메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

Structural Ensembles of Membrane-bound α-Synuclein Reveal the Molecular Determinants of Synaptic Vesicle Affinity

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; PROTEIN BINDING; SNCA PROTEIN, HUMAN;

EID: 84976448182     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep27125     Document Type: Article
Times cited : (79)

References (61)
  • 1
    • 84869109864 scopus 로고    scopus 로고
    • Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • Luk, K. C. et al. Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 338, 949-953 (2012).
    • (2012) Science , vol.338 , pp. 949-953
    • Luk, K.C.1
  • 2
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. Protein folding and misfolding. Nature 426, 884-890 (2003).
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 3
    • 70349503591 scopus 로고    scopus 로고
    • Biophysics of Parkinsons disease: Structure and aggregation of alpha-synuclein
    • Uversky, V. N. & Eliezer, D. Biophysics of Parkinsons disease: structure and aggregation of alpha-synuclein. Curr Protein Pept Sci 10, 483-499 (2009).
    • (2009) Curr Protein Pept Sci , vol.10 , pp. 483-499
    • Uversky, V.N.1    Eliezer, D.2
  • 4
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F. & Dobson, C. M. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75, 333-366 (2006).
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 5
    • 84905372211 scopus 로고    scopus 로고
    • Soluble, prefibrillar alpha-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction
    • Luth, E. S., Stavrovskaya, I. G., Bartels, T., Kristal, B. S. & Selkoe, D. J. Soluble, prefibrillar alpha-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction. J Biol Chem 289, 21490-21507 (2014).
    • (2014) J Biol Chem , vol.289 , pp. 21490-21507
    • Luth, E.S.1    Stavrovskaya, I.G.2    Bartels, T.3    Kristal, B.S.4    Selkoe, D.J.5
  • 7
    • 33646451063 scopus 로고    scopus 로고
    • Elevated levels of oxidized cholesterol metabolites in Lewy body disease brains accelerate alpha-synuclein fibrilization
    • Bosco, D. A. et al. Elevated levels of oxidized cholesterol metabolites in Lewy body disease brains accelerate alpha-synuclein fibrilization. Nat Chem Biol 2, 249-253 (2006).
    • (2006) Nat Chem Biol , vol.2 , pp. 249-253
    • Bosco, D.A.1
  • 8
    • 84904654854 scopus 로고    scopus 로고
    • Cold denaturation of alpha-synuclein amyloid fibrils
    • Ikenoue, T. et al. Cold denaturation of alpha-synuclein amyloid fibrils. Angew Chem Int Ed Engl 53, 7799-7804 (2014).
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 7799-7804
    • Ikenoue, T.1
  • 9
    • 84883688262 scopus 로고    scopus 로고
    • Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
    • Jucker, M. & Walker, L. C. Self-propagation of pathogenic protein aggregates in neurodegenerative diseases. Nature 501, 45-51 (2013).
    • (2013) Nature , vol.501 , pp. 45-51
    • Jucker, M.1    Walker, L.C.2
  • 10
    • 84904515491 scopus 로고    scopus 로고
    • Co-existence of two different alpha-synuclein oligomers with different core structures determined by hydrogen/deuterium exchange mass spectrometry
    • Paslawski, W., Mysling, S., Thomsen, K., Jorgensen, T. J. & Otzen, D. E. Co-existence of two different alpha-synuclein oligomers with different core structures determined by hydrogen/deuterium exchange mass spectrometry. Angew Chem Int Ed Engl 53, 7560-7563 (2014).
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 7560-7563
    • Paslawski, W.1    Mysling, S.2    Thomsen, K.3    Jorgensen, T.J.4    Otzen, D.E.5
  • 11
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinsons disease
    • Polymeropoulos, M. H. et al. Mutation in the alpha-synuclein gene identified in families with Parkinsons disease. Science 276, 2045-2047 (1997).
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1
  • 12
    • 0242300619 scopus 로고    scopus 로고
    • Alpha-Synuclein locus triplication causes Parkinsons disease
    • Singleton, A. B. et al. alpha-Synuclein locus triplication causes Parkinsons disease. Science 302, 841 (2003).
