McKeith, I. G.
et al. Consensus guidelines for the clinical and pathologic diagnosis of dementia with Lewy bodies (DLB): report of the consortium on DLB international workshop. Neurology
47, 1113–1124 (1996).
Braak, H. & Braak, E.
Pathoanatomy of Parkinson's disease. J. Neurol.
247, II3–II10 (2000). A detailed description of the pathoanatomy that occurs in PD.
Vekrellis, K., Xilouri, M., Emmanouilidou, E., Rideout, H. J. & Stefanis, L.
Pathological roles of α-synuclein in neurological disorders. Lancet Neurol.
10, 1015–1025 (2011).
Chartier-Harlin, M. C.
et al. α-synuclein locus duplication as a cause of familial Parkinson's disease. Lancet
364, 1167–1169 (2004).
et al. Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease. Nature Genet.
18, 106–108 (1998).
Polymeropoulos, M. H.
et al. Mutation in the α-synuclein gene identified in families with Parkinson's disease. Science
276, 2045–2047 (1997).
Zarranz, J. J.
et al. The new mutation, E46K, of α-synuclein causes Parkinson and Lewy body dementia. Ann. Neurol.
55, 164–173 (2004).
et al. Genome-wide association study reveals genetic risk underlying Parkinson's disease. Nature Genet.
41, 1308–1312 (2009).
Conway, K. A., Harper, J. D. & Lansbury, P. T.
Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease. Nature Med.
4, 1318–1320 (1998).
Tsigelny, I. F.
et al. Mechanisms of hybrid oligomer formation in the pathogenesis of combined Alzheimer's and Parkinson's diseases. PLoS ONE
3, e3135 (2008).
Oueslati, A., Fournier, M. & Lashuel, H. A.
Role of post-translational modifications in modulating the structure, function and toxicity of α-synuclein: implications for Parkinson's disease pathogenesis and therapies. Prog. Brain Res.
183, 115–145 (2010).
et al. Aggregation of α-synuclein promotes progressive in vivo neurotoxicity in adult rat dopaminergic neurons. Acta Neuropathol.
123, 671–683 (2011).
Galvin, J. E., Lee, V. M. & Trojanowski, J. Q.
Synucleinopathies: clinical and pathological implications. Arch. Neurol.
58, 186–190 (2001).
et al. α-Synuclein disrupts stress signaling by inhibiting polo-like kinase Cdc5/Plk2. Proc. Natl Acad. Sci. USA
109, 16119–16124 (2012).
et al. The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron
14, 467–475 (1995). This study identified NAC as a presynaptic protein.
Jakes, R., Spillantini, M. G. & Goedert, M.
Identification of two distinct synucleins from human brain. FEBS Lett.
345, 27–32 (1994).
Withers, G. S., George, J. M., Banker, G. A. & Clayton, D. F.
Delayed localization of synelfin (synuclein, NACP) to presynaptic terminals in cultured rat hippocampal neurons. Brain Res. Dev. Brain Res.
99, 87–94 (1997).
Kahle, P. J.
et al. Subcellular localization of wild-type and Parkinson's disease-associated mutant α-synuclein in human and transgenic mouse brain. J. Neurosci.
20, 6365–6373 (2000).
Lee, S. J., Jeon, H. & Kandror, K. V.
α-synuclein is localized in a subpopulation of rat brain synaptic vesicles. Acta Neurobiol. Exp.
68, 509–515 (2008).
et al. Semi-quantitative analysis of α-synuclein in subcellular pools of rat brain neurons: an immunogold electron microscopic study using a C-terminal specific monoclonal antibody. Brain Res.
1244, 40–52 (2008).
Cabin, D. E.
et al. Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking α-synuclein. J. Neurosci.
22, 8797–8807 (2002).
et al. Mice lacking α-synuclein display functional deficits in the nigrostriatal dopamine system. Neuron.
25, 239–252 (2000).
Murphy, D. D., Rueter, S. M., Trojanowski, J. Q. & Lee, V. M.
