2016
Modulation of VEGF receptor 2 signaling by protein phosphatases
Corti F, Simons M. Modulation of VEGF receptor 2 signaling by protein phosphatases. Pharmacological Research 2016, 115: 107-123. PMID: 27888154, PMCID: PMC5205541, DOI: 10.1016/j.phrs.2016.11.022.Peer-Reviewed Original ResearchConceptsProtein phosphatasePhosphorylation of serineVascular endothelial growth factor receptor 2 signalingSignal transduction cascadePrecise biological roleSpecific signaling pathwaysKinase biologyEukaryotic cellsSignal terminatorRegulatory subunitPositive regulatorTransduction cascadePhosphorylation stateBiological roleContext of cancerParticular proteinDifferent proteinsGenome sequencingSignaling pathwaysVEGF receptor 2Receptor 2 signalingVEGF signalsProteinPhosphataseGenetic models
2015
Deciphering Signaling Pathway Networks to Understand the Molecular Mechanisms of Metformin Action
Sun J, Zhao M, Jia P, Wang L, Wu Y, Iverson C, Zhou Y, Bowton E, Roden D, Denny J, Aldrich M, Xu H, Zhao Z. Deciphering Signaling Pathway Networks to Understand the Molecular Mechanisms of Metformin Action. PLOS Computational Biology 2015, 11: e1004202. PMID: 26083494, PMCID: PMC4470683, DOI: 10.1371/journal.pcbi.1004202.Peer-Reviewed Original ResearchConceptsGWAS datasetsPathway networkDisease genesGenome-wide association study datasetDrug targetsSignal transduction networksSignal transduction cascadeMultiple signaling pathwaysDrug-induced gene expressionNovel drug targetsTransduction networksTransduction cascadeEnrichment analysisGene expressionCommon genesMolecular mechanismsSignaling pathwaysGenesNovel MycLiterature miningMolecular modePathwayMetformin actionDrug actionDisease pathogenesis
2011
A conserved PTEN/FOXO pathway regulates neuronal morphology during C. elegans development
Christensen R, de la Torre-Ubieta L, Bonni A, Colón-Ramos DA. A conserved PTEN/FOXO pathway regulates neuronal morphology during C. elegans development. Development 2011, 138: 5257-5267. PMID: 22069193, PMCID: PMC3210501, DOI: 10.1242/dev.069062.Peer-Reviewed Original ResearchMeSH KeywordsAnalysis of VarianceAnimalsAnimals, Genetically ModifiedCaenorhabditis elegansCaenorhabditis elegans ProteinsForkhead Transcription FactorsImmunohistochemistryMicroscopy, FluorescenceNeuritesNeurogenesisPhosphatidylinositol 3-KinaseProtein IsoformsRNA InterferenceRNA, Small InterferingSignal TransductionTranscription FactorsTransgenesConceptsDAF-16/FOXOPI3KDAF-18/PTENC. elegans developmentSignal transduction cascadeNeurite outgrowthMajor negative regulatorPI3K pathway activityDaf-18Caenorhabditis elegansDAF-16Transduction cascadeFOXO pathwayNegative regulatorNeuronal cell morphologyNovel roleFOXOMammalian neuronsCorrect developmentPathway activityF isoformsNovel mechanismCell morphologyPathwayNeuronal morphologyHigh Throughput Determination of TGFβ1/SMAD3 Targets in A549 Lung Epithelial Cells
Zhang Y, Handley D, Kaplan T, Yu H, Bais AS, Richards T, Pandit KV, Zeng Q, Benos PV, Friedman N, Eickelberg O, Kaminski N. High Throughput Determination of TGFβ1/SMAD3 Targets in A549 Lung Epithelial Cells. PLOS ONE 2011, 6: e20319. PMID: 21625455, PMCID: PMC3098871, DOI: 10.1371/journal.pone.0020319.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceCell LineChromatin ImmunoprecipitationDNA PrimersElectrophoretic Mobility Shift AssayEpithelial CellsHumansLungOligonucleotide Array Sequence AnalysisPromoter Regions, GeneticProtein BindingReverse Transcriptase Polymerase Chain ReactionSmad3 ProteinTransforming Growth Factor beta1ConceptsGene expression microarraysLung epithelial cellsMolecular pathwaysTranscriptional regulationExpression microarraysGlobal transcriptional regulationTGFβ1/Smad3Epithelial cellsHuman promoter regionsSignal transduction cascadeTarget gene expressionEpithelial cell phenotypeGene expression analysisTranscription factor Smad3Primary lung epithelial cellsSmad3 targetsQuantitative real-time RT-PCRFOXA2 promoterHuman A549 alveolar epithelial cellsChromatin immunoprecipitationTransduction cascadeTarget genesA549 lung epithelial cellsExpression analysisGene expressionRenal Cystic Disease Proteins Play Critical Roles in the Organization of the Olfactory Epithelium
