1. Introduction 22. What is the significance of the shared structural properties of disease-
associated protein fibrils? 32.1 Mechanism of amyloid fibril formation in vitro 62.1. 1 In vitro …

Familial amyloidotic polyneuropathy (FAP) is an inherited autosomal dominant disease that
is commonly caused by accumulation of deposits of transthyretin (TTR) amyloid around …

The transthyretin (TTR) amyloidoses are human diseases in which the misfolded TTR
protein aggregates in tissues with subsequent visceral, peripheral, and autonomic nerve …

The deposition of fibrils and amorphous aggregates of transthyretin (TTR) in patient tissues
is a hallmark of TTR amyloid disease, but the molecular details of amyloidogenesis are …

Amyloid transthyretin (ATTR) amyloidosis is characterized by the abnormal accumulation of
ATTR fibrils in multiple organs. However, the structure of ATTR fibrils from the eye is poorly …

The unique enhanced sensitivity of vibrational circular dichroism (VCD) to the formation and
development of amyloid fibrils in solution is extended to four additional fibril-forming proteins …

The formation of protein fibrils, and in particular amyloid fibrils, underlies many human
diseases. Understanding fibril formation mechanisms is important for understanding disease …

The kinetics of spontaneous assembly of amyloid fibrils of wild-type β2-microglobulin (β2M)
in vitro, under acid conditions (pH 2.5) and low ionic strength, has been followed using …

Although abundant evidence suggests that amyloid accumulation plays a significant role in
the pathogenesis of degenerative disease, the mechanism of amyloid formation and toxicity …

Familial amyloidotic polyneuropathy is an autosomal dominant disorder mainly
characterized by the extracellular deposition of transthyretin, with special involvement of the …