2022
Structural Insights into Binding of Remdesivir Triphosphate within the Replication–Transcription Complex of SARS-CoV‑2
Wang J, Shi Y, Reiss K, Maschietto F, Lolis E, Konigsberg WH, Lisi GP, Batista VS. Structural Insights into Binding of Remdesivir Triphosphate within the Replication–Transcription Complex of SARS-CoV‑2. Biochemistry 2022, 61: 1966-1973. PMID: 36044776, PMCID: PMC9469760, DOI: 10.1021/acs.biochem.2c00341.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine MonophosphateAdenosine TriphosphateAlanineAntiviral AgentsCoronavirus RNA-Dependent RNA PolymeraseCOVID-19 Drug TreatmentDeoxyribonucleotidesHydrogenNucleotidesRibonucleotidesRNA, ViralSARS-CoV-2ConceptsReplication-transcription complexStructural basisCryo-EM structureAdenosine monophosphateRemdesivir triphosphateStructural insightsDuplex productsPrimer extensionNucleotide selectivityBase pairsNucleotide incorporationIncoming substrateRibosyl moietyActive complexSARS-CoV-2 inhibitorsNew detailed informationTriphosphateComplexesMolecular dynamics simulationsAdenosine triphosphate
2021
Mechanism of Inhibition of the Reproduction of SARS-CoV‑2 and Ebola Viruses by Remdesivir
Wang J, Reiss K, Shi Y, Lolis E, Lisi GP, Batista VS. Mechanism of Inhibition of the Reproduction of SARS-CoV‑2 and Ebola Viruses by Remdesivir. Biochemistry 2021, 60: 1869-1875. PMID: 34110129, PMCID: PMC8204756, DOI: 10.1021/acs.biochem.1c00292.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine MonophosphateAlanineAntiviral AgentsBase PairingCoronavirus RNA-Dependent RNA PolymeraseEbolavirusEnzyme InhibitorsModels, MolecularProtein BiosynthesisRNARNA, MessengerRNA, ViralSARS-CoV-2Virus Replication