0 a protein that collects in some of the body's tissues and organs, as a feature of some diseases --
Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition.
This review will focus on in vitro studies aimed at the characterization of an intermediate on the amyloid pathway as one potential toxic species.
Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro.
Once formed, amyloid structures are not dependent on the presence of mobile water and are not significantly distorted when mobile water is removed by lyophilization.
The larger number of equatorial reflections reflect the presence of protofilaments in amyloid fibrils.
Thus, there are no absolutely universal molecular structural features in amyloid fibrils, apart from the cross-b motif.
Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation.
The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain.
