{"external_id":{"pmid":["33631104"]},"type":"journal_article","citation":{"ieee":"J. P. K. Bravo, T. L. Dangerfield, D. W. Taylor, and K. A. Johnson, “Remdesivir is a delayed translocation inhibitor of SARS-CoV-2 replication,” Molecular Cell, vol. 81, no. 7. Elsevier, p. 1548–1552.e4, 2021.","ista":"Bravo JPK, Dangerfield TL, Taylor DW, Johnson KA. 2021. Remdesivir is a delayed translocation inhibitor of SARS-CoV-2 replication. Molecular Cell. 81(7), 1548–1552.e4.","chicago":"Bravo, Jack Peter Kelly, Tyler L. Dangerfield, David W. Taylor, and Kenneth A. Johnson. “Remdesivir Is a Delayed Translocation Inhibitor of SARS-CoV-2 Replication.” Molecular Cell. Elsevier, 2021. https://doi.org/10.1016/j.molcel.2021.01.035.","short":"J.P.K. Bravo, T.L. Dangerfield, D.W. Taylor, K.A. Johnson, Molecular Cell 81 (2021) 1548–1552.e4.","ama":"Bravo JPK, Dangerfield TL, Taylor DW, Johnson KA. Remdesivir is a delayed translocation inhibitor of SARS-CoV-2 replication. Molecular Cell. 2021;81(7):1548-1552.e4. doi:10.1016/j.molcel.2021.01.035","apa":"Bravo, J. P. K., Dangerfield, T. L., Taylor, D. W., & Johnson, K. A. (2021). Remdesivir is a delayed translocation inhibitor of SARS-CoV-2 replication. Molecular Cell. Elsevier. https://doi.org/10.1016/j.molcel.2021.01.035","mla":"Bravo, Jack Peter Kelly, et al. “Remdesivir Is a Delayed Translocation Inhibitor of SARS-CoV-2 Replication.” Molecular Cell, vol. 81, no. 7, Elsevier, 2021, p. 1548–1552.e4, doi:10.1016/j.molcel.2021.01.035."},"main_file_link":[{"url":"https://doi.org/10.1101/2020.12.14.422718 ","open_access":"1"}],"pmid":1,"_id":"15140","month":"04","issue":"7","day":"01","keyword":["Cell Biology","Molecular Biology"],"article_processing_charge":"No","publication_identifier":{"issn":["1097-2765"]},"title":"Remdesivir is a delayed translocation inhibitor of SARS-CoV-2 replication","volume":81,"scopus_import":"1","status":"public","author":[{"last_name":"Bravo","orcid":"0000-0003-0456-0753","full_name":"Bravo, Jack Peter Kelly","first_name":"Jack Peter Kelly","id":"96aecfa5-8931-11ee-af30-aa6a5d6eee0e"},{"last_name":"Dangerfield","full_name":"Dangerfield, Tyler L.","first_name":"Tyler L."},{"last_name":"Taylor","first_name":"David W.","full_name":"Taylor, David W."},{"last_name":"Johnson","first_name":"Kenneth A.","full_name":"Johnson, Kenneth A."}],"oa":1,"quality_controlled":"1","doi":"10.1016/j.molcel.2021.01.035","date_created":"2024-03-20T10:42:53Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2021","abstract":[{"lang":"eng","text":"Remdesivir is a nucleoside analog approved by the US FDA for treatment of COVID-19. Here, we present a 3.9-Å-resolution cryo-EM reconstruction of a remdesivir-stalled RNA-dependent RNA polymerase complex, revealing full incorporation of 3 copies of remdesivir monophosphate (RMP) and a partially incorporated fourth RMP in the active site. The structure reveals that RMP blocks RNA translocation after incorporation of 3 bases following RMP, resulting in delayed chain termination, which can guide the rational design of improved antiviral drugs."}],"page":"1548-1552.e4","publication":"Molecular Cell","publisher":"Elsevier","article_type":"original","date_published":"2021-04-01T00:00:00Z","date_updated":"2024-06-04T06:00:56Z","oa_version":"Preprint","intvolume":" 81","extern":"1","publication_status":"published","language":[{"iso":"eng"}]}