2023
Reply to: Targeted protein S-nitrosylation of ACE2 inhibits SARS-CoV-2 infection
Oh C, Piña-Crespo J, Talantova M, Carnevale L, Stoneham C, Lewinski M, Guatelli J, Lipton S. Reply to: Targeted protein S-nitrosylation of ACE2 inhibits SARS-CoV-2 infection. Nature Chemical Biology 2023, 19: 1306-1308. PMID: 37798355, DOI: 10.1038/s41589-023-01425-z.Peer-Reviewed Original Research
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 ResearchMeSH KeywordsAngiotensin-Converting Enzyme 2COVID-19HumansPeptidyl-Dipeptidase AProtein BindingSARS-CoV-2ConceptsSARS-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
2001
Erythropoietin-mediated neuroprotection involves cross-talk between Jak2 and NF-κB signalling cascades
Digicaylioglu M, Lipton S. Erythropoietin-mediated neuroprotection involves cross-talk between Jak2 and NF-κB signalling cascades. Nature 2001, 412: 641-647. PMID: 11493922, DOI: 10.1038/35088074.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCell NucleusCells, CulturedDNAErythropoietinGenes, ReporterJanus Kinase 2NeuronsNeuroprotective AgentsNF-kappa BNitric OxideN-MethylaspartateProtein BindingProtein TransportProtein-Tyrosine KinasesProto-Oncogene ProteinsRatsReceptors, ErythropoietinSignal TransductionSuperoxide DismutaseTumor Necrosis Factor-alphaConceptsHypoxia-inducible factor-1EPO receptorForm of JAK2Transcription factor hypoxia-inducible factor-1NF-κB-dependent transcriptionNF-κB functionActivation of JAK2Subsequent nuclear translocationTranscription factor NF-κBNF-κBFactor NF-κBSignaling cascadesNitric oxideKinase 2NF-κB signaling cascadesHypoxic-ischemic preconditioningNuclear translocationNeuroprotective genesFactor 1JAK2Neuroprotective pathwaysNeuronal apoptosisCerebrocortical neuronsEPO effectsDegenerative damage
1999
Absence of binding activity of neuron-restrictive silencer factor is necessary, but not sufficient for transcription of NMDA receptor subunit type 1 in neuronal cells
Okamoto S, Sherman K, Lipton S. Absence of binding activity of neuron-restrictive silencer factor is necessary, but not sufficient for transcription of NMDA receptor subunit type 1 in neuronal cells. Brain Research 1999, 74: 44-54. PMID: 10640675, DOI: 10.1016/s0169-328x(99)00250-8.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCell DifferentiationDown-RegulationGene Expression RegulationHeLa CellsHumansLuciferasesMutationNeuronsPromoter Regions, GeneticProtein BindingReceptors, N-Methyl-D-AspartateRecombinant Fusion ProteinsRepressor ProteinsResponse ElementsRNA, MessengerSequence Homology, Nucleic AcidTranscription FactorsTranscription, GeneticTumor Cells, CulturedConceptsNRSF/RESTNeuron-restrictive silencer factorPromoter activityNR1 geneSilencer factorCell linesNRSE/RE1Set of genesNeuronal cellsType I geneNonneuronal cell linesREST proteinNeuronal cell lineI geneP19 cellsConsensus sequenceNeuronal differentiationGenesHeLa cellsTranscriptionNonneuronal cellsIndependent mannerNeuronal specificityMRNA levelsExpression
1998
Synergistic Activation of theN-Methyl-d-aspartate Receptor Subunit 1 Promoter by Myocyte Enhancer Factor 2C and Sp1*
Krainc D, Bai G, Okamoto S, Carles M, Kusiak J, Brent R, Lipton S. Synergistic Activation of theN-Methyl-d-aspartate Receptor Subunit 1 Promoter by Myocyte Enhancer Factor 2C and Sp1*. Journal Of Biological Chemistry 1998, 273: 26218-26224. PMID: 9748305, DOI: 10.1074/jbc.273.40.26218.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCell LineDNA-Binding ProteinsEpidermal Growth FactorFibroblast Growth Factor 2Gene Expression Regulation, DevelopmentalMEF2 Transcription FactorsMyogenic Regulatory FactorsNerve Tissue ProteinsNuclear ProteinsPromoter Regions, GeneticProtein BindingReceptors, N-Methyl-D-AspartateRNA, MessengerSp1 Transcription FactorTranscriptional ActivationConceptsMyocyte enhancer factor 2CSp1 sitesSp1 proteinMEF2 siteFactor 2CNMDA receptor subunit 1Results of yeastNR1 promoterMuscle transcription factorsCo-immunoprecipitation experimentsDifferentiated P19 cellsGrowth factorGrowth factor regulationTwo-hybridActivation domainSp1 cDNAEssential subunitTranscription factorsEpidermal growth factorP19 cellsFactor regulationPromoter activityFibroblast growth factorBasic fibroblast growth factorNeuronal development
1995
An astrocytic binding site for neuronal Thy-1 and its effect on neurite outgrowth.
Dreyer E, Leifer D, Heng J, McConnell J, Gorla M, Levin L, Barnstable C, Lipton S. An astrocytic binding site for neuronal Thy-1 and its effect on neurite outgrowth. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 11195-11199. PMID: 7479964, PMCID: PMC40598, DOI: 10.1073/pnas.92.24.11195.Peer-Reviewed Original ResearchConceptsNeurite outgrowthThy-1 functionsNeuronal Thy-1Thy-1Abundant glycoproteinMammalian neuronsNervous systemAnti-idiotype monoclonal antibodyCentral nervous system neuronsMonoclonal antibodiesBinding sitesCentral nervous systemAnti-idiotype antibodiesCertain monoclonal antibodiesBinding assaysCompetitive binding assaysProteinOutgrowthSystem neuronsDendritic developmentAntibodiesNeuronsSitesGlycoproteinCells
1990
Neuronal injury due to HIV-1 envelope protein is blocked by anti-gp120 antibodies but not by anti-CD4 antibodies.
Kaiser P, Offermann J, Lipton S. Neuronal injury due to HIV-1 envelope protein is blocked by anti-gp120 antibodies but not by anti-CD4 antibodies. Neurology 1990, 40: 1757-61. PMID: 2234433, DOI: 10.1212/wnl.40.11.1757.Peer-Reviewed Original ResearchConceptsAnti-CD4 antibodiesNeuronal injuryHuman immunodeficiency virus type 1Retinal ganglion cell neuronsImmunodeficiency virus type 1Absence of superinfectionHIV-1 envelope proteinAnti-gp120 antibodiesGanglion cell neuronsRat T cellsForm of neurotoxicityVirus type 1Envelope proteinNeurologic manifestationsVisual lossImmunodeficiency syndromeCentral neuronsT cellsT lymphocytesHIV-1Protein gp120CD4 moleculeCell neuronsGp120Type 1