Amyloid Fibrils of the HET-s(218–289) Prion Form a β Solenoid with a Triangular Hydrophobic Core

By C. Wasmer, A. Lange, H. Van Melckebeke, Ansgar B. Siemer, Roland Riek, B. Meier. Science, 2008

968 citations recorded by the source corpus.

Subfields: Molecular Biology, Nutrition and Dietetics, Physiology

View Paper: https://www.semanticscholar.org/paper/f1e24c4df354468cce90f8056193318e59fc75dd

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Citations in the corpus

Structure of the Bacterial Cytoskeleton Protein Bactofilin by NMR Chemical Shifts and Sequence Variation. (2016, background): “The modeled structures were presented as left-handed helices, although their orientation appears to have been dictated by the templates used to model the structures rather than by direct information, since both left- and right-handed b-helices are found in nature (11,12).”
Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril (2016, background): “Although it comprises some of the amyloid-typical structural motifs such as in-register cross–β-sheet secondary structures and Asn/Gln ladders, the complexity of the fold appears to be dictated by burying maximally the hydrophobic side chains—a feature imposed by free energy minimization and also ob”
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “anserina (residues 218–289) using ssNMR (73, 103).”
Nanomechanics of functional and pathological amyloid materials. (2011, background): “These fibrils are generally organized in a similar manner at the molecular level; they are characterized by β-strands that are oriented perpendicularly to the fibril axis, and connected through a dense hydrogen-bonding network, which results in supramolecular β-sheets that often extend continuously ”
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils (2008, background): “have recently reported a full structural model for amyloid fibrils formed by residues 218–289 of the Podospora anserina HET-s protein (39).”