{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Schamoni-Kast K"],"funding":["European Research Council"],"pagination":["8244"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12420816"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["In coronavirus (CoV) infection, polyproteins (pp1a/pp1ab) are processed into non-structural proteins (nsps), which largely form the replication/transcription complex (RTC). The polyprotein processing and complex formation is critical and offers potential therapeutic targets. However, the interplay of polyprotein processing and RTC-assembly remains poorly understood. Here, we study two key aspects: The order of polyprotein processing by viral main protease M<sup>pro</sup> and its influence on complex formation with the methyltransferase nsp16. Moreover, we establish an approach to determine rate constants k from cleavage sites in structured CoV polyprotein based on native mass spectrometry (MS). The high sensitivity and precision of our method allow quantification of multi-reaction kinetics"],"journal":["Nature communications"],"pubmed_title":["The kinetics of nsp7-11 polyprotein processing and impact on complexation with nsp16 among human coronaviruses."],"pmcid":["PMC12420816"],"funding_grant_id":["759661"],"pubmed_authors":["Damjanovic T","Said FA","Uetrecht C","Schamoni-Kast K","Toker S","Krichel B","Kierspel T"],"additional_accession":[]},"is_claimable":false,"name":"The kinetics of nsp7-11 polyprotein processing and impact on complexation with nsp16 among human coronaviruses.","description":"In coronavirus (CoV) infection, polyproteins (pp1a/pp1ab) are processed into non-structural proteins (nsps), which largely form the replication/transcription complex (RTC). The polyprotein processing and complex formation is critical and offers potential therapeutic targets. However, the interplay of polyprotein processing and RTC-assembly remains poorly understood. Here, we study two key aspects: The order of polyprotein processing by viral main protease M<sup>pro</sup> and its influence on complex formation with the methyltransferase nsp16. Moreover, we establish an approach to determine rate constants k from cleavage sites in structured CoV polyprotein based on native mass spectrometry (MS). The high sensitivity and precision of our method allow quantification of multi-reaction kinetics","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-06-02T20:21:13.83Z","creation":"2026-04-20T03:10:02.198Z"},"accession":"S-EPMC12420816","cross_references":{"pubmed":["40925907"],"doi":["10.1038/s41467-025-61554-y"]}}