{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T21:53:38Z","timestamp":1790373218273,"version":"4.1.0"},"reference-count":231,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2026,4,10]],"date-time":"2026-04-10T00:00:00Z","timestamp":1775779200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000065","name":"NINDS","doi-asserted-by":"publisher","award":["R01 NS105874"],"award-info":[{"award-number":["R01 NS105874"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000065","name":"NINDS","doi-asserted-by":"publisher","award":["R01 GM122763"],"award-info":[{"award-number":["R01 GM122763"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"award":["R01 NS105874"],"award-info":[{"award-number":["R01 NS105874"]}],"id":[{"id":"https:\/\/ror.org\/01s5ya894","id-type":"ROR","asserted-by":"publisher"}]},{"award":["R01 GM122763"],"award-info":[{"award-number":["R01 GM122763"]}],"id":[{"id":"https:\/\/ror.org\/01s5ya894","id-type":"ROR","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000928","name":"Welch Foundation","doi-asserted-by":"publisher","award":["Q-2097-20220331"],"award-info":[{"award-number":["Q-2097-20220331"]}],"id":[{"id":"10.13039\/100000928","id-type":"DOI","asserted-by":"publisher"}]},{"award":["Q-2097-20220331"],"award-info":[{"award-number":["Q-2097-20220331"]}],"id":[{"id":"https:\/\/ror.org\/00np6vq88","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Neurodegenerative diseases arise when normally functional aggregation-prone proteins transition into stable cross-\u03b2 amyloid fibrils. Although these fibrils share a conserved architecture, the pathways that lead to fibrillation vary across proteins and cellular environments. Liquid\u2013liquid phase separation is now recognized as a central organizer of intracellular biochemistry that modulates protein aggregation. Physiological condensation can buffer aggregation by maintaining macromolecular solubility and providing partner interactions that compete against pathological protein\u2013protein interactions. However, condensates can transform and age into gel-like states that can favor the emergence of \u03b2-rich oligomers and solid-state fibrils. Across six disease-linked proteins that include Tau, \u03b1-synuclein, amyloid-\u03b2, TDP-43, FUS, and hnRNPA1, we compare how sequence-encoded interaction motifs, cellular cofactors, and interfacial microenvironments shape the balance between physiological condensates and pathological amyloids. Here, we highlight the unifying drivers of aggregation and intervention points that preserve native function while limiting toxic amyloid formation.<\/jats:p>","DOI":"10.3390\/biom16040560","type":"journal-article","created":{"date-parts":[[2026,4,10]],"date-time":"2026-04-10T09:08:12Z","timestamp":1775812092000},"page":"560","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Condensate State as Determinant of Amyloid Pathology in Neurodegeneration"],"prefix":"10.3390","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8493-0015","authenticated-orcid":false,"given":"Lathan","family":"Lucas","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Pharmacology, Baylor College of Medicine, Houston, TX 77030, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3175-5700","authenticated-orcid":false,"given":"Josephine C.","family":"Ferreon","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Pharmacology, Baylor College of Medicine, Houston, TX 77030, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8538-1732","authenticated-orcid":false,"given":"Allan Chris M.","family":"Ferreon","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Pharmacology, Baylor College of Medicine, Houston, TX 77030, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,4,10]]},"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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