Non-synonymous single nucleotide polymorphisms (nsSNPs) are single base changes
leading to a change to the amino acid sequence of the encoded protein. Many of these …

Understanding the mechanisms underlying protein misfolding and aggregation has become
a central issue in biology and medicine. Compelling evidence show that the formation of …

Protein misfolding and aggregation are associated with a number of human degenerative
diseases. In spite of the enormous research efforts to develop effective strategies aimed at …

The process of transthyretin (TTR) misfolding and aggregation, including amyloid formation,
appears to cause a number of degenerative diseases. During amyloid formation, the native …

The subject of the review is on hereditary transthyretin (TTR) amyloidosis which is a
genetically transmitted disease that results from a mutation in the gene encoding the plasma …

Clustering methods have been widely used to group together similar conformational states
from molecular simulations of biomolecules in solution. For applications such as the …

Amyloid formation of natively folded proteins involves global and/or local unfolding of the
native state to form aggregation-prone intermediates. Here we report solid-state nuclear …

Objects: This study was intended to find out more about the clinical characterizations of
patients carrying transthyretin (TTR) E61K (p. Glu81Lys) gene mutation and the biochemical …

During amyloidogenesis, proteins undergo conformational changes that allow them to
aggregate and assemble into insoluble, fibrillar structures. Soluble oligomers that form …

Abstract Objective Ala97Ser (A97S) is the major transthyretin (TTR) mutation in Taiwanese
patients of familial amyloid polyneuropathy (FAP), characterized by a late‐onset but rapidly …