Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 17, Issue 1, Pages 48-57Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2007.01.007
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Funding
- NIA NIH HHS [R01 AG19322, R01 AG18416] Funding Source: Medline
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Amyloid formation reactions exhibit two classes of polymorphisms: the metastable intermediates commonly observed during amyloid formation and the range of conformationally distinct mature fibrils often seen at the reaction endpoint. Although recent data suggest that spherical oligomers and protofibrils in most cases are not obligate intermediates of amyloid assembly, oligomeric states might sometimes serve as on-pathway intermediates. Mature amyloid polymorphs self-propagate as a result of the normally very high fidelity of amyloid elongation, giving rise to strain behavior and species barriers in prion phenomena. Oligomers, protofibrils and various polymorphic forms of mature amyloid fibrils seem to be distinguished by differences in atomic structure that give rise to differences in observed morphologies.
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