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| Title | Apolipoprotein A-IV fibrils: structural diagnosis of mixed cardiac amyloidosis. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 16, Issue 1, Page 9276, Year 2025 |
| Publish date | Oct 20, 2025 |
Authors | Shintaro Aibara / Astrid Kassner / Edmond Wong / Karin Klingel / Monika Papworth / Magnus Althage / Qing-Dong Wang / Claudia Correia / Hendrik Milting / Taiana Maia de Oliveira / ![]() |
| PubMed Abstract | Cardiac amyloidosis (CA) occurs when misfolded proteins deposit as fibrils in the extracellular space of the heart. The fibrillogenic properties of apolipoprotein A-IV (ApoAIV) have been ...Cardiac amyloidosis (CA) occurs when misfolded proteins deposit as fibrils in the extracellular space of the heart. The fibrillogenic properties of apolipoprotein A-IV (ApoAIV) have been histologically observed and associated with CA pathogenesis. We report the structure of an ApoAIV amyloid from a patient's heart, which coexist amongst transthyretin (TTR) amyloids. These cases of undetected mixed CA highlight the importance of developing broad-spectrum anti-amyloid treatments to improve outcomes in patients. |
External links | Nat Commun / PubMed:41115976 / PubMed Central |
| Methods | EM (helical sym.) |
| Resolution | 3.0 - 3.3 Å |
| Structure data | EMDB-52456, PDB-9hx3: EMDB-52457, PDB-9hx4: |
| Source |
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Keywords | PROTEIN FIBRIL / amyloid / fibril / transthyretin / Apolipoprotein |
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homo sapiens (human)
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