2023
Cell circuits between leukemic cells and mesenchymal stem cells block lymphopoiesis by activating lymphotoxin beta receptor signaling
Feng X, Sun R, Lee M, Chen X, Guo S, Geng H, Müschen M, Choi J, Pereira J. Cell circuits between leukemic cells and mesenchymal stem cells block lymphopoiesis by activating lymphotoxin beta receptor signaling. ELife 2023, 12: e83533. PMID: 36912771, PMCID: PMC10042536, DOI: 10.7554/elife.83533.Peer-Reviewed Original ResearchConceptsMesenchymal stem cellsLymphotoxin beta receptorLeukemic cellsBeta receptorsLeukemic cell growthBone marrow microenvironmentStem cellsTransplant recipientsAML cellsMyeloblastic leukemiaMouse modelBone marrowLeukemia growthLymphotoxin α1β2Marrow microenvironmentPharmacological disruptionLymphopoiesisReceptorsHematopoietic outputMolecular mechanismsErythropoiesisDNA damage response pathwayCell growthCellsPhysiological mechanisms
2022
Dysregulated stem cell niches and altered lymphocyte recirculation cause B and T cell lymphopenia in WHIM syndrome
Zehentmeier S, Lim VY, Ma Y, Fossati J, Ito T, Jiang Y, Tumanov AV, Lee HJ, Dillinger L, Kim J, Csomos K, Walter JE, Choi J, Pereira JP. Dysregulated stem cell niches and altered lymphocyte recirculation cause B and T cell lymphopenia in WHIM syndrome. Science Immunology 2022, 7: eabo3170. PMID: 36149943, PMCID: PMC9614684, DOI: 10.1126/sciimmunol.abo3170.Peer-Reviewed Original ResearchConceptsSecondary lymphoid organsWHIM syndromeMesenchymal stem cellsInterleukin-7B lymphopeniaBone marrowBM mesenchymal stem cellsT cell numbersIL-7 productionT-cell lymphopeniaLymphotoxin beta receptorEarly progenitor stageLymphoid organsCell lymphopeniaMouse modelBeta receptorsB cellsB cell developmentLymphopeniaStromal cellsLeukocyte retentionSyndromeGOF mutationsLymphopoietic activityCritical pathways
2019
Loss of the TAM Receptor Axl Ameliorates Severe Zika Virus Pathogenesis and Reduces Apoptosis in Microglia
Hastings AK, Hastings K, Uraki R, Hwang J, Gaitsch H, Dhaliwal K, Williamson E, Fikrig E. Loss of the TAM Receptor Axl Ameliorates Severe Zika Virus Pathogenesis and Reduces Apoptosis in Microglia. IScience 2019, 13: 339-350. PMID: 30884311, PMCID: PMC6424058, DOI: 10.1016/j.isci.2019.03.003.Peer-Reviewed Original ResearchZIKV infectionZIKV pathogenesisVirus infectionAxl-deficient miceZika virus pathogenesisRole of AxlZika virus infectionAlpha/beta receptorTAM receptor AxlInterferon alpha/beta receptorTAM receptorsVirus pathogenesisMouse modelEntry receptorBeta receptorsReceptor AxlViral infectionAXL inhibitorAxl receptorInfectionPathogenesisAxlMiceLess apoptosisReceptorsModeling Arboviral Infection in Mice Lacking the Interferon Alpha/Beta Receptor
Marín-Lopez A, Calvo-Pinilla E, Moreno S, Utrilla-Trigo S, Nogales A, Brun A, Fikrig E, Ortego J. Modeling Arboviral Infection in Mice Lacking the Interferon Alpha/Beta Receptor. Viruses 2019, 11: 35. PMID: 30625992, PMCID: PMC6356211, DOI: 10.3390/v11010035.Peer-Reviewed Original ResearchConceptsMouse modelAnimal modelsArbovirus infectionInterferon α/β receptorAlpha/beta receptorAppropriate animal modelsNatural hostInterferon alpha/beta receptorSafe therapyProtective efficacyArboviral infectionsImmune responseAdult miceBeta receptorsNew vaccinesDisease pathogenesisExtrapolation of findingsΒ receptorExperimental infectionBiosafety level 3MiceInfectionStatistical significanceVirusPathogenesis
2009
Artificial Transmembrane Oncoproteins Smaller than the Bovine Papillomavirus E5 Protein Redefine Sequence Requirements for Activation of the Platelet-Derived Growth Factor β Receptor