Pluznick JL, Rodriguez-Gil DJ, Hull M, Mistry K, Gattone V, Johnson CA, Weatherbee S, Greer CA, Caplan MJ. Renal Cystic Disease Proteins Play Critical Roles in the Organization of the Olfactory Epithelium. PLOS ONE 2011, 6: e19694. PMID: 21614130, PMCID: PMC3094399, DOI: 10.1371/journal.pone.0019694.Peer-Reviewed Original ResearchConceptsRenal cystic diseaseOlfactory sensory neuronsOlfactory epitheliumCystic diseaseMutant animalsMature olfactory sensory neuronsMurine olfactory epitheliumDendritic knobsOlfactory adenylate cyclaseReceptor expressionSensory neuronsTransduction cascadeLaminar organizationDisease proteinMicrotubule architectureMKS1Syndrome 1Reduced expressionAdenylate cyclaseRT-PCRMKS3DiseaseProteinPhysiological activityObvious alterationsPhosphate Sensing
Bergwitz C, Jüppner H. Phosphate Sensing. Advances In Kidney Disease And Health 2011, 18: 132-144. PMID: 21406298, PMCID: PMC3059779, DOI: 10.1053/j.ackd.2011.01.004.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsAmino acid sequence conservationNumerous cellular functionsMulti-protein complexesDifferent signal transduction cascadesSignal transduction cascadeExpression of genesSignal transduction cascadesEukaryotic organismsMulticellular organismsMetazoan cellsMetazoan orthologsSequence conservationCellular functionsPHO pathwayTransduction cascadePlasma membraneAmbient phosphateCell metabolismExtracellular phosphateYeastGrowth of tissuesPhosphate sensorPhosphate homeostasisPhosphate uptakeCirculating phosphate levels
2010
Bone Morphogenetic Protein Signaling: Implications in Urology
Jeong J, Kang D, Lee G, Kim I. Bone Morphogenetic Protein Signaling: Implications in Urology. Investigative And Clinical Urology 2010, 51: 511-517. PMID: 20733955, PMCID: PMC2924553, DOI: 10.4111/kju.2010.51.8.511.Peer-Reviewed Original ResearchBone morphogenetic proteinSmall molecule inhibitorsBMP signalingTransmembrane serine/threonine kinase receptorsSerine/threonine kinase receptorsSubsequent signal transduction cascadesMolecule inhibitorsFirst small-molecule inhibitorSignal transduction cascadeMultiple key stepsSmad-independent pathwaysDiverse human diseasesHeteromeric complexesTransduction cascadeEmbryonic developmentInhibitory SmadsMorphogenetic proteinsReceptor domainHuman diseasesKinase receptorsCritical functionsPathwayCritical roleNovel therapeuticsSignaling
2009
Membrane-initiated actions of estrogen on the endothelium
Kim KH, Bender JR. Membrane-initiated actions of estrogen on the endothelium. Molecular And Cellular Endocrinology 2009, 308: 3-8. PMID: 19549586, PMCID: PMC2701909, DOI: 10.1016/j.mce.2009.03.025.Peer-Reviewed Original ResearchConceptsEndothelial nitric oxide synthaseNumerous signal transduction cascadesSignal transduction cascadeNitric oxideEndothelial cellsNon-genomic actionsAction of estrogenNitric oxide synthaseCaveolar membranesEstrogen receptor alphaTransduction cascadeC-SrcN-terminusShort isoformHuman endothelial cellsRapid activationProduct nitric oxideVascular studiesOxide synthaseReceptor alphaEstrogenVascular structuresER46Favorable effectCritical role
2008
Substrate Discrimination among Mitogen-activated Protein Kinases through Distinct Docking Sequence Motifs*
