{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,19]],"date-time":"2026-08-19T19:01:00Z","timestamp":1787166060442,"version":"build-2736575974"},"reference-count":32,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2005,6,9]],"date-time":"2005-06-09T00:00:00Z","timestamp":1118275200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Peptide Science"],"published-print":{"date-parts":[[2006,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Oligopeptidase B is a serine endopeptidase found in prokaryotes, unicellular eukaryotes and higher plants. The enzyme has been shown recently to play a central role in the pathogenesis of several parasitic diseases such as African trypanosomiasis, and to be a potential therapeutic target. This study reports that protamine, a basic peptide rich in arginine, is a potent inhibitor at the nanomolar level of oligopeptidase B from\n                    <jats:italic>E. coli<\/jats:italic>\n                    and wheat. Protamines 1B, 2C, 3A and TP17 displayed similar inhibitory activities and were capable of binding strongly to oligopeptidase B without proteolytic cleavage. The concentration of protamine needed for 50% inhibition (IC\n                    <jats:sub>50<\/jats:sub>\n                    ) of oligopeptidase B was 10\n                    <jats:sup>4<\/jats:sup>\n                    \u2010fold lower than the IC\n                    <jats:sub>50<\/jats:sub>\n                    of trypsin. Oligopeptidase B was highly sensitive to inhibition by protamines even in the presence of serum (IC\n                    <jats:sub>50<\/jats:sub>\n                    , 1 \u00b5\n                    <jats:sc>M<\/jats:sc>\n                    ). These data indicate that protamines might provide information useful for the design of more specific synthetic oligopeptidase B inhibitors. Copyright \u00a9 2005 European Peptide Society and John Wiley &amp; Sons, Ltd.\n                  <\/jats:p>","DOI":"10.1002\/psc.683","type":"journal-article","created":{"date-parts":[[2005,6,9]],"date-time":"2005-06-09T13:16:32Z","timestamp":1118322992000},"page":"65-71","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Protamine: a unique and potent inhibitor of oligopeptidase B"],"prefix":"10.1002","volume":"12","author":[{"given":"Akihiko","family":"Tsuji","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tadashi","family":"Yoshimoto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Keizo","family":"Yuasa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshiko","family":"Matsuda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2005,6,9]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj2790907"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.jbchem.a123577"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.2004.04199.x"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2744(79)90053-6"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444998004181"},{"key":"e_1_2_1_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1093-3263(99)00042-X"},{"key":"e_1_2_1_8_2","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-0134(199707)28:3<375::AID-PROT7>3.0.CO;2-B"},{"key":"e_1_2_1_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81416-6"},{"key":"e_1_2_1_10_2","doi-asserted-by":"crossref","first-page":"7771","DOI":"10.1016\/S0021-9258(19)40882-X","article-title":"Protease II from Escherichia coli. 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