Structural Classification of Toxic Amyloid Oligomers*

By C. Glabe. Journal of Biological Chemistry, 2008

788 citations recorded by the source corpus.

Amyloid oligomers are believed to play important causal roles in many types of amyloid-related degenerative diseases. Many different laboratories have reported amyloid oligomers that differ in size, morphology, toxicity, and method of preparation or purification, raising the question of the structural relationships among these oligomer preparations. The structural plasticity that has been reported to occur in amyloids formed from the same protein sequence indicates that it is quite possible that different oligomer preparations may represent distinct structural variants. In view of the difficulty in determining the precise structure of amyloids, conformation- and epitope-specific antibodies may provide a facile means of classifying amyloid oligomer structures. Conformation-dependent antibodies that recognize generic epitopes that are specifically associated with distinct aggregation states of many different amyloid-forming sequences indicate that there are at least two fundamentally distinct types of amyloid oligomers: fibrillar and prefibrillar oligomers. Classification of amyloid oligomers according to their underlying structures may be a more useful and rational approach than relying on differences in size and morphology.

Subfields: Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/66061bada80fce103eff35dee8f3f4c2000b92ac

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In Molecular Biology

1. David B. Teplow
2. E. Thies
3. M. Condron
4. A. Andersson
5. Jessica W. Wu
6. H. Zempel
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In Physiology

1. L. Mucke
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4. David B. Teplow
5. E. Thies
6. M. Condron
7. A. Andersson
8. Jessica W. Wu

Citations in the corpus

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• Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. (2011, background): “Also in type 2 diabetic baboons, amyloid was found both extracellularly and within -cells (120).”
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• Aβ Oligomers Cause Localized Ca2+ Elevation, Missorting of Endogenous Tau into Dendrites, Tau Phosphorylation, and Destruction of Microtubules and Spines (2010, background): “On the SDS gels, the different media (F12 or Nb) yielded similar bands, with the caveat that these gels can obscure the coexistence of multiple oligomeric species (Glabe, 2008).”
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• Amyloid-β Induced Neuronal Dysfunction in Alzheimer’s Disease: From Synapses toward Neural Networks (2010, background): “Human Aβ can exist in diverse assembly states, including monomers, dimers, trimers, tetramers, dodecamers, higher-order oligomers and protofibrils, as well as mature fibrils, which can form microscopically visible amyloid plaques in brain tissue”