2024
Gastrodenol suppresses NLRP3/GSDMD mediated pyroptosis and ameliorates inflammatory diseases
Chen P, Wang Y, Tang H, Liu Z, Wang J, Wang T, Xu Y, Ji S. Gastrodenol suppresses NLRP3/GSDMD mediated pyroptosis and ameliorates inflammatory diseases. Cellular Immunology 2024, 405: 104888. PMID: 39486308, DOI: 10.1016/j.cellimm.2024.104888.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCytokinesEncephalomyelitis, Autoimmune, ExperimentalFemaleGasderminsHumansInflammasomesInflammationIntracellular Signaling Peptides and ProteinsLipopolysaccharidesMacrophagesMiceMice, Inbred C57BLNLR Family, Pyrin Domain-Containing 3 ProteinPeritonitisPhosphate-Binding ProteinsPyroptosisConceptsNucleotide-binding oligomerization domain-like receptor family pyrin domain-containing protein 3Caspase activationRecruitment domainNLRP3 oligomerizationPyrin domain-containing protein 3Gasdermin D (GSDMD)-mediated pyroptosisProtein 3PyroptosisSecretion of pro-inflammatory cytokinesOligomerizationHydrogen bondsApoptosis-associated speck like proteinInflammatory diseasesTherapeutic strategiesHelicobacter pyloriPro-inflammatory cytokinesCaspaseExperimental autoimmune encephalomyelitisLipopolysaccharide (LPS)-inducedProteinGasdermin
2021
Insights into the structure and RNA-binding specificity of Caenorhabditis elegans Dicer-related helicase 3 (DRH-3)
Li K, Zheng J, Wirawan M, Trinh NM, Fedorova O, Griffin PR, Pyle AM, Luo D. Insights into the structure and RNA-binding specificity of Caenorhabditis elegans Dicer-related helicase 3 (DRH-3). Nucleic Acids Research 2021, 49: 9978-9991. PMID: 34403472, PMCID: PMC8464030, DOI: 10.1093/nar/gkab712.Peer-Reviewed Original ResearchConceptsC-terminal domainN-terminal domainDRH-3RNA interferenceTandem caspase activationSimilar domain architectureEndogenous RNAi pathwaysRNA helicase familyDouble-stranded RNACARDs of RIGUnique structural dynamicsGermline developmentEvolutionary divergenceChromosome segregationRNAi pathwayCaenorhabditis elegansDomain architectureHelicase familyCaspase activationDistinct foldsRecruitment domainMolecular understandingRLR familyRNA duplexesRNA
2018
HDX-MS reveals dysregulated checkpoints that compromise discrimination against self RNA during RIG-I mediated autoimmunity
Zheng J, Wang C, Chang M, Devarkar S, Schweibenz B, Crynen G, Garcia-Ordonez R, Pascal B, Novick S, Patel S, Marcotrigiano J, Griffin P. HDX-MS reveals dysregulated checkpoints that compromise discrimination against self RNA during RIG-I mediated autoimmunity. Nature Communications 2018, 9: 5366. PMID: 30560918, PMCID: PMC6299088, DOI: 10.1038/s41467-018-07780-z.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAutoimmunityCaspase Activation and Recruitment DomainDEAD Box Protein 58Deuterium Exchange MeasurementGain of Function MutationGuanosineImmunity, InnateInterferon-Induced Helicase, IFIH1Mass SpectrometryMethylationModels, MolecularMutagenesis, Site-DirectedProtein BindingReceptors, ImmunologicRecombinant ProteinsRNA CapsRNA, Double-StrandedRNA, ViralSignal Transduction
2009
Bacterial proteins as potential drugs in the treatment of leukemia
Kwan JM, Fialho AM, Kundu M, Thomas J, Hong CS, Gupta T, Chakrabarty AM. Bacterial proteins as potential drugs in the treatment of leukemia. Leukemia Research 2009, 33: 1392-1399. PMID: 19250673, DOI: 10.1016/j.leukres.2009.01.024.Peer-Reviewed Original ResearchConceptsBacterial proteinsSerine/threonine kinaseLeukemia cell linesCaspase recruitment domainCell linesAkt-Ser-473Cell cycle arrestG2/M phaseThreonine kinaseLike domainCARD domainRecruitment domainProtein stabilizationCycle arrestM phaseHL60 cellsProteinActive formPeripheral blood mononuclear cellsBlood mononuclear cellsLeukemia cellsCancer typesAzurinCytotoxic effectsTreatment of leukemia
2002
mda-5: An interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties
Kang DC, Gopalkrishnan RV, Wu Q, Jankowsky E, Pyle AM, Fisher PB. mda-5: An interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties. Proceedings Of The National Academy Of Sciences Of The United States Of America 2002, 99: 637-642. PMID: 11805321, PMCID: PMC117358, DOI: 10.1073/pnas.022637199.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid SequenceAnimalsApoptosisCell DifferentiationCell DivisionCloning, MolecularDEAD-box RNA HelicasesDNA, ComplementaryGrowth InhibitorsHumansInterferon Type IInterferon-Induced Helicase, IFIH1MelanomaMolecular Sequence DataRecombinant ProteinsRNA HelicasesRNA, Double-StrandedSequence Homology, Amino AcidTumor Cells, CulturedTumor Stem Cell AssayConceptsRNA-dependent ATPase activityCaspase recruitment domainHelicase motifsHuman melanoma cellsRecruitment domainRNA helicase motifsRNA-dependent ATPaseMDA-5RNA helicase domainPutative RNA helicaseMelanoma cellsEarly response genesATPase activityProtein kinase C activationGrowth-suppressive propertiesMelanoma differentiation-associated gene 5Appropriate pharmacological manipulationKinase C activationHypothetical proteinsRNA helicaseHelicase domainDifferentiation-associated gene 5Mediator of IFNSubtraction hybridizationMda-5 expression
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