{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,27]],"date-time":"2026-01-27T22:38:13Z","timestamp":1769553493231,"version":"3.49.0"},"reference-count":41,"publisher":"Oxford University Press (OUP)","issue":"9","license":[{"start":{"date-parts":[[2004,11,1]],"date-time":"2004-11-01T00:00:00Z","timestamp":1099267200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2004,11,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>From the implications of the complement system in a large number of diseases, an urgent need for therapeutics effecting reduced complement activity in vivo has emerged. In this study we report the design of a novel class of enzymes of human origin that obliterate functional complement by a noninhibitory, catalytic mechanism. Combining the framework of human C3 and the enzymatic mechanism of cobra venom factor, a nontoxic snake venom protein, we established molecules capable of forming stable C3 convertase complexes. Although the half-life of naturally occurring C3 convertase complexes ranges between 1 and 2 min, these complexes exhibit a half-life of up to several hours. Because the overall identity to human C3 could be extended to &amp;gt;90%, the novel C3 derivatives can be assumed to exhibit low immunogenicity and, therefore, represent promising candidates for therapeutic reduction of complement activity in vivo.<\/jats:p>","DOI":"10.4049\/jimmunol.173.9.5540","type":"journal-article","created":{"date-parts":[[2014,4,21]],"date-time":"2014-04-21T00:56:18Z","timestamp":1398041778000},"page":"5540-5545","source":"Crossref","is-referenced-by-count":24,"title":["Complement Inactivation by Recombinant Human C3 Derivatives"],"prefix":"10.1093","volume":"173","author":[{"given":"Johanna","family":"Ko\u0308lln","sequence":"first","affiliation":[{"name":"Institut fu\u0308r Biochemie und Lebensmittelchemie, Abteilung fu\u0308r Biochemie, und Molekularbiologie, Universita\u0308t Hamburg , Hamburg ,","place":["Germany"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Edzard","family":"Spillner","sequence":"additional","affiliation":[{"name":"Institut fu\u0308r Biochemie und Lebensmittelchemie, Abteilung fu\u0308r Biochemie, und Molekularbiologie, Universita\u0308t Hamburg , Hamburg ,","place":["Germany"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jo\u0308rg","family":"Andra\u0308","sequence":"additional","affiliation":[{"name":"Institut fu\u0308r Biochemie und Lebensmittelchemie, Abteilung fu\u0308r Biochemie, und Molekularbiologie, Universita\u0308t Hamburg , Hamburg ,","place":["Germany"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Katrin","family":"Klensang","sequence":"additional","affiliation":[{"name":"Institut fu\u0308r Biochemie und Lebensmittelchemie, Abteilung fu\u0308r Biochemie, und Molekularbiologie, Universita\u0308t Hamburg , Hamburg ,","place":["Germany"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Reinhard","family":"Bredehorst","sequence":"additional","affiliation":[{"name":"Institut fu\u0308r Biochemie und Lebensmittelchemie, Abteilung fu\u0308r Biochemie, und Molekularbiologie, Universita\u0308t Hamburg , Hamburg ,","place":["Germany"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2004,11,1]]},"reference":[{"key":"2025032707161261100_R1","first-page":"147","volume-title":"J. 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