{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T13:54:36Z","timestamp":1790776476669,"version":"4.1.0"},"reference-count":221,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2022,3,14]],"date-time":"2022-03-14T00:00:00Z","timestamp":1647216000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Demensfonden","award":["2020"],"award-info":[{"award-number":["2020"]}]},{"name":"Norrl\u00e4ndska Hj\u00e4rtfonden","award":["2021"],"award-info":[{"award-number":["2021"]}]},{"DOI":"10.13039\/501100004200","name":"Stiftelsen Olle Engkvist Byggm\u00e4stare","doi-asserted-by":"publisher","award":["199-0469"],"award-info":[{"award-number":["199-0469"]}],"id":[{"id":"10.13039\/501100004200","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Insamlingsstiftelsen at Ume\u00e5 University","award":["FS 2.1.6-2396-18"],"award-info":[{"award-number":["FS 2.1.6-2396-18"]}]},{"name":"FAMY-Norrbotten","award":["03\/2021"],"award-info":[{"award-number":["03\/2021"]}]},{"name":"Wallenberg centrum f\u00f6r molekyl\u00e4r medicin","award":["Dnr FS 2.1.6-1860-18"],"award-info":[{"award-number":["Dnr FS 2.1.6-1860-18"]}]},{"name":"Bioteknikmedel","award":["medical faculty, Ume\u00e5 University"],"award-info":[{"award-number":["medical faculty, Ume\u00e5 University"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Amyloid formation is a pathological process associated with a wide range of degenerative disorders, including Alzheimer\u2019s disease, Parkinson\u2019s disease, and diabetes mellitus type 2. During disease progression, abnormal accumulation and deposition of proteinaceous material are accompanied by tissue degradation, inflammation, and dysfunction. Agents that can interfere with the process of amyloid formation or target already formed amyloid assemblies are consequently of therapeutic interest. In this context, a few endogenous proteins have been associated with an anti-amyloidogenic activity. Here, we review the properties of transthyretin, apolipoprotein E, clusterin, and BRICHOS protein domain which all effectively interfere with amyloid in vitro, as well as displaying a clinical impact in humans or animal models. Their involvement in the amyloid formation process is discussed, which may aid and inspire new strategies for therapeutic interventions.<\/jats:p>","DOI":"10.3390\/biom12030446","type":"journal-article","created":{"date-parts":[[2022,3,15]],"date-time":"2022-03-15T03:06:10Z","timestamp":1647313570000},"page":"446","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Endogenous Human Proteins Interfering with Amyloid Formation"],"prefix":"10.3390","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9070-6215","authenticated-orcid":false,"given":"Anna L.","family":"Gharibyan","sequence":"first","affiliation":[{"name":"Department of Clinical Microbiology, Ume\u00e5 University, 901 87 Ume\u00e5, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sanduni","family":"Wasana Jayaweera","sequence":"additional","affiliation":[{"name":"Department of Clinical Microbiology, Ume\u00e5 University, 901 87 Ume\u00e5, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manuela","family":"Lehmann","sequence":"additional","affiliation":[{"name":"Department of Public Health and Clinical Medicine, Ume\u00e5 University, 901 87 Ume\u00e5, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Intissar","family":"Anan","sequence":"additional","affiliation":[{"name":"Department of Public Health and Clinical Medicine, Ume\u00e5 University, 901 87 Ume\u00e5, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anders","family":"Olofsson","sequence":"additional","affiliation":[{"name":"Department of Clinical Microbiology, Ume\u00e5 University, 901 87 Ume\u00e5, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,3,14]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1146\/annurev-biochem-061516-045115","article-title":"Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade","volume":"86","author":"Chiti","year":"2017","journal-title":"Annu. 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