Cell Biology and Pathophysiology of α-Synuclein

Proteomics Analysis Identifies Phosphorylation-dependent α-Synuclein Protein Interactions

McFarland, M. A., Ellis, C. E., Markey, S. P., & Nussbaum, R. L. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800116-mcp200 · Cited by 176

Fibrillization of ?-synuclein and tau in familial Parkinson's disease caused by the A53T ?-synuclein mutation

KOTZBAUER, P. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2004.01.007 · Cited by 176

CHIP Targets Toxic α-Synuclein Oligomers for Degradation

Tetzlaff, J. E., Putcha, P., Outeiro, T. F., Ivanov, A., Berezovska, O., Hyman, B. T., & McLean, P. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802283200 · Cited by 175

Monoubiquitylation of α-Synuclein by Seven in Absentia Homolog (SIAH) Promotes Its Aggregation in Dopaminergic Cells

Rott, R., Szargel, R., Haskin, J., Shani, V., Shainskaya, A., Manov, I., Liani, E., Avraham, E., & Engelender, S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m704809200 · Cited by 174

Lewy body in neurodegeneration with brain iron accumulation type 1 is immunoreactive for α-synuclein

Arawaka, S., Saito, Y., Murayama, S., & Mori, H. (1998) · Neurology · doi:10.1212/wnl.51.3.887 · Cited by 172

Stimulation of breast cancer invasion and metastasis by synuclein gamma.

Jia, T., Liu, Y. E., Liu, J., & Shi, Y. E. (1999) · PubMed · Cited by 171

A new brain‐specific 14‐kDa protein is a phosphoprotein: Its complete amino acid sequence and evidence for phosphorylation

NAKAJO, S., TSUKADA, K., OMATA, K., NAKAMURA, Y., & NAKAYA, K. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18337.x · Cited by 170

Expression Pattern of Synucleins (Non‐Aβ Component of Alzheimer's Disease Amyloid Precursor Protein/α‐Synuclein) During Murine Brain Development

Hsu, L. J., Mallory, M., Xia, Y., Veinbergs, I., Hashimoto, M., Yoshimoto, M., Thal, L. J., Saitoh, T., & Masliah, E. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71010338.x · Cited by 170

Ubiquitination of -synuclein by Siah-1 promotes -synuclein aggregation and apoptotic cell death

Lee, J. T., Wheeler, T. C., Li, L., & Chin, L.-S. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm363 · Cited by 170

Persyn, a Member of the Synuclein Family, Has a Distinct Pattern of Expression in the Developing Nervous System

Buchman, V. L., Hunter, H. J. A., Pinõn, L. G. P., Thompson, J., Privalova, E. M., Ninkina, N. N., & Davies, A. M. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-22-09335.1998 · Cited by 169

Characterization of Semisynthetic and Naturally Nα-Acetylated α-Synuclein in Vitro and in Intact Cells

Fauvet, B., Fares, M.-B., Samuel, F., Dikiy, I., Tandon, A., Eliezer, D., & Lashuel, H. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.383711 · Cited by 169

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(2000) · doi:10.1016/s0306-4522(00)00077-4 · Cited by 167

Nitration inhibits fibrillation of human α‐synuclein in vitro by formation of soluble oligomers

Yamin, G., Uversky, V. N., & Fink, A. L. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00367-3 · Cited by 167

N-Alpha-Acetylation of α-Synuclein Increases Its Helical Folding Propensity, GM1 Binding Specificity and Resistance to Aggregation

Bartels, T., Kim, N. C., Luth, E. S., & Selkoe, D. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103727 · Cited by 164

Increased striatal dopamine release and hyperdopaminergic‐like behaviour in mice lacking both alpha‐synuclein and gamma‐synuclein

Senior, S. L., Ninkina, N., Deacon, R., Bannerman, D., Buchman, V. L., Cragg, S. J., & Wade‐Martins, R. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06055.x · Cited by 164

Lrrk2 phosphorylates alpha synuclein at serine 129: Parkinson disease implications

Qing, H., Wong, W., McGeer, E. G., & McGeer, P. L. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.06.142 · Cited by 163

Structural and Functional Implications of C-Terminal Regions of α-Synuclein

Kim, T. D., Paik, S. R., & Yang, C.-H. (2002) · Biochemistry · doi:10.1021/bi026284c · Cited by 162

