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
2021
Noncoding RNAs: biology and applications—a Keystone Symposia report
Cable J, Heard E, Hirose T, Prasanth KV, Chen L, Henninger JE, Quinodoz SA, Spector DL, Diermeier SD, Porman AM, Kumar D, Feinberg MW, Shen X, Unfried JP, Johnson R, Chen C, Wilusz JE, Lempradl A, McGeary SE, Wahba L, Pyle AM, Hargrove AE, Simon MD, Marcia M, Przanowska RK, Chang HY, Jaffrey SR, Contreras LM, Chen Q, Shi J, Mendell JT, He L, Song E, Rinn JL, Lalwani MK, Kalem MC, Chuong EB, Maquat LE, Liu X. Noncoding RNAs: biology and applications—a Keystone Symposia report. Annals Of The New York Academy Of Sciences 2021, 1506: 118-141. PMID: 34791665, PMCID: PMC9808899, DOI: 10.1111/nyas.14713.Peer-Reviewed Original ResearchConceptsPIWI-interacting RNAsKeystone Symposia reportPotential drug targetsRNA biologyHuman transcriptomeEpigenetic modificationsKeystone eSymposiumNoncoding RNAsCell signalingBasic biologyDrug targetsRNABiologyDisease mechanismsNucleotidesSpeciesTranscriptomeImportant roleRNAsTranscriptionSymposium reportSignalingTranslationRoleTargetThe 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 featuresReceptors
2020
Small-Molecule Antagonists of the RIG‑I Innate Immune Receptor
Rawling DC, Jagdmann GE, Potapova O, Pyle AM. Small-Molecule Antagonists of the RIG‑I Innate Immune Receptor. ACS Chemical Biology 2020, 15: 311-317. PMID: 31944652, DOI: 10.1021/acschembio.9b00810.Peer-Reviewed Original ResearchConceptsInnate immune systemRIG-I receptorRole of RIGSmall molecule antagonistsPotent RIGAutoimmune disordersAntimicrobial therapyRange of diseasesImmune systemInterferon responseVertebrate innate immune systemImmune receptorsReceptorsNew drug design strategiesAntagonistRNA virusesDrug design strategiesCOPD
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 virusCellsOverhangMoleculesSignalingRNA binding activates RIG-I by releasing an autorepressed signaling domain
Dickey TH, Song B, Pyle AM. RNA binding activates RIG-I by releasing an autorepressed signaling domain. Science Advances 2019, 5: eaax3641. PMID: 31616790, PMCID: PMC6774723, DOI: 10.1126/sciadv.aax3641.Peer-Reviewed Original Research
2013
Parts, assembly and operation of the RIG-I family of motors
Rawling DC, Pyle AM. Parts, assembly and operation of the RIG-I family of motors. Current Opinion In Structural Biology 2013, 25: 25-33. PMID: 24878341, PMCID: PMC4070197, DOI: 10.1016/j.sbi.2013.11.011.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsDEAD-box RNA HelicasesHumansMolecular Motor ProteinsRNA, ViralSignal Transduction