Amyloidosis is a diverse group of protein conformational disorder which is caused by
accumulation and deposition of insoluble protein fibrils in vital tissues or organs, instigating …

The misfolding of normally soluble proteins causes their aggregation and deposition in the
tissues which disrupts the normal structure and function of the corresponding organs. The …

AGel amyloidosis, formerly known as familial amyloidosis of the Finnish-type, is caused by
pathological aggregation of proteolytic fragments of plasma gelsolin. So far, four mutations …

Transmissible spongiform encephalopathies (TSEs) or prion diseases are fatal
neurodegenerative diseases with no approved therapeutics. TSE pathology is characterized …

In the disease familial amyloidosis, Finnish type (FAF), also known as AGel amyloidosis
(AGel), the mechanism by which point mutations in the calcium-regulated actin-severing …

Inherited glaucoma is a recent addition to the inventory of diseases arising due to protein
misfolding. Mutations in the olfactomedin (OLF) domain of myocilin are the most common …

Here, we report that minimal functional gelsolin ie fragment 28–161 can display F-actin
depolymerizing property even after heating the protein to 80° C. Small angle X-ray scattering …

Herein, we report novel neuroprotective activity of the neurohypophyseal hormone analogue
desmopressin (DDAVP) against toxic conformations of human prion protein. Systematic …

The emergence of drug-resistant Mycobacterium tuberculosis (Mtb) stains has escalated the
need for developing more efficient drugs and therapeutic strategies against tuberculosis …

Compelling evidence implicates self-assembly of amyloid-β (A β 1–42) peptides into soluble
oligomers and fibrils as a major underlying event in Alzheimer's disease (AD) pathogenesis …