Sheridan DL, Kong Y, Parker SA, Dalby KN, Turk BE. Substrate Discrimination among Mitogen-activated Protein Kinases through Distinct Docking Sequence Motifs*. Journal Of Biological Chemistry 2008, 283: 19511-19520. PMID: 18482985, PMCID: PMC2443660, DOI: 10.1074/jbc.m801074200.Peer-Reviewed Original ResearchConceptsDEF sitesProtein kinaseMAPK isoformsSequence requirementsMAPK signal transduction cascadePhosphorylation site motifsMAPK family membersSignal transduction cascadePeptide library screenDocking motifExtracellular stimuliMAPK interactionPhosphorylation sitesSequence motifsTransduction cascadeSite motifSubstrate specificityKey residuesSequence specificityLibrary screenUnique sequencesIndividual MAPKsCellular responsesComputational docking studiesExquisite specificityVascular cell signaling by membrane estrogen receptors
Kim KH, Moriarty K, Bender JR. Vascular cell signaling by membrane estrogen receptors. Steroids 2008, 73: 864-869. PMID: 18325557, PMCID: PMC2519041, DOI: 10.1016/j.steroids.2008.01.008.Peer-Reviewed Original ResearchConceptsNumerous signal transduction cascadesEndothelial nitric oxide synthaseCaveolin-1 interactionSignal transduction cascadeEndothelial cellsNon-genomic actionsTranscriptional regulationPI3K/AktMembrane estrogen receptorsCaveolar membranesTransduction cascadeC-SrcCell signalingN-terminusHuman endothelial cellsRapid activationMolecular studiesConsequent activationVascular cellsNumerous animalsNitric oxideMultiple biological effectsEstrogen receptor alphaFavorable estrogenic effectsER46
2005
Subunit arrangement and function in NMDA receptors
Furukawa H, Singh SK, Mancusso R, Gouaux E. Subunit arrangement and function in NMDA receptors. Nature 2005, 438: 185-192. PMID: 16281028, DOI: 10.1038/nature04089.Peer-Reviewed Original ResearchConceptsHeteromeric ion channelsNR1-NR2AMammalian central nervous systemSlow channel openingChannel openingHeterodimer interfaceTransduction cascadeIon channel openingSubunit arrangementSubunit interfaceIon channelsNR2 subunitsReceptor functionChannel deactivationNMDA receptorsNMDA receptor functionReceptorsExcitatory neurotransmissionFunctional unitsCentral nervous systemNR1GlutamateGlycineNervous systemHeterodimers
2004
Sphingosine-1-phosphate mediates calcium signaling in guinea pig enteroglial cells
Segura BJ, Zhang W, Xiao L, Turner D, Cowles RA, Logsdon C, Mulholland MW. Sphingosine-1-phosphate mediates calcium signaling in guinea pig enteroglial cells. Journal Of Surgical Research 2004, 116: 42-54. PMID: 14732348, DOI: 10.1016/s0022-4804(03)00281-6.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological TransportCalciumCalcium ChannelsCalcium SignalingCulture TechniquesDose-Response Relationship, DrugDrug Administration ScheduleEnzyme ActivationGuinea PigsImmunohistochemistryInositol 1,4,5-Trisphosphate ReceptorsLysophospholipidsMyenteric PlexusNeurogliaPertussis ToxinReceptors, Cytoplasmic and NuclearReceptors, G-Protein-CoupledRNA, MessengerSphingolipidsSphingosineType C PhospholipasesConceptsSignal transduction cascadeEnteric nervous systemEnteric gliaLipid lysophosphatidic acidMajor cell typesRT-PCR analysisTransduction cascadeGlial cellsNervous systemEDG-1Trisphosphate receptorCalcium signalingLysophosphatidic acidCell typesExtracellular receptorsPhospholipase CEdg-3Enteric glial cellsBioactive lipidsEdg-5S1P effectsSphingomyelin metabolitesDigestive activityImmunocytochemical analysisEnteric neurons
2002
Rapid vascular cell responses to estrogen and membrane receptors
Haynes MP, Li L, Russell KS, Bender JR. Rapid vascular cell responses to estrogen and membrane receptors. Vascular Pharmacology 2002, 38: 99-108. PMID: 12379956, DOI: 10.1016/s0306-3623(02)00133-7.Peer-Reviewed Original ResearchConceptsSignal transduction cascadeTransduction cascadeG protein-coupled receptorsMembrane-localized estrogen receptorsEstrogen receptorTranscription factorsMAP kinaseApparent coronary heart diseaseRapid consequencesCellular responsesCellular localizationMembrane receptorsCoronary heart diseaseAge-matched malesEffects of estrogenVascular cell responsesSmooth muscle cellsVariety of estrogenVascular cellsMuscle cellsComplex formationPremenopausal womenHeart diseaseVascular wallMarked gender differences