Synucleins are developmentally expressed, and α-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons. J. Neurosci.
20, 3214–3220 (2000).
Yavich, L., Tanila, H., Vepsalainen, S. & Jakala, P.
Role of α-synuclein in presynaptic dopamine recruitment. J. Neurosci.
24, 11165–11170 (2004).
Scott, D. A.
et al. A pathologic cascade leading to synaptic dysfunction in α-synuclein-induced neurodegeneration. J. Neurosci.
30, 8083–8095 (2010).
Nemani, V. M.
et al. Increased expression of α-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis. Neuron
65, 66–79 (2010). This study found that α-syn overexpression inhibited neurotransmitter release by reducing the size of the synaptic vesicle recycling pool.
Gaugler, M. N.
et al. Nigrostriatal overabundance of α-synuclein leads to decreased vesicle density and deficits in dopamine release that correlate with reduced motor activity. Acta Neuropathol.
123, 653–669 (2012).
Lundblad, M., Decressac, M., Mattsson, B. & Bjorklund, A.
Impaired neurotransmission caused by overexpression of α-synuclein in nigral dopamine neurons. Proc. Natl Acad. Sci. USA
109, 3213–3219 (2012).
Larsen, K. E.
et al. α-synuclein overexpression in PC12 and chromaffin cells impairs catecholamine release by interfering with a late step in exocytosis. J. Neurosci.
26, 11915–11922 (2006).
Scott, D. & Roy, S.
α-synuclein inhibits intersynaptic vesicle mobility and maintains recycling-pool homeostasis. J. Neurosci.
32, 10129–10135 (2012).
Payton, J. E., Perrin, R. J., Woods, W. S. & George, J. M.
Structural determinants of PLD2 inhibition by α-synuclein. J. Mol. Biol.
337, 1001–1009 (2004).
Dalfo, E. & Ferrer, I.
α-synuclein binding to rab3a in multiple system atrophy. Neurosci. Lett.
380, 170–175 (2005).
et al. α-synuclein promotes SNARE-complex assembly in vivo and in vitro. Science
329, 1663–1667 (2010). This paper identifies α-synuclein as a non-classical chaperone that binds and promotes SNARE-complex assembly.
et al. Double-knockout mice for α- and β-synucleins: effect on synaptic functions. Proc. Natl Acad. Sci. USA
101, 14966–14971 (2004).
Chandra, S., Gallardo, G., Fernandez-Chacon, R., Schluter, O. M. & Sudhof, T. C.
α-synuclein cooperates with CSPα in preventing neurodegeneration. Cell
123, 383–396 (2005).
et al. Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease. Proc. Natl Acad. Sci. USA
90, 11282–11286 (1993). This is the first report of the NAC being a 140-amino-acid protein.
Ulmer, T. S., Bax, A., Cole, N. B. & Nussbaum, R. L.
Structure and dynamics of micelle-bound human α-synuclein. J. Biol. Chem.
280, 9595–9603 (2005).
Eliezer, D., Kutluay, E., Bussell, R. Jr & Browne, G.
Conformational properties of α-synuclein in its free and lipid-associated states. J. Mol. Biol.
307, 1061–1073 (2001).
Masliah, E., Iwai, A., Mallory, M., Ueda, K. & Saitoh, T.
Altered presynaptic protein NACP is associated with plaque formation and neurodegeneration in Alzheimer's disease. Am. J. Pathol.
148, 201–210 (1996).
Spillantini, M. G.
et al. α-synuclein in Lewy bodies. Nature
388, 839–840 (1997).
Hashimoto, M., Takenouchi, T., Mallory, M., Masliah, E. & Takeda, A.
The role of NAC in amyloidogenesis in Alzheimer's disease. Am. J. Pathol.
156, 734–736 (2000).
El-Agnaf, O. M., Jakes, R., Curran, M. D. & Wallace, A.
Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of α-synuclein protein implicated in Parkinson's disease. FEBS Lett.
440, 67–70 (1998).
Giasson, B. I., Murray, I. V., Trojanowski, J. Q. & Lee, V. M.