Talbert-Slagle K, Marlatt S, Barrera FN, Khurana E, Oates J, Gerstein M, Engelman DM, Dixon AM, DiMaio D. Artificial Transmembrane Oncoproteins Smaller than the Bovine Papillomavirus E5 Protein Redefine Sequence Requirements for Activation of the Platelet-Derived Growth Factor β Receptor. Journal Of Virology 2009, 83: 9773-9785. PMID: 19605488, PMCID: PMC2748040, DOI: 10.1128/jvi.00946-09.Peer-Reviewed Original ResearchConceptsPDGF beta receptorTransmembrane domainBPV E5Transmembrane proteinBovine papillomavirus E5 proteinPlatelet-derived growth factor beta receptorArtificial transmembrane proteinsLigand-independent receptor activationPrimary amino acid sequenceSimilar cellular proteinsSmall artificial proteinsGrowth factor β receptorHomodimeric transmembrane proteinAmino acid sequenceGrowth factor beta receptorConsecutive amino acidsC-terminal cysteineSame cellular targetsNew genetic techniquesBeta receptorsCellular proteinsAcid sequenceE5 proteinGenetic techniquesSequence requirements
2004
IκB Kinase Complex α Kinase Activity Controls Chemokine and High Endothelial Venule Gene Expression in Lymph Nodes and Nasal-Associated Lymphoid Tissue
Drayton DL, Bonizzi G, Ying X, Liao S, Karin M, Ruddle NH. IκB Kinase Complex α Kinase Activity Controls Chemokine and High Endothelial Venule Gene Expression in Lymph Nodes and Nasal-Associated Lymphoid Tissue. The Journal Of Immunology 2004, 173: 6161-6168. PMID: 15528353, DOI: 10.4049/jimmunol.173.10.6161.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell DifferentiationChemokinesEndothelium, LymphaticEnzyme ActivationGene Expression Regulation, DevelopmentalI-kappa B KinaseLigandsLymph NodesLymphoid TissueLymphotoxin beta ReceptorMiceMice, Inbred C57BLMice, KnockoutMice, Mutant StrainsNasal MucosaProtein Serine-Threonine KinasesProtein SubunitsReceptors, Tumor Necrosis FactorConceptsHigh endothelial venulesSecondary lymphoid organogenesisLymph nodesAlternative NF-kappaB pathwayPeripheral node addressinNF-kappaB pathwayLymphoid tissueLymphoid organogenesisNasal-associated lymphoid tissueCell adhesion molecule-1Lymphoid chemokines CCL19Adhesion molecule-1GlyCAM-1Lymphotoxin beta receptorPathway activityNALT developmentChemokines CCL19Endothelial venulesBeta receptorsMolecule-1Mutant miceTarget genesCritical roleGene expressionReduced expression
2000
Bovine Papillomavirus E5 Protein Induces the Formation of Signal Transduction Complexes Containing Dimeric Activated Platelet-derived Growth Factor β Receptor and Associated Signaling Proteins*
Lai C, Henningson C, DiMaio D. Bovine Papillomavirus E5 Protein Induces the Formation of Signal Transduction Complexes Containing Dimeric Activated Platelet-derived Growth Factor β Receptor and Associated Signaling Proteins*. Journal Of Biological Chemistry 2000, 275: 9832-9840. PMID: 10734138, DOI: 10.1074/jbc.275.13.9832.Peer-Reviewed Original ResearchConceptsBovine papillomavirus E5 proteinE5 proteinPDGF beta receptorBeta receptor complexCellular platelet-derived growth factor (PDGF) beta receptorReceptor complexPlatelet-derived growth factor beta receptorPlatelet-derived growth factor β receptorRas-GTPase activating proteinAssembly of multiproteinSignal transduction complexGrowth factor β receptorGrowth factor beta receptorCell growth transformationTransduction complexBeta receptorsP85 subunitSignaling proteinsPhospholipase CgammaActivating proteinReceptor dimersConstitutive activationInactive receptorProteinReceptor molecules
1999
