low-frequency fluctuationDepressive disorderSuicidal ideationWhole-brain functional connectivity analysisMDD pathophysiologyDrug-naive MDD patientsResting-state fMRI scansAmplitude of low-frequency fluctuation valuesFunctional brain abnormalitiesAnterior cingulate gyrusSuperior frontal gyrusFunctional connectivity analysisOxidative stress markersAbnormal brain functionLow-frequency fluctuationsPlasma oxidative stress markersMDD patientsFrontal gyrusFMRI scanningFirst-episodeCingulate gyrusBrain regionsConnectivity analysis
2023
SOD2 in platelets: with age comes responsibility
Jain K, Gu S, Hwa J. SOD2 in platelets: with age comes responsibility. Journal Of Thrombosis And Haemostasis 2023, 21: 1077-1081. PMID: 36716965, DOI: 10.1016/j.jtha.2023.01.016.Commentaries, Editorials and Letters
2021
Honokiol regulates mitochondrial substrate utilization and cellular fatty acid metabolism in diabetic mice heart
Jayakumari N, Rajendran R, Sivasailam A, Parambil S, Reghuvaran A, Sreelatha H, Gopala S. Honokiol regulates mitochondrial substrate utilization and cellular fatty acid metabolism in diabetic mice heart. European Journal Of Pharmacology 2021, 896: 173918. PMID: 33529726, DOI: 10.1016/j.ejphar.2021.173918.Peer-Reviewed Original ResearchMeSH KeywordsAcetylationAMP-Activated Protein KinasesAnimalsAntioxidantsBiphenyl CompoundsCD36 AntigensDiabetes Mellitus, ExperimentalDiabetes Mellitus, Type 2Energy MetabolismFatty AcidsLignansMaleMice, Inbred C57BLMitochondria, HeartMyocytes, CardiacNF-E2-Related Factor 2Oxidative StressPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaPPAR alphaStreptozocinSuperoxide DismutaseConceptsComplex IFatty acid metabolismMitochondrial metabolic changesAcetylation/deacetylation mechanismCellular fatty acid metabolismFatty acid respirationAcid metabolismHonokiol treatmentMitochondrial substrate utilizationMouse cardiac mitochondriaCardiac mitochondriaType 2 diabetes mellitusNuclear transcription factorPeroxisome proliferator-activated receptor αProtein functionProliferator-activated receptor αAcetylated proteinsTranscription factorsDiabetic mouse heartsCardiac mitochondrial dysfunctionCardiac mitochondrial functionDeacetylation mechanismExpression of clusterMitochondrial functionMitochondrial dysfunctionIntravenous infusion of mesenchymal stem cells delays disease progression in the SOD1G93A transgenic amyotrophic lateral sclerosis rat model
Magota H, Sasaki M, Kataoka-Sasaki Y, Oka S, Ukai R, Kiyose R, Onodera R, Kocsis JD, Honmou O. Intravenous infusion of mesenchymal stem cells delays disease progression in the SOD1G93A transgenic amyotrophic lateral sclerosis rat model. Brain Research 2021, 1757: 147296. PMID: 33516815, DOI: 10.1016/j.brainres.2021.147296.Peer-Reviewed Original ResearchConceptsBlood-spinal cord barrierQuantitative reverse transcription polymerase chain reactionIntravenous infusionDisease progressionMotor neuronsMSC groupLocomotor functionOpen-field locomotor functionPreservation of microvasculatureHind limb functionCommon clinical featuresEvans blue leakageMotor neuron lossReverse transcription-polymerase chain reactionTranscription-polymerase chain reactionDevastating neurodegenerative diseaseBBB scoringBSCB functionRotarod testingClinical featuresNeuron lossLimb functionNeurotrophic factorCurative strategiesSpinal cord
