{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T18:37:14Z","timestamp":1790707034367,"version":"4.1.0"},"reference-count":17,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2020,11,17]],"date-time":"2020-11-17T00:00:00Z","timestamp":1605571200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004937","name":"Bundesministerium f\u00fcr Forschung und Technologie","doi-asserted-by":"publisher","award":["05K18FLA"],"award-info":[{"award-number":["05K18FLA"]}],"id":[{"id":"10.13039\/501100004937","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["Precision Medicine Inflammation \u2010 RTF\u2010V"],"award-info":[{"award-number":["Precision Medicine Inflammation \u2010 RTF\u2010V"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["SFB877\u2010Z2"],"award-info":[{"award-number":["SFB877\u2010Z2"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Proteomics"],"published-print":{"date-parts":[[2021,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The genome of coronaviruses, including SARS\u2010CoV\u20102, encodes for two proteases, a papain like (PL<jats:sup>pro<\/jats:sup>) protease and the so\u2010called main protease (M<jats:sup>pro<\/jats:sup>), a chymotrypsin\u2010like cysteine protease, also named 3CL<jats:sup>pro<\/jats:sup> or non\u2010structural protein 5 (nsp5). M<jats:sup>pro<\/jats:sup> is activated by autoproteolysis and is the main protease responsible for cutting the viral polyprotein into functional units. Aside from this, it is described that M<jats:sup>pro<\/jats:sup> proteases are also capable of processing host proteins, including those involved in the host innate immune response. To identify substrates of the three main proteases from SARS\u2010CoV, SARS\u2010CoV\u20102, and hCoV\u2010NL63 coronviruses, an LC\u2010MS based N\u2010terminomics in vitro analysis is performed using recombinantly expressed proteases and lung epithelial and endothelial cell lysates as substrate pools. For SARS\u2010CoV\u20102 M<jats:sup>pro<\/jats:sup>, 445 cleavage events from more than 300 proteins are identified, while 151 and 331 M<jats:sup>pro<\/jats:sup> derived cleavage events are identified for SARS\u2010CoV and hCoV\u2010NL63, respectively. These data enable to better understand the cleavage site specificity of the viral proteases and will help to identify novel substrates in vivo. All data are available via ProteomeXchange with identifier PXD021406.<\/jats:p>","DOI":"10.1002\/pmic.202000246","type":"journal-article","created":{"date-parts":[[2020,10,28]],"date-time":"2020-10-28T05:03:33Z","timestamp":1603861413000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":84,"title":["N\u2010Terminomics for the Identification of In Vitro Substrates and Cleavage Site Specificity of the SARS\u2010CoV\u20102 Main Protease"],"prefix":"10.1002","volume":"21","author":[{"given":"Tomas","family":"Koudelka","sequence":"first","affiliation":[{"name":"Systematic Proteome Research and Bioanalytics Institute for Experimental Medicine, Christian\u2010Albrechts\u2010Universit\u00e4t zu Kiel  Kiel 24105 Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juliane","family":"Boger","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry University of Luebeck  Luebeck 23562 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