https://socictopen.socict.org/files/original/43055fe4722af8baae747e4c075edda5.pdf 7672a5246bca6d3f7097750becb5f7ed Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Coronavirus Description An account of the resource Dominio científico: Coronavirus Text A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text. Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Small molecule inhibitors of the SARS-CoV Nsp15 endoribonuclease Creator An entity primarily responsible for making the resource J Ortiz-Alcantara, K Bhardwaj, S Palaninathan, et al Description An account of the resource J Ortiz-Alcantara1, K Bhardwaj2, S Palaninathan1, M Frieman3, RS Baric3, CC Kao21Department of Biochemistry and Biophysics, Texas A&M University College Station, TX, USA; 2Department of Molecular Cellular Biochemistry, Indiana University, Bloomington IN, USA; 3Department of Epidemiology, School of Public Health, University of North Carolina at Chapel Hill, Chapel Hill, NC, USAAbstract: The severe acute respiratory syndrome (SARS) virus encodes several unusual RNA processing enzymes, including Nsp15, an endoribonuclease that preferentially cleaves 3’ of uridylates through a ribonuclease A (RNase A)-like mechanism. Crystal structures of Nsp15 confirmed that the Nsp15 active site is structurally similar to that of RNase A. These similarities and our molecular docking analysis lead us to hypothesize that previously characterized RNase A inhibitors will also inhibit the SARS-CoV Nsp15. Benzopurpurin B, C-467929, C-473872, N-306711, N-65828, N-103019 and congo red were tested for effects on Nsp15 endoribonuclease activity. A fluorescence assay revealed that the IC50 values for inhibiting endoribonuclease activity were between 0.2 µM and 40 µM. These compounds were demonstrated to bind SARS-CoV Nsp15 by a differential scanning fluorimetry assay. Benzopurpurin B also inhibited the endoribonuclease activities of the Nsp15 orthologs from two other coronaviruses: mouse hepatitis virus (MHV) and infectious bronchitis virus (IBV). Benzopurpurin B, C-473872, and congo red reduced infectivity of MHV in L2 cells by 8- to 26- fold. The more effective drugs caused a decrease in MHV RNA accumulation. All three compounds reduced the infectivity of the SARS-CoV in Vero cells.Keywords: SARS, endoribonuclease, small molecule inhibitors Date A point or period of time associated with an event in the lifecycle of the resource 2010 Identifier An unambiguous reference to the resource within a given context DOI: Source A related resource from which the described resource is derived Virus Adaptation and Treatment Publisher An entity responsible for making the resource available Dove Medical Press Coverage The spatial or temporal topic of the resource, the spatial applicability of the resource, or the jurisdiction under which the resource is relevant Microbiology Language A language of the resource EN