2020
Clinical implications of oxidative stress in schizophrenia: Acute relapse and chronic stable phase
Chien Y, Hwu H, Hwang T, Hsieh M, Liu C, Lin-Shiau S, Liu C. Clinical implications of oxidative stress in schizophrenia: Acute relapse and chronic stable phase. Progress In Neuro-Psychopharmacology And Biological Psychiatry 2020, 99: 109868. PMID: 31954755, DOI: 10.1016/j.pnpbp.2020.109868.Peer-Reviewed Original ResearchConceptsChronic stable schizophreniaNon-psychiatric controlsDisorganized symptomsChronic stable patientsStable schizophreniaWeeks of antipsychotic treatmentStages of schizophreniaAcute relapseClinical implicationsAntipsychotic treatmentNegative symptomsSchizophreniaStable patientsOxidative stressPlatelet superoxide dismutasePlatelet oxidative stressTreatment responseNitric oxideLipid peroxidationLevels of nitric oxideSymptomsSuperoxide dismutaseTreatment effectsRelapsed patientsRelapse
2018
Sin1 (Stress-Activated Protein Kinase-Interacting Protein) Regulates Ischemia-Induced Microthrombosis Through Integrin αIIbβ3-Mediated Outside-In Signaling and Hypoxia Responses in Platelets
Xu Y, Ouyang X, Yan L, Zhang M, Hu Z, Gu J, Fan X, Zhang L, Zhang J, Xue S, Chen G, Su B, Liu J. Sin1 (Stress-Activated Protein Kinase-Interacting Protein) Regulates Ischemia-Induced Microthrombosis Through Integrin αIIbβ3-Mediated Outside-In Signaling and Hypoxia Responses in Platelets. Arteriosclerosis Thrombosis And Vascular Biology 2018, 38: 1. PMID: 30571167, DOI: 10.1161/atvbaha.118.311822.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdultAgedAged, 80 and overAnimalsBlood PlateletsCarrier ProteinsCell HypoxiaDisease Models, AnimalFemaleHumansMaleMechanistic Target of Rapamycin Complex 2Mice, Inbred C57BLMice, KnockoutMiddle AgedMyocardial InfarctionPhosphorylationPlatelet ActivationPlatelet Glycoprotein GPIIb-IIIa ComplexProto-Oncogene Proteins c-aktReactive Oxygen SpeciesSignal TransductionSirtuin 3Superoxide DismutaseThrombosisConceptsOxygen speciesTarget AktSIN1Reactive oxygen speciesHypoxia responseNovel roleMyocardial infarctionIntegrin αIIbβ3Downstream signalsValuable therapeutic targetCell proliferationAktDeficiency micePhosphorylationST-segment elevation myocardial infarctionPlatelet activationLeft anterior descending (LAD) obstructionPump coronary artery bypassSignalingSpeciesTherapeutic targetΑIIbβ3Coronary artery bypassChronic low-dose exposure of nonylphenol alters energy homeostasis in the reproductive system of female rats
Di QN, Cao WX, Xu R, Lu L, Xu Q, Wang XB. Chronic low-dose exposure of nonylphenol alters energy homeostasis in the reproductive system of female rats. Toxicology And Applied Pharmacology 2018, 348: 67-75. PMID: 29641977, DOI: 10.1016/j.taap.2018.04.007.Peer-Reviewed Original ResearchMeSH KeywordsAMP-Activated Protein KinasesAnimalsCarnitine O-PalmitoyltransferaseEndocrine DisruptorsEndometrial HyperplasiaEndometriumEnergy MetabolismEstradiolFatty AcidsFemaleGlutathioneLiverMalondialdehydeMetabolomicsOogenesisOvaryOxidation-ReductionPhenolsPPAR gammaRats, Sprague-DawleyReproductionRisk AssessmentSuperoxide DismutaseConceptsFemale reproductive toxicityReproductive toxicityFemale ratsCarnitine