Article
Amyloid: morphology and toxicity.
Clinical chemistry and laboratory medicine - 1 Dec 2002
Olofsson Anders, Ostman Johan, Lundgren Erik
Abstract excerpt
We have expressed transthyretin (TTR) mutants which have significantly destabilised tetramers that aggregate into amyloid fibrils via a series of intermediates. We used atomic force microscopy to follow the morphology of aggregates during fibril formation. Initially, amorphous aggregates are formed that subsequently mature into fibrillar structures. This observation is interpreted as an optimisation of...
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