Atomic structures of amyloid cross-beta spines reveal varied steric zippers.

By M. Sawaya, S. Sambashivan, R. Nelson, M. Ivanova, Stuart A. Sievers, M. Apostol, Michael J. Thompson, M. Balbirnie, J. Wiltzius, Heather T Mcfarlane and 3 more. Nature, 2007

608 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/8b7d5b9c6ae4f199d34b00c16acc180b48f174b1

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Citations in the corpus

The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease (2012, background): “Even under physiological conditions, it is now clear that certain primary sequences enable proteins to adopt a range of alternative structures that are each capable of conformational self-replication via templating the conversion of other copies of the same protein (Alberti et al., 2009; Gendoo and ”
Stress granules as crucibles of ALS pathogenesis (2013, background): “Disease-linked mutations in the prion-like domain of hnRNPA1 and hnRNPA2/B1 introduce a potent steric zipper, which can form two self-complementary sheets that comprise the spine of an amyloid fibril (Sawaya et al., 2007).”
The RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed Necrosis (2012, unknown): “This type of packing is remarkably similar to the structure of the VQIVYK sequence from tau (PDB 2ON9) (Sawaya et al., 2007), a microtubule-associated protein that plays an important role in stabilizing axonal microtubules.”
Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy (2015, background): “We also found that the structure of the amyloid fibrils of GNNQQNY peptide fragment of Sup35 yeast prion is markedly different from the crystal structure determined by Eisenberg and coworkers (33) indicating potential differences of crystallized and soluble amyloid fibril proteins (SI Results, Table”
MAVS Forms Functional Prion-Like Aggregates To Activate and Propagate Antiviral Innate Immune Response (2011, background): “Many prions form amyloids consisting predominantly of b sheets that may be detected with dyes such as Congo red (Chien et al., 2004; Sawaya et al., 2007).”
Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils (2010, background): “Though recent work has yielded atomicresolution insight into microcrystalline self-assemblies, which could in principle be used as the starting structure for systematic mutagenesis experiments for ThT binding, the surface properties of the short peptide subunits cannot be precisely manipulated witho”
Α-synuclein misfolding and Parkinson's disease. (2012, background): “These studies were later confirmed by X-ray diffraction ofmany short amyloid peptides, including a small segment from α-synuclein [64, 67].”