    • (2003) Science , vol.302 , pp. 841
    • Singleton, A.B.1
  • 13
    • 37849028683 scopus 로고    scopus 로고
    • Red blood cells are the major source of alpha-synuclein in blood
    • Barbour, R. et al. Red blood cells are the major source of alpha-synuclein in blood. Neurodegener Dis 5, 55-59 (2008).
    • (2008) Neurodegener Dis , vol.5 , pp. 55-59
    • Barbour, R.1
  • 14
    • 0023722437 scopus 로고
    • Synuclein: A neuron-specific protein localized to the nucleus and presynaptic nerve terminal
    • Maroteaux, L., Campanelli, J. T. & Scheller, R. H. Synuclein: A neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J Neurosci 8, 2804-2815 (1988).
    • (1988) J Neurosci , vol.8 , pp. 2804-2815
    • Maroteaux, L.1    Campanelli, J.T.2    Scheller, R.H.3
  • 15
    • 77958449984 scopus 로고    scopus 로고
    • Alpha-Synuclein: Membrane interactions and toxicity in Parkinsons disease
    • Auluck, P. K., Caraveo, G. & Lindquist, S. alpha-Synuclein: membrane interactions and toxicity in Parkinsons disease. Annu Rev Cell Dev Biol 26, 211-233 (2010).
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 211-233
    • Auluck, P.K.1    Caraveo, G.2    Lindquist, S.3
  • 16
    • 33746533924 scopus 로고    scopus 로고
    • Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinsons models
    • Cooper, A. A. et al. Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinsons models. Science 313, 324-328 (2006).
    • (2006) Science , vol.313 , pp. 324-328
    • Cooper, A.A.1
  • 17
    • 84904006504 scopus 로고    scopus 로고
    • Synucleins regulate the kinetics of synaptic vesicle endocytosis
    • Vargas, K. J. et al. Synucleins regulate the kinetics of synaptic vesicle endocytosis. J Neurosci 34, 9364-9376 (2014).
    • (2014) J Neurosci , vol.34 , pp. 9364-9376
    • Vargas, K.J.1
  • 18
    • 41649117989 scopus 로고    scopus 로고
    • Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae
    • Soper, J. H. et al. Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae. Mol Biol Cell 19, 1093-1103 (2008).
    • (2008) Mol Biol Cell , vol.19 , pp. 1093-1103
    • Soper, J.H.1
  • 19
    • 84862893457 scopus 로고    scopus 로고
    • Impact of N-Terminal acetylation of alpha-synuclein on its random coil and lipid binding properties
    • Maltsev, A. S., Ying, J. & Bax, A. Impact of N-Terminal acetylation of alpha-synuclein on its random coil and lipid binding properties. Biochemistry 51, 5004-5013 (2012).
    • (2012) Biochemistry , vol.51 , pp. 5004-5013
    • Maltsev, A.S.1    Ying, J.2    Bax, A.3
  • 20
    • 67649380327 scopus 로고    scopus 로고
    • Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy
    • Bodner, C. R., Dobson, C. M. & Bax, A. Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy. J Mol Biol 390, 775-790 (2009).
    • (2009) J Mol Biol , vol.390 , pp. 775-790
    • Bodner, C.R.1    Dobson, C.M.2    Bax, A.3
  • 21
    • 84937730909 scopus 로고    scopus 로고
    • Alpha-synuclein function and dysfunction on cellular membranes
    • Snead, D. & Eliezer, D. Alpha-synuclein function and dysfunction on cellular membranes. Exp Neurobiol 23, 292-313 (2014).
    • (2014) Exp Neurobiol , vol.23 , pp. 292-313
    • Snead, D.1    Eliezer, D.2
  • 22
    • 0037016741 scopus 로고    scopus 로고
    • Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form
    • Lee, H. J., Choi, C. & Lee, S. J. Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form. J Biol Chem 277, 671-678 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 671-678
    • Lee, H.J.1    Choi, C.2    Lee, S.J.3
  • 23
    • 84923362547 scopus 로고    scopus 로고
    • Lipid vesicles trigger alpha-synuclein aggregation by stimulating primary nucleation
    • Galvagnion, C. et al. Lipid vesicles trigger alpha-synuclein aggregation by stimulating primary nucleation. Nat Chem Biol 11, 229-234 (2015).
