2023
Endothelial nitric oxide synthase (eNOS) S1176 phosphorylation status governs atherosclerotic lesion formation
Nguyen T, Rahman N, Sessa W, Lee M. Endothelial nitric oxide synthase (eNOS) S1176 phosphorylation status governs atherosclerotic lesion formation. Frontiers In Cardiovascular Medicine 2023, 10: 1279868. PMID: 38034389, PMCID: PMC10683645, DOI: 10.3389/fcvm.2023.1279868.Peer-Reviewed Original ResearchAtherosclerotic plaque formationPlaque formationAkt1 null miceSingle amino acid substitutionMutant miceLesion formationImportance of AktUnique expression patternGene expression analysisIndex of atherosclerosisFavorable lipid profileVascular protective roleAtherosclerotic lesion formationAthero-protective effectsEndothelial NO generationAmino acid substitutionsDouble knockout miceDeletion backgroundPhosphorylation sitesAspartate substitutionPhosphorylation statusExpression analysisEnzyme functionExpression patternsENOS deletion3108 – PHOSPHORYLATION OF RUNX1 PROMOTES MEGAKARYOCYTIC FATE IN MEGAKARYOCYTE-ERYTHROID PROGENITOR FATE SPECIFICATION
Kwon N, Lu Y, Thompson E, Wang L, Zhang P, Krause D. 3108 – PHOSPHORYLATION OF RUNX1 PROMOTES MEGAKARYOCYTIC FATE IN MEGAKARYOCYTE-ERYTHROID PROGENITOR FATE SPECIFICATION. Experimental Hematology 2023, 124: s104. DOI: 10.1016/j.exphem.2023.06.215.Peer-Reviewed Original ResearchMegakaryocyte-erythroid progenitorsFate specificationHEL cellsGene expressionSingle-cell RNA-seq dataPost-translational modificationsDifferential gene expressionRNA-seq dataChromatin localizationRNA-seqPhosphorylation statusRUNX1 overexpressionE progenitorsTranscriptional activityKey regulatorRUNX1 mRNAMK progenitorsT residuesGenesErythroid progenitorsRUNX1MKPProgenitorsProtein levelsSpecification mechanism
2021
Individual-oocyte transcriptomic analysis shows that genotoxic chemotherapy depletes human primordial follicle reserve in vivo by triggering proapoptotic pathways without growth activation
Titus S, Szymanska K, Musul B, Turan V, Taylan E, Garcia- Milian R, Mehta S, Oktay K. Individual-oocyte transcriptomic analysis shows that genotoxic chemotherapy depletes human primordial follicle reserve in vivo by triggering proapoptotic pathways without growth activation. Scientific Reports 2021, 11: 407. PMID: 33431979, PMCID: PMC7801500, DOI: 10.1038/s41598-020-79643-x.Peer-Reviewed Original ResearchMeSH KeywordsAdultAnimalsAntineoplastic Combined Chemotherapy ProtocolsApoptosisCyclophosphamideDNA DamageFemaleGene Expression ProfilingHeterograftsHumansMiceMice, Inbred NODMice, SCIDOocytesOogenesisOvarian FollicleOvarian ReserveOvarySignal TransductionSingle-Cell AnalysisTranscriptomeYoung AdultConceptsPrimordial follicle oocytesFollicle lossGrowth activationHuman ovarian xenograft modelPI3K/PTEN/AktFollicle oocytesDNA damagePI3K/PTEN/Akt pathwayOvarian reserve depletionPrimordial follicle reservePTEN/AKT pathwayIngenuity Pathway AnalysisOvarian xenograft modelPTEN/AKTSevere DNA damageExpression of AktGonadotoxic chemotherapyAnti-apoptotic Bcl2Early menopauseFollicle reserveTranscriptomic analysisCyclophosphamide injectionHuman ovaryPhosphorylation statusRNA sequencing
2015
Conformation-Dependent Human p52Shc Phosphorylation by Human c‑Src
Tsutsui Y, Johnson J, Demeler B, Kinter M, Hays F. Conformation-Dependent Human p52Shc Phosphorylation by Human c‑Src. Biochemistry 2015, 54: 3469-3482. PMID: 25961473, PMCID: PMC12151137, DOI: 10.1021/acs.biochem.5b00122.Peer-Reviewed Original ResearchMeSH KeywordsCell MembraneCSK Tyrosine-Protein KinaseExtracellular Signal-Regulated MAP KinasesGRB2 Adaptor ProteinHumansMAP Kinase Signaling SystemPhosphatidylinositol PhosphatesPhosphorylationProtein StabilityProto-Oncogene Proteins p21(ras)Shc Signaling Adaptor ProteinsSrc Homology 2 Domain-Containing, Transforming Protein 1src-Family KinasesConceptsHuman c-SrcMembrane-mimetic environmentsC-SrcPhosphorylation sitesAdaptor proteinGrb2 adaptor proteinPhosphorylation-dependent interactionPhosphorylation levelsRas/MAPKAmount of phosphorylationActive c-SrcCascade activationProtein phosphorylationMass spectrometry analysisComplex assemblyPhosphorylation statePhosphorylation statusP52ShcTyrosine residuesPhosphatidylinositol 4Tyrosine kinaseBiophysical characterizationInitial binding interactionGrb2Functional linkage
2011
Building Blocks of the Nexin-Dynein Regulatory Complex in Chlamydomonas Flagella*
Lin J, Tritschler D, Song K, Barber CF, Cobb JS, Porter ME, Nicastro D. Building Blocks of the Nexin-Dynein Regulatory Complex in Chlamydomonas Flagella*. Journal Of Biological Chemistry 2011, 286: 29175-29191. PMID: 21700706, PMCID: PMC3190725, DOI: 10.1074/jbc.m111.241760.Peer-Reviewed Original ResearchConceptsNexin-dynein regulatory complexRegulatory complexImportant regulatory nodeTwo-dimensional electrophoresisRegulatory nodesProtein phosphorylationSignal transductionPhosphorylation statusMALDI-TOF mass spectrometryDynein motorsDynein activityChlamydomonas flagellaMotile ciliaRegulatory functionsPhosphorylated isoformsCoordination of thousandsFlagellar axonemeBiochemical comparisonRadial spokesPCR analysisFlagellar bendingIsoform patternFlagellaMolecular compositionProtein
