Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone
proteins that play a critical role in mitigating and preventing protein aggregation under stress …

Protein aggregation causes many devastating neurological and systemic diseases and
represents a major problem in the preparation of recombinant proteins in biotechnology …

Amyloid diseases, including Alzheimer's, Parkinson's, and the prion conditions, are each
associated with a particular protein in fibrillar form. These amyloid fibrils were long …

Cataracts reduce vision in 50% of individuals over 70 years of age and are a common form
of blindness worldwide. Cataracts are caused when damage to the major lens crystallin …

Osteoarthritis (OA) has long been viewed as a degenerative disease of cartilage, but
accumulating evidence indicates that inflammation has a critical role in its pathogenesis. In …

The small heat shock protein (sHSP) αB-crystallin (αB) plays a key role in the cellular
protection system against stress. For decades, high-resolution structural studies on …

Amyloid and amyloid-like fibrils are self-assembling protein nanostructures, of interest for
their robust material properties and inherent biological compatibility as well as their putative …

Improper protein folding (misfolding) can lead to the formation of disordered (amorphous) or
ordered (amyloid fibril) aggregates. The major lens protein, α-crystallin, is a member of the …

The fibrillation propensity of the multidomain protein human serum albumin (HSA) was
analyzed under different solution conditions. The aggregation kinetics, protein …

Small heat shock proteins (sHSPs) are ATP-independent chaperones that delay formation of
harmful protein aggregates. sHSPs' role in protein homeostasis has been appreciated for …