A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly. J. Biol. Chem.
276, 2380–2386 (2001). This study showed that the middle hydrophobic domain of α-syn is necessary and sufficient for fibrillization.
Luk, K. C.
et al. Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells. Proc. Natl Acad. Sci. USA
106, 20051–20056 (2009). These authors showed that α-syn seeds can recruit endogenous soluble α-syn protein to form pathological species.
Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A. & Lansbury, P. T. Jr.
NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry
35, 13709–13715 (1996).
et al. α-synuclein in the central nervous system and from erythrocytes, mammalian cells and E. coli exists predominantly as a disordered monomer. J. Biol. Chem.
287, 15345–15364 (2012). This study reassessed the oligomeric state of α-syn and demonstrated that native α-syn exists predominantly as an unfolded monomer and not a tetramer.
Ramakrishnan, M., Jensen, P. H. & Marsh, D.
Association of α-synuclein and mutants with lipid membranes: spin-label ESR and polarized IR. Biochemistry
45, 3386–3395 (2006).
Ullman, O., Fisher, C. K. & Stultz, C. M.
Explaining the structural plasticity of α-synuclein. J. Am. Chem. Soc.
133, 19536–19546 (2011).
et al. Oxidative stress induces amyloid-like aggregate formation of NACP/α-synuclein in vitro. Neuroreport
10, 717–721 (1999).
et al. Tissue transglutaminase catalyzes the formation of α-synuclein crosslinks in Parkinson's disease. FASEB J.
18, 932–934 (2004).
Paleologou, K. E.
et al. Phosphorylation at S87 is enhanced in synucleinopathies, inhibits α-synuclein oligomerization, and influences synuclein-membrane interactions. J. Neurosci.
30, 3184–3198 (2010).
et al. Aggregation promoting C-terminal truncation of α-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations. Proc. Natl Acad. Sci. USA
102, 2162–2167 (2005).
Dufty, B. M.
et al. Calpain-cleavage of α-synuclein: connecting proteolytic processing to disease-linked aggregation. Am. J. Pathol.
170, 1725–1738 (2007).
Perrin, R. J., Woods, W. S., Clayton, D. F. & George, J. M.
Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins. J. Biol. Chem.
276, 41958–41962 (2001).
et al. The formation of highly soluble oligomers of α-synuclein is regulated by fatty acids and enhanced in Parkinson's disease. Neuron
37, 583–595 (2003).
et al. N-terminal region of α-synuclein is essential for the fatty acid-induced oligomerization of the molecules. FEBS Lett.
582, 3693–3700 (2008).
et al. Abnormal distribution of the non-Aβ component of Alzheimer's disease amyloid precursor/α-synuclein in Lewy body disease as revealed by proteinase K and formic acid pretreatment. Lab. Invest.
78, 1169–1177 (1998).
Suh, Y. H. & Checler, F.
Amyloid precursor protein, presenilins, and α-synuclein: molecular pathogenesis and pharmacological applications in Alzheimer's disease. Pharmacol. Rev.
54, 469–525 (2002).
et al. The synaptic protein NACP is abnormally expressed during the progression of Alzheimer's disease. Brain Res.
720, 230–234 (1996).
Kragh, C. L., Ubhi, K., Wyss-Corey, T. & Masliah, E.
Autophagy in dementias. Brain Pathol.
22, 99–109 (2012).
et al. First appraisal of brain pathology owing to A30P mutant α-synuclein. Ann. Neurol.
67, 684–689 (2010).
Maraganore, D. M.
et al. Collaborative analysis of α-synuclein gene promoter variability and Parkinson disease. JAMA
296, 661–670 (2006).
et al. α-synuclein degradation by serine protease neurosin: implication for pathogenesis of synucleinopathies. Hum. Mol. Genet.
12, 2625–2635 (2003).
Klucken, J., Shin, Y., Masliah, E., Hyman, B. T. & McLean, P. J.
Hsp70 reduces α-synuclein aggregation and toxicity. J. Biol. Chem.
