Oligomeric intermediates are non-fibrillar polypeptide assemblies that occur during amyloid
fibril formation and that are thought to underlie the aetiology of amyloid diseases, such as …

Amyloid is aggregated protein in the form of insoluble fibrils. Amyloid deposition in human
tissue—amyloidosis—is associated with a number of diseases including all common …

The aggregation of the amyloid β peptide (Aβ) into amyloid fibrils is a defining characteristic
of Alzheimer's disease. Because of the complexity of this aggregation process, effective …

Antibodies commonly accumulate charged mutations in their complementarity-determining
regions (CDRs) during affinity maturation to enhance electrostatic interactions. However …

The monoclonal antibody 2A4 binds an epitope derived from a cleavage site of serum
amyloid protein A (sAA) containing a-Glu-Asp-amino acid pairing. In addition to its reactivity …

There are at least 20 distinct types of systemic amyloidosis, all of which result in the organ-
compromising accumulation of extracellular amyloid deposits. Amyloidosis is challenging to …

Oligomers are intermediates of the β-amyloid (Aβ) peptide fibrillogenic pathway and are
putative pathogenic culprits in Alzheimer's disease (AD). Here we report the …

The deposition of misfolded peptides and proteins in the form of amyloid fibrils is the
hallmark of nearly fifty medical disorders, including Alzheimer's disease, Parkinson's …

Antibodies that preferentially and specifically target pathological oligomeric protein and
peptide assemblies, as opposed to their monomeric and amyloid counterparts, provide …

Pattern-recognition receptors have been highly conserved in evolution. They recognize
danger signals including both pathogen-and damage-associated molecular patterns, also …