    • (2015) Nat Chem Biol , vol.11 , pp. 229-234
    • Galvagnion, C.1
  • 24
    • 12944304172 scopus 로고    scopus 로고
    • Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations
    • Dedmon, M. M., Lindorff-Larsen, K., Christodoulou, J., Vendruscolo, M. & Dobson, C. M. Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations. J Am Chem Soc 127, 476-477 (2005).
    • (2005) J Am Chem Soc , vol.127 , pp. 476-477
    • Dedmon, M.M.1    Lindorff-Larsen, K.2    Christodoulou, J.3    Vendruscolo, M.4    Dobson, C.M.5
  • 25
    • 84901812732 scopus 로고    scopus 로고
    • Direct observation of the three regions in alpha-synuclein that determine its membrane-bound behaviour
    • Fusco, G. et al. Direct observation of the three regions in alpha-synuclein that determine its membrane-bound behaviour. Nat Commun 5, 3827 (2014).
    • (2014) Nat Commun , vol.5 , pp. 3827
    • Fusco, G.1
  • 26
    • 75749093356 scopus 로고    scopus 로고
    • Differential phospholipid binding of alpha-synuclein variants implicated in Parkinsons disease revealed by solution NMR spectroscopy
    • Bodner, C. R., Maltsev, A. S., Dobson, C. M. & Bax, A. Differential phospholipid binding of alpha-synuclein variants implicated in Parkinsons disease revealed by solution NMR spectroscopy. Biochemistry 49, 862-871 (2010).
    • (2010) Biochemistry , vol.49 , pp. 862-871
    • Bodner, C.R.1    Maltsev, A.S.2    Dobson, C.M.3    Bax, A.4
  • 27
    • 84874644235 scopus 로고    scopus 로고
    • Site-specific interaction between alpha-synuclein and membranes probed by NMRobserved methionine oxidation rates
    • Maltsev, A. S., Chen, J., Levine, R. L. & Bax, A. Site-specific interaction between alpha-synuclein and membranes probed by NMRobserved methionine oxidation rates. J Am Chem Soc 135, 2943-2946 (2013).
    • (2013) J Am Chem Soc , vol.135 , pp. 2943-2946
    • Maltsev, A.S.1    Chen, J.2    Levine, R.L.3    Bax, A.4
  • 28
    • 77956373672 scopus 로고    scopus 로고
    • 19F NMR studies of alpha-synuclein-membrane interactions
    • Wang, G. F., Li, C. & Pielak, G. J. 19F NMR studies of alpha-synuclein-membrane interactions. Protein Sci 19, 1686-1691 (2010).
    • (2010) Protein Sci , vol.19 , pp. 1686-1691
    • Wang, G.F.1    Li, C.2    Pielak, G.J.3
  • 29
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human alpha-synuclein
    • Ulmer, T. S., Bax, A., Cole, N. B. & Nussbaum, R. L. Structure and dynamics of micelle-bound human alpha-synuclein. J Biol Chem 280, 9595-9603 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 30
    • 79958727550 scopus 로고    scopus 로고
    • Alpha-synuclein populates both elongated and broken helix states on small unilamellar vesicles
    • Lokappa, S. B. & Ulmer, T. S. Alpha-synuclein populates both elongated and broken helix states on small unilamellar vesicles. J Biol Chem 286, 21450-21457 (2011).
    • (2011) J Biol Chem , vol.286 , pp. 21450-21457
    • Lokappa, S.B.1    Ulmer, T.S.2
  • 31
    • 58149380718 scopus 로고    scopus 로고
    • Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement
    • Jao, C. C., Hegde, B. G., Chen, J., Haworth, I. S. & Langen, R. Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement. Proc Natl Acad Sci USA 105, 19666-19671 (2008).
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19666-19671
    • Jao, C.C.1    Hegde, B.G.2    Chen, J.3    Haworth, I.S.4    Langen, R.5
  • 32
    • 77958482255 scopus 로고    scopus 로고
    • The N-Terminus of the intrinsically disordered protein alpha-synuclein triggers membrane binding and helix folding
    • Bartels, T. et al. The N-Terminus of the intrinsically disordered protein alpha-synuclein triggers membrane binding and helix folding. Biophys J 99, 2116-2124 (2010).
