{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,25]],"date-time":"2026-03-25T09:59:46Z","timestamp":1774432786132,"version":"3.50.1"},"reference-count":43,"publisher":"Wiley","issue":"21","license":[{"start":{"date-parts":[[2023,8,7]],"date-time":"2023-08-07T00:00:00Z","timestamp":1691366400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["19K07012"],"award-info":[{"award-number":["19K07012"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100016925","name":"Takeda Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100016925","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2023,11]]},"abstract":"<jats:p>\n                    Transthyretin (TTR) is a carrier protein for thyroid hormone thyroxine (T\n                    <jats:sub>4<\/jats:sub>\n                    ) in plasma, placental cytosol, and cerebrospinal fluid. While the potential toxicity of small molecules that compete with T\n                    <jats:sub>4<\/jats:sub>\n                    for binding to TTR should be carefully studied, these small molecules can also serve as anti\u2010ATTR amyloidosis drugs by stabilizing the TTR structure. Here, we demonstrated that rafoxanide, an EU\u2010approved anthelmintic drug for domesticated animals, binds to the T\n                    <jats:sub>4<\/jats:sub>\n                    \u2010binding site of TTR. An intrinsic fluorescence quenching assay showed that rafoxanide also binds to the thyroid hormone\u2010related proteins, including serum albumin and thyroid hormone receptor \u03b2. Rafoxanide strongly inhibited TTR amyloidogenesis in fibrillization assay, but the binding of rafoxanide to TTR was interfered with in\u00a0human plasma, probably due to interactions with thyroid hormone\u2010related proteins. Protein crystallography provided clues for the optimization of binding affinity and selectivity. Our findings emphasize the importance of considering rafoxanide as both a possible thyroid\u2010disrupting chemical and a lead compound for the development of new ATTR amyloidosis inhibitors.\n                  <\/jats:p>","DOI":"10.1111\/febs.16915","type":"journal-article","created":{"date-parts":[[2023,7,31]],"date-time":"2023-07-31T06:58:55Z","timestamp":1690786735000},"page":"5158-5170","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Rafoxanide, a salicylanilide anthelmintic, interacts with human plasma protein transthyretin"],"prefix":"10.1111","volume":"290","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5362-8606","authenticated-orcid":false,"given":"Takeshi","family":"Yokoyama","sequence":"first","affiliation":[{"name":"Faculty of Pharmaceutical Sciences University of Toyama  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