<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>289</volume><submitter>Choudhary S</submitter><funding>Indian Council of Medical Research (ICMR), New Delhi</funding><pubmed_abstract>The rapid emergence of novel coronavirus, SARS-coronavirus 2 (SARS-CoV-2), originated from Wuhan, China, imposed a global health emergency. Angiotensin-converting enzyme 2 (ACE2) receptor serves as an entry point for this deadly virus while the proteases like furin, transmembrane protease serine 2 (TMPRSS2) and 3 chymotrypsin-like protease (3CLpro) are involved in the further processing and replication of SARS-CoV-2. The interaction of SP with ACE2 and these proteases results in the SARS-CoV-2 invasion and fast epidemic spread. The small molecular inhibitors are reported to limit the interaction of SP with ACE2 and other proteases. Arbidol, a membrane fusion inhibitor approved for influenza virus is currently undergoing clinical trials against COVID-19. In this context, we report some anal</pubmed_abstract><journal>Virus research</journal><pagination>198146</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7455547</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Scaffold morphing of arbidol (umifenovir) in search of multi-targeting therapy halting the interaction of SARS-CoV-2 with ACE2 and other proteases involved in COVID-19.</pubmed_title><pmcid>PMC7455547</pmcid><pubmed_authors>Choudhary S</pubmed_authors><pubmed_authors>Silakari O</pubmed_authors></additional><is_claimable>false</is_claimable><name>Scaffold morphing of arbidol (umifenovir) in search of multi-targeting therapy halting the interaction of SARS-CoV-2 with ACE2 and other proteases involved in COVID-19.</name><description>The rapid emergence of novel coronavirus, SARS-coronavirus 2 (SARS-CoV-2), originated from Wuhan, China, imposed a global health emergency. Angiotensin-converting enzyme 2 (ACE2) receptor serves as an entry point for this deadly virus while the proteases like furin, transmembrane protease serine 2 (TMPRSS2) and 3 chymotrypsin-like protease (3CLpro) are involved in the further processing and replication of SARS-CoV-2. The interaction of SP with ACE2 and these proteases results in the SARS-CoV-2 invasion and fast epidemic spread. The small molecular inhibitors are reported to limit the interaction of SP with ACE2 and other proteases. Arbidol, a membrane fusion inhibitor approved for influenza virus is currently undergoing clinical trials against COVID-19. In this context, we report some anal</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Nov</publication><modification>2026-04-07T21:39:23.551Z</modification><creation>2020-09-04T07:06:44Z</creation></dates><accession>S-EPMC7455547</accession><cross_references><pubmed>32866534</pubmed><doi>10.1016/j.virusres.2020.198146</doi></cross_references></HashMap>