The hidden world of amyloid biology has suddenly snapped into atomic-level focus,
revealing over 80 amyloid protein fibrils, both pathogenic and functional. Unlike globular …

Ribonucleases (RNases) are a large number of enzymes gathered into different bacterial or
eukaryotic superfamilies. Bovine pancreatic RNase A, bovine seminal BS-RNase, human …

Atypical amyloid generation, folding, aggregation and impaired clearance are characteristic
pathological features of human neurodegenerative disorders including Alzheimer's disease …

Since the inception of the human microbiome project (HMP) by the US National Institutes of
Health (NIH) in 2007 there has been a keen resurgence in our recognition of the human …

Amyloid fibers, once exclusively associated with disease, are acquiring utility as a class of
biological nanomaterials. Here we introduce a method that utilizes the atomic structures of …

Amyloid fibrils are proteinaceous aggregates associated with diseases in humans and
animals. The fibrils are defined by intermolecular interactions between the fibril-forming …

TDP-43 can form pathological proteinaceous aggregates linked to ALS and FTLD. Within the
putative aggregation domain, engineered repeats of residues 341–366 can recruit …

TDP-43 is a nuclear protein whose abnormal aggregates are implicated in ALS and FTLD.
Recently, an Asn/Gln rich C-terminal segment of TDP-43 has been shown to produce …

Amyloid diseases are characterized by the accumulation of insoluble, β‐strand‐rich
aggregates. The underlying structural conversions are closely associated with cellular …

Protein stability is not just an academic matter. Biotechnology, Cell Biology and Drug Design
are some of the fields where both theoretical and practical knowledge of protein stability is …