2020
Guanylate-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
2013
TDAG51 deficiency promotes oxidative stress-induced apoptosis through the generation of reactive oxygen species in mouse embryonic fibroblasts
Park E, Kim J, Ha T, Choi J, Soo Hong K, Rho J. TDAG51 deficiency promotes oxidative stress-induced apoptosis through the generation of reactive oxygen species in mouse embryonic fibroblasts. Experimental & Molecular Medicine 2013, 45: e35-e35. PMID: 23928855, PMCID: PMC3789259, DOI: 10.1038/emm.2013.67.Peer-Reviewed Original ResearchConceptsMouse embryonic fibroblastsApoptotic cell deathCell deathOxidative stress-induced apoptotic cell deathReactive oxygen speciesPleckstrin homology-like domain familyPromotes oxidative stress-induced apoptosisActivation of caspase-3Stress responseStress-induced cell deathT-cell death-associated genePro-apoptotic functionOxidative stress-induced cell deathOxidative stress-induced apoptosisTDAG51 deficiencyDeath-associated genesStress-induced apoptosisReceptor-mediated cell deathPro-apoptotic genesResponse to oxidative stressCellular stress responseEndoplasmic reticulum stressOxygen speciesProduction of intracellular reactive oxygen speciesIntracellular reactive oxygen species
2007
Early embryonic lethality caused by targeted disruption of the TRAF-interacting protein (TRIP) gene
Park E, Choi S, Kim J, Jeong Y, Choe J, Park C, Choi Y, Rho J. Early embryonic lethality caused by targeted disruption of the TRAF-interacting protein (TRIP) gene. Biochemical And Biophysical Research Communications 2007, 363: 971-977. PMID: 17927961, DOI: 10.1016/j.bbrc.2007.09.103.Peer-Reviewed Original ResearchConceptsTumor necrosis factor receptor (TNFR)-associated factorsTRAF-interacting proteinCylindromatosis tumor suppressor geneFamilial cylindromatosis tumour suppressor geneHomozygous mouse embryosComplex in vitroEarly embryonic lethalityTumor suppressor geneExcessive cell deathNF-kappaB signalingAdaptor moleculeEmbryonic lethalityProliferation defectEmbryonic development in vivoSignaling in vitroSuppressor geneSignaling cascadesCell deathActivity in vitroDevelopment in vivoTargeted disruptionNF-kappaB activation in vitroFunctional roleCell proliferationMouse embryos