Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils

By A. Petkova, Richard Leapman, Zhihong Guo, Wai-Ming Yau, Mark P. Mattson, R. Tycko. Science, 2005

1,536 citations recorded by the source corpus.

Subfields: Biomaterials, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/1eeeb1f86280d2935e8826bf14f5c4c1981454d2

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Citations in the corpus

Distinct tau prion strains propagate in cells and mice and define different tauopathies (2014, background): “For example, amyloid b protein forms at least two distinct, self-propagating fibrillar conformations in vitro (Petkova et al., 2005) and in vivo (Lu et al., 2013).”
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “systems, a given polymorph can seed the same type of structure, as shown for Aβ40 twisted fibrils and striated ribbons formed under quiescent and agitated conditions, respectively, which propagate the same structure even if they are used to seed fibril growth under the different conditions (117).”
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils (2008, methodology): “Selfpropagating variations in the molecular structures of amyloid fibrils or amyloid-like aggregates formed by a single protein are believed to be responsible for the existence of multiple strains of mammalian prion diseases (6, 7) and yeast prion phenotypes (8–11), and may produce variations in the”
Aβ(1–42) Fibril Structure Illuminates Self-recognition and Replication of Amyloid in Alzheimer’s (2015, background): “The stable structural models that meet NMR constransts have two unique features: (1) Phe19, Phe20, and Val24 are buried inside turn, and all charged residues from Glu22 to Lys28 are exposed to solvation; and (2) Lys28 forms salt bridge with the C-terminal of Ala42, which was confirmed by the subsequ”
Functional Amyloid Formation within Mammalian Tissue (2005, background): “Proteins typically adopt a well-defined three-dimensional structure, but can misfold and form aggregates with a specific cross-β sheet fold called amyloid [”