| [1] Spillantini M G, Schmidt M L, Lee V M Y, et al. ?-Synuclein in Lewy bodies[J]. Nature, 1997, 388(6 645): 839－840. [2] Giasson B I, Murray I V J, Trojanowski J Q, et al. A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly[J]. J Biol Chem, 2001, 276(4): 2 380－2 386. [3] Bousset L, Pieri L, Ruiz-Arlandis G, et al. Structural and functional characterization of two α-synuclein strains[J]. Nature communications, 2013, 4(2 575): 1－13. [4] Hoyer W, Cherny D, Subramaniam V, et al. Impact of the acidic C-terminal region comprising amino acids 109-140 on α-synuclein aggregation in vitro[J]. Biochemistry, 2004, 43(51): 16 233－16 242. [5] Dedmon M M, Lindorff-Larsen K, Christodoulou J, et al. Mapping long-range interactions in α-synuclein using spin-label NMR and ensemble molecular dynamics simulations[J]. J Am Chem Soc, 2004, 127(2): 476－477. [6] Bertoncini C W, Fernandez C O, Griesinger C, et al. Familial mutants of α-synuclein with increased neurotoxicity have a destabilized conformation[J]. J Biol Chem, 2005, 280(35): 30 649－30 652. [7] Bertoncini C W, Jung Y S, Fernandez C O, et al. Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein[J]. P Natl Acad Sci USA, 2005, 102(5): 1 430－1 435.[8] Bussell R, Eliezer D. Residual structure and dynamics in parkinson's disease-associated mutants of α-synuclein[J]. J Biol Chem, 2001, 276(49): 45 996－46 003. [9] Fernández C O, Hoyer W, Zweckstetter M, et al. NMR of α-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation[J]. EMBO J, 2004, 23(10): 2 039－2 046. [10] Li C, Lutz E A, Slade K M, et al. 19F NMR studies of α-synuclein conformation and fibrillation[J]. Biochemistry, 2009, 48(36): 8 578－8 584. [11] Wang G F, Li C, Pielak G J. 19F NMR studies of α-synuclein-membrane interactions[J]. Protein Science, 2010, 19(9): 1 686－1 691. [12] Wang G F, Li C, Pielak G J. Probing the micelle-bound aggregation-prone state of α-synuclein with 19F NMR spectroscopy[J]. Chem Bio Chem, 2010, 11(14): 1 993－1 996. [13] Cobb S L, Murphy C D. 19F NMR applications in chemical biology[J]. J Fluorine Chem, 2009, 130(2): 132－143. [14] Kitevski-LeBlanc J L, Prosser R S. Current applications of 19F NMR to studies of protein structure and dynamics[J]. Prog Nucl Magn Reson Spectr, 2012, 62: 1－33. [15] Zhang Z, Dai C, Bai J, et al. Ca2+ modulating α-synuclein membrane transient interactions revealed by solution NMR spectroscopy[J]. Biochimica et Biophysica Acta (BBA) - Biomembranes, 2014, 1 838(3): 853－858. [16] Hoyer W, Antony T, Cherny D, et al. Dependence of α-synuclein aggregate morphology on solution conditions[J]. J Mol Biol, 2002, 322(2): 383－393. [17] Gerig J. Fluorine NMR of proteins[J]. Prog Nucl Magn Reson Spectr, 1994, 26: 293－370. |