279, 25497–25502 (2004).
McNaught, K. S.
et al. Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures. J. Neurochem.
81, 301–306 (2002).
McNaught, K. S.
et al. Proteasome inhibition causes nigral degeneration with inclusion bodies in rats. Neuroreport
13, 1437–1441 (2002).
Webb, J. L., Ravikumar, B., Atkins, J., Skepper, J. N. & Rubinsztein, D. C.
α-Synuclein is degraded by both autophagy and the proteasome. J. Biol. Chem.
278, 25009–25013 (2003).
Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T. & Sulzer, D.
Impaired degradation of mutant α-synuclein by chaperone-mediated autophagy. Science
305, 1292–1295 (2004). This paper identified lysosomes for degradation of wild-type α-syn by the chaperone-mediated autophagy pathway.
et al. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein. Proc. Natl Acad. Sci. USA
106, 13010–13015 (2009).
et al. Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in α-synuclein models of Parkinson's and Lewy body diseases. J. Neurosci.
29, 13578–13588 (2009).
et al. Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of α-synucleinopathy. PLoS ONE
5, e9313 (2010).
Diffuse Lewy body disease in Japan. J. Neurol.
237, 197–204 (1990).
Dickson, D. W.
et al. Diffuse Lewy body disease: light and electron microscopic immunocytochemistry of senile plaques. Acta Neuropathol.
78, 572–584 (1989).
Braak, H., Sastre, M. & Del Tredici, K.
Development of α-synuclein immunoreactive astrocytes in the forebrain parallels stages of intraneuronal pathology in sporadic Parkinson's disease. Acta Neuropathol.
114, 231–241 (2007). Paper reporting the association of α-syn with reactive astrocytes in clinically diagnosed PD cases.
Lee, H. J.
et al. Direct transfer of α-synuclein from neuron to astroglia causes inflammatory responses in synucleinopathies. J. Biol. Chem.
285, 9262–9272 (2010).
Kahle, P. J.
et al. Selective insolubility of α-synuclein in human Lewy body diseases is recapitulated in a transgenic mouse model. Am. J. Pathol.
159, 2215–2225 (2001).
et al. Aggregation of α-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies. Am. J. Pathol.
152, 879–884 (1998).
Lee, M. K.
et al. Human α-synuclein-harboring familial Parkinson's disease-linked Ala-53 → Thr mutation causes neurodegenerative disease with α-synuclein aggregation in transgenic mice. Proc. Natl Acad. Sci. USA
99, 8968–8973 (2002).
Tsigelny, I. F.
et al. Role of α-synuclein penetration into the membrane in the mechanisms of oligomer pore formation. FEBS J.
279, 1000–1013 (2012). Computational modelling shows that α-synuclein can form ring-like structures that penetrate the membrane.
Bellucci, A., Navarria, L., Zaltieri, M., Missale, C. & Spano, P.
α-synuclein synaptic pathology and its implications in the development of novel therapeutic approaches to cure Parkinson's disease. Brain Res.
1432, 95–113 (2012).
Schulz-Schaeffer, W. J.
The synaptic pathology of α-synuclein aggregation in dementia with Lewy bodies, Parkinson's disease and Parkinson's disease dementia. Acta Neuropathol.
120, 131–143 (2010).
et al. SNARE protein redistribution and synaptic failure in a transgenic mouse model of Parkinson's disease. Brain
133, 2032–2044 (2010).
et al. Mechanisms of protein oligomerization: inhibitor of functional amyloids templates α-synuclein fibrillation. J. Am. Chem. Soc.
134, 3439–3444 (2012).
Conway, K. A.
et al. Accelerated oligomerization by Parkinson's disease linked α-synuclein mutants. Ann. NY Acad. Sci.
920, 42–45 (2000).
et al. Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell
149, 1048–1059 (2012).
Danzer, K. M.
et al. Different species of α-synuclein oligomers induce calcium influx and seeding. J. Neurosci.
27, 9220–9232 (2007).