The Bovine Papillomavirus E5 Protein Requires a Juxtamembrane Negative Charge for Activation of the Platelet-Derived Growth Factor β Receptor and Transformation of C127 Cells
Klein O, Kegler-Ebo D, Su J, Smith S, DiMaio D. The Bovine Papillomavirus E5 Protein Requires a Juxtamembrane Negative Charge for Activation of the Platelet-Derived Growth Factor β Receptor and Transformation of C127 Cells. Journal Of Virology 1999, 73: 3264-3272. PMID: 10074180, PMCID: PMC104090, DOI: 10.1128/jvi.73.4.3264-3272.1999.Peer-Reviewed Original ResearchConceptsPlatelet-derived growth factor beta receptorPDGF beta receptorGrowth factor beta receptorE5 proteinBovine papillomavirus E5 proteinCell transformationHomodimeric transmembrane proteinSustained receptor activationC127 mouse fibroblastsExtracellular juxtamembrane regionBeta receptorsE5 dimerE5 mutantsDouble mutantJuxtamembrane regionTransmembrane proteinC127 cellsC-terminusAcidic residuesE5 geneMutantsPosition 33Mouse fibroblastsProteinSalt bridge
1998
Bovine papillomavirus E5 protein induces oligomerization and trans-phosphorylation of the platelet-derived growth factor β receptor
Lai C, Henningson C, DiMaio D. Bovine papillomavirus E5 protein induces oligomerization and trans-phosphorylation of the platelet-derived growth factor β receptor. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 15241-15246. PMID: 9860953, PMCID: PMC28027, DOI: 10.1073/pnas.95.26.15241.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAnimalsBovine papillomavirus 1CattleCell LineCell Line, TransformedCross-Linking ReagentsDimerizationHumansKineticsMacromolecular SubstancesMiceOncogene Proteins, ViralPhosphorylationProtein-Tyrosine KinasesReceptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorRecombinant ProteinsSequence DeletionTransfectionConceptsBovine papillomavirus E5 proteinE5 proteinPDGF beta receptorCellular platelet-derived growth factor (PDGF) beta receptorKinase-negative mutant receptorPlatelet-derived growth factor beta receptorPlatelet-derived growth factor β receptorChemical cross-linking experimentsGrowth factor β receptorConstitutive tyrosine phosphorylationGrowth factor beta receptorLigand-independent fashionCross-linking experimentsReceptor tyrosine kinasesStable complexesExtracts of cellsPDGF beta-receptor activationIntramolecular autophosphorylationBeta receptorsCoimmunoprecipitation experimentsTransmembrane proteinReceptor activationTyrosine phosphorylationReceptor dimerizationMutant receptorsRole of Glutamine 17 of the Bovine Papillomavirus E5 Protein in Platelet-Derived Growth Factor β Receptor Activation and Cell Transformation
Klein O, Polack G, Surti T, Kegler-Ebo D, Smith S, DiMaio D. Role of Glutamine 17 of the Bovine Papillomavirus E5 Protein in Platelet-Derived Growth Factor β Receptor Activation and Cell Transformation. Journal Of Virology 1998, 72: 8921-8932. PMID: 9765437, PMCID: PMC110309, DOI: 10.1128/jvi.72.11.8921-8932.1998.Peer-Reviewed Original ResearchConceptsBovine papillomavirus E5 proteinPDGF beta receptorE5 proteinTransform cellsCellular platelet-derived growth factor (PDGF) beta receptorAmino acidsBa/F3 hematopoietic cellsPosition 17Cell transformationPlatelet-derived growth factor beta receptorHomodimeric transmembrane proteinReceptor tyrosine phosphorylationGrowth factor beta receptorReceptor tyrosine kinasesPDGF receptor tyrosine kinaseReceptor activationPossible amino acidsBeta receptorsStable complexesComplex formationMutant proteinsTransmembrane domainTransmembrane proteinGrowth factor-beta (TGF-beta) receptor activationTyrosine phosphorylation
1997
