Cell Biology and Pathophysiology of α-Synuclein

α-Synuclein in Lewy bodies

Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382

Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease

Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240

α-Synuclein Locus Triplication Causes Parkinson's Disease

Singleton, A. B., Farrer, M., Johnson, J., Singleton, A., Hague, S., Kachergus, J., Hulihan, M., Peuralinna, T., Dutra, A., Nussbaum, R., et al. (2003) · Science · doi:10.1126/science.1090278 · Cited by 4,383

AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease

Krüger, R., Kuhn, W., Müller, T., Woitalla, D., Graeber, M., Kösel, S., Przuntek, H., Epplen, J. T., Schols, L., & Riess, O. (1998) · Nature Genetics · doi:10.1038/ng0298-106 · Cited by 3,836

α-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies

Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., & Goedert, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6469 · Cited by 2,868

The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementia

Zarranz, J. J., Alegre, J., Gómez‐Esteban, J. C., Lezcano, E., Ros, R., Ampuero, I., Vidal, L., Hoenicka, J., Rodriguez, O., Atarés, B., et al. (2004) · Annals of Neurology · doi:10.1002/ana.10795 · Cited by 2,737

Stages in the development of Parkinson’s disease-related pathology

Braak, H., Ghebremedhin, E., Rüb, U., Bratzke, H., & Del Tredici, K. (2004) · Cell and Tissue Research · doi:10.1007/s00441-004-0956-9 · Cited by 2,689

Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice

Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563

α-Synuclein is phosphorylated in synucleinopathy lesions

Fujiwara, H., Hasegawa, M., Dohmae, N., Kawashima, A., Masliah, E., Goldberg, M. S., Shen, J., Takio, K., & Iwatsubo, T. (2002) · Nature Cell Biology · doi:10.1038/ncb748 · Cited by 2,132

Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy

Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024

Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024

Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation

Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845

α-Synuclein Promotes SNARE-Complex Assembly in Vivo and in Vitro

Burré, J., Sharma, M., Tsetsenis, T., Buchman, V., Etherton, M. R., & Südhof, T. C. (2010) · Science · doi:10.1126/science.1195227 · Cited by 1,812

Transmission and spreading of tauopathy in transgenic mouse brain

Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803

Dopaminergic Loss and Inclusion Body Formation in α-Synuclein Mice: Implications for Neurodegenerative Disorders

Masliah, E., Rockenstein, E., Veinbergs, I., Mallory, M., Hashimoto, M., Takeda, A., Sagara, Y., Sisk, A., & Mucke, L. (2000) · Science · doi:10.1126/science.287.5456.1265 · Cited by 1,765

Mice Lacking α-Synuclein Display Functional Deficits in the Nigrostriatal Dopamine System

Abeliovich, A., Schmitz, Y., Fariñas, I., Choi-Lundberg, D., Ho, W.-H., Castillo, P. E., Shinsky, N., Verdugo, J. M. G., Armanini, M., Ryan, A., et al. (2000) · Neuron · doi:10.1016/s0896-6273(00)80886-7 · Cited by 1,722

Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils

Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687

Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal

Maroteaux, L., Campanelli, J., & Scheller, R. (1988) · The Journal of Neuroscience · doi:10.1523/jneurosci.08-08-02804.1988 · Cited by 1,641

Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies.

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Stabilization of α-Synuclein Secondary Structure upon Binding to Synthetic Membranes

Davidson, W. S., Jonas, A., Clayton, D. F., & George, J. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9443 · Cited by 1,585

The ubiquitin pathway in Parkinson's disease

Leroy, E., Boyer, R., Auburger, G., Leube, B., Ulm, G., Mezey, E., Harta, G., Brownstein, M. J., Jonnalagada, S., Chernova, T., et al. (1998) · Nature · doi:10.1038/26652 · Cited by 1,571

Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death

Volpicelli-Daley, L. A., Luk, K. C., Patel, T. P., Tanik, S. A., Riddle, D. M., Stieber, A., Meaney, D. F., Trojanowski, J. Q., & Lee, V. M.-Y. (2011) · Neuron · doi:10.1016/j.neuron.2011.08.033 · Cited by 1,569

Oxidative Damage Linked to Neurodegeneration by Selective α-Synuclein Nitration in Synucleinopathy Lesions

Giasson, B. I., Duda, J. E., Murray, I. V. J., Chen, Q., Souza, J. M., Hurtig, H. I., Ischiropoulos, H., Trojanowski, J. Q., & -Y. Lee, V. M. (2000) · Science · doi:10.1126/science.290.5493.985 · Cited by 1,546

NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively Unfolded

Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A., & Lansbury, P. T. (1996) · Biochemistry · doi:10.1021/bi961799n · Cited by 1,523

Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease

Conway, K. A., Harper, J. D., & Lansbury, P. T. (1998) · Nature Medicine · doi:10.1038/3311 · Cited by 1,499

Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein

Desplats, P., Lee, H.-J., Bae, E.-J., Patrick, C., Rockenstein, E., Crews, L., Spencer, B., Masliah, E., & Lee, S.-J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903691106 · Cited by 1,485

Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.