Pathological biochemistry of α-synucleinopathy. Neuropathology
27, 474–478 (2007).
Oueslati, A., Paleologou, K. E., Schneider, B. L., Aebischer, P. & Lashuel, H. A.
Mimicking phosphorylation at serine 87 inhibits the aggregation of human α-synuclein and protects against its toxicity in a rat model of Parkinson's disease. J. Neurosci.
32, 1536–1544 (2012).
Souza, J. M., Giasson, B. I., Chen, Q., Lee, V. M. & Ischiropoulos, H.
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, 18344–18349 (2000).
Uversky, V. N., Li, J. & Fink, A. L.
Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein — a possible molecular link between Parkinson's disease and heavy metal exposure. J. Biol. Chem.
276, 44284–44296 (2001).
Conway, K. A., Rochet, J. C., Bieganski, R. M. & Lansbury, P. T. Jr.
Kinetic stabilization of the α-synuclein protofibril by a dopamine-α-synuclein adduct. Science
294, 1346–1349 (2001).
Conway, K. A.
et al. Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl Acad. Sci. USA
97, 571–576 (2000).
Hsu, L. J.
et al. α-synuclein promotes mitochondrial deficit and oxidative stress. Am. J. Pathol.
157, 401–410 (2000).
et al. The role of α-synuclein assembly and metabolism in the pathogenesis of Lewy body disease. J. Mol. Neurosci.
24, 343–352 (2004).
Alim, M. A.
et al. Demonstration of a role for α-synuclein as a functional microtubule-associated protein. J. Alzheimers Dis.
6, 435–442 (2004).
da Silveira, S. A.
et al. Phosphorylation does not prompt, nor prevent, the formation of α-synuclein toxic species in a rat model of Parkinson's disease. Hum. Mol. Genet.
18, 872–887 (2009).
Gorbatyuk, O. S.
et al. The phosphorylation state of Ser-129 in human α-synuclein determines neurodegeneration in a rat model of Parkinson disease. Proc. Natl Acad. Sci. USA
105, 763–768 (2008).
et al. In vivo demonstration that α-synuclein oligomers are toxic. Proc. Natl Acad. Sci. USA
108, 4194–4199 (2011).
et al. Aβ42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Aβ42 species. J. Biol. Chem.
286, 8585–8596 (2011).
et al. Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death. J. Neurosci.
25, 1071–1080 (2005).
et al. Accumulation of toxic α-synuclein oligomer within endoplasmic reticulum occurs in α-synucleinopathy in vivo. J. Neurosci.
32, 3301–3305 (2012).
et al. Non-classical exocytosis of α-synuclein is sensitive to folding states and promoted under stress conditions. J. Neurochem.
113, 1263–1274 (2010).
Danzer, K. M.
et al. Heat-shock protein 70 modulates toxic extracellular α-synuclein oligomers and rescues trans-synaptic toxicity. FASEB J.
25, 326–336 (2011).
et al. Lysosomal dysfunction increases exosome-mediated α-synuclein release and transmission. Neurobiol. Dis.
42, 360–367 (2011).
Lee, H. J.
et al. Assembly-dependent endocytosis and clearance of extracellular α-synuclein. Int. J. Biochem. Cell. Biol.
40, 1835–1849 (2008).
et al. Cell-produced α-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival. J. Neurosci.
30, 6838–6851 (2010). The first report that α-syn is secreted by externalized vesicles in a calcium-dependent manner.
Jao, C. C., Hegde, B. G., Chen, J., Haworth, I. S. & Langen, R.
Structure of membrane-bound α-synuclein from site-directed spin labeling and computational refinement. Proc. Natl Acad. Sci. USA
105, 19666–19671 (2008).
Volpicelli-Daley, L. A.
et al. Exogenous α-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death. Neuron
72, 57–71 (2011).
et al. α-synuclein alters Notch-1 expression and neurogenesis in mouse embryonic stem cells and in the hippocampus of transgenic mice. J. Neurosci.
28, 4250–4260 (2008).
