The aggregation of a polypeptide chain into amyloid fibrils and their accumulation and
deposition into insoluble plaques and intracellular inclusions is the hallmark of several …

Peptides or proteins convert under some conditions from their soluble forms into highly
ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging …

The deposition of proteins in the form of amyloid fibrils and plaques is the characteristic
feature of more than 20 degenerative conditions affecting either the central nervous system …

The conversion of proteins from their soluble states into well-organized fibrillar aggregates is
associated with a wide range of pathological conditions, including neurodegenerative …

The conversion of proteins from their native state to misfolded oligomers is associated with,
and thought to be the cause of, a number of human diseases, including Alzheimer's disease …

The data reported in the past 5 years have highlighted new aspects of protein misfolding
and aggregation. Firstly, it appears that protein aggregation may be a generic property of …

Stress granules (SGs) are highly conserved cytoplasmic condensates that assemble in
response to stress and contribute to maintaining protein homeostasis. These membraneless …

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 …

Transthyretin (TTR) is a plasma homotetrameric protein implicated in fatal systemic
amyloidoses. TTR tetramer dissociation precedes pathological TTR aggregation. Native …