2008
Vascular 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 cascadeCell signalingC-SrcN-terminusHuman endothelial cellsRapid activationMolecular studiesConsequent activationVascular cellsNumerous animalsNitric oxideMultiple biological effectsEstrogen receptor alphaFavorable estrogenic effectsER46
2003
Plasma membrane localization and function of the estrogen receptor α variant (ER46) in human endothelial cells
Li L, Haynes MP, Bender JR. Plasma membrane localization and function of the estrogen receptor α variant (ER46) in human endothelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 4807-4812. PMID: 12682286, PMCID: PMC153637, DOI: 10.1073/pnas.0831079100.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAnimalsBase SequenceCell LineCell MembraneCOS CellsEndothelium, VascularEstrogen Receptor alphaGenes, ReporterGenetic VariationHumansNitric Oxide SynthaseNitric Oxide Synthase Type IIIProtein Processing, Post-TranslationalReceptors, EstrogenRecombinant ProteinsRNA, MessengerSubcellular FractionsTranscriptional ActivationTransfectionConceptsPlasma membranePalmitoylation-dependent mannerPlasma membrane localizationInhibition of palmitoylationFull-length ER alphaReporter gene transactivationCOS-7 cellsEndothelial cell proteinsMembrane localizationAlternative splicingEstrogen receptor α variantsOestrogen receptor-alpha variantsN-terminusHuman endothelial cellsCell proteinsER46Synthase pathwayAcid labelingHy926 cellsNonendothelial cellsENOS activationENOS phosphorylationCellsEndothelial cellsMembrane
1999
A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2
Liu Y, Pan J, Zhang C, Fan W, Collinge M, Bender J, Weissman S. A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 4313-4318. PMID: 10200259, PMCID: PMC16329, DOI: 10.1073/pnas.96.8.4313.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceB-LymphocytesCalcium-Binding ProteinsCarrier ProteinsCell Cycle ProteinsCell LineChromosomes, Artificial, YeastCOS CellsGenes, MHC Class IHL-60 CellsHumansJurkat CellsMad2 ProteinsMolecular Sequence DataPolymerase Chain ReactionRepressor ProteinsSequence AlignmentSequence Homology, Amino AcidT-LymphocytesTransfectionTumor Cells, CulturedUbiquitinsConceptsSpindle assembly checkpoint protein Mad2Two-hybrid screeningCheckpoint protein Mad2Ubiquitin-like proteinHuman MHC class I regionCell cycle checkpointsMHC class I regionSpindle assemblyI geneProtein stabilityCell developmentDendritic cell developmentClass I regionImmunoprecipitation studiesCell growthMad2Gamma-interferon inductionProteinProtein expressionFAT10I regionCellsLymphoblastoid linesAnaphaseTranscription