α-Synuclein immunoreactivity in dementia with Lewy bodies: morphological staging and comparison with ubiquitin immunostaining

Gómez-Tortosa, E., Newell, K., Irizarry, M. C., Sanders, J. L., & Hyman, B. T. (2000) · Acta Neuropathologica · doi:10.1007/s004010051135 · Cited by 162

α-Synuclein Is Phosphorylated by Members of the Src Family of Protein-tyrosine Kinases

Ellis, C. E., Schwartzberg, P. L., Grider, T. L., Fink, D. W., & Nussbaum, R. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010316200 · Cited by 161

DJ-1 interactions with α-synuclein attenuate aggregation and cellular toxicity in models of Parkinson’s disease

Zondler, L., Miller-Fleming, L., Repici, M., Gonçalves, S., Tenreiro, S., Rosado-Ramos, R., Betzer, C., Straatman, K. R., Jensen, P. H., Giorgini, F., et al. (2014) · Cell Death & Disease · doi:10.1038/cddis.2014.307 · Cited by 161

Distinct cleavage patterns of normal and pathologic forms of α‐synuclein by calpain I in vitro

Mishizen‐Eberz, A. J., Guttmann, R. P., Giasson, B. I., Day, G. A., Hodara, R., Ischiropoulos, H., Lee, V. M. ‐., Trojanowski, J. Q., & Lynch, D. R. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01878.x · Cited by 160

Alpha-synuclein degradation by serine protease neurosin: implication for pathogenesis of synucleinopathies

Iwata, A. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg283 · Cited by 159

The Newly Discovered Parkinson’s Disease Associated Finnish Mutation (A53E) Attenuates α-Synuclein Aggregation and Membrane Binding

Ghosh, D., Sahay, S., Ranjan, P., Salot, S., Mohite, G. M., Singh, P. K., Dwivedi, S., Carvalho, E., Banerjee, R., Kumar, A., et al. (2014) · Biochemistry · doi:10.1021/bi5010365 · Cited by 158

Impairment of microtubule‐dependent trafficking by overexpression of α‐synuclein

Lee, H., Khoshaghideh, F., Lee, S., & Lee, S. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.05210.x · Cited by 158

Co‐ordinate transcriptional regulation of dopamine synthesis genes by α‐synuclein in human neuroblastoma cell lines

Baptista, M. J., O’Farrell, C., Daya, S., Ahmad, R., Miller, D. W., Hardy, J., Farrer, M. J., & Cookson, M. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01742.x · Cited by 154

Loss of Epigenetic Control of Synuclein-γ Gene as a Molecular Indicator of Metastasis in a Wide Range of Human Cancers

Liu, H., Liu, W., Wu, Y., Zhou, Y., Xue, R., Luo, C., Wang, L., Zhao, W., Jiang, J., & Liu, J. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1089 · Cited by 154

α-synuclein phosphorylation and truncation are normal events in the adult human brain

Muntané, G., Ferrer, I., & Martínez‐Vicente, M. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.10.042 · Cited by 153

Bacterial in-cell NMR of human α-synuclein: a disordered monomer by nature?

Binolfi, A., Theillet, F., & Selenko, P. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120096 · Cited by 152

Curcumin protects against A53T alpha-synuclein-induced toxicity in a PC12 inducible cell model for Parkinsonism

Liu, Z., Yu, Y., Li, X., Ross, C. A., & Smith, W. W. (2011) · Pharmacological Research · doi:10.1016/j.phrs.2011.01.004 · Cited by 152

Helix periodicity, topology, and dynamics of membrane‐associated α‐Synuclein

Bussell, R., Ramlall, T. F., & Eliezer, D. (2005) · Protein Science · doi:10.1110/ps.041255905 · Cited by 147

α-Synuclein Interacts with Phospholipase D Isozymes and Inhibits Pervanadate-induced Phospholipase D Activation in Human Embryonic Kidney-293 Cells

Ahn, B., Rhim, H., Kim, S. Y., Sung, Y., Lee, M., Choi, J., Wolozin, B. L., Chang, J., Lee, Y. H., Kwon, T. K., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110414200 · Cited by 140

Alpha synuclein is present in Lewy bodies in sporadic Parkinson's disease

Mezey, É., Dehejia, A. M., Harta, G., Suchy, S. F., Nussbaum, R. L., Brownstein, M. J., & Polymeropoulos, M. H. (1998) · Molecular Psychiatry · doi:10.1038/sj.mp.4000446 · Cited by 139