    • (2010) Biophys J , vol.99 , pp. 2116-2124
    • Bartels, T.1
  • 33
    • 70349627256 scopus 로고    scopus 로고
    • Fast and accurate predictions of protein NMR chemical shifts from interatomic distances
    • Kohlhoff, K. J., Robustelli, P., Cavalli, A., Salvatella, X. & Vendruscolo, M. Fast and accurate predictions of protein NMR chemical shifts from interatomic distances. J Am Chem Soc 131, 13894-13895 (2009).
    • (2009) J Am Chem Soc , vol.131 , pp. 13894-13895
    • Kohlhoff, K.J.1    Robustelli, P.2    Cavalli, A.3    Salvatella, X.4    Vendruscolo, M.5
  • 34
    • 77955498721 scopus 로고    scopus 로고
    • Using NMR chemical shifts as structural restraints in molecular dynamics simulations of proteins
    • Robustelli, P., Kohlhoff, K., Cavalli, A. & Vendruscolo, M. Using NMR chemical shifts as structural restraints in molecular dynamics simulations of proteins. Structure 18, 923-933 (2010).
    • (2010) Structure , vol.18 , pp. 923-933
    • Robustelli, P.1    Kohlhoff, K.2    Cavalli, A.3    Vendruscolo, M.4
  • 35
    • 84898851755 scopus 로고    scopus 로고
    • Conformational recognition of an intrinsically disordered protein
    • Krieger, J. M. et al. Conformational recognition of an intrinsically disordered protein. Biophys J 106, 1771-1779 (2014).
    • (2014) Biophys J , vol.106 , pp. 1771-1779
    • Krieger, J.M.1
  • 36
    • 77956478902 scopus 로고    scopus 로고
    • SPARTA+ : A modest improvement in empirical NMR chemical shift prediction by means of an artificial neural network
    • Shen, Y. & Bax, A. SPARTA+ : A modest improvement in empirical NMR chemical shift prediction by means of an artificial neural network. J Biomol NMR 48, 13-22 (2010).
    • (2010) J Biomol NMR , vol.48 , pp. 13-22
    • Shen, Y.1    Bax, A.2
  • 37
    • 84858634014 scopus 로고    scopus 로고
    • Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts
    • Camilloni, C., De Simone, A., Vranken, W. F. & Vendruscolo, M. Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts. Biochemistry 51, 2224-2231 (2012).
    • (2012) Biochemistry , vol.51 , pp. 2224-2231
    • Camilloni, C.1    De Simone, A.2    Vranken, W.F.3    Vendruscolo, M.4
  • 38
    • 77956320641 scopus 로고    scopus 로고
    • Alpha-synuclein in alpha-helical conformation at air-water interface: Implication of conformation and orientation changes during its accumulation/aggregation
    • Wang, C., Shah, N., Thakur, G., Zhou, F. & Leblanc, R. M. Alpha-synuclein in alpha-helical conformation at air-water interface: implication of conformation and orientation changes during its accumulation/aggregation. Chem Commun (Camb) 46, 6702-6704 (2010).
    • (2010) Chem Commun (Camb) , vol.46 , pp. 6702-6704
    • Wang, C.1    Shah, N.2    Thakur, G.3    Zhou, F.4    Leblanc, R.M.5
  • 39
    • 84902960606 scopus 로고    scopus 로고
    • Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations
    • De Simone, A., Mote, K. R. & Veglia, G. Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations. Biophys J 106, 2566-2576 (2014).
    • (2014) Biophys J , vol.106 , pp. 2566-2576
    • De Simone, A.1    Mote, K.R.2    Veglia, G.3
  • 40
    • 0037071786 scopus 로고    scopus 로고
    • Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: Effects of surface charge and peptide concentration
    • Magzoub, M., Eriksson, L. E. & Graslund, A. Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: effects of surface charge and peptide concentration. Biochim Biophys Acta 1563, 53-63 (2002).