2001
PECAM‐1 shedding during apoptosis generates a membrane‐anchored truncated molecule with unique signaling characteristics
ILAN N, MOHSENIN A, CHEUNG L, MADRI J. PECAM‐1 shedding during apoptosis generates a membrane‐anchored truncated molecule with unique signaling characteristics. The FASEB Journal 2001, 15: 362-372. PMID: 11156952, DOI: 10.1096/fj.00-0372com.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid Chloromethyl KetonesAnimalsAntigens, CDApoptosisBlood PlateletsCaspasesCattleCell DivisionCell LineCell MembraneCells, CulturedColonic NeoplasmsCulture MediaDipeptidesEndothelium, VascularEnzyme InhibitorsHumansPlatelet Endothelial Cell Adhesion Molecule-1Sequence DeletionSignal TransductionTransfectionTumor Cells, CulturedUmbilical VeinsConceptsFull-length PECAM-1Signal transduction cascadeSignal transduction eventsCaspase-8 cleavageCell proliferationPECAM-1SW480 colon carcinoma cellsCaspase substratesSHP-2Transduction cascadeTransduction eventsGrowth factor receptorCell adhesion moleculeGene constructsCell surface moleculesColon carcinoma cellsSoluble proteinStable expressionCell deathCulture mediumMatrix metalloproteinaseCell surfaceJNK phosphorylationUnique functionFactor receptor
2000
Molecular basis of semaphorin‐mediated axon guidance
Nakamura F, Kalb R, Strittmatter S. Molecular basis of semaphorin‐mediated axon guidance. Developmental Neurobiology 2000, 44: 219-229. PMID: 10934324, DOI: 10.1002/1097-4695(200008)44:2<219::aid-neu11>3.0.co;2-w.Peer-Reviewed Original ResearchConceptsGrowth cone collapseSemaphorin guidance cuesMonomeric G proteinsSignal transduction cascadeGuidance cuesAxon guidance eventsCone collapseGrowth cone motilityCaenorhabditis elegansActin cytoskeletonTransmembrane proteinFilopodial tipsNeuropilin-1Transduction cascadeMolecular basisComplex interactsIntracellular domainPrototypic memberGrowth cone turningRac1 activityAxon guidanceG proteinsRepulsive guidance cuesNeuronal proteinsAxonal guidanceThe c-Jun NH2-terminal Kinase Promotes Insulin Resistance during Association with Insulin Receptor Substrate-1 and Phosphorylation of Ser307 *
Davis R, Aguirre V, Uchida T, Yenush L, White M. The c-Jun NH2-terminal Kinase Promotes Insulin Resistance during Association with Insulin Receptor Substrate-1 and Phosphorylation of Ser307 *. Journal Of Biological Chemistry 2000, 275: 9047-9054. PMID: 10722755, DOI: 10.1074/jbc.275.12.9047.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAnisomycinCHO CellsCricetinaeHumansInsulinInsulin Receptor Substrate ProteinsInsulin ResistanceJNK Mitogen-Activated Protein KinasesMiceMitogen-Activated Protein KinasesMolecular Sequence DataPhosphoproteinsPhosphorylationProtein BindingReceptor, InsulinRecombinant ProteinsSerineSignal TransductionTumor Necrosis Factor-alphaConceptsInsulin-stimulated tyrosine phosphorylationIRS-1Serine 307Tyrosine phosphorylationInsulin receptor substrate-1IRS-1 functionSignal transduction cascadePhosphorylation of Ser307Receptor substrate-1Chinese hamster ovary cellsIRS proteinsActivity of JNKJNK associatesPhosphorylation sitesHamster ovary cellsTransduction cascadeSerine phosphorylationTerminal kinaseSubstrate-1PhosphorylationStrong activatorPromotes Insulin ResistanceJNK phosphorylationOvary cellsJNKThe Regulation of Normal Melanocyte Proliferation
Halaban R. The Regulation of Normal Melanocyte Proliferation. Pigment Cell & Melanoma Research 2000, 13: 4-14. PMID: 10761990, DOI: 10.1034/j.1600-0749.2000.130103.x.Peer-Reviewed Original ResearchConceptsTranscription factorsIntracellular signal transduction cascadesE2F transcription factorsImmediate early response genesSignal transduction cascadeHepatocyte growth factor/scatter factorGrowth factorGrowth factor/scatter factorE2F transcriptional activityCyclin-dependent kinasesSynergistic growth factorsNormal human melanocytesPocket proteinsRetinoblastoma familyPeptide growth factorsStem cell factorTransduction cascadeNormal melanocyte proliferationEctopic expressionResponse genesTranscriptional activityFibroblast growth factorMolecular eventsHuman melanocytesIntermediate effectors