Identification of amino acids in the transmembrane and juxtamembrane domains of the platelet-derived growth factor receptor required for productive interaction with the bovine papillomavirus E5 protein
Petti L, Reddy V, Smith S, DiMaio D. Identification of amino acids in the transmembrane and juxtamembrane domains of the platelet-derived growth factor receptor required for productive interaction with the bovine papillomavirus E5 protein. Journal Of Virology 1997, 71: 7318-7327. PMID: 9311809, PMCID: PMC192076, DOI: 10.1128/jvi.71.10.7318-7327.1997.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBovine papillomavirus 1CattleCell LineCell MembraneErbB ReceptorsHumansInterleukin-3KineticsLeucineLysineMiceMolecular Sequence DataMutagenesis, Site-DirectedOncogene Proteins v-sisOncogene Proteins, ViralPoint MutationPolymerase Chain ReactionProtein Structure, SecondaryRatsReceptor, ErbB-2Receptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorReceptors, VirusRecombinant Fusion ProteinsRetroviridae Proteins, OncogenicSequence AlignmentThreonineTransfectionConceptsBovine papillomavirus E5 proteinE5 proteinTransmembrane domainPDGF beta receptorAmino acidsCellular platelet-derived growth factor (PDGF) beta receptorReceptor mutantsJuxtamembrane domainPlatelet-derived growth factor beta receptorPutative transmembrane domainsMurine Ba/F3 cellsCarboxyl-terminal domainBa/F3 cellsV-sisReceptor tyrosine phosphorylationExtracellular juxtamembrane domainGrowth factor beta receptorSpecific amino acidsProductive interactionReceptor activationPlatelet-derived growth factor receptorAcidic amino acidsComplex formationThreonine residuesBeta receptors
1995
Mutational analysis of the interaction between the bovine papillomavirus E5 transforming protein and the endogenous beta receptor for platelet-derived growth factor in mouse C127 cells
Nilson L, Gottlieb R, Polack G, DiMaio D. Mutational analysis of the interaction between the bovine papillomavirus E5 transforming protein and the endogenous beta receptor for platelet-derived growth factor in mouse C127 cells. Journal Of Virology 1995, 69: 5869-5874. PMID: 7543592, PMCID: PMC189463, DOI: 10.1128/jvi.69.9.5869-5874.1995.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesBovine papillomavirus 1Cell LineDNA Mutational AnalysisDown-RegulationFrameshift MutationKineticsMiceMolecular Sequence DataMutagenesisMutagenesis, Site-DirectedOncogene Proteins, ViralPhosphotyrosinePoint MutationProtein-Tyrosine KinasesReceptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorRecombinant ProteinsTyrosineConceptsMouse C127 cellsE5 proteinReceptor tyrosine phosphorylationTyrosine phosphorylationPDGF beta receptorC127 cellsPDGF receptorWild-type E5 proteinBovine papillomavirus E5 proteinCarboxyl-terminal cysteine residueCell transformationPlatelet-derived growth factor beta receptorMembrane-associated proteinsSustained receptor activationPDGF receptor activationMutation of glutamineTransformation-competent mutantsGrowth factor beta receptorBovine papillomavirus E5Carboxyl-terminal positionBeta receptorsHigh-level expressionPlatelet-derived growth factorStable complex formationReceptor activationLigand-Independent Activation of the Platelet-Derived Growth Factor β Receptor: Requirements for Bovine Papillomavirus E5-Induced Mitogenic Signaling
