High-avidity binding drives nucleation of amyloidogenic transthyretin monomer
Amyloidosis involves stepwise growth of fibrils assembled from soluble precursors. Transthyretin (TTR) naturally folds into a stable tetramer, whereas conditions and mutations that foster aberrant monomer formations facilitate TTR oligomeric aggregation and subsequent fibril extension. We investigat...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
American Society for Clinical investigation
2022-04-01
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| Series: | JCI Insight |
| Subjects: | |
| Online Access: | https://doi.org/10.1172/jci.insight.150131 |