Recent experiments have shown that the Taiwan mutation (D7H) slows the fibril formation of
amyloid peptides Aβ40 and Aβ42. Motivated by this finding, we have studied the influence of …

Amyloid β‐proteins spontaneously aggregate and build plaques in the brains of Alzheimer's
disease patients. The polypeptide has been the subject of extensive in vitro and …

Aβ peptides cleaved from the amyloid precursor protein are the main components of senile
plaques in Alzheimer's disease. Aβ peptides adopt a conformation mixture of random coil, β …

A limitation of the amyloid hypothesis in explaining the development of neurodegenerative
diseases is that the level of amyloidogenic polypeptide in vivo is below the critical …

Amyloid-like fibrils are found in many fatal diseases, such as Alzheimer's disease,
Parkinson's disease, type II diabetes mellitus, and prion diseases. Recently, the structural …

Amyloid fibrils formed from unrelated proteins often share morphological similarities,
suggesting common biophysicalmechanisms for amyloidogenesis. Biochemical studies of …

78a Sunday, February 18, 2018 characterize the complexes of Hsp70 and TMR-amylin.
Radius of gyration of the complexes were below the detection limit of MALS. Molecular …

Recent evidence suggests that amyloidogenic oligomers may be the toxic species in cell
cultures. Thus, it is crucial to understand their structure and oligomerization mechanism in …

There is now substantial evidence that soluble oligomers are primary toxic agents in amyloid
diseases. The development of an antibody recognizing the toxic soluble oligomeric forms of …

Amyloid β (Aβ) monomers are the smallest assembly units, and play an important role in
most of the individual processes involved in amyloid fibril formation. An important question is …