Adjunct Faculty
Adjunct faculty typically have an academic or research appointment at another institution and contribute or collaborate with one or more School of Medicine faculty members or programs.
Adjunct rank detailsStuart Lipton, MD, PhD
Adjunct Professor of NeurologyAbout
Research
Publications
2026
Aberrant Protein S‐Nitrosylation Mimics the Effect of Rare Genetic Mutations in Neurodegenerative Diseases
Wang Y, Lipton S. Aberrant Protein S‐Nitrosylation Mimics the Effect of Rare Genetic Mutations in Neurodegenerative Diseases. Journal Of Neurochemistry 2026, 170: e70365. PMID: 41635116, PMCID: PMC12981794, DOI: 10.1111/jnc.70365.Peer-Reviewed Original ResearchConceptsGenome wide association studiesPost-translational modificationsAberrant S-nitrosylationRare genetic mutationsS-nitrosylationGenetic mutationsPost-translational modification of proteinsAlzheimer's diseaseAmyotrophic lateral sclerosis/frontotemporal dementiaDiseased brainS-nitrosylated proteinsModification of proteinsProtein S-nitrosylationGenetic risk factorsAssociation studiesProtein functionEnvironmental factorsRisk gene variantsHuman geneticsProteomic analysisEnvironmental stressSynaptic dysfunctionRedox biologyGene variantsFunctional consequencesAutophagy Activators Normalize Aberrant Tau Proteostasis and Rescue Synapses in Human Familial Alzheimer's Disease iPSC‐Derived Cortical Organoids
Labra S, Compher J, Prabhavalkar A, Almaraz M, Kwong C, Baal C, Talantova M, Dolatabadi N, Piña‐Sanz J, Wang Y, Yoon L, Ghatak S, Gao Z, Zhang Y, Trudler D, Massey L, Lin W, Balistreri A, Bula M, Schork N, Mondala T, Head S, Kelly J, Lipton S. Autophagy Activators Normalize Aberrant Tau Proteostasis and Rescue Synapses in Human Familial Alzheimer's Disease iPSC‐Derived Cortical Organoids. Advanced Science 2026, 13: e14783. PMID: 41591759, DOI: 10.1002/advs.202514783.Peer-Reviewed Original ResearchConceptsSingle-cell RNA sequencing analysisAlzheimer's diseaseFamilial AD mutationsAD patient brainsIsogenic wild-typeP-tau accumulationHigh-molecular-weightMonomeric tauTau proteostasisAD mutationsCause of dementiaAD pathogenesisAmyloid-betaAD phenotypeSynapse lossAnalysis of ADSynaptic lossMolecular mechanismsWild-typePatient's brainPluripotent stem cellsAutophagy activationMolecular abnormalitiesDisease modelsAccumulation
2025
Alzheimer's Disease Pathogenesis Perturbs Specific Spatial Protein Isoforms
McClatchy D, Labra S, Baal C, Lipton S, Yates J. Alzheimer's Disease Pathogenesis Perturbs Specific Spatial Protein Isoforms. Alzheimer's & Dementia 2025, 21: e103003. PMCID: PMC12728306, DOI: 10.1002/alz70855_103003.Peer-Reviewed Original ResearchUnique subcellular compartmentsIdentical proteinsSubcellular compartmentsAlzheimer's diseaseReciprocal expression patternProtein degradation rateBiological processesUnbiased mass spectrometryProcess of vesicle transportNucleo-cytoplasmic traffickingPulse-chase strategyAD mouse modelVesicle transportProtein traffickingProtein mislocalizationAD pathogenesisProtein isoformsUnique proteinsHuman brain samplesQuantitative MSProtein identificationQuantitative MS analysisBiological fractionationAD organoidsDruggable pathwaysProteome-wide profiling of S-nitrosylated proteins using the SNOTRAP probe and mass spectrometry-based detection
Yang H, Amal H, Tannenbaum S, Lipton S. Proteome-wide profiling of S-nitrosylated proteins using the SNOTRAP probe and mass spectrometry-based detection. Nature Protocols 2025, 1-26. PMID: 41258014, PMCID: PMC13004284, DOI: 10.1038/s41596-025-01282-1.Peer-Reviewed Original ResearchProteome-wide profilingS-nitrosylated proteinsProtein S-nitrosylationS-nitrosylationIn situ labelingSample preparationSNO-proteinsProteome-wide approachMS-based identificationPost-translational modificationsCellular signal transductionMass spectrometry-based detectionTissue sample preparationOrbitrap MSMS measurementsS-nitrosylation reactionLabel-free quantificationS-nitrosoproteomeStreptavidin captureProtein stabilitySignal transductionArgon atmosphereDisease-modifying therapeuticsMouse tissuesLow abundanceThe transcriptional and cellular landscape of cognitive resilience to Alzheimer’s disease