Activated Fyn Phosphorylates α-Synuclein at Tyrosine Residue 125

Nakamura, T., Yamashita, H., Takahashi, T., & Nakamura, S. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.4253 · Cited by 138

The Expression of α-, β-, and γ-Synucleins in Olfactory Mucosa from Patients with and without Neurodegenerative Diseases

Duda, J. E., Shah, U., Arnold, S. E., Lee, V. M. ‐., & Trojanowski, J. Q. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7228 · Cited by 137

Ubiquitination of α-Synuclein

Nonaka, T., Iwatsubo, T., & Hasegawa, M. (2004) · Biochemistry · doi:10.1021/bi0485528 · Cited by 137

Allostery in a Disordered Protein: Oxidative Modifications to α-Synuclein Act Distally To Regulate Membrane Binding

Sevcsik, E., Trexler, A., Dunn, J. M., & Rhoades, E. R. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2009554 · Cited by 136

Increased Expression of Rat Synuclein in the Substantia Nigra Pars Compacta Identified by mRNA Differential Display in a Model of Developmental Target Injury

Kholodilov, N. G., Neystat, M., Tinmarla, F. O., Steven, E. L., Larsen, K. E., Sulzer, D., & Burke, R. E. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0732586.x · Cited by 136

Nuclear and neuritic distribution of serine-129 phosphorylated α-synuclein in transgenic mice

Schell, H., Hasegawa, T., Neumann, M., & Kahle, P. J. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.03.002 · Cited by 135

Paramagnetism-Based NMR Restraints Provide Maximum Allowed Probabilities for the Different Conformations of Partially Independent Protein Domains

Bertini, I., Gupta, Y. K., Luchinat, C., Parigi, G., Peana, M., Sgheri, L., & Yuan, J. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0726613 · Cited by 133

Preferentially Increased Nitration of α-Synuclein at Tyrosine-39 in a Cellular Oxidative Model of Parkinson’s Disease

Danielson, S. R., Held, J. M., Schilling, B., Oo, M. L., Gibson, B. W., & Andersen, J. K. (2009) · Analytical Chemistry · doi:10.1021/ac901176t · Cited by 130

Phosphorylation of α-synuclein characteristic of synucleinopathy lesions is recapitulated in α-synuclein transgenic Drosophila

Takahashi, M., Kanuka, H., Fujiwara, H., Koyama, A., Hasegawa, M., Miura, M., & Iwatsubo, T. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(02)01258-2 · Cited by 129

Expression of α-synuclein, a presynaptic protein implicated in Parkinson’s disease, in erythropoietic lineage

Nakai, M., Fujita, M., Waragai, M., Sugama, S., Wei, J., Akatsu, H., Ohtaka‐Maruyama, C., Okado, H., & Hashimoto, M. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.108 · Cited by 129

Hyperphosphorylated Tau in an α-synuclein-overexpressing transgenic model of Parkinson’s disease: Tauopathy in transgenic mice and PD

Haggerty, T., Credle, J. J., Rodriguez, O. C., Wills, J., Oaks, A. W., Masliah, E., & Sidhu, A. (2011) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2011.07660.x · Cited by 129

Methionine Sulfoxide Reductase A and a Dietary Supplement S -Methyl- L -Cysteine Prevent Parkinson's-Like Symptoms

Wassef, R., Haenold, R., Hansel, A., Brot, N., Heinemann, S. H., & Hoshi, T. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0322-07.2007 · Cited by 128

Structural changes in α‐synuclein affect its chaperone‐like activity in vitro

Kim, T. D., Paik, S. R., Yang, C., & Kim, J. (2000) · Protein Science · doi:10.1110/ps.9.12.2489 · Cited by 127

Signs of Degeneration in 12–22-Year Old Grafts of Mesencephalic Dopamine Neurons in Patients with Parkinson's Disease

Kurowska, Z., Englund, E. M., Widner, H., Lindvall, O., Li, J., & Brundin, P. (2011) · Journal of Parkinson s Disease · doi:10.3233/jpd-2011-11004 · Cited by 126

Developmental expression of α-synuclein in rat hippocampus and cerebral cortex

Petersen, K. L., Olesen, O. F., & Mikkelsen, J. D. (1999) · Neuroscience · doi:10.1016/s0306-4522(98)00596-x · Cited by 125