1996
Inhibition of Tumor Necrosis Factor Signal Transduction in Endothelial Cells by Dimethylaminopurine*
Marino M, Dunbar J, Wu L, Ngaiza J, Han H, Guo D, Matsushita M, Nairn A, Zhang Y, Kolesnick R, Jaffe E, Donner D. Inhibition of Tumor Necrosis Factor Signal Transduction in Endothelial Cells by Dimethylaminopurine*. Journal Of Biological Chemistry 1996, 271: 28624-28629. PMID: 8910494, DOI: 10.1074/jbc.271.45.28624.Peer-Reviewed Original ResearchMeSH KeywordsAdenineAnimalsCattleEndothelium, VascularEnzyme InhibitorsEukaryotic Initiation Factor-4EHistaminePeptide Elongation Factor 2Peptide Elongation FactorsPeptide Initiation FactorsPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene Proteins c-rafSignal TransductionTumor Necrosis Factor-alphaConceptsBovine aortic endothelial cellsElongation factor 2Distinct signal transduction cascadesEukaryotic initiation factor 4ETNF signal transduction pathwayEF-2 phosphorylationC-Jun N-terminal kinaseSignal transduction cascadeInitiation factor 4EProtein kinase activitySignal transduction pathwaysEndothelial cellsN-terminal kinaseTNF actionPhosphorylation cascadeEIF-4ESignal transductionTransduction cascadeTransduction pathwaysResponse of BAECsJun-B expressionKinase activityProtein synthesisPhosphorylationCell typesMg2+ as an Extracellular Signal: Environmental Regulation of Salmonella Virulence
Véscovi E, Soncini F, Groisman E. Mg2+ as an Extracellular Signal: Environmental Regulation of Salmonella Virulence. Cell 1996, 84: 165-174. PMID: 8548821, DOI: 10.1016/s0092-8674(00)81003-x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial ProteinsBase SequenceCationsGene Expression Regulation, BacterialHydrogen-Ion ConcentrationKineticsMagnesiumMolecular Sequence DataMutationPeptidesPhenotypeProtein ConformationSalmonella typhimuriumSensitivity and SpecificitySignal TransductionTranscription FactorsVirulenceConceptsPhoP/PhoQ systemTranscription of PhoPSignal transduction cascadeVirulence regulatory systemGene expression patternsPeriplasmic domainWild-type SalmonellaExtracellular signalsTransduction cascadeSalmonella virulenceExpression patternsFirst messengersPhoPRegulatory systemGenesPhoQSalmonella typhimuriumPhysiological concentrationsDivalent cationsTranscriptionConcentration of Mg2LociMg2DomainVirulence
1995
An activated mutant of the a subunit of Go increases neurite outgrowth via protein kinase C
Xie R, Li L, Goshima Y, Strittmatter S. An activated mutant of the a subunit of Go increases neurite outgrowth via protein kinase C. Brain Research 1995, 87: 77-86. PMID: 7554235, DOI: 10.1016/0165-3806(95)00061-h.Peer-Reviewed Original ResearchMeSH KeywordsAlkaloidsAnimalsCalciumCalcium Channel BlockersCalcium-Transporting ATPasesDose-Response Relationship, DrugEnzyme InhibitorsEthers, CyclicGallic AcidGTP-Binding ProteinsMutationNeuritesOkadaic AcidPC12 CellsProtein Kinase CRatsSecond Messenger SystemsStaurosporineTerpenesThapsigarginTransfectionConceptsProtein kinase CAlpha oKinase CNeurite outgrowthNeuronal growth cone membraneProtein phosphatase inhibitorSignal transduction cascadeDifferent signal transduction cascadesNeurite extensionGrowth cone membranePhorbol ester treatmentPhosphatase inhibitorTransduction cascadeOkadaic acidEster treatmentPhorbol esterCone membraneNeurite elongationMutantsIntracellular mechanismsKinase inhibitorsOutgrowthSubunitsIntracellular calcium levelsPresence of agents
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