α-Synuclein in Central Nervous System and from Erythrocytes, Mammalian Cells, and Escherichia coli Exists Predominantly as Disordered Monomer
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Bartels, 2011, α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation, Nature, 477, 107, 10.1038/nature10324
Wang, 2011, A soluble α-synuclein construct forms a dynamic tetramer, Proc. Natl. Acad. Sci., 108, 17797, 10.1073/pnas.1113260108
Spillantini, 1998, α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson disease and dementia with Lewy bodies, Proc. Natl. Acad. Sci., 95, 6469, 10.1073/pnas.95.11.6469
Baba, 1998, Aggregation of α-synuclein in Lewy bodies of sporadic Parkinson disease and dementia with Lewy bodies, Am. J. Pathol., 152, 879
Weinreb, 1996, NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded, Biochemistry, 35, 13709, 10.1021/bi961799n
Conway, 1998, Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease, Nat. Med., 4, 1318, 10.1038/3311
Chartier-Harlin, 2004, α-Synuclein locus duplication as a cause of familial Parkinson disease, Lancet, 364, 1167, 10.1016/S0140-6736(04)17103-1
Singleton, 2003, α-Synuclein locus triplication causes Parkinson disease, Science, 302, 841, 10.1126/science.1090278
Polymeropoulos, 1997, Mutation in the α-synuclein gene identified in families with Parkinson disease, Science, 276, 2045, 10.1126/science.276.5321.2045
Zarranz, 2004, The new mutation, E46K, of α-synuclein causes Parkinson and Lewy body dementia, Ann. Neurol., 55, 164, 10.1002/ana.10795
Muñoz, 1997, Identification of Spanish familial Parkinson disease and screening for the A53T mutation of the α-synuclein gene in early onset patients, Neurosci. Lett., 235, 57, 10.1016/S0304-3940(97)00710-6
Duda, 2000, Widespread nitration of pathological inclusions in neurodegenerative synucleinopathies, Am. J. Pathol., 157, 1439, 10.1016/S0002-9440(10)64781-5
Giasson, 2000, Oxidative damage linked to neurodegeneration by selective α-synuclein nitration in synucleinopathy lesions, Science, 290, 985, 10.1126/science.290.5493.985
Souza, 2000, Dityrosine cross-linking promotes formation of stable α-synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies, J. Biol. Chem., 275, 18344, 10.1074/jbc.M000206200
Yamin, 2003, Nitration inhibits fibrillation of human α-synuclein in vitro by formation of soluble oligomers, FEBS Lett., 542, 147, 10.1016/S0014-5793(03)00367-3
Binolfi, 2006, Interaction of α-synuclein with divalent metal ions reveals key differences: a link between structure, binding specificity, and fibrillation enhancement, J. Am. Chem. Soc., 128, 9893, 10.1021/ja0618649
Santner, 2010, Metalloproteomics and metal toxicology of α-synuclein, Metallomics, 2, 378, 10.1039/b926659c
Lücking, 2000, α-Synuclein and Parkinson disease, Cell. Mol. Life Sci., 57, 1894, 10.1007/PL00000671
Uversky, 2009, Biophysics of Parkinson disease. Structure and aggregation of α-synuclein, Curr. Protein Pept. Sci., 10, 483, 10.2174/138920309789351921
Ringrose, 2008, Highly efficient depletion strategy for the two most abundant erythrocyte-soluble proteins improves proteome coverage dramatically, J. Proteome Res., 7, 3060, 10.1021/pr8001029
Han, 2010, A comparative study of common techniques used to measure hemolysis in stored red cell concentrates, Vox Sang., 98, 116, 10.1111/j.1423-0410.2009.01249.x
Eliezer, 2001, Conformational properties of α-synuclein in its free and lipid-associated states, J. Mol. Biol., 307, 1061, 10.1006/jmbi.2001.4538
Delaglio, 1995, NMRPipe. A multidimensional spectral processing system based on UNIX pipes, J Biomol NMR, 6, 277, 10.1007/BF00197809
Johnson, 1994, NMR View. A Computer Program for the Visualization and Analysis of NMR Data, J. Biomol. NMR, 4, 603, 10.1007/BF00404272