The Transgenic Overexpression of α-Synuclein and Not Its Related Pathology Associates with Complex I Inhibition

Loeb, V., Yakunin, E., Saada, A., & Sharon, R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.061051 · Cited by 124

Inhibition of tyrosine hydroxylase expression in α-synuclein-transfected dopaminergic neuronal cells

Yu, S., Zuo, X., Li, Y., Zhang, C., Zhou, M., Zhang, Y. A., Uéda, K., & Chan, P. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.05.118 · Cited by 123

Amino acid sequence motifs and mechanistic features of the membrane translocation of α‐synuclein

Ahn, K. J., Paik, S. R., Chung, K. C., & Kim, J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03731.x · Cited by 123

Binding of α-Synuclein Affects the Lipid Packing in Bilayers of Small Vesicles

Kamp, F., & Beyer, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512292200 · Cited by 123

Characterization of Conformational and Dynamic Properties of Natively Unfolded Human and Mouse α-Synuclein Ensembles by NMR: Implication for Aggregation

Wu, K., Kim, S., Fela, D. A., & Baum, J. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.03.017 · Cited by 122

Multiple phosphorylation of α‐synuclein by protein tyrosine kinase Syk prevents eosin‐induced aggregation

Negro, A., Brunati, A. M., Donella‐Deana, A., Massimino, M. L., & Pinna, L. A. (2001) · The FASEB Journal · doi:10.1096/fj.01-0517fje · Cited by 121

Oral N-Acetyl-Cysteine Attenuates Loss of Dopaminergic Terminals in α-Synuclein Overexpressing Mice

Clark, J., Clore, E. L., Zheng, K., Adame, A., Masliah, E., & Simon, D. K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012333 · Cited by 121

Dyrk1A Phosphorylates α-Synuclein and Enhances Intracellular Inclusion Formation

Kim, E. J., Sung, J. Y., Lee, H. J., Rhim, H., Hasegawa, M., Iwatsubo, T., Min, D. S., Kim, J., Paik, S. R., & Chung, K. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606147200 · Cited by 120

NACP, a Synaptic Protein Involved in Alzheimer's Disease, Is Differentially Regulated during Megakaryocyte Differentiation

Hashimoto, M., Yoshimoto, M., Sisk, A., Hsu, L. J., Sundsmo, M. P., Kittel, Á., Saitoh, T., Miller, A. L., & Masliah, E. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6978 · Cited by 120

Persyn, a member of the synuclein family, influences neurofilament network integrity

Buchman, V. L., Adu, J., Piñón, L. G. P., Ninkina, N. N., & Davies, A. M. (1998) · Nature Neuroscience · doi:10.1038/349 · Cited by 119

Synphilin-1 Is Developmentally Localized to Synaptic Terminals, and Its Association with Synaptic Vesicles Is Modulated by α-Synuclein

Ribeiro, C. S., Carneiro, K., Ross, C. A., Menezes, J. R. L., & Engelender, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201115200 · Cited by 119

Localization of a novel type trypsin‐like serine protease, neurosin, in brain tissues of Alzheimer's disease and Parkinson's disease

Ogawa, K., Yamada, T., Tsujioka, Y., Taguchi, J., Takahashi, M., Tsuboi, Y., Fujino, Y., Nakajima, M., Yamamoto, T., Akatsu, H., et al. (2000) · Psychiatry and Clinical Neurosciences · doi:10.1046/j.1440-1819.2000.00731.x · Cited by 116

α-Synuclein Membrane Association Is Regulated by the Rab3a Recycling Machinery and Presynaptic Activity*

Chen, R. H., Wislet‐Gendebien, S., Samuel, F., Visanji, N. P., Zhang, G., Marsilio, D., Langman, T., Fraser, P. E., & Tandon, A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.439497 · Cited by 116

Serine 129 Phosphorylation Reduces the Ability of α-Synuclein to Regulate Tyrosine Hydroxylase and Protein Phosphatase 2A in Vitro and in Vivo

Lou, H., Montoya, S. E., Alerte, T. N. M., Wang, J., Wu, J., Peng, X., Hong, C.-S., Friedrich, E. E., Mader, S. A., Pedersen, C. J., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.100867 · Cited by 115

Oxidative stress‐induced phosphorylation, degradation and aggregation of α‐synuclein are linked to upregulated CK2 and cathepsin D

