2024
Covalent Polymer‐RNA Conjugates for Potent Activation of the RIG‐I Pathway
Palmer C, Pastora L, Kimmel B, Pagendarm H, Kwiatkowski A, Stone P, Arora K, Francini N, Fedorova O, Pyle A, Wilson J. Covalent Polymer‐RNA Conjugates for Potent Activation of the RIG‐I Pathway. Advanced Healthcare Materials 2024, e2303815. PMID: 38648653, PMCID: PMC11493851, DOI: 10.1002/adhm.202303815.Peer-Reviewed Original ResearchChemical design principlesActivation of RIG-I.Retinoic acid-inducible gene ICovalent conjugationRIG-I pathwayNuclease degradationThioether linkageRIG-I.Gene IRNA ligandsElectrostatic interactionsRIG-IDevelopment of therapeuticsPotent activityOligonucleotide therapeuticsNucleaseRNAAnalog carrierNanoparticlesDrug delivery barriersConjugatePolymeric carriersImmunostimulatory activityThioethersIn vivo delivery
2014
The RIG-I ATPase core has evolved a functional requirement for allosteric stabilization by the Pincer domain
Rawling DC, Kohlway AS, Luo D, Ding SC, Pyle AM. The RIG-I ATPase core has evolved a functional requirement for allosteric stabilization by the Pincer domain. Nucleic Acids Research 2014, 42: 11601-11611. PMID: 25217590, PMCID: PMC4191399, DOI: 10.1093/nar/gku817.Peer-Reviewed Original ResearchConceptsATPase coreRetinoic acid-inducible gene IAcid-inducible gene INon-self RNASeries of mutationsActivity of RIGMetazoan cellsHelicase coreAllosteric controlTerminal domainPattern recognition receptorsAlpha-helixBiophysical analysisGene IAllosteric stabilizationType I interferonEnzymatic activityRecognition receptorsViral RNAStructural studiesRNAI interferonAdjacent domainsDomainImportant role