{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T20:55:48Z","timestamp":1791320148124,"version":"4.3.1"},"reference-count":32,"publisher":"S. Karger AG","issue":"3","license":[{"start":{"date-parts":[[2010,8,13]],"date-time":"2010-08-13T00:00:00Z","timestamp":1281657600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.karger.com\/Services\/SiteLicenses"},{"start":{"date-parts":[[2010,8,13]],"date-time":"2010-08-13T00:00:00Z","timestamp":1281657600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.karger.com\/Services\/SiteLicenses"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Neurodegener Dis"],"published-print":{"date-parts":[[2011]]},"abstract":"<jats:p>&lt;i&gt;Background\/Aims:&lt;\/i&gt; Amyloid-\u03b2 (A\u03b2) protofibrils are neurotoxic soluble intermediates in the A\u03b2 aggregation process eventually forming senile plaques in Alzheimer\u2019s disease. This A\u03b2 species is a potential biomarker for Alzheimer\u2019s disease and also a promising target for immunotherapy. In this study, we investigated the characteristics of conformation-dependent A\u03b2 antibodies specific for A\u03b2 protofibrils. &lt;i&gt;Methods:&lt;\/i&gt; Mice were immunized with A\u03b2 protofibrils to generate hybridomas producing A\u03b2-specific monoclonal antibodies. Binding of antibodies to different A\u03b2 conformations was investigated with inhibition ELISA. The antibodies\u2019 complementarity-determining region (CDR) sequences were determined and compared. &lt;i&gt;Results:&lt;\/i&gt; A majority of the antibodies were of the IgM class, all selectively binding to aggregated A\u03b2. Two IgG antibodies were generated: one with selective affinity for A\u03b2 protofibrils and the other bound A\u03b2 in all conformations. A high degree of similarity between the heavy-chain CDRs of the conformation-dependent antibodies was found, and all high-affinity A\u03b2 antibodies displayed a high degree of sequence similarity in the light-chain CDRs. &lt;i&gt;Conclusion:&lt;\/i&gt; Sequence similarity in the heavy-chain CDRs is associated with conformation selectivity of the antibodies, while sequence similarity in the light-chain CDRs correlates with the affinity for A\u03b2.<\/jats:p>","DOI":"10.1159\/000316530","type":"journal-article","created":{"date-parts":[[2010,8,18]],"date-time":"2010-08-18T07:43:24Z","timestamp":1282117404000},"page":"117-123","source":"Crossref","is-referenced-by-count":35,"title":["Heavy-Chain Complementarity-Determining Regions Determine Conformation Selectivity of Anti-A\u03b2 Antibodies"],"prefix":"10.1159","volume":"8","author":[{"given":"Dag","family":"Sehlin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie","family":"Hedlund","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna","family":"Lord","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hillevi","family":"Englund","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P\u00e4r","family":"Gellerfors","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Staffan","family":"Paulie","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lars","family":"Lannfelt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frida 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