palmitoyltransferase IEnergy homeostasisSerum 17β-estradiol levelsChronic low-dose exposurePeroxisome proliferator-activated receptor gammaImpaired fatty acid oxidationProliferator-activated receptor gammaReproductive systemHigh-dose exposureLow-dose exposureHuman exposure scenariosNP exposureFatty acid oxidationKey reproductive tissuesEndometrium hyperplasiaL-carnitineReceptor gammaPotential biomarkersComprehensive metabolomic studyEndocrine-disrupting chemicalsMetabolic profileDevelopmental toxicity
2015
Deficiency of Superoxide Dismutase Impairs Protein C Activation and Enhances Susceptibility to Experimental Thrombosis
Dayal S, Gu S, Hutchins R, Wilson K, Wang Y, Fu X, Lentz S. Deficiency of Superoxide Dismutase Impairs Protein C Activation and Enhances Susceptibility to Experimental Thrombosis. Arteriosclerosis Thrombosis And Vascular Biology 2015, 35: 1798-1804. PMID: 26069236, PMCID: PMC4514539, DOI: 10.1161/atvbaha.115.305963.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarotid Artery InjuriesCarotid Artery, CommonCatalaseDisease Models, AnimalEnzyme ActivationHumansMice, 129 StrainMice, TransgenicOxidation-ReductionOxidative StressProtein CSuperoxide DismutaseSuperoxide Dismutase-1SuperoxidesThrombomodulinThrombosisVena Cava, InferiorVenous ThrombosisConceptsSod1(-/-) miceSuperoxide dismutase-1Activation of protein CProtein C activationProtein CInferior vena cava ligationLevels of protein CEndothelial protein C receptorVena cava ligationC activityImpaired protein C activationReactive oxygen speciesGeneration of activated protein CProtein C receptorExpression of thrombomodulinCarotid artery thrombosisThrombosis in vivoIn vitro studiesSod1(-/-Thrombin in vivoLevels of reactive oxygen speciesElevated levels of reactive oxygen speciesVenous thrombosisProthrombotic effectsMurine modelIn vivo systemic chlorogenic acid therapy under diabetic conditions: Wound healing effects and cytotoxicity/genotoxicity profile
Bagdas D, Etoz B, Gul Z, Ziyanok S, Inan S, Turacozen O, Gul N, Topal A, Cinkilic N, Tas S, Ozyigit M, Gurun M. In vivo systemic chlorogenic acid therapy under diabetic conditions: Wound healing effects and cytotoxicity/genotoxicity profile. Food And Chemical Toxicology 2015, 81: 54-61. PMID: 25846499, DOI: 10.1016/j.fct.2015.04.001.Peer-Reviewed Original ResearchConceptsSide effectsOxidative stressStreptozotocin-induced diabetic ratsChronic antioxidant treatmentEndogenous antioxidant defense systemNitric oxide levelsWound healingBlood glucose levelsSystemic antioxidant therapyDays of treatmentPossible side effectsDiabetic wound repairLipid peroxidation levelsChlorogenic acidAcid therapyDiabetic ratsHistopathological examinationPossible pro-oxidative effectsPro-oxidative effectsAntioxidant intakePivotal organAntioxidant therapyDiabetic conditionsAntioxidant balanceGlucose levelsAutophagy Alleviates Melamine-Induced Cell Death in PC12 Cells Via Decreasing ROS Level