Takahashi, M., Ko, L., Kulathingal, J., Jiang, P., Sevlever, D., & Yen, S.-H. C. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05736.x · Cited by 114

Activity‐dependent secretion of alpha‐synuclein by enteric neurons

Paillusson, S., Clairembault, T., Biraud, M., Neunlist, M., & Derkinderen, P. (2012) · Journal of Neurochemistry · doi:10.1111/jnc.12131 · Cited by 110

Superoxide dismutase overexpression protects dopaminergic neurons in a Drosophila model of Parkinson's disease

Botella, J., Bayersdorfer, F., & Schneuwly, S. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.11.013 · Cited by 110

Conversion of Wild-type α-Synuclein into Mutant-type Fibrils and Its Propagation in the Presence of A30P Mutant

Yonetani, M., Nonaka, T., Masuda, M., Inukai, Y., Oikawa, T., Hisanaga, S., & Hasegawa, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807482200 · Cited by 109

Ribosylation Rapidly Induces α-Synuclein to Form Highly Cytotoxic Molten Globules of Advanced Glycation End Products

Chen, L., Yan, W., Wang, X., & He, R. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009052 · Cited by 108

Purification and Characterization of a Novel Brain‐Specific 14‐kDa Protein

Nakajo, S., Omata, K., Aiuchi, T., Shibayama, T., Okahashi, I., Ochiai, H., Nakai, Y., Nakaya, K., & Nakamura, Y. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb05792.x · Cited by 108

Organization, expression and polymorphism of the human persyn gene

Ninkina, N. N., Alimova-Kost, M. V., Paterson, J. W., Delaney, L., Cohen, B. B., Imreh, S., Gnuchev, N. V., Davies, A. M., & Buchman, V. L. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.9.1417 · Cited by 108

Antiparallel Arrangement of the Helices of Vesicle-Bound α-Synuclein

Drescher, M., Veldhuis, G., van Rooijen, B. D., Milikisyants, S., Subramaniam, V., & Huber, M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja801594s · Cited by 106

α-Synuclein: Multiple System Atrophy PrionsPreprint

Woerman, A. L., Watts, J. C., Aoyagi, A., Giles, K., Middleton, L. T., & Prusiner, S. B. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024588 · Cited by 106

Novel Immunolocalization of α-Synuclein in Human Muscle of Inclusion-Body Myositis, Regenerating and Necrotic Muscle Fibers, and at Neuromuscular Junctions

Askanas, V., Engel, W. K., Alvarez, R. B., McFerrin, J., & Broccolini, A. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.7.592 · Cited by 104

Alterations in corticostriatal synaptic plasticity in mice overexpressing human α-synuclein

Watson, J. B., Hatami, A., David, H., Masliah, E., Roberts, K., Evans, C., & Levine, M. S. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.01.021 · Cited by 103

Chaperone-mediated autophagy in aging and neurodegeneration: Lessons from α-synuclein

Bandyopadhyay, U., & Cuervo, A. M. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.05.019 · Cited by 103

γ‐Synuclein and the progression of cancer

Ahmad, M., Attoub, S., Singh, M. N., Martin, F. L., & El‐Agnaf, O. M. A. (2007) · The FASEB Journal · doi:10.1096/fj.07-8379rev · Cited by 103

Inhibition of Vesicular Monoamine Transporter-2 Activity in α-Synuclein Stably Transfected SH-SY5Y Cells

Guo, J. T., Chen, A. Q., Kong, Q., Zhu, H., Ma, C. M., & Qin, C. (2007) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-007-9227-0 · Cited by 102

Casein kinase 2 is the major enzyme in brain that phosphorylates Ser129 of human α‐synuclein: Implication for α‐synucleinopathies

Ishii, A., Nonaka, T., Taniguchi, S., Saito, T., Arai, T., Mann, D. M. A., Iwatsubo, T., Hisanaga, S., Goedert, M., & Hasegawa, M. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.08.067 · Cited by 101

Acute increase of α-synuclein inhibits synaptic vesicle recycling evoked during intense stimulation

Busch, D. J., Oliphint, P. A., Walsh, R. B., Banks, S. M. L., Woods, W. S., George, J. M., & Morgan, J. R. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-02-0708 · Cited by 101

Localization of phosphoneuroprotein 14 (PNP 14) and its mRNA expression in rat brain determined by immunocytochemistry and in situ hybridization

