Euisoon Park
Associate Research ScientistCards
About
Research
Publications
2024
Corrigendum to 'Strenuous expression of porcine epidemic diarrhea virus ORF3 protein suggests host resistance' [Vet. Microbiol., Vol. 297, Oct. 2024, 110193]
Kamau A, Yu J, Park E, Rho J, Hong E, Shin H. Corrigendum to 'Strenuous expression of porcine epidemic diarrhea virus ORF3 protein suggests host resistance' [Vet. Microbiol., Vol. 297, Oct. 2024, 110193]. Veterinary Microbiology 2024, 110253. PMID: 39289106, DOI: 10.1016/j.vetmic.2024.110253.Peer-Reviewed Original ResearchNative architecture of a human GBP1 defense complex for cell-autonomous immunity to infection
Zhu S, Bradfield C, Maminska A, Park E, Kim B, Kumar P, Huang S, Kim M, Zhang Y, Bewersdorf J, MacMicking J. Native architecture of a human GBP1 defense complex for cell-autonomous immunity to infection. Science 2024, 383: eabm9903. PMID: 38422126, DOI: 10.1126/science.abm9903.Peer-Reviewed Original ResearchConceptsGuanylate-binding proteinsCaspase-4Surface of Gram-negative bacteriaGuanosine triphosphate hydrolysisImmunity to infectionInnate immunity to infectionCryo-electron tomographyGram-negative bacteriaImmunity proteinSignaling platformsMembrane insertionHuman cellsNative structureCombat infectionsLipopolysaccharide releaseGasdermin DExtended conformationLiving organismsProteinDefense complexCellsNative architectureGBP1BacteriaInfection
2023
PLSCR1 is a cell-autonomous defence factor against SARS-CoV-2 infection
Xu D, Jiang W, Wu L, Gaudet R, Park E, Su M, Cheppali S, Cheemarla N, Kumar P, Uchil P, Grover J, Foxman E, Brown C, Stansfeld P, Bewersdorf J, Mothes W, Karatekin E, Wilen C, MacMicking J. PLSCR1 is a cell-autonomous defence factor against SARS-CoV-2 infection. Nature 2023, 619: 819-827. PMID: 37438530, PMCID: PMC10371867, DOI: 10.1038/s41586-023-06322-y.Peer-Reviewed Original ResearchConceptsC-terminal β-barrel domainSpike-mediated fusionCell-autonomous defenseLarge-scale exome sequencingΒ-barrel domainGenome-wide CRISPRSARS-CoV-2 infectionHost cell cytosolScramblase activityPhospholipid scramblaseLive SARS-CoV-2 infectionHuman lung epitheliumPLSCR1SARS-CoV-2 USASingle-molecule switchingSARS-CoV-2 variantsExome sequencingHuman populationRestriction factorsViral RNANew SARS-CoV-2 variantsSARS-CoV-2Robust activityLung epitheliumDefense factorsTDAG51 promotes transcription factor FoxO1 activity during LPS‐induced inflammatory responses
Park E, Jeon H, Lee N, Yu J, Park H, Satoh T, Akira S, Furuyama T, Lee C, Choi J, Rho J. TDAG51 promotes transcription factor FoxO1 activity during LPS‐induced inflammatory responses. The EMBO Journal 2023, 42: e111867. PMID: 37203866, PMCID: PMC10308371, DOI: 10.15252/embj.2022111867.Peer-Reviewed Original ResearchConceptsBone marrow-derived macrophagesInflammatory mediator productionInflammatory responseMediator productionTranscription factor FOXO1Lethal shockLPS-induced inflammatory responseSerum proinflammatory cytokine levelsToll-like receptor (TLR)-mediated inflammatory responsesFoxO1 activitySystemic inflammatory responseProinflammatory cytokine levelsMarrow-derived macrophagesTLR2/4 signaling pathwayFoxO1 nuclear accumulationT cellsCytokine levelsLipopolysaccharide (LPS)-induced inflammatory responsesTDAG51 deficiencyDouble deficiencyLPS-induced inflammatory mediator productionLPS stimulationInnate immunityCytoplasmic translocationLPS
2021
Selenoprotein W ensures physiological bone remodeling by preventing hyperactivity of osteoclasts
Kim H, Lee K, Kim J, Kim M, Kim J, Lee H, Chung Y, Shin H, Kim T, Park E, Rho J, Lee S, Kim N, Lee S, Choi Y, Jeong D. Selenoprotein W ensures physiological bone remodeling by preventing hyperactivity of osteoclasts. Nature Communications 2021, 12: 2258. PMID: 33859201, PMCID: PMC8050258, DOI: 10.1038/s41467-021-22565-7.Peer-Reviewed Original ResearchConceptsSelenoprotein WCell-cell fusionRNA sequencing analysisProfile of receptor activationOsteoclast differentiationNuclear factor of activated T cells cytoplasmic 1Bone remodelingBone mass phenotypeOsteoclastogenesis in vitroNuclear translocation of NF-kBTranslocation of NF-kBPhysiological bone remodelingBlocks osteoporosisNuclear translocationNuclear factorOsteoclastogenic genesMechanism of actionMass phenotypeBone metabolismBone resorptionReceptor activationOsteoclast maturationCytoplasmic 1Osteoclast formationNF-kB
