{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T13:00:28Z","timestamp":1788872428062,"version":"build-2803163510"},"reference-count":24,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2005,12,9]],"date-time":"2005-12-09T00:00:00Z","timestamp":1134086400000},"content-version":"vor","delay-in-days":4970,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100006310","name":"Swedish Medical Research Council","doi-asserted-by":"crossref","award":["5647"],"award-info":[{"award-number":["5647"]}],"id":[{"id":"10.13039\/501100006310","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Swedish Association Against Rheumatism"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Arthritis &amp; Rheumatism"],"published-print":{"date-parts":[[1992,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    <jats:italic>Objective.<\/jats:italic>\n                    We describe a dysfunction of C3 in a patient with a systemic lupus erythematosus (SLE)\u2010like syndrome. Alternative pathway complement function was absent, but classical pathway complement function was partially intact.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:italic>Methods.<\/jats:italic>\n                    We used functional, preparative, and immunochemical techniques in the study.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:italic>Results.<\/jats:italic>\n                    The patient's C3 proved normally susceptible to trypsin proteolysis and partially resistant to classical pathway, but completely resistant to alternative pathway, convertase\u2010dependent cleavage.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:italic>Conclusion.<\/jats:italic>\n                    The dysfunction, thus, was caused by a failure of C3 to interact with the C3 convertases, rather than by a lack of a proteinase\u2010sensitive cleavage site in the deficient protein.\n           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