Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR.

By H. Heise, W. Hoyer, S. Becker, O. Andronesi, D. Riedel, M. Baldus. Proceedings of the National Academy of Sciences of the United States of America, 2005

605 citations recorded by the source corpus.

Subfields: Neurology, Organic Chemistry, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/622917cb944f2fc6ea6bcefed6a52663c8dc7e8e

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Citations in the corpus

Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “…2014 ssNMR/fibrils Gath et al. 2014 ssNMR/ribbons Comellas et al. 2011 ssNMR Vilar et al. 2008 H/D slow Vilar et al. 2008 ssNMR very slow Chen et al. 2007 EPR Heise et al. 2005 ssNMR-B Heise et al. 2005 ssNMR-A Del Mar et al. 2005 H/D-mass spectrometry Miake et al. 2002 limited…”
Structures of α-Synuclein Filaments from Multiple System Atrophy (2020, background): “6 protein in vitro have been shown to encompass 70 amino acids, extending approximately from residues 30-100 (41-44).”
Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein (2012, background): “…to the multiple permutations of interstrand hydrogen bonding interactions and in part to the fact that the b sheet rich species are likely to have a significant fraction of their hydrophobic side chains exposed to the solvent as found in amyloid fibrils (Heise et al., 2005; Vilar et al., 2008).”
In vivo demonstration that α-synuclein oligomers are toxic (2011, methodology): “Residues from approximately 30 to 110 of α-syn form the core of the fibrils, whereas the approximately 30 N-terminal residues are heterogeneous and the approximately 30 C-terminal residues are flexible (13, 14, 16, 17).”