Featured Publications
FADD regulates NF-κB activation and promotes ubiquitination of cFLIPL to induce apoptosis
Ranjan K, Pathak C. FADD regulates NF-κB activation and promotes ubiquitination of cFLIPL to induce apoptosis. Scientific Reports 2016, 6: 22787. PMID: 26972597, PMCID: PMC4789601, DOI: 10.1038/srep22787.Peer-Reviewed Original ResearchMeSH KeywordsA549 CellsAnimalsApoptosisBaculoviral IAP Repeat-Containing 3 ProteinBlotting, WesternCASP8 and FADD-Like Apoptosis Regulating ProteinCaspase 8Cell LineCell SurvivalFas-Associated Death Domain ProteinHCT116 CellsHEK293 CellsHeLa CellsHT29 CellsHumansInhibitor of Apoptosis ProteinsMCF-7 CellsMiceNF-kappa BNIH 3T3 CellsProtein BindingRepressor ProteinsRNA InterferenceTumor Necrosis Factor-alphaUbiquitinationUbiquitin-Protein LigasesConceptsCell deathProcaspase-8Molecular mechanismsCellular FLICE-like inhibitory proteinFLICE-like inhibitory proteinExpression of cFLIPLCell death signalingApoptosis protein 2Apoptotic cell death signalingHEK 293T cellsNovel molecular mechanismApoptotic cell deathNF-κB activationFasL stimulationCellular inhibitorE3 ubiquitinTNF-α stimulationDeath domainDeath inducingDeath signalingEctopic expressionFADDCaspase-8NF-κBCell survival
2020
Cell-Penetrable Peptide-Conjugated FADD Induces Apoptosis and Regulates Inflammatory Signaling in Cancer Cells
Ranjan K, Waghela BN, Vaidya FU, Pathak C. Cell-Penetrable Peptide-Conjugated FADD Induces Apoptosis and Regulates Inflammatory Signaling in Cancer Cells. International Journal Of Molecular Sciences 2020, 21: 6890. PMID: 32961826, PMCID: PMC7555701, DOI: 10.3390/ijms21186890.Peer-Reviewed Original ResearchConceptsFADD proteinCancer cellsAnti-apoptotic genesCaveolar pathwayDeath domainCellular pathwaysCancer cell proliferationCytosolic expressionFADD expressionCell deathApoptosis inducersInduces ApoptosisExpression of FasProteinCell proliferationApoptosisNF-κB activationSimultaneous regulationInflammatory signalingExpressionCellsNLRP3 inflammasome primingRegulationPathwayInflammasome priming
2016
Expression of cFLIPL Determines the Basal Interaction of Bcl‐2 With Beclin‐1 and Regulates p53 Dependent Ubiquitination of Beclin‐1 During Autophagic Stress
Ranjan K, Pathak C. Expression of cFLIPL Determines the Basal Interaction of Bcl‐2 With Beclin‐1 and Regulates p53 Dependent Ubiquitination of Beclin‐1 During Autophagic Stress. Journal Of Cellular Biochemistry 2016, 117: 1757-1768. PMID: 26682748, DOI: 10.1002/jcb.25474.Peer-Reviewed Original ResearchConceptsAutophagic stressDependent ubiquitinationBeclin-1Bcl-2Cell deathExpression of cFLIPLCo-immunoprecipitation analysisRegulation of autophagyHEK 293T cellsDifferent physiological processesAnti-apoptotic proteinsCellular homeostasisCellular stressEctopic expressionKnockdown cellsJNK1 activationCanonical interactionsProtein HMGB1Physiological processesBasal interactionCFLIPLSelective knockdownUbiquitinationAutophagyH2 O2