Wang H, Gao N, Li Z, Yang Z, Zhang T. Autophagy Alleviates Melamine-Induced Cell Death in PC12 Cells Via Decreasing ROS Level. Molecular Neurobiology 2015, 53: 1718-1729. PMID: 25724280, DOI: 10.1007/s12035-014-9073-2.Peer-Reviewed Original ResearchConceptsPC12 cellsLC3-II/LC3Western blot assaysCell deathReactive oxygen species levelsSuperoxide dismutase activityMDA levelsOxygen species levelsGeneration of ROSATG-7Autophagy markersBlot assaysIncrease of autophagosomesBeclin-1Oxidative stressDismutase activityROS levelsRapamycinExcessive generationExpression levelsCell viabilityOxidative damageAutophagyMalondialdehydeDeathThe distinct genetic pattern of ALS in Turkey and novel mutations
Özoğuz A, Uyan Ö, Birdal G, Iskender C, Kartal E, Lahut S, Ömür Ö, Agim ZS, Eken A, Sen NE, Kavak P, Saygı C, Sapp PC, Keagle P, Parman Y, Tan E, Koç F, Deymeer F, Oflazer P, Hanağası H, Gürvit H, Bilgiç B, Durmuş H, Ertaş M, Kotan D, Akalın M, Güllüoğlu H, Zarifoğlu M, Aysal F, Döşoğlu N, Bilguvar K, Günel M, Keskin Ö, Akgün T, Özçelik H, Landers JE, Brown RH, Başak A. The distinct genetic pattern of ALS in Turkey and novel mutations. Neurobiology Of Aging 2015, 36: 1764.e9-1764.e18. PMID: 25681989, PMCID: PMC6591733, DOI: 10.1016/j.neurobiolaging.2014.12.032.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdolescentAdultAgedAmyotrophic Lateral SclerosisAutophagy-Related ProteinsC9orf72 ProteinCell Cycle ProteinsCytoskeletal ProteinsDNA-Binding ProteinsExomeFemaleGenetic Association StudiesGuanine Nucleotide Exchange FactorsHumansIntracellular Signaling Peptides and ProteinsMaleMembrane Transport ProteinsMiddle AgedMutationNerve Tissue ProteinsNuclear ProteinsOncogene ProteinsProtein Deglycase DJ-1Protein Serine-Threonine KinasesProteinsRNA-Binding Protein FUSSequestosome-1 ProteinSuperoxide DismutaseSuperoxide Dismutase-1Transcription Factor TFIIIATRPM Cation ChannelsTurkeyUbiquitinsYoung AdultConceptsALS patientsFamilial ALS patientsSporadic ALS casesSALS patientsALS populationALS casesFamilial ALSSOD1 mutationsSQSTM1 genePatientsDistinct genetic patternsAmyotrophic lateral sclerosis mutationsExome sequencingDistinct genetic backgroundsGene mutationsSpectrum of mutationsNovel mutationsC9orf72Genetic backgroundALSMutationsPopulationSPG11TARDBP
2014
Attachment of Cell-Binding Ligands to Arginine-Rich Cell-Penetrating Peptides Enables Cytosolic Translocation of Complexed siRNA
Zeller S, Choi CS, Uchil PD, Ban HS, Siefert A, Fahmy TM, Mothes W, Lee SK, Kumar P. Attachment of Cell-Binding Ligands to Arginine-Rich Cell-Penetrating Peptides Enables Cytosolic Translocation of Complexed siRNA. Cell Chemical Biology 2014, 22: 50-62. PMID: 25544044, PMCID: PMC4320807, DOI: 10.1016/j.chembiol.2014.11.009.Peer-Reviewed Original ResearchSelective degeneration of a physiological subtype of spinal motor neuron in mice with SOD1-linked ALS
Hadzipasic M, Tahvildari B, Nagy M, Bian M, Horwich AL, McCormick DA. Selective degeneration of a physiological subtype of spinal motor neuron in mice with SOD1-linked ALS. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 16883-16888. PMID: 25385594, PMCID: PMC4250117, DOI: 10.1073/pnas.1419497111.Peer-Reviewed Original ResearchMeSH KeywordsAmyotrophic Lateral SclerosisAnimalsMiceMotor NeuronsPatch-Clamp TechniquesSpinal CordSuperoxide DismutaseSuperoxide Dismutase-1ConceptsMN cell bodiesMotor neuronsMo of ageCell bodiesSpinal cordSpinal cord tissue slicesWhole-cell patch-clamp recordingsCell patch-clamp recordingsAdult mouse spinal cordIntrinsic electrophysiologic propertiesTwitch muscleSpinal motor neuronsLower extremity musclesTransgenic mouse modelMouse motor neuronsPatch-clamp recordingsAmyotrophic lateral sclerosisMouse spinal cordSlow-twitch muscleSteady-state firing ratePhysiological subtypesRetrograde tracingAcute slicesExtremity musclesPathophysiologic events
