{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T13:48:26Z","timestamp":1791294506376,"version":"4.1.0"},"reference-count":40,"publisher":"Wiley","issue":"27","license":[{"start":{"date-parts":[[2014,4,23]],"date-time":"2014-04-23T00:00:00Z","timestamp":1398211200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"SERC scheme","award":["SR\/S1\/PC\/27\/2009"],"award-info":[{"award-number":["SR\/S1\/PC\/27\/2009"]}]},{"name":"SERC scheme","award":["BT\/53\/NE\/TBP\/2010"],"award-info":[{"award-number":["BT\/53\/NE\/TBP\/2010"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Angew Chem Int Ed"],"published-print":{"date-parts":[[2014,7]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Small oligomers of the amyloid\u2005\u03b2 (A\u03b2) peptide, rather than the monomers or the fibrils, are suspected to initiate Alzheimer\u2032s disease (AD). However, their low concentration and transient nature under physiological conditions have made structural investigations difficult. A method for addressing such problems has been developed by combining rapid fluorescence techniques with slower two\u2010dimensional solid\u2010state NMR methods. The smallest A\u03b2\n                    <jats:sub>40<\/jats:sub>\n                    oligomers that demonstrate a potential sign of toxicity, namely, an enhanced affinity for cell membranes, were thus probed. The two hydrophobic regions (residues 10\u201321 and 30\u201340) have already attained the conformation that is observed in the fibrils. However, the turn region (residues 22\u201329) and the N\u2010terminal tail (residues 1\u20139) are strikingly different. Notably, ten of eleven known A\u03b2\u2005mutants that are linked to familial AD map to these two regions. Our results provide potential structural cues for AD therapeutics and also suggest a general method for determining transient protein structures.\n                  <\/jats:p>","DOI":"10.1002\/anie.201402636","type":"journal-article","created":{"date-parts":[[2014,4,23]],"date-time":"2014-04-23T07:27:01Z","timestamp":1398238021000},"page":"6888-6892","source":"Crossref","is-referenced-by-count":94,"title":["Significant Structural Differences between Transient Amyloid\u2010\u03b2 Oligomers and Less\u2010Toxic Fibrils in Regions Known To Harbor Familial Alzheimer\u2032s Mutations"],"prefix":"10.1002","volume":"53","author":[{"given":"Bidyut","family":"Sarkar","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Venus 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