Uéda, K., Fukushima, H., Masliah, E., Xia, Y., Iwai, A., Yoshimoto, M., Otero, D. A., Kondo, J., Ihara, Y., & Saitoh, T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11282 · Cited by 1,480

α-Synuclein Is Degraded by Both Autophagy and the Proteasome

Webb, J. L., Ravikumar, B., Atkins, J., Skepper, J. N., & Rubinsztein, D. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300227200 · Cited by 1,429

Phosphorylation of Ser-129 Is the Dominant Pathological Modification of α-Synuclein in Familial and Sporadic Lewy Body Disease

Anderson, J. P., Walker, D. E., Goldstein, J. M., de Laat, R., Banducci, K., Caccavello, R. J., Barbour, R., Huang, J., Kling, K., Lee, M., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600933200 · Cited by 1,416

α-Synuclein Blocks ER-Golgi Traffic and Rab1 Rescues Neuron Loss in Parkinson's Models

Cooper, A. A., Gitler, A. D., Cashikar, A., Haynes, C. M., Hill, K. J., Bhullar, B., Liu, K., Xu, K., Strathearn, K. E., Liu, F., et al. (2006) · Science · doi:10.1126/science.1129462 · Cited by 1,376

The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system

Iwai, A., Masliah, E., Yoshimoto, M., Ge, N., Flanagan, L., Rohan de Silva, H. A., Kittel, A., & Saitoh, T. (1995) · Neuron · doi:10.1016/0896-6273(95)90302-x · Cited by 1,316

Aggregated α‐synuclein activates microglia: a process leading to disease progression in Parkinson's disease

Zhang, W., Wang, T., Pei, Z., Miller, D. S., Wu, X., Block, M. L., Wilson, B., Zhang, W., Zhou, Y., Hong, J.-S., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-2751com · Cited by 1,265

α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

Bartels, T., Choi, J. G., & Selkoe, D. J. (2011) · Nature · doi:10.1038/nature10324 · Cited by 1,263

Propagation of Tau Misfolding from the Outside to the Inside of a Cell

Frost, B., Jacks, R. L., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808759200 · Cited by 1,252

Cell-produced α-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival

Emmanouilidou, E., Melachroinou, K., Roumeliotis, T., Garbis, S. D., Ntzouni, M., Margaritis, L. H., Stefanis, L., & Vekrellis, K. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5699-09.2010 · Cited by 1,115

Conformational properties of α-synuclein in its free and lipid-associated states 1 1Edited by P. E. Wright

Eliezer, D., Kutluay, E., Bussell, R., & Browne, G. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4538 · Cited by 1,090

Mitochondrial Import and Accumulation of α-Synuclein Impair Complex I in Human Dopaminergic Neuronal Cultures and Parkinson Disease Brain

Devi, L., Raghavendran, V., Prabhu, B. M., Avadhani, N. G., & Anandatheerthavarada, H. K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710012200 · Cited by 1,080

Identification of two distinct synucleins from human brain

Jakes, R., Spillantini, M. G., & Goedert, M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00395-5 · Cited by 1,080

Sirtuin 2 Inhibitors Rescue α-Synuclein-Mediated Toxicity in Models of Parkinson's Disease

Outeiro, T. F., Kontopoulos, E., Altmann, S. M., Kufareva, I., Strathearn, K. E., Amore, A. M., Volk, C. B., Maxwell, M. M., Rochet, J.-C., McLean, P. J., et al. (2007) · Science · doi:10.1126/science.1143780 · Cited by 1,062

Increased Expression of α-Synuclein Reduces Neurotransmitter Release by Inhibiting Synaptic Vesicle Reclustering after Endocytosis

Nemani, V. M., Lu, W., Berge, V., Nakamura, K., Onoa, B., Lee, M. K., Chaudhry, F. A., Nicoll, R. A., & Edwards, R. H. (2010) · Neuron · doi:10.1016/j.neuron.2009.12.023 · Cited by 1,056

Causal relation between α-synuclein locus duplication as a cause of familial Parkinson's disease

Ibáñez, P., Bonnet, A.-M., Débarges, B., Lohmann, E., Tison, F., Agid, Y., Dürr, A., Brice, A., & Pollak, P. (2004) · The Lancet · doi:10.1016/s0140-6736(04)17104-3 · Cited by 1,044

α-Synuclein Cooperates with CSPα in Preventing Neurodegeneration

Chandra, S., Gallardo, G., Fernández-Chacón, R., Schlüter, O. M., & Südhof, T. C. (2005) · Cell · doi:10.1016/j.cell.2005.09.028 · Cited by 966

Structure and Dynamics of Micelle-bound Human α-Synuclein

Ulmer, T. S., Bax, A., Cole, N. B., & Nussbaum, R. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411805200 · Cited by 966

Imputation of sequence variants for identification of genetic risks for Parkinson's disease: a meta-analysis of genome-wide association studies

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Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein

Giasson, B. I., Forman, M. S., Higuchