Article
The hydrophobic residue Leu73 is crucial for the high stability and low aggregation properties of murine transthyretin.
The Biochemical journal - 30 Sept 2022
Nakagawa Mei, Obita Takayuki, Mizuguchi Mineyuki
Abstract excerpt
Destabilization of human transthyretin leads to its aggregation into amyloid fibrils, which causes a rare, progressive and fatal systemic disorder called ATTR amyloidosis. By contrast, murine transthyretin is known to be very stable and therefore does not aggregate into amyloid fibrils in vivo or in vitro. We examined the hydrophobic residues responsible for the high-stability and low-aggregation properties of...
Topics
- Amyloid
- Amyloidosis
- Animals
- Humans
- Hydrophobic and Hydrophilic Interactions
- Mammals
- Mice
- Mutation
- Prealbumin
- Urea