Protein misfolding and aggregation are known to play a crucial role in a number of important
human diseases (Alzheimer's, Parkinson's, prion, diabetes, cataracts, etc.) as well as in a …

Non-fibrillar soluble oligomeric forms of amyloid-β peptide (oAβ) and tau proteins are likely
to play a major role in Alzheimer's disease (AD). The prevailing hypothesis on the disease …

Protein is an important component of human tissues and cells, which is closely related to
various life activities. Therefore, studying the conformation of proteins can not only provide …

Background Overexpression and abnormal accumulation of aggregated α-synuclein (αS)
have been linked to Parkinson's disease (PD) and other synucleinopathies. αS can misfold …

In Alzheimer's disease (AD), tau aggregates into fibrils and higher order neurofibrillary
tangles, a key histopathological feature of AD. However, soluble oligomeric tau species may …

Neuropathologic and genetics studies as well as transgenic animal models have provided
strong evidence linking misfolding and aggregation of α-synuclein to the progression of …

Protein misfolding and aggregation is a critically important feature in many devastating
neurodegenerative diseases, therefore characterization of the CSF concentration profiles of …

Soluble antibody fragments are desirable not only as potential therapeutic and diagnostic
agents for extracellular targets but also as 'intrabodies' for functional genomics, proteomics …

While accumulation and deposition of beta amyloid (Aβ) is a primary pathological feature of
Alzheimer's disease (AD), increasing evidence has implicated small, soluble oligomeric …

Background Misfolding-and aggregation-prone proteins underlying Parkinson's,
Huntington's and Machado-Joseph diseases, namely α-synuclein, huntingtin, and ataxin-3 …