Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers.

Conformation-dependent anti-amyloid oligomer antibodies.

Structural classification of toxic amyloid oligomers.

Humoral immune response to fibrillar beta-amyloid peptide.

Formation of soluble amyloid oligomers and amyloid fibrils by the multifunctional protein vitronectin.

Protein denaturation and aggregation: Cellular responses to denatured and aggregated proteins.

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis.

Conformation-sensitive antibodies against alzheimer amyloid-beta by immunization with a thioredoxin-constrained B-cell epitope peptide.

Vaccination with soluble Abeta oligomers generates toxicity-neutralizing antibodies.

Drusen deposits associated with aging and age-related macular degeneration contain nonfibrillar amyloid oligomers.

Toxic human islet amyloid polypeptide (h-IAPP) oligomers are intracellular, and vaccination to induce anti-toxic oligomer antibodies does not prevent h-IAPP-induced beta-cell apoptosis in h-IAPP transgenic mice.

Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases.

Conformational Abs recognizing a generic amyloid fibril epitope.

Inhibition of human IAPP fibril formation does not prevent beta-cell death: evidence for distinct actions of oligomers and fibrils of human IAPP.

Prefibrillar amyloid aggregates could be generic toxins in higher organisms.

Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils.

Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases.

Methylene blue inhibits amyloid Abeta oligomerization by promoting fibrillization.

Structural models of amyloid-like fibrils.

Production and characterization of RNA aptamers specific for amyloid fibril epitopes.