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Caption: Common among many amyloid-associated diseases, such as Alzheimer's disease, is the ability of their associated proteins to convert into toxic oligomeric forms, often referred to as amyloid oligomers. The X-ray derived atomic structure of a six-stranded beta-sheet rich oligomeric structure of an amyloidogenic peptide derived from alphaB crystallin, which we term cylindrin, is shown in the background in blue and yellow ribbon representation. In the foreground, key specifications of the cylindrin's architecture are illustrated, including dimensions, symmetry, and side chain packing within the central dry cavity. Cylindrin exhibits molecular properties similar to other amyloid forming proteins, and may represent the common architecture of amyloidengic proteins in their oligomeric, toxic form. This image relates to a paper that appeared in the March 9, 2012, issue of Science, published by AAAS. The paper, by A. Laganowsky at Howard Hughes Medical Institute in Los Angeles, Calif., and colleagues was titled, "Atomic View of a Toxic Amyloid Small Oligomer."
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