{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,28]],"date-time":"2026-08-28T00:32:43Z","timestamp":1787877163543,"version":"build-2784847793"},"reference-count":63,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2023,8,21]],"date-time":"2023-08-21T00:00:00Z","timestamp":1692576000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100007300","name":"China Medical University","doi-asserted-by":"publisher","award":["CMU111-MF-29"],"award-info":[{"award-number":["CMU111-MF-29"]}],"id":[{"id":"10.13039\/501100007300","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Microbiol."],"abstract":"<jats:p>The main protease (M<jats:sup>pro<\/jats:sup>) plays a crucial role in coronavirus, as it cleaves viral polyproteins and host cellular proteins to ensure successful replication. In this review, we discuss the preference in the recognition sequence of M<jats:sup>pro<\/jats:sup> based on sequence-based studies and structural information and highlight the recent advances in computational and experimental approaches that have aided in discovering novel M<jats:sup>pro<\/jats:sup> substrates. In addition, we provide an overview of the current understanding of M<jats:sup>pro<\/jats:sup> host substrates and their implications for viral replication and pathogenesis. As M<jats:sup>pro<\/jats:sup> has emerged as a promising target for the development of antiviral drugs, further insight into its substrate specificity may contribute to the design of specific inhibitors.<\/jats:p>","DOI":"10.3389\/fmicb.2023.1251705","type":"journal-article","created":{"date-parts":[[2023,8,21]],"date-time":"2023-08-21T08:49:22Z","timestamp":1692607762000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":23,"title":["Characterization of host substrates of SARS-CoV-2 main protease"],"prefix":"10.3389","volume":"14","author":[{"given":"Ivonne","family":"Melano","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yan-Chung","family":"Lo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wen-Chi","family":"Su","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2023,8,21]]},"reference":[{"key":"ref1","doi-asserted-by":"publisher","first-page":"10223","DOI":"10.1128\/MCB.24.23.10223-10235.2004","article-title":"Nuclear speckle-associated protein Pnn\/Drs binds to the transcriptional corepressor Ctbp and relieves Ctbp-mediated repression of the E-cadherin gene","volume":"24","author":"Alpatov","year":"2004","journal-title":"Mol. 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