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

      Science (New York, N.Y.)

      Tumor Cells, Cultured, Aged, Solubility, Rabbits, Protein Conformation, immunology, chemistry, Peptide Fragments, Neurofibrillary Tangles, Molecular Mimicry, Microscopy, Electron, Microscopy, Confocal, Humans, Cell Survival, Brain Chemistry, pathology, Brain, toxicity, analysis, Biopolymers, Antibody Specificity, Antibodies, Animals, Amyloid beta-Peptides, Amyloid, metabolism, Alzheimer Disease, Aged, 80 and over

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          Abstract

          Soluble oligomers are common to most amyloids and may represent the primary toxic species of amyloids, like the Abeta peptide in Alzheimer's disease (AD). Here we show that all of the soluble oligomers tested display a common conformation-dependent structure that is unique to soluble oligomers regardless of sequence. The in vitro toxicity of soluble oligomers is inhibited by oligomer-specific antibody. Soluble oligomers have a unique distribution in human AD brain that is distinct from fibrillar amyloid. These results indicate that different types of soluble amyloid oligomers have a common structure and suggest they share a common mechanism of toxicity.

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          Journal
          10.1126/science.1079469
          12702875

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