2022
Targeted protein S-nitrosylation of ACE2 inhibits SARS-CoV-2 infection
Oh C, Nakamura T, Beutler N, Zhang X, Piña-Crespo J, Talantova M, Ghatak S, Trudler D, Carnevale L, McKercher S, Bakowski M, Diedrich J, Roberts A, Woods A, Chi V, Gupta A, Rosenfeld M, Kearns F, Casalino L, Shaabani N, Liu H, Wilson I, Amaro R, Burton D, Yates J, Becker C, Rogers T, Chatterjee A, Lipton S. Targeted protein S-nitrosylation of ACE2 inhibits SARS-CoV-2 infection. Nature Chemical Biology 2022, 19: 275-283. PMID: 36175661, PMCID: PMC10127945, DOI: 10.1038/s41589-022-01149-6.Peer-Reviewed Original ResearchConceptsSARS-CoV-2 infectionViral entrySevere acute respiratory syndrome coronavirus 2Acute respiratory syndrome coronavirus 2Respiratory syndrome coronavirus 2Coronavirus disease 2019 (COVID-19) pandemicSyndrome coronavirus 2Prevention of infectionSARS-CoV-2 spike proteinDisease 2019 pandemicSpread of infectionCoronavirus 2Channel blockadeS-nitrosylationEnzyme 2Binding of ACE2InfectionSpike proteinACE2Envelope proteinProtein S-nitrosylationIon channelsNon-toxic compoundsNovel avenuesAngiotensin
2000
Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation
Choi Y, Tenneti L, Le D, Ortiz J, Bai G, Chen H, Lipton S. Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation. Nature Neuroscience 2000, 3: 15-21. PMID: 10607390, DOI: 10.1038/71090.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineChromatography, High Pressure LiquidCysteineDose-Response Relationship, DrugEthyl MethanesulfonateHumansIndicators and ReagentsIon TransportMesylatesMutagenesis, Site-DirectedN-MethylaspartateNitric OxideNitroso CompoundsOocytesPatch-Clamp TechniquesPeptide FragmentsReceptors, N-Methyl-D-AspartateS-NitrosothiolsTransfectionXenopus laevisConceptsS-nitrosylationMolecular basisIon channelsCritical cysteine residuesEndogenous S-nitrosylationSite-directed mutagenesisEndogenous nitric oxideIon channel activityNR2A subunitNitric oxideCysteine residuesSingle cysteineIon channel modulationChannel activityPhysiological conditionsSubunitsChannel modulationCell systemNMDA receptorsMutagenesisCysteineResiduesRegulationAlanineModulation
1997
Suppression of neuronal apoptosis by S-nitrosylation of caspases
Tenneti L, D'Emilia D, Lipton S. Suppression of neuronal apoptosis by S-nitrosylation of caspases. Neuroscience Letters 1997, 236: 139-142. PMID: 9406756, DOI: 10.1016/s0304-3940(97)00780-5.Peer-Reviewed Original ResearchConceptsS-nitrosylationInterleukin-1beta-converting enzyme-like proteasesCritical cysteine residuesEnzyme-like proteasesApoptotic cell deathHuman embryonic kidneyTranscription factorsEnzyme familyCysteine residuesG proteinsEmbryonic kidneyCell deathCaspasesIon channelsPrimary cerebrocortical neuronsPhysiological activityEnzyme activityActive siteApoptosisNeuronal apoptosisCerebrocortical neuronsFamilyProteinProteaseEnzymeAgonist-induced closure of constitutively open γ-aminobutyric acid channels with mutated M2 domains
Pan Z, Zhang D, Zhang X, Lipton S. Agonist-induced closure of constitutively open γ-aminobutyric acid channels with mutated M2 domains. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 6490-6495. PMID: 9177245, PMCID: PMC21077, DOI: 10.1073/pnas.94.12.6490.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCloning, MolecularFemaleGABA AgonistsGABA AntagonistsGamma-Aminobutyric AcidIon Channel GatingIon ChannelsMacromolecular SubstancesMembrane PotentialsMolecular Sequence DataMutagenesis, Site-DirectedOocytesOrganophosphorus CompoundsPoint MutationRatsReceptors, GABAReceptors, GlycineReceptors, NicotinicRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidVirulence Factors, BordetellaXenopus laevisConceptsLigand-gated ion channelsChannel gatingIon channelsAmino acid residuesAminobutyric acid channelsSingle-point mutantsAbsence of ligandChannel pore regionStructure-function relationshipsPoint mutantsAcid channelImportant new insightsAllosteric transitionSubunit resultsAcid residuesM2 domainConstitutive currentReceptor proteinPore regionAgonist bindingAgonist regulationSubstituting alanineM2 regionSpontaneous channel openingChannel opening
1993
Expression of endogenous NMDAR1 transcripts without receptor protein suggests post-transcriptional control in PC12 cells.
Sucher N, Brose N, Deitcher D, Awobuluyi M, Gasic G, Bading H, Cepko C, Greenberg M, Jahn R, Heinemann S, Lipton S. Expression of endogenous NMDAR1 transcripts without receptor protein suggests post-transcriptional control in PC12 cells. Journal Of Biological Chemistry 1993, 268: 22299-22304. PMID: 8226739, DOI: 10.1016/s0021-9258(18)41528-1.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAnimalsAstrocytesBase SequenceCell DifferentiationCell LineCells, CulturedDimethylphenylpiperazinium IodideDNA PrimersGene ExpressionGene Expression Regulation, NeoplasticGenetic VariationHippocampusHumansKidneyMacromolecular SubstancesMembrane PotentialsMolecular Sequence DataMolecular WeightN-MethylaspartateNerve Growth FactorsPC12 CellsPolymerase Chain ReactionReceptors, N-Methyl-D-AspartateRNA, MessengerSynaptic MembranesTranscription, GeneticTransfectionConceptsNMDAR1 proteinPC12 cellsPost-transcriptional controlPost-transcriptional mechanismsNative PC12 cellsParticular cell typeUndifferentiated rat pheochromocytoma (PC12) cellsExpression of RNAPC12 cell lineTranslational regulationIsoform CRat pheochromocytoma cellsNorthern hybridizationExpression vectorReceptor proteinCell typesIon channelsProteinFunctional NMDACell linesPheochromocytoma cellsCytomegalovirus promoterModel systemRNAExpression
1992
Memantine prevents HIV coat protein-induced neuronal injury in vitro.
Lipton S. Memantine prevents HIV coat protein-induced neuronal injury in vitro. Neurology 1992, 42: 1403-5. PMID: 1620355, DOI: 10.1212/wnl.42.7.1403.Peer-Reviewed Original ResearchConceptsNeuronal injuryNeuronal damageHIV-1 coat protein gp120Cognitive/motor complexRat retinal ganglion cellsN-methyl-D-aspartate receptorsHuman immunodeficiency virusPossible protective effectNMDA receptor-operated ion channelsRetinal ganglion cellsReceptor-operated ion channelsMicroM memantineNeurologic deficitsImmunodeficiency virusGanglion cellsNMDA antagonistsProtective effectProtein gp120Therapeutic potentialGp120InjuryMemantineMotor complexConcurrent activationIon channels