<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><submitter>Ciccozzi M</submitter><funding>Sapienza Università di Roma</funding><pubmed_abstract>The SARS-CoV-2 Spike receptor binding domain and N-terminal domain interact with each other in an intricate mechanism. Mutations modulate the interplay between the Spike and host molecules. This editorial comments on the intricacies of SARS-CoV-2 Spike interactions.</pubmed_abstract><journal>Future virology</journal><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9987531</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Two sides of the same coin: the N-terminal and the receptor binding domains of SARS-CoV-2 Spike.</pubmed_title><pmcid>PMC9987531</pmcid><funding_grant_id>RP12117A7670A1E8</funding_grant_id><pubmed_authors>Pascarella S</pubmed_authors><pubmed_authors>Ciccozzi M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Two sides of the same coin: the N-terminal and the receptor binding domains of SARS-CoV-2 Spike.</name><description>The SARS-CoV-2 Spike receptor binding domain and N-terminal domain interact with each other in an intricate mechanism. Mutations modulate the interplay between the Spike and host molecules. This editorial comments on the intricacies of SARS-CoV-2 Spike interactions.</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Feb</publication><modification>2024-11-15T19:18:41.475Z</modification><creation>2024-11-15T19:18:41.475Z</creation></dates><accession>S-EPMC9987531</accession><cross_references><pubmed>36896145</pubmed><doi>10.2217/fvl-2022-0181</doi></cross_references></HashMap>