Drummond-Barbosa D, Vaillancourt R, Kazlauskas A, DiMaio D. Ligand-Independent Activation of the Platelet-Derived Growth Factor β Receptor: Requirements for Bovine Papillomavirus E5-Induced Mitogenic Signaling. Molecular And Cellular Biology 1995, 15: 2570-2581. PMID: 7739538, PMCID: PMC230487, DOI: 10.1128/mcb.15.5.2570.Peer-Reviewed Original ResearchConceptsE5 proteinPDGF beta receptorTyrosine phosphorylationMitogenic signalsMitogenic signalingReceptor mutantsSH2 domain-containing proteinsPlatelet-derived growth factor beta receptorPDGF beta receptor tyrosine kinaseDomain-containing proteinsPhosphorylation of substratesInterleukin-3Tyrosine phosphorylation sitesGrowth factor β receptorBa/F3 cellsReceptor tyrosine phosphorylationGrowth factor beta receptorLigand-independent activationReceptor tyrosine kinasesTyrosine kinase activityBovine papillomavirus E5Beta receptorsComplex formationPhosphorylation sitesReceptor autophosphorylationAn intact PDGF signaling pathway is required for efficient growth transformation of mouse C127 cells by the bovine papillomavirus E5 protein.
Riese D, DiMaio D. An intact PDGF signaling pathway is required for efficient growth transformation of mouse C127 cells by the bovine papillomavirus E5 protein. Oncogene 1995, 10: 1431-9. PMID: 7731695.Peer-Reviewed Original ResearchConceptsBPV E5 proteinPDGF beta receptorE5 proteinE5 geneC127 cellsBovine papillomavirus E5 proteinPDGF beta-receptor genePlatelet-derived growth factor beta receptorGrowth transformationBovine papillomavirus type 1 E5 proteinC127 cell linesMembrane-associated proteinsMouse C127 cellsHeterologous cell typesV-sis oncogeneDNA synthesisGrowth factor beta receptorStable growth transformationBeta receptor geneCell linesBeta receptorsBPV E5Reduced DNA synthesisMouse C127Genetic support
1994
Unique profiles of the alpha 1-, alpha 2-, and beta-adrenergic receptors in the developing cortical plate and transient embryonic zones of the rhesus monkey
Lidow, Rakic P. Unique profiles of the alpha 1-, alpha 2-, and beta-adrenergic receptors in the developing cortical plate and transient embryonic zones of the rhesus monkey. Journal Of Neuroscience 1994, 14: 4064-4078. PMID: 8027763, PMCID: PMC6577033, DOI: 10.1523/jneurosci.14-07-04064.1994.Peer-Reviewed Original ResearchConceptsTransient embryonic zonesBeta-adrenergic receptorsCortical plateAdrenergic receptor subtypesSubplate zoneReceptor subtypesCerebral wallRhesus monkeysAlpha 1Alpha 1 sitesAlpha 2Alpha 2 receptorsAlpha 1 receptorsEmbryonic zonesIntensive proliferative activityReceptor autoradiographyCortical neuronsSubventricular zoneCortical developmentOccipital lobeBeta receptorsAdrenergic receptorsAdrenergic sitesVisual cortexGerminal zoneSpecific interaction between the bovine papillomavirus E5 transforming protein and the beta receptor for platelet-derived growth factor in stably transformed and acutely transfected cells
Petti L, DiMaio D. Specific interaction between the bovine papillomavirus E5 transforming protein and the beta receptor for platelet-derived growth factor in stably transformed and acutely transfected cells. Journal Of Virology 1994, 68: 3582-3592. PMID: 8189497, PMCID: PMC236862, DOI: 10.1128/jvi.68.6.3582-3592.1994.Peer-Reviewed Original ResearchConceptsPDGF beta receptorE5 proteinPlatelet-derived growth factorEGF receptorEpidermal growth factorGrowth factor receptorCOS cellsTumorigenic transformationBovine fibroblastsPDGF receptorHeterologous cell systemFactor receptorNIH 3T3 cellsGrowth factorBovine papillomavirus E5Beta receptorsMembrane proteinsTransient overexpressionRodent fibroblastsCell typesProteinBovine papillomavirusPotential targetSpecific interactionsEpithelial cells
1992
Stable association between the bovine papillomavirus E5 transforming protein and activated platelet-derived growth factor receptor in transformed mouse cells.
