{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T14:20:55Z","timestamp":1789914055028,"version":"4.0.1"},"reference-count":12,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2006,1,15]]},"abstract":"<jats:p>Many viral proteins undergo proteolytic processing events that are required for virus infection and virion assembly. In this issue of Biochemical Journal, Strongin and co-workers report that the NS3 protease from West Nile virus unexpectedly cleaves certain substrates at pairs of basic residues, a specificity that resembles that of the furin-like PCs (proprotein convertases). This led to the demonstration that furin\/PC inhibitors containing poly(D-arginine) are also potent inhibitors of NS3, and that anthrax toxin protective antigen and myelin basic protein are potential NS3 substrates. Structural modelling based on Dengue virus NS3 provided a possible rationale for the observed cleavage specificity of West Nile virus NS3.<\/jats:p>","DOI":"10.1042\/bj20051787","type":"journal-article","created":{"date-parts":[[2006,3,2]],"date-time":"2006-03-02T09:20:39Z","timestamp":1141291239000},"update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Unexpected similarity between the cytosolic West Nile virus NS3 and the secretory furin-like serine proteinases"],"prefix":"10.1042","volume":"393","author":[{"given":"Nabil\u00a0G.","family":"Seidah","sequence":"first","affiliation":[{"name":"Laboratory of Biochemical Neuroendocrinology, Clinical Research Institute of Montreal, 110 Pine Ave West, Montreal, QC, H2W 1R7, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2005,12,23]]},"reference":[{"key":"2021112217160469600_B1","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/S0006-8993(99)01909-5","article-title":"Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides","volume":"848","author":"Seidah","year":"1999","journal-title":"Brain Res."},{"key":"2021112217160469600_B2","doi-asserted-by":"crossref","first-page":"12701","DOI":"10.1073\/pnas.221447598","article-title":"The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1\/S1P","volume":"98","author":"Lenz","year":"2001","journal-title":"Proc. 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