Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations.
By Matthew M Dedmon, K. Lindorff‐Larsen, J. Christodoulou, Michele Vendruscolo, Christopher M. Dobson. Journal of the American Chemical Society, 2005
692 citations recorded by the source corpus.
Subfields: Biophysics, Neurology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/c6a33086050ff4f0328513e5848a2cee382c9ae7
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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): “…helicity suggests that a-synuclein may possess more tertiary structure than g-synuclein, consistent with the identification of tertiary contacts involving the C terminus of a-synuclein (Bernadó et al. 2005; Dedmon et al. 2005), which is not conserved with g-synuclein and is 13 residues longer.”
- Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles (2015, background): “…protein of this length (23 Å) rather than an unfolded protein (50 Å) of this length (Marsh and Forman-Kay, 2010; Wilkins et al., 1999), indicating that the Ddx4 N-terminal intrinsically disordered region maintains transient tertiary contacts that keep the protein compact (Dedmon et al., 2005).”
- Intrinsically Semi-disordered State and Its Role in Induced Folding and Protein Aggregation (2013, methodology): “The separation of two domains around residue 100 is consistent with compaction ratios obtained from combined NMR experiments and replica exchange molecular dynamics simulations [27] as well as the partial condensation in the central region (30–100) from molecular dynamics simulation with restraints ”
- Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. (2005, result): “These results are in agreement with recent structural studies that suggested that the C terminus region of the full-length a-synuclein, which is known to inhibit its aggregation,(87,88) has the tendency to interact with the NAC region, thus partially shielding it from forming intermolecular aggregat”
- Α-synuclein misfolding and Parkinson's disease. (2012, positive): “Analogous PRE experiments, in which the nitroxide radical MTSL was attached to the introduced cysteines at positions 18, 90, and 140, suggested that the numerous long-range interactions were present, leading to the formation of a hydrophobic cluster that comprised the C-terminal part of the highly h”