Letarov, A., Manival, X., Desplats, C. & Krisch, H. M.
gpwac of the T4-type bacteriophages: structure, function, and evolution of a segmented coiled-coil protein that controls viral infectivity. J. Bacteriol.
187, 1055–1066 (2005).
et al. The specific monocarboxylate transporter-1 (MCT-1) inhibitor, AR-C117977, induces donor-specific suppression, reducing acute and chronic allograft rejection in the rat. Transplantation
84, 1191–1199 (2007).
Karlsson, J., Petersen, A., Gido, G., Wieloch, T. & Brundin, P.
Combining neuroprotective treatment of embryonic nigral donor tissue with mild hypothermia of the graft recipient. Cell Transplant.
14, 301–309 (2005).
Karlsson, J., Emgard, M., Gido, G., Wieloch, T. & Brundin, P.
Increased survival of embryonic nigral neurons when grafted to hypothermic rats. Neuroreport
11, 1665–1668 (2000).
Frodl, E. M., Duan, W. M., Sauer, H., Kupsch, A. & Brundin, P.
Human embryonic dopamine neurons xenografted to the rat: effects of cryopreservation and varying regional source of donor cells on transplant survival, morphology and function. Brain Res.
647, 286–298 (1994).
Kordower, J. H., Freeman, T. B. & Olanow, C. W.
Neuropathology of fetal nigral grafts in patients with Parkinson's disease. Mov. Disord.
13, 88–95 (1998).
et al. Forkhead box protein p1 is a transcriptional repressor of immune signaling in the CNS: implications for transcriptional dysregulation in Huntington disease. Hum. Mol. Genet.
21, 3097–3111 (2012).
Nonaka, T., Watanabe, S. T., Iwatsubo, T. & Hasegawa, M.
Seeded aggregation and toxicity of α-synuclein and tau: cellular models of neurodegenerative diseases. J. Biol. Chem.
285, 34885–34898 (2010).
Luk, K. C.
et al. Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice. J. Exp. Med.
209, 975–986 (2012).
et al. Direct observation of Aβ amyloid fibril growth and inhibition. J. Mol. Biol.
344, 757–767 (2004).
Lashuel, H. A.
et al. New class of inhibitors of amyloid-β fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease. J. Biol. Chem.
277, 42881–42890 (2002).
Di Giovanni, S.
et al. Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of α-synuclein and β-amyloid and protect against amyloid-induced toxicity. J. Biol. Chem.
285, 14941–14954 (2010).
et al. Small molecule inhibitors of α-synuclein filament assembly. Biochemistry
45, 6085–6094 (2006).
Porat, Y., Abramowitz, A. & Gazit, E.
Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism. Chem. Biol. Drug Des.
67, 27–37 (2006).
et al. Oligomeric-induced activity by thienyl pyrimidine compounds traps prion infectivity. J. Neurosci.
31, 14882–14892 (2011).
Hirohata, M., Ono, K., Morinaga, A. & Yamada, M.
Non-steroidal anti-inflammatory drugs have potent anti-fibrillogenic and fibril-destabilizing effects for α-synuclein fibrils in vitro. Neuropharmacology
54, 620–627 (2008).
Bartels, T., Choi, J. G. & Selkoe, D. J.
α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature
477, 107–110 (2011).
et al. A soluble α-synuclein construct forms a dynamic tetramer. Proc. Natl Acad. Sci. USA
108, 17797–17802 (2011).
et al. Semisynthesis and characterization of N-terminally acetylated α-synuclein: implications for aggregation and cellular properties. J. Biol. Chem.
287, 28243–2862 (2012).
Shaikh, S. & Nicholson, L. F.
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, 2071–2082 (2008).
Hashimoto, M., Takeda, A., Hsu, L. J., Takenouchi, T. & Masliah, E.
Role of cytochrome c as a stimulator of α-synuclein aggregation in Lewy body disease. J. Biol. Chem.
274, 28849–28852 (1999).
Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T. & Lansbury, P. T. Jr.
Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature
418, 291 (2002).