{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T19:16:36Z","timestamp":1790622996722,"version":"4.1.0"},"reference-count":35,"publisher":"Wiley","issue":"16","license":[{"start":{"date-parts":[[2014,3,12]],"date-time":"2014-03-12T00:00:00Z","timestamp":1394582400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Angew Chem Int Ed"],"published-print":{"date-parts":[[2014,4,14]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The misfolding and aggregation of the protein \u03b1\u2010synuclein (\u03b1\u2010syn), which results in the formation of amyloid fibrils, is involved in the pathogenesis of Parkinson\u2019s disease and other synucleinopathies. The emergence of amyloid toxicity is associated with the formation of partially folded aggregation intermediates. Here, we engineered a class of binding proteins termed \u03b2\u2010wrapins (\u03b2\u2010wrap proteins) with affinity for \u03b1\u2010synuclein (\u03b1\u2010syn). The NMR structure of an \u03b1\u2010syn:\u03b2\u2010wrapin complex reveals a \u03b2\u2010hairpin of \u03b1\u2010syn comprising the sequence region \u03b1\u2010syn(37\u201354). The \u03b2\u2010wrapin inhibits \u03b1\u2010syn aggregation and toxicity at substoichiometric concentrations, demonstrating that it interferes with the nucleation of aggregation.<\/jats:p>","DOI":"10.1002\/anie.201309001","type":"journal-article","created":{"date-parts":[[2014,3,12]],"date-time":"2014-03-12T08:45:16Z","timestamp":1394613916000},"page":"4227-4230","source":"Crossref","is-referenced-by-count":133,"title":["Sequestration of a \u03b2\u2010Hairpin for Control of \u03b1\u2010Synuclein Aggregation"],"prefix":"10.1002","volume":"53","author":[{"given":"Ewa 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