Khera N, Raju R, Lipton S. The transcriptional and cellular landscape of cognitive resilience to Alzheimer’s disease. Frontiers In Molecular Neuroscience 2025, 18: 1665802. PMID: 41293128, PMCID: PMC12640947, DOI: 10.3389/fnmol.2025.1665802.Peer-Reviewed Original ResearchAlzheimer's diseasePathological features of Alzheimer's diseaseCellular landscapeNon-cell autonomous effectsFeatures of Alzheimer's diseaseAD-related dementiaMisfolded protein accumulationCell typesTranscriptional changesProtein accumulationTranscriptional driversGene expressionSynaptic stabilityCognitive resilienceCognitive functionDrug developmentCellsPreserving cognitive functionGenesCognitive healthAlzheimerPatient's capacityGasotransmitter signaling in the brain: New frontiers for therapeutics
Paul B, Ignarro L, Lipton S. Gasotransmitter signaling in the brain: New frontiers for therapeutics. Neurotherapeutics 2025, 22: e00784. PMID: 41188152, PMCID: PMC12664559, DOI: 10.1016/j.neurot.2025.e00784.Peer-Reviewed Original ResearchClassically activated macrophages undergo functionally significant nucleotide metabolism remodelling driven by nitric oxide
John S, Seim G, Erazo-Flores B, Votava J, Urquiza U, Arp N, Steill J, Freeman J, Carnevale L, Roberts I, Qing X, Lipton S, Stewart R, Knoll L, Fan J. Classically activated macrophages undergo functionally significant nucleotide metabolism remodelling driven by nitric oxide. Nature Metabolism 2025, 7: 1681-1702. PMID: 40759751, PMCID: PMC12356500, DOI: 10.1038/s42255-025-01337-3.Peer-Reviewed Original ResearchConceptsDe novo synthesisNucleotide metabolismDynamic reprogrammingTranscriptional downregulationRegulation of nucleotide metabolismDe novo synthesis of purinesPurine salvageDe novo synthesis of pyrimidinesSynthesis of purinesIntracellular parasite Toxoplasma gondiiSynthesis of pyrimidinesRegulatory mechanismsCytidine triphosphateMetabolic remodelingNucleotideUridine monophosphateFunctional significanceParasite Toxoplasma gondiiMetabolismNitric oxidePurinePurine basesMacrophage migrationImmune responseActivated macrophagesAberrant S-nitrosylation in the TCA cycle contributes to mitochondrial dysfunction, energy compromise, and synapse loss in neurodegenerative diseases
Nakamura T, Sharma A, Lipton S. Aberrant S-nitrosylation in the TCA cycle contributes to mitochondrial dysfunction, energy compromise, and synapse loss in neurodegenerative diseases. Neurotherapeutics 2025, 22: e00708. PMID: 40730758, PMCID: PMC12664530, DOI: 10.1016/j.neurot.2025.e00708.Peer-Reviewed Original ResearchPosttranslational modificationsMitochondrial energy productionMitochondrial dysfunctionS-nitrosylationMitochondrial metabolismSynapse lossTricarboxylic acid cycle enzymesElectron transport chain proteinsAberrant posttranslational modificationsAberrant S-nitrosylationNeurodegenerative diseasesS-nitrosylation of cysteine residuesMitochondrial bioenergetic functionProtein S-nitrosylationA-ketoglutarate dehydrogenaseMitochondrial dynamicsNitro-oxidative stressTCA cycleModels of neurodegenerative diseasesCycle enzymesBioenergetic functionCysteine residuesChain proteinSynaptic degenerationA-ketoglutarateRedox modulation of the complement cascade contributes to synapse loss in Alzheimer's disease
Oh C, Wang Y, Lipton S. Redox modulation of the complement cascade contributes to synapse loss in Alzheimer's disease. Neurotherapeutics 2025, 22: e00707. PMID: 40713246, PMCID: PMC12664466, DOI: 10.1016/j.neurot.2025.e00707.Peer-Reviewed Original ResearchAberrant S-nitrosylationAlzheimer's diseaseRedox-mediated posttranslational modificationSynaptic lossNitric oxide (NO)-related speciesReactive nitrogen speciesPhagocytosis of synapsesProgression of ADCorrelated to cognitive declineComplement systemPosttranslational modificationsInnate immune systemSenile plaquesSynapse lossS-nitrosylationDying CellsImmune responseRedox modulationComplement cascadeSpeciesCentral nervous systemComplement proteinsNitrosative stressComplementAlzheimerPotential Disease-Modifying Pharmacological Therapy for Alzheimer’s Disease by Protecting Synapses Via Prevention of Hyperexcitability and E/I Imbalance
Ghatak S, Lipton S. Potential Disease-Modifying Pharmacological Therapy for Alzheimer’s Disease by Protecting Synapses Via Prevention of Hyperexcitability and E/I Imbalance. 2025, 317-329. DOI: 10.1007/978-3-031-89307-0_18.Peer-Reviewed Original ResearchGlutamatergic signalingNMDA receptorsExtrasynaptic NMDA receptorsAberrant glutamatergic signalingOpen channel blockerAlzheimer's diseasePluripotent stem cellsDisease-modifying pharmacological therapyAD model systemsDisease-modifying therapiesToxic effectsPharmacological therapyInhibitory responsesE/I imbalanceNeuronal cell deathSynaptic activityExcessive electrical activityNeuronal survivalHuman AD patientsStem cellsHippocampal circuitsTherapeutic targetEarly stages of Alzheimer's diseaseCell deathDisease