    • (2002) Biochim Biophys Acta , vol.1563 , pp. 53-63
    • Magzoub, M.1    Eriksson, L.E.2    Graslund, A.3
  • 41
    • 84925882058 scopus 로고    scopus 로고
    • Computational design and experimental characterization of peptides intended for pH-dependent membrane insertion and pore formation
    • Zhang, Y. et al. Computational design and experimental characterization of peptides intended for pH-dependent membrane insertion and pore formation. ACS Chem Biol 10, 1082-1093 (2015).
    • (2015) ACS Chem Biol , vol.10 , pp. 1082-1093
    • Zhang, Y.1
  • 42
    • 84929095631 scopus 로고    scopus 로고
    • Interaction between the NS4B amphipathic helix, AH2, and charged lipid headgroups alters membrane morphology and AH2 oligomeric state-implications for the hepatitis C virus life cycle
    • Ashworth Briggs, E. L. et al. Interaction between the NS4B amphipathic helix, AH2, and charged lipid headgroups alters membrane morphology and AH2 oligomeric state-implications for the hepatitis C virus life cycle. Biochim Biophys Acta 1848, 1671-1677 (2015).
    • (2015) Biochim Biophys Acta , vol.1848 , pp. 1671-1677
    • Ashworth Briggs, E.L.1
  • 43
    • 84886402422 scopus 로고    scopus 로고
    • Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholamban
    • Gustavsson, M. et al. Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholamban. Proc Natl Acad Sci USA 110, 17338-17343 (2013).
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 17338-17343
    • Gustavsson, M.1
  • 44
    • 84896266359 scopus 로고    scopus 로고
    • Artificial heme-proteins: Determination of axial ligand orientations through paramagnetic NMR shifts
    • Vicari, C. et al. Artificial heme-proteins: determination of axial ligand orientations through paramagnetic NMR shifts. Chem Commun (Camb) 50, 3852-3855 (2014).
    • (2014) Chem Commun (Camb) , vol.50 , pp. 3852-3855
    • Vicari, C.1
  • 45
    • 65549107985 scopus 로고    scopus 로고
    • The first N-Terminal amino acids of alpha-synuclein are essential for alpha-helical structure formation in vitro and membrane binding in yeast
    • Vamvaca, K., Volles, M. J. & Lansbury, P. T., Jr. The first N-Terminal amino acids of alpha-synuclein are essential for alpha-helical structure formation in vitro and membrane binding in yeast. J Mol Biol 389, 413-424 (2009).
    • (2009) J Mol Biol , vol.389 , pp. 413-424
    • Vamvaca, K.1    Volles, M.J.2    Lansbury, P.T.3
  • 46
    • 38349160161 scopus 로고    scopus 로고
    • The Parkinsons disease protein alpha-synuclein disrupts cellular Rab homeostasis
    • Gitler, A. D. et al. The Parkinsons disease protein alpha-synuclein disrupts cellular Rab homeostasis. Proc Natl Acad Sci USA 105, 145-150 (2008).
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 145-150
    • Gitler, A.D.1
  • 47
    • 84879033702 scopus 로고    scopus 로고
    • Native alpha-synuclein induces clustering of synaptic-vesicle mimics via binding to phospholipids and synaptobrevin-2/VAMP2
    • Diao, J. et al. Native alpha-synuclein induces clustering of synaptic-vesicle mimics via binding to phospholipids and synaptobrevin-2/VAMP2. Elife 2, e00592 (2013).
    • (2013) Elife , vol.2 , pp. e00592
    • Diao, J.1
  • 48
    • 73549085595 scopus 로고    scopus 로고
    • Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis
    • Nemani, V. M. et al. Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis. Neuron 65, 66-79 (2010).
    • (2010) Neuron , vol.65 , pp. 66-79
    • Nemani, V.M.1
  • 49
    • 33845952600 scopus 로고    scopus 로고
    • Cytosolic proteins regulate alpha-synuclein dissociation from presynaptic membranes
    • Wislet-Gendebien, S. et al. Cytosolic proteins regulate alpha-synuclein dissociation from presynaptic membranes. J Biol Chem 281, 32148-32155 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 32148-32155
    • Wislet-Gendebien, S.1
  • 50
    • 22244442489 scopus 로고    scopus 로고
    • The biochemistry of Parkinsons disease
    • Cookson, M. R. The biochemistry of Parkinsons disease. Annu Rev Biochem 74, 29-52 (2005).
