{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T15:59:36Z","timestamp":1790870376883,"version":"4.1.0"},"reference-count":161,"publisher":"MDPI AG","issue":"23","license":[{"start":{"date-parts":[[2024,11,27]],"date-time":"2024-11-27T00:00:00Z","timestamp":1732665600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["JCM"],"abstract":"<jats:p>Amyloids consist of fibrils that can be formed by a large variety of different precursor proteins. In localized amyloidosis, amyloids accumulate at the production site with a single organ being affected, whereas in systemic amyloidosis several organs are affected, with the heart being the most common, followed by the kidneys, liver, and the nervous system. The two most frequent systemic amyloidosis types affecting the heart in the vast majority (&gt;95%) of cases are immunoglobulin light chain (AL) amyloidosis and transthyretin (TTR) amyloidosis (ATTR amyloidosis). Patients with amyloid cardiopathy (CA) often present with non-specific heart failure symptoms as well as other clinical manifestations depending on the organ or systems involved. However, there are some findings associated with amyloidosis called \u201cred flags\u201d (clinical, echocardiographic, magnetic resonance imaging), which may assist in guiding the physician to the correct diagnosis. The present state-of-the-art review summarizes the features of the various cardiac phenotypic expressions of amyloidosis, proposes a simplified pathway for its diagnosis, and highlights the rapidly evolving therapeutic landscape.<\/jats:p>","DOI":"10.3390\/jcm13237210","type":"journal-article","created":{"date-parts":[[2024,11,27]],"date-time":"2024-11-27T10:05:56Z","timestamp":1732701956000},"page":"7210","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Amyloids and the Heart: An Update"],"prefix":"10.3390","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6433-4016","authenticated-orcid":false,"given":"Filippos","family":"Triposkiadis","sequence":"first","affiliation":[{"name":"School of Medicine, European University Cyprus, 2404 Nicosia, Cyprus"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5740-9670","authenticated-orcid":false,"given":"Alexandros","family":"Briasoulis","sequence":"additional","affiliation":[{"name":"Department of Clinical Therapeutics, Faculty of Medicine, Alexandra Hospital, National and Kapodistrian University of Athens, 11528 Athens, Greece"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9439-3946","authenticated-orcid":false,"given":"Andrew","family":"Xanthopoulos","sequence":"additional","affiliation":[{"name":"Department of Cardiology, University Hospital of Larissa, 41110 Larissa, Greece"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,11,27]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"112","DOI":"10.4161\/pri.2.3.7488","article-title":"Amyloid fibrils: Abnormal protein assembly","volume":"2","author":"Rambaran","year":"2008","journal-title":"Prion"},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Chatani, E., Yuzu, K., Ohhashi, Y., and Goto, Y. 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