High-avidity binding drives nucleation of amyloidogenic transthyretin monomer
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DOI: 10.1172/jci.insight.150131
Abstract: 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.… read more here.
Keywords: binding drives; ttr; avidity binding; monomer ... See more keywords