    • (2005) Annu Rev Biochem , vol.74 , pp. 29-52
    • Cookson, M.R.1
  • 51
    • 84942522975 scopus 로고    scopus 로고
    • Structure of the toxic core of alpha-synuclein from invisible crystals
    • Rodriguez, J. A. et al. Structure of the toxic core of alpha-synuclein from invisible crystals. Nature 525, 486-490 (2015).
    • (2015) Nature , vol.525 , pp. 486-490
    • Rodriguez, J.A.1
  • 52
    • 84961718093 scopus 로고    scopus 로고
    • Solid-state NMR structure of a pathogenic fibril of full-length human alpha-synuclein
    • Tuttle, M. D. et al. Solid-state NMR structure of a pathogenic fibril of full-length human alpha-synuclein. Nat Struct Mol Biol, 23, 409-15 (2016).
    • (2016) Nat Struct Mol Biol , vol.23 , pp. 409-415
    • Tuttle, M.D.1
  • 53
    • 0033121293 scopus 로고    scopus 로고
    • 13C-1H dipolar recoupling under very fast magic-Angle spinning using virtual pulses
    • Takegoshi, K. & Terao, T. 13C-1H dipolar recoupling under very fast magic-Angle spinning using virtual pulses. Solid State Nucl Magn Reson 13, 203-212 (1999).
    • (1999) Solid State Nucl Magn Reson , vol.13 , pp. 203-212
    • Takegoshi, K.1    Terao, T.2
  • 54
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., Kutzner, C., van der Spoel, D. & Lindahl, E. GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theor Comput 4, 435-447 (2008).
    • (2008) J Chem Theor Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 55
    • 77953513118 scopus 로고    scopus 로고
    • Improved side-chain torsion potentials for the Amber ff99SB protein force field
    • Lindorff-Larsen, K. et al. Improved side-chain torsion potentials for the Amber ff99SB protein force field. Proteins 78, 1950-1958 (2010).
    • (2010) Proteins , vol.78 , pp. 1950-1958
    • Lindorff-Larsen, K.1
  • 56
    • 2942622288 scopus 로고    scopus 로고
    • Development of an improved four-site water model for biomolecular simulations: TIP4P-Ew
    • Horn, H. W. et al. Development of an improved four-site water model for biomolecular simulations: TIP4P-Ew. J Chem Phys 120, 9665-9678 (2004).
    • (2004) J Chem Phys , vol.120 , pp. 9665-9678
    • Horn, H.W.1
  • 57
    • 84858321169 scopus 로고    scopus 로고
    • Derivation and systematic validation of a refined all-Atom force field for phosphatidylcholine lipids
    • Jambeck, J. P. & Lyubartsev, A. P. Derivation and systematic validation of a refined all-Atom force field for phosphatidylcholine lipids. J Phys Chem B 116, 3164-3179 (2012).
    • (2012) J Phys Chem B , vol.116 , pp. 3164-3179
    • Jambeck, J.P.1    Lyubartsev, A.P.2
  • 58
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess, B., Bekker, H., Berendsen, H. W. & Fraaije, J. G. LINCS: A linear constraint solver for molecular simulations. J Comput Chem 18, 1463-1472 (1997).
    • (1997) J Comput Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.W.3    Fraaije, J.G.4
  • 59
    • 0033104039 scopus 로고    scopus 로고
    • New tricks for modelers from the crystallography toolkit: The particle mesh Ewald algorithm and its use in nucleic acid simulations
    • Darden, T., Perera, L., Li, L. & Pedersen, L. New tricks for modelers from the crystallography toolkit: The particle mesh Ewald algorithm and its use in nucleic acid simulations. Structure 7, R55-60 (1999).
    • (1999) Structure , vol.7 , pp. R55-R60
    • Darden, T.1    Perera, L.2    Li, L.3    Pedersen, L.4
  • 60
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi, G., Donadio, D. & Parrinello, M. Canonical sampling through velocity rescaling. J Chem Phys 126, 014101 (2007).
    • (2007) J Chem Phys , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 61
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637 (1983).
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.