Wishart, 1995, 1H, 13C, and 15N chemical shift referencing in biomolecular NMR, J. Biomol. NMR, 6, 135, 10.1007/BF00211777
Tinsley, 2010, Sensitive and specific detection of α-synuclein in human plasma, J. Neurosci. Res., 88, 2693, 10.1002/jnr.22417
Perrin, 2003, Epitope mapping and specificity of the anti-α-synuclein monoclonal antibody Syn-1 in mouse brain and cultured cell lines, Neurosci. Lett., 349, 133, 10.1016/S0304-3940(03)00781-X
Mbefo, 2010, Phosphorylation of synucleins by members of the Polo-like kinase family, J. Biol. Chem., 285, 2807, 10.1074/jbc.M109.081950
Lee, 2002, Human α-synuclein-harboring familial Parkinson disease-linked Ala-53 → Thr mutation causes neurodegenerative disease with α-synuclein aggregation in transgenic mice, Proc. Natl. Acad. Sci., 99, 8968, 10.1073/pnas.132197599
Rockenstein, 1995, Levels and alternative splicing of amyloid β protein precursor (APP) transcripts in brains of APP transgenic mice and humans with Alzheimer disease, J. Biol. Chem., 270, 28257, 10.1074/jbc.270.47.28257
Dusonchet, 2009, Targeted overexpression of the parkin substrate Pael-R in the nigrostriatal system of adult rats to model Parkinson disease, Neurobiol Dis, 35, 32, 10.1016/j.nbd.2009.03.013
Lennox, 1989, Diffuse Lewy body disease. Correlative neuropathology using anti-ubiquitin immunocytochemistry, J. Neurol. Neurosurg. Psychiatry, 52, 1236, 10.1136/jnnp.52.11.1236
Pham, 2010, Progressive accumulation of amyloid-α oligomers in Alzheimer disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins, FEBS J., 277, 3051, 10.1111/j.1742-4658.2010.07719.x
Anderson, 2006, Phosphorylation of Ser-129 is the dominant pathological modification of α-synuclein in familial and sporadic Lewy body disease, J. Biol. Chem., 281, 29739, 10.1074/jbc.M600933200
Ohrfelt, 2011, Identification of novel α-synuclein isoforms in human brain tissue by using an online nanoLC-ESI-FTICR-MS method, Neurochem. Res., 36, 2029, 10.1007/s11064-011-0527-x
Uéda, 1993, Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease, Proc. Natl. Acad. Sci., 90, 11282, 10.1073/pnas.90.23.11282
Jakes, 1994, Identification of two distinct synucleins from human brain, FEBS Lett., 345, 27, 10.1016/0014-5793(94)00395-5
Anderson, 2010, Identification of a helical intermediate in trifluoroethanol-induced α-synuclein aggregation, Proc. Natl. Acad. Sci., 107, 18850, 10.1073/pnas.1012336107
Bussell, 2001, Residual structure and dynamics in Parkinson disease-associated mutants of α-synuclein, J. Biol. Chem., 276, 45996, 10.1074/jbc.M106777200
Georgieva, 2008, Membrane-bound α-synuclein forms an extended helix. Long distance pulsed ESR measurements using vesicles, bicelles, and rod-like micelles, J. Am. Chem. Soc., 130, 12856, 10.1021/ja804517m
Georgieva, 2010, The lipid-binding domain of wild type and mutant α-synuclein. Compactness and interconversion between the broken and extended helix forms, J. Biol. Chem., 285, 28261, 10.1074/jbc.M110.157214
Paleologou, 2010, Phosphorylation at Ser-87 is enhanced in synucleinopathies, inhibits α-synuclein oligomerization, and influences synuclein-membrane interactions, J. Neurosci., 30, 3184, 10.1523/JNEUROSCI.5922-09.2010
Paleologou, 2008, Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of α-synuclein, J. Biol. Chem., 283, 16895, 10.1074/jbc.M800747200
Rospigliosi, 2009, E46K Parkinson-linked mutation enhances C-terminal to N-terminal contacts in α-synuclein, J. Mol. Biol., 388, 1022, 10.1016/j.jmb.2009.03.065
Sung, 2007, Residual structure, backbone dynamics, and interactions within the synuclein family, J. Mol. Biol., 372, 689, 10.1016/j.jmb.2007.07.008
Croke, 2008, Hydrogen exchange of monomeric α-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli, Protein Sci., 17, 1434, 10.1110/ps.033803.107