Petti L, DiMaio D. Stable association between the bovine papillomavirus E5 transforming protein and activated platelet-derived growth factor receptor in transformed mouse cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 6736-6740. PMID: 1323117, PMCID: PMC49578, DOI: 10.1073/pnas.89.15.6736.Peer-Reviewed Original ResearchConceptsE5 proteinPlatelet-derived growth factorGrowth factor receptor activationPDGF receptorMouse C127 cellsBovine papillomavirus E5Platelet-derived growth factor receptorShorter proteinTransforming proteinCoimmunoprecipitation analysisGrowth factor receptorReceptor transmitsStable associationC127 cellsTumorigenic transformationMouse cellsProteinBovine papillomavirusFactor receptorDistinct mechanismsStable complexesGrowth factorReceptor activationImportant targetBeta receptors
1990
A base mutation of the C-erbA beta thyroid hormone receptor in a kindred with generalized thyroid hormone resistance. Molecular heterogeneity in two other kindreds.
Usala S, Tennyson G, Bale A, Lash R, Gesundheit N, Wondisford F, Accili D, Hauser P, Weintraub B. A base mutation of the C-erbA beta thyroid hormone receptor in a kindred with generalized thyroid hormone resistance. Molecular heterogeneity in two other kindreds. Journal Of Clinical Investigation 1990, 85: 93-100. PMID: 2153155, PMCID: PMC296391, DOI: 10.1172/jci114438.Peer-Reviewed Original ResearchConceptsGeneralized thyroid hormone resistanceC-erbA betaThyroid hormone resistanceHormone resistanceBase substitutionsT3-binding domainC-erbA beta geneThyroid hormone receptor genesBeta thyroid hormone receptorThyroid hormone receptorC-erbA beta thyroid hormone receptorHormone receptor geneProline codonsGenomic DNAThyroid hormone actionAltered baseBeta cDNASecondary structureBeta geneNuclear receptorsBase mutationMaximum logarithmPosition 448Receptor geneBeta receptors
1989
The Characterization of Beta-Adrenergic Receptor Subtypes of the Upper and Lower Renal Pelvis in Rabbits
Kondo S, Latifpour J, Morita T, Weiss R. The Characterization of Beta-Adrenergic Receptor Subtypes of the Upper and Lower Renal Pelvis in Rabbits. Journal Of Urology 1989, 142: 1099-1101. PMID: 2571737, DOI: 10.1016/s0022-5347(17)39004-3.Peer-Reviewed Original ResearchConceptsBeta-adrenergic receptorsBeta 2 subtypeRenal pelvisRabbit renal pelvisLower pelvisSelective antagonistBeta-2 selective antagonistBeta-adrenergic receptor subtypesUpper renal pelvisBeta 2 receptorsRadioligand binding techniquesBeta-1 selective antagonistReceptor subtypesBeta receptorsPelvisBeta 1ReceptorsSubtypesICIBinding techniquesSaturation studiesSignificant differencesSites BmaxAntagonistGreater proportion
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