Nakajo, S., Shioda, S., Nakai, Y., & Nakaya, K. (1994) · Molecular Brain Research · doi:10.1016/0169-328x(94)90187-2 · Cited by 100

Role of α-synuclein in synaptic glutamate release

Gureviciene, I., Gurevicius, K., & Tanila, H. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.06.016 · Cited by 99

Structural Determinants of PLD2 Inhibition by α-Synuclein

Payton, J. E., Perrin, R. J., Woods, W. S., & George, J. M. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.014 · Cited by 99

The modification of α-synuclein by dicarbonyl compounds inhibits its fibril-forming process

Lee, D., Park, C. W., Paik, S. R., & Choi, K. Y. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.11.016 · Cited by 99

α‐Synuclein induces apoptosis by altered expression in human peripheral lymphocytes in Parkinson’s disease

Kim, S., Jeon, B. S., Heo, C., Im, P. S., Ahn, T., Seo, J., Kim, H., Park, C. H., Choi, S. H., Cho, S., et al. (2004) · The FASEB Journal · doi:10.1096/fj.04-1917fje · Cited by 99

Abnormal α-Synuclein Interactions with Rab Proteins in α-Synuclein A30P Transgenic Mice

Dalfó, E., Gómez‐Isla, T., Rosa, J. L., Bodelón, M. N., Tejedor, M. C., Barrachina, M., Ambrosio, S., & Ferrer, I. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.4.302 · Cited by 98

Expression Patterns of α-Synuclein in Human Hematopoietic Cells and in Drosophila at Different Developmental Stages

Shin, E., Cho, S. E., Lee, D.-K., Hur, M., Paik, S. R., Park, J. H., & Kim, J. (2000) · Molecules and Cells · doi:10.1007/s10059-000-0065-x · Cited by 97

Tyrosine 125 of α-synuclein plays a critical role for dimerization following nitrative stress

Takahashi, T., Yamashita, H., Nakamura, T., Nagano, Y., & Nakamura, S. (2002) · Brain Research · doi:10.1016/s0006-8993(02)02498-8 · Cited by 97

Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation

Kim, Y. M., Jang, W. H., Quezado, M., Oh, Y., Chung, K. C., Junn, E., & Mouradian, M. M. (2011) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2011.04.015 · Cited by 96

Advanced glycation end products induce in vitro cross‐linking of α‐synuclein and accelerate the process of intracellular inclusion body formation

Shaikh, S. B., & Nicholson, L. F. B. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21644 · Cited by 95

Increased α-synuclein aggregation following limited cleavage by certain matrix metalloproteinases

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Double-stranded DNA Stimulates the Fibrillation of α-Synuclein in vitro and is Associated with the Mature Fibrils: An Electron Microscopy Study

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Interplay between Sumoylation and Phosphorylation for Protection against α-Synuclein Inclusions

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Role of Advanced Glycation on Aggregation and DNA Binding Properties of α-Synuclein

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Molecular interaction of α-synuclein with tubulin influences on the polymerization of microtubule in vitro and structure of microtubule in cells

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Aggregation of α-Synuclein in S. cerevisiae is Associated with Defects in Endosomal Trafficking and Phospholipid Biosynthesis

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Alpha‐synuclein overexpression in mice alters synaptic communication in the corticostriatal pathway

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Abnormal compartmentalization of norepinephrine in mouse dentate gyrus in α‐synuclein knockout and A30P transgenic mice

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Cloning and Characterization of the cDNA Encoding a Novel Brain‐Specific 14‐kDa Protein

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Four Copies of SNCA Responsible for Autosomal Dominant Parkinson’s Disease in Two Italian Siblings

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O‐GlcNAc Modification Prevents Peptide‐Dependent Acceleration of α‐Synuclein Aggregation

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α-Synuclein Expression Levels Do Not Significantly Affect Proteasome Function and Expression in Mice and Stably Transfected PC12 Cell Lines

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α-Synuclein Expression in Rat Substantia Nigra Suppresses Phospholipase D2 Toxicity and Nigral Neurodegeneration

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Stress-Induced Aggregation Profiles of GST−α-Synuclein Fusion Proteins: Role of the C-Terminal Acidic Tail of α-Synuclein in Protein Thermosolubility and Stability

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α-Synuclein binding to rab3a in multiple system atrophy

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Parkinson Disease Epidemiology, Pathology, Genetics, and Pathophysiology

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