Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation.

By Louise C. Serpell, J. Berriman, R. Jakes, M. Goedert, R. Crowther. Proceedings of the National Academy of Sciences of the United States of America, 2000

744 citations recorded by the source corpus.

Subfields: Neurology, Physiology

View Paper: https://www.semanticscholar.org/paper/6fdeb6da18f1e798fab9255003128103f8a43f8b

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Citations in the corpus

Sensitivity of secondary structure propensities to sequence differences between α‐ and γ‐synuclein: Implications for fibrillation (2006, background): “In addition, both b- and g-synuclein were shown to inhibit a-synuclein fibrillation in vitro (Uversky et al. 2002). a-Synuclein amyloid has been shown to involve residues 39–101 (Del Mar et al. 2005), and the N-terminal 87 residues are sufficient for fibrillation (Serpell et al. 2000).”
In vivo demonstration that α-synuclein oligomers are toxic (2011, background): “Structurally, amyloid fibrils of α-syn are composed of cross-β-sheets (15).”
Prion-like spreading of pathological α-synuclein in brain (2013, background): “2), we can conclude that the structural difference between soluble and filamentous forms of -synuclein, i.e. cross-b structure in the -synuclein fibrils (Serpell et al., 2000) is critical for the pathogenesis.”
Alpha-synuclein and neurodegenerative diseases (2001, background): “Full-length α-synuclein seems to be present, its carboxy-terminal region being exposed on the filament surfac”
Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death (2011, positive): “…or a synthetic peptide containing only the NAC domain (amino acid residues 61–95), assemble into α-syn amyloid fibrils, and nucleate full length α-syn fibrillization (Giasson et al., 2001; Han et al., 1995; Kessler et al., 2003; Luk et al., 2009; Murray et al., 2003; Serpell et al., 2000).”
Towards an Understanding of the Temperature/ Pressure Configurational and Free-Energy Landscape of Biomolecules (2007, neutral): “, for a-synuclein in Lewy bodies in Parkinson’s disease [114]).”
Helix periodicity, topology, and dynamics of membrane‐associated α‐Synuclein (2005, background): “The lipid-free protein can form similar amyloid fibrils in vitro (Hashimoto et al. 1998; Conway et al. 2000; Serpell et al. 2000), suggesting that this form of the protein may be important for in vivo pathogenesis.”
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers (2008, background): “Next, we investigated the effect of EGCG on αS fibrillogenesis by negative-stain EM. In the absence of EGCG, we observed formation of predominantly fibrillar αS structures with a diameter of ~5–15 nm and a length of ~0.5–2 μm (Fig. 1c), supporting the results of the ThT assays and of previously publ”