Fernández, 2004, NMR of α-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation, EMBO J., 23, 2039, 10.1038/sj.emboj.7600211
Li, 2009, 19F NMR studies of α-synuclein conformation and fibrillation, Biochemistry, 48, 8578, 10.1021/bi900872p
McNulty, 2006, Temperature-induced reversible conformational change in the first 100 residues of α-synuclein, Protein Sci., 15, 602, 10.1110/ps.051867106
Rasia, 2005, Structural characterization of copper(II) binding to α-synuclein. Insights into the bioinorganic chemistry of Parkinson disease, Proc. Natl. Acad. Sci., 102, 4294, 10.1073/pnas.0407881102
Segers-Nolten, 2008, Tissue transglutaminase modulates α-synuclein oligomerization, Protein Sci., 17, 1395, 10.1110/ps.036103.108
Wu, 2009, Structural reorganization of α-synuclein at low pH observed by NMR and REMD simulations, J. Mol. Biol., 391, 784, 10.1016/j.jmb.2009.06.063
Azeredo da Silveira, 2009, Phosphorylation does not prompt, nor prevent, the formation of α-synuclein toxic species in a rat model of Parkinson disease, Hum. Mol. Genet., 18, 872
El-Agnaf, 2006, Detection of oligomeric forms of α-synuclein protein in human plasma as a potential biomarker for Parkinson's disease, FASEB J., 20, 419, 10.1096/fj.03-1449com
Lee, 2001, Self-oligomerization and protein aggregation of α-synuclein in the presence of Coomassie Brilliant Blue, Eur. J. Biochem., 268, 295, 10.1046/j.1432-1033.2001.01877.x
Paik, 1999, Copper(II)-induced self-oligomerization of α-synuclein, Biochem. J., 340, 821, 10.1042/bj3400821
Cole, 2002, Lipid droplet binding and oligomerization properties of the Parkinson disease protein α-synuclein, J. Biol. Chem., 277, 6344, 10.1074/jbc.M108414200
Shaikh, 2008, Advanced glycation end products induce in vitro cross-linking of α-synuclein and accelerate the process of intracellular inclusion body formation, J. Neurosci. Res., 86, 2071, 10.1002/jnr.21644
Walker, 2002, 57
Selkoe, 2011, Nondenaturing purification of α-synuclein from erythrocytes, Protocol Exchange
Smith, 1988, Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase, Gene, 67, 31, 10.1016/0378-1119(88)90005-4
Lim, 1994, Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV, Protein Sci., 3, 2233, 10.1002/pro.5560031209
Parker, 1990, Crystallization of glutathione S-transferase from human placenta, J. Mol. Biol., 213, 221, 10.1016/S0022-2836(05)80183-4
Ji, 1992, The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3–3 and glutathione at 2.2-Å resolution, Biochemistry, 31, 10169, 10.1021/bi00157a004
Ferguson, 1964, Starch gel electrophoresis. Application to the classification of pituitary proteins and polypeptides, Metabolism, 13, 985, 10.1016/S0026-0495(64)80018-4
Wu, 2008, Characterization of conformational and dynamic properties of natively unfolded human and mouse α-synuclein ensembles by NMR. Implication for aggregation, J. Mol. Biol., 378, 1104, 10.1016/j.jmb.2008.03.017
Marsh, 2006, Sensitivity of secondary structure propensities to sequence differences between α- and γ-synuclein. Implications for fibrillation, Protein Sci., 15, 2795, 10.1110/ps.062465306
Bertoncini, 2005, Familial mutants of α-synuclein with increased neurotoxicity have a destabilized conformation, J. Biol. Chem., 280, 30649, 10.1074/jbc.C500288200
Kang, 2003, Enhanced oligomerization of the α-synuclein mutant by the Cu,Zn-superoxide dismutase and hydrogen peroxide system, Mol. Cells, 15, 87, 10.1016/S1016-8478(23)13712-5
Krishnan, 2003, Oxidative dimer formation is the critical rate-limiting step for Parkinson disease α-synuclein fibrillogenesis, Biochemistry, 42, 829, 10.1021/bi026528t
Dedmon, 2005, Mapping long range interactions in α-synuclein using spin-label NMR and ensemble molecular dynamics simulations, J. Am. Chem. Soc., 127, 476, 10.1021/ja044834j
