2023
The E3 ligase Riplet promotes RIG-I signaling independent of RIG-I oligomerization
Wang W, Götte B, Guo R, Pyle A. The E3 ligase Riplet promotes RIG-I signaling independent of RIG-I oligomerization. Nature Communications 2023, 14: 7308. PMID: 37951994, PMCID: PMC10640585, DOI: 10.1038/s41467-023-42982-0.Peer-Reviewed Original Research
2022
The RIG-I receptor adopts two different conformations for distinguishing host from viral RNA ligands
Wang W, Pyle AM. The RIG-I receptor adopts two different conformations for distinguishing host from viral RNA ligands. Molecular Cell 2022, 82: 4131-4144.e6. PMID: 36272408, PMCID: PMC9707737, DOI: 10.1016/j.molcel.2022.09.029.Peer-Reviewed Original ResearchMeSH KeywordsCarrier ProteinsDEAD Box Protein 58DEAD-box RNA HelicasesImmunity, InnateLigandsRNA, Double-StrandedRNA, ViralConceptsRNA moleculesRNA ligandsHigh-resolution cryo-EM structuresCryo-EM structureDouble-stranded RNARIG-I receptorInduction of autoimmunityViral RNA moleculesAutoinhibited conformationInnate immune receptorsHost RNARelated RNAProtein foldsMolecular basisUnique molecular featuresHigh-affinity conformationAntiviral sensingHost cellsRNA virusesRNA releaseImmune receptorsRNAViral RNAExquisite selectivityMolecular features
2021
The molecular mechanism of RIG‐I activation and signaling
Thoresen D, Wang W, Galls D, Guo R, Xu L, Pyle AM. The molecular mechanism of RIG‐I activation and signaling. Immunological Reviews 2021, 304: 154-168. PMID: 34514601, PMCID: PMC9293153, DOI: 10.1111/imr.13022.Peer-Reviewed Original ResearchMeSH KeywordsDEAD-box RNA HelicasesImmunity, InnateInterferon-Induced Helicase, IFIH1RNA, Double-StrandedRNA, ViralSignal TransductionConceptsRIG-I activationTranscription of interferonEvolutionary implicationsAdapter proteinHost RNAPathogenic RNAsPattern recognition receptorsCell biologyInactive conformationMolecular mechanismsRNA virusesRole of RIGRNA duplexesInitial RNARNAStructural determinantsRecognition receptorsInnate immunityViral RNAInterferon expressionImportant receptorViral pathogensCellular spaceMolecular featuresReceptorsInsights 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
2019
RIG-I Recognition of RNA Targets: The Influence of Terminal Base Pair Sequence and Overhangs on Affinity and Signaling
Ren X, Linehan MM, Iwasaki A, Pyle AM. RIG-I Recognition of RNA Targets: The Influence of Terminal Base Pair Sequence and Overhangs on Affinity and Signaling. Cell Reports 2019, 29: 3807-3815.e3. PMID: 31851914, DOI: 10.1016/j.celrep.2019.11.052.Peer-Reviewed Original ResearchConceptsRNA moleculesRIG-I activationBase pair sequenceHost RNA moleculesViral RNA moleculesRIG-I recognitionMolecular basisRNA variantsRNA targetsPair sequenceHuman cellsBase pairsImmune receptorsMechanisms of evasionTerminal base pairsLigand affinityWhole animalInterferon responseDeadly pathogenRNA therapeuticsMarburg virusCellsOverhangMoleculesSignaling
2004
Backbone tracking by the SF2 helicase NPH-II
Kawaoka J, Jankowsky E, Pyle AM. Backbone tracking by the SF2 helicase NPH-II. Nature Structural & Molecular Biology 2004, 11: 526-530. PMID: 15146171, DOI: 10.1038/nsmb771.Peer-Reviewed Original Research
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