2009
Dephosphorylation of the C-terminal Tyrosyl Residue of the DNA Damage-related Histone H2A.X Is Mediated by the Protein Phosphatase Eyes Absent*
Krishnan N, Jeong DG, Jung SK, Ryu SE, Xiao A, Allis CD, Kim SJ, Tonks NK. Dephosphorylation of the C-terminal Tyrosyl Residue of the DNA Damage-related Histone H2A.X Is Mediated by the Protein Phosphatase Eyes Absent*. Journal Of Biological Chemistry 2009, 284: 16066-16070. PMID: 19351884, PMCID: PMC2713548, DOI: 10.1074/jbc.c900032200.Peer-Reviewed Original ResearchMeSH KeywordsCell Line, TumorDNA DamageDNA-Binding ProteinsElectrochemistryHistonesHumansIntracellular Signaling Peptides and ProteinsMetalsNuclear ProteinsPhosphorylationProtein Structure, TertiaryProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine PhosphatasesRNA InterferenceSubstrate SpecificityTransfectionTyrosineConceptsEyes AbsentDNA damage responseTyr-142Damage responseTyrosyl residuesProtein tyrosine phosphataseDNA damage repairAtypical kinaseHistone H2A.X.Haloacid dehalogenaseMammalian cellsHistone H2A.XDisplayed specificityElevated basal phosphorylationPhosphorylation statusRNA interferenceDamage repairPhysiological substratesH2A.XNovel roleBasal phosphorylationImportant regulatorDephosphorylationResiduesWSTF
2001
Phosphorylation of the Saccharomyces cerevisiae La protein does not appear to be required for its functions in tRNA maturation and nascent RNA stabilization.
Long K, Cedervall T, Walch-Solimena C, Noe D, Huddleston M, Annan R, Wolin S. Phosphorylation of the Saccharomyces cerevisiae La protein does not appear to be required for its functions in tRNA maturation and nascent RNA stabilization. RNA 2001, 7: 1589-602. PMID: 11720288, PMCID: PMC1370201.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAutoantigensBinding SitesCell NucleolusCell NucleusFungal ProteinsMolecular Sequence DataPeptide MappingPhosphorylationProtein IsoformsRibonucleoproteinsRibonucleoproteins, Small NuclearRNARNA StabilityRNA, FungalRNA, TransferRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsLa proteinAbundant nuclear phosphoproteinRNA polymerase III transcriptsS. cerevisiae proteinTwo-dimensional gel electrophoresisRole of phosphorylationPolymerase III transcriptsCerevisiae proteinsNascent RNANascent transcriptsS. pombeSchizosaccharomyces pombeLhp1pPhosphorylation sitesYeast SaccharomycesProtein functionMutant versionSubcellular locationFirst proteinHuman proteinsNuclear phosphoproteinExonucleolytic degradationSerine phosphorylationPhosphorylation statusRNA stabilizationSustained Activation of Extracellular Signal‐Regulated Kinase (ERK) Signaling in Human Prostate Cancer LNCaP Cells Depleted of Androgen
Drew L, Fine R, Raffo A, Petrylak D. Sustained Activation of Extracellular Signal‐Regulated Kinase (ERK) Signaling in Human Prostate Cancer LNCaP Cells Depleted of Androgen. The Prostate Journal 2001, 3: 105-117. DOI: 10.1046/j.1525-1411.2001.32003.x.Peer-Reviewed Original ResearchHuman prostate cancer LNCaP cellsERK phosphorylationMitogen-activated protein kinase cascadeProstate cancer LNCaP cellsProtein kinase cascadeC-Jun N-terminal kinaseMAPK kinase activityPhosphorylation/activityLNCaP cellsProtein levelsN-terminal kinaseMEK inhibitor U0126Formation of neuritesTyrosine kinase receptorsKinase cascadeExtracellular signalsAndrogen-sensitive human prostate cancer LNCaP cellsPhosphorylation statusKinase activityPotential role
1996
Insulin-like growth factor-1 induces rapid tyrosine phosphorylation of the vav proto-oncogene product.
Uddin S, Yetter A, Katzav S, Hofmann C, White M, Platanias L. Insulin-like growth factor-1 induces rapid tyrosine phosphorylation of the vav proto-oncogene product. Experimental Hematology 1996, 24: 622-7. PMID: 8605967.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell Cycle ProteinsCell LineHumansInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor IIntracellular Signaling Peptides and ProteinsMicePhosphoproteinsPhosphorylationPhosphotyrosineProtein-Tyrosine KinasesProto-Oncogene MasProto-Oncogene ProteinsProto-Oncogene Proteins c-vavSignal TransductionConceptsSrc homology 2 domainVav proto-oncogene productGuanine exchange factorAntiphosphotyrosine monoclonal antibodyProto-oncogene productInsulin-like growth factor 1 receptorIGF-1 stimulationGrowth factor 1 receptorHematopoietic cell proliferationFactor 1 receptorExchange factorSH3 domainTyrosine phosphorylationPhosphorylation statusLigand bindingMediate signalsHematopoietic cellsImmunoblotting experimentsHematopoietic originCell proliferationCell linesHuman myeloma cell linesMyeloma cell linesCellsPhosphorylation
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