2013
Effects of Systemic Chlorogenic Acid on Random-Pattern Dorsal Skin Flap Survival in Diabetic Rats
Bagdas D, Etoz B, Ozturkoglu S, Cinkilic N, Ozyigit M, Gul Z, Buyukcoskun N, Ozluk K, Gurun M. Effects of Systemic Chlorogenic Acid on Random-Pattern Dorsal Skin Flap Survival in Diabetic Rats. Biological And Pharmaceutical Bulletin 2013, 37: 361-370. PMID: 24389556, DOI: 10.1248/bpb.b13-00635.Peer-Reviewed Original ResearchConceptsSkin flap survivalFlap survivalDiabetic ratsNondiabetic ratsCapillary densityBlood perfusionVascular endothelial growth factor (VEGF) expressionPostoperative day 7Nitric oxide levelsMale Wistar ratsDorsal skin flapDorsal skin flap modelSkin flap modelGrowth factor expressionPotent antioxidant effectsChlorogenic acidRegional blood perfusionCGA treatmentWistar ratsSOD levelsOxide levelsSkin flapsNO levelsFlap tissueDay 7UCP2 overexpression worsens mitochondrial dysfunction and accelerates disease progression in a mouse model of amyotrophic lateral sclerosis
Peixoto PM, Kim HJ, Sider B, Starkov A, Horvath TL, Manfredi G. UCP2 overexpression worsens mitochondrial dysfunction and accelerates disease progression in a mouse model of amyotrophic lateral sclerosis. Molecular And Cellular Neuroscience 2013, 57: 104-110. PMID: 24141050, PMCID: PMC3891658, DOI: 10.1016/j.mcn.2013.10.002.Peer-Reviewed Original ResearchConceptsAmyotrophic lateral sclerosisDouble transgenic miceFamilial amyotrophic lateral sclerosisMouse modelLateral sclerosisMitochondrial dysfunctionTransgenic miceMutant SOD1 mouse modelHuman UCP2Brain mitochondriaSOD1 mutant miceUCP2 overexpressionPotential neuroprotective effectsProtection of neuronsSOD1 mouse modelCentral nervous systemReactive oxygen species productionDisease courseG93A miceNeuroprotective effectsNeuroprotective roleFree radical generationDisease progressionOxygen species productionInjury paradigmsRapid and Permanent Neuronal Inactivation In Vivo via Subcellular Generation of Reactive Oxygen with the Use of KillerRed
Williams DC, Bejjani RE, Ramirez PM, Coakley S, Kim SA, Lee H, Wen Q, Samuel A, Lu H, Hilliard MA, Hammarlund M. Rapid and Permanent Neuronal Inactivation In Vivo via Subcellular Generation of Reactive Oxygen with the Use of KillerRed. Cell Reports 2013, 5: 553-563. PMID: 24209746, PMCID: PMC3877846, DOI: 10.1016/j.celrep.2013.09.023.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCaenorhabditis elegansGABAergic NeuronsGreen Fluorescent ProteinsLightMicroscopy, VideoReactive Oxygen SpeciesSuperoxide DismutaseConceptsReactive oxygen speciesC. elegansGenetic toolsOrganelle fragmentationPlasma membraneSpecific developmental outcomesSubcellular responsesCell deathKillerRedReactive oxygenOxygen speciesTargeted cellCircuit functionSingle light stimulusSingle animalInactivationElegansCellsVivoCell bodiesSpeciesNeuronal degenerationNeuronsAnimalsNeuronal inactivationGlutaredoxin 1 is a major player in copper metabolism in neuroblastoma cells
De Benedetto ML, Capo CR, Ferri A, Valle C, Polimanti R, Carrì MT, Rossi L. Glutaredoxin 1 is a major player in copper metabolism in neuroblastoma cells. Biochimica Et Biophysica Acta 2013, 1840: 255-261. PMID: 24041990, DOI: 10.1016/j.bbagen.2013.09.008.Peer-Reviewed Original ResearchMeSH KeywordsApoptosisBlotting, WesternCation Transport ProteinsCell ProliferationChromatography, AffinityCopperCopper Transporter 1GlutaredoxinsGlutathioneHumansMitochondriaNeuroblastomaOxidation-ReductionReal-Time Polymerase Chain ReactionReverse Transcriptase Polymerase Chain ReactionRNA, MessengerSuperoxide DismutaseSuperoxide Dismutase-1Tumor Cells, CulturedConceptsIntracellular copper levelsCopper transporter 1Copper-induced toxicityHomeostasis of copperCopper metabolismCopper-binding propertiesGRX1 overexpressionProtein chaperonesHuman neuroblastoma SH-SY5Y cellsCopper overloadCopper chaperoneMajor playersNeuroblastoma SH-SY5Y cellsThioredoxin familyProtein disulfidesGrx1Glutaredoxin-1SH-SY5Y cellsSmall proteinsCuSO4 treatmentNeuronal cellsMixed disulfidesChaperonesControl cellsEnzyme activityThe role of solvent exclusion in the interaction between D124 and the metal site in SOD1: implications for ALS
Mera-Adasme R, Suomivuori C, Fierro A, Pesonen J, Sundholm D. The role of solvent exclusion in the interaction between D124 and the metal site in SOD1: implications for ALS. JBIC Journal Of Biological Inorganic Chemistry 2013, 18: 931-938. PMID: 24026444, DOI: 10.1007/s00775-013-1039-8.Peer-Reviewed Original ResearchConceptsMetal sitesExclusion of solvent moleculesDensity functional theory calculationsFirst-sphere ligandsElectrostatic loopSecond-sphere ligandFunctional theory calculationsMolecular dynamics simulationsMetal-site structuresSolvent moleculesTheory calculationsSolvent exclusionZinc sitesStructural changesDynamics simulationsZinc ionsKinetic trapsD124MetalLigandSite interactionsCopper-zincCalculationsThe proteinAmyotrophic lateral sclerosisPalmitoylation of Superoxide Dismutase 1 (SOD1) Is Increased for Familial Amyotrophic Lateral Sclerosis-linked SOD1 Mutants*
Antinone SE, Ghadge GD, Lam TT, Wang L, Roos RP, Green WN. Palmitoylation of Superoxide Dismutase 1 (SOD1) Is Increased for Familial Amyotrophic Lateral Sclerosis-linked SOD1 Mutants*. Journal Of Biological Chemistry 2013, 288: 21606-21617. PMID: 23760509, PMCID: PMC3724620, DOI: 10.1074/jbc.m113.487231.Peer-Reviewed Original ResearchMeSH KeywordsAmyotrophic Lateral SclerosisAnimalsBlotting, WesternCell Line, TumorCell MembraneCysteineDisulfidesHEK293 CellsHumansLipoylationLuminescent ProteinsMass SpectrometryMiceMice, TransgenicMutationNeuronsOxidation-ReductionProtein Processing, Post-TranslationalSpinal CordSuperoxide DismutaseSuperoxide Dismutase-1ConceptsWild-type SOD1Familial amyotrophic lateral sclerosisSuperoxide dismutase 1Copper chaperoneCysteine mutagenesisReversible post-translational modificationAcyl-biotin exchangeDisulfide bondingPost-translational modificationsMass spectrometryWild-type superoxide dismutase 1PalmitoylationSOD1 maturationMotor neuron cell lineProtein structureSOD1 mutantsNeuron cell lineAmyotrophic lateral sclerosisZn-superoxide dismutaseHEK cellsResidues 6ChaperonesCell linesMutagenesisDismutase 1
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