<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>14(2)</volume><submitter>Ramdhan P</submitter><pubmed_abstract>Methyltransferase enzymes have been associated with different processes within cells and viruses. Specifically, within viruses, methyltransferases are used to form the 5'cap-0 structure for optimal evasion of the host innate immune system. In this paper, we seek to discuss the various methyltransferases that exist within single-stranded RNA (ssRNA) viruses along with their respective inhibitors. Additionally, the importance of motifs such as the KDKE tetrad and glycine-rich motif in the catalytic activity of methyltransferases is discussed.</pubmed_abstract><journal>Viruses</journal><pagination>379</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8880702</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Targeting Viral Methyltransferases: An Approach to Antiviral Treatment for ssRNA Viruses.</pubmed_title><pmcid>PMC8880702</pmcid><pubmed_authors>Li C</pubmed_authors><pubmed_authors>Ramdhan P</pubmed_authors></additional><is_claimable>false</is_claimable><name>Targeting Viral Methyltransferases: An Approach to Antiviral Treatment for ssRNA Viruses.</name><description>Methyltransferase enzymes have been associated with different processes within cells and viruses. Specifically, within viruses, methyltransferases are used to form the 5'cap-0 structure for optimal evasion of the host innate immune system. In this paper, we seek to discuss the various methyltransferases that exist within single-stranded RNA (ssRNA) viruses along with their respective inhibitors. Additionally, the importance of motifs such as the KDKE tetrad and glycine-rich motif in the catalytic activity of methyltransferases is discussed.</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Feb</publication><modification>2025-04-04T07:55:03.478Z</modification><creation>2025-04-04T07:55:03.478Z</creation></dates><accession>S-EPMC8880702</accession><cross_references><pubmed>35215972</pubmed><doi>10.3390/v14020379</doi></cross_references></HashMap>