2020
T-Cell Death-Associated Gene 51 Is a Novel Negative Regulator of PPARγ That Inhibits PPARγ-RXRα Heterodimer Formation in Adipogenesis
Kim S, Lee N, Park E, Yun H, Ha T, Jeon H, Yu J, Choi S, Shin B, Yu J, Dal Rhee S, Choi Y, Rho J. T-Cell Death-Associated Gene 51 Is a Novel Negative Regulator of PPARγ That Inhibits PPARγ-RXRα Heterodimer Formation in Adipogenesis. Molecules And Cells 2020, 44: 1-12. PMID: 33335079, PMCID: PMC7854182, DOI: 10.14348/molcells.2020.0143.Peer-Reviewed Original ResearchConceptsLigand-independent mannerRepeat domainRetinoid X receptorBinding domainNegative regulatorHeterodimer formationEarly stage of adipogenic differentiationActivation function-2 domainPleckstrin homology-likeT-cell death-associated geneDNA-binding domainDeletion mutant analysisDeath-associated genesStage of adipogenic differentiationLigand-binding domainMutant analysisGlutamine repeatsCell fateTranscriptional activityPeroxisome proliferator-activated receptor gTDAG51 expressionAdipocyte differentiationHeterodimer complexTDAG51Adipogenic cell fateGuanylate-binding proteins convert cytosolic bacteria into caspase-4 signaling platforms
Wandel MP, Kim BH, Park ES, Boyle KB, Nayak K, Lagrange B, Herod A, Henry T, Zilbauer M, Rohde J, MacMicking JD, Randow F. Guanylate-binding proteins convert cytosolic bacteria into caspase-4 signaling platforms. Nature Immunology 2020, 21: 880-891. PMID: 32541830, PMCID: PMC7381384, DOI: 10.1038/s41590-020-0697-2.Peer-Reviewed Original ResearchConceptsGuanylate-binding proteinsCaspase-4 activationCaspase-4Human caspase-4Pyroptotic cell deathGram-negative bacteriaCytosolic bacteriaReplicative nicheEvolutionary evidenceIntracellular bacteriaCell deathMultiple antagonistsNeighboring cellsCaspase-11BacteriaAntibacterial defenseBacterial challengeGasderminShigella flexneriProteinDependent pyroptosisActivationPathwayBacterial lipopolysaccharideGBP2
2019
TDAG51 is a crucial regulator of maternal care and depressive-like behavior after parturition
Yun H, Park E, Choi S, Shin B, Yu J, Yu J, Amarasekara D, Kim S, Lee N, Choi J, Choi Y, Rho J. TDAG51 is a crucial regulator of maternal care and depressive-like behavior after parturition. PLOS Genetics 2019, 15: e1008214. PMID: 31251738, PMCID: PMC6599150, DOI: 10.1371/journal.pgen.1008214.Peer-Reviewed Original ResearchConceptsDepressive-like behaviorPostpartum depressionDevelopment of postpartum depressionImpaired maternal behaviorRegulation of maternal careMonoamine neurotransmitter levelsCombination of physical changesNest-building testInfluence of genetic risk factorsTDAG51 deficiencyMaternity careGenetic risk factorsPup retrievalMental disordersPsychiatric illnessNeurotransmitter levelsMaternal behaviorPostpartumRisk factorsDepressionBuilding testsT-cell death-associated geneDeath-associated genesNursesCareInterferon-induced guanylate-binding proteins: Guardians of host defense in health and disease
Tretina K, Park ES, Maminska A, MacMicking JD. Interferon-induced guanylate-binding proteins: Guardians of host defense in health and disease. Journal Of Experimental Medicine 2019, 216: 482-500. PMID: 30755454, PMCID: PMC6400534, DOI: 10.1084/jem.20182031.Peer-Reviewed Original ResearchConceptsGuanylate-binding proteinsNumerous host cell typesHost cell typesImportant human diseasesCritical rheostatBasic biologyMicrobial pathogensHost defense activitiesHuman diseasesSimilar functionsCell typesHomeostatic settingsGTPasesInnate immunityDefense activitiesHost defenseInflammatory syndromeNeoplastic diseaseClinical approachTissue damageBacterial infectionsCentral orchestratorDiseaseIFNRheostat
2016
Porcine amino peptidase N domain VII has critical role in binding and entry of porcine epidemic diarrhea virus
Kamau A, Park J, Park E, Yu J, Rho J, Shin H. Porcine amino peptidase N domain VII has critical role in binding and entry of porcine epidemic diarrhea virus. Virus Research 2016, 227: 150-157. PMID: 27732876, PMCID: PMC7114530, DOI: 10.1016/j.virusres.2016.10.004.Peer-Reviewed Original ResearchConceptsPorcine aminopeptidase NPorcine epidemic diarrhea virusNIH3T3 cellsDomain VIIDiarrhea virusPorcine epidemic diarrhea virus infectionDeletion mutantsMutantsEnteric diseaseDomain IIIIntestinal cellsVero cellsAminopeptidase NTime course testIndirect plaquesTherapeutic developmentCellsBindingPorcineVirus