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

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Nanoparticles present enormous surface areas and are found to enhance the rate of protein
fibrillation by decreasing the lag time for nucleation. Protein fibrillation is involved in many …

All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from
proteins associated with different diseases remains unclear. Here, we combine cryo-EM and …

Aβ fibrils (or Abeta nanowires, NWs) have been implicated in many neurodegenerative
disorders such as Alzheimer disease (AD).[1] Both soluble oligomers and mature fibrils from …

Although most proteins can assemble into amyloid-like fibrils in vitro under extreme
conditions, how proteins form amyloid fibrils in vivo remains unresolved. Identifying rare …

Protein misfolding and aggregation cause serious degenerative conditions such as
Alzheimer's, Parkinson, and prion diseases. Damage to membranes is thought to be one of …

Numerous studies of amyloid assembly have indicated that partially folded protein species
are responsible for initiating aggregation. Despite their importance, the structural and …

The aggregation of the natively disordered protein, Tau, to form lesions called neurofibrillary
tangles is a characteristic feature of several neurodegenerative tauopathies. The polyanion …

The humoral innate immune response consists of multiple components, including the
naturally occurring antibodies (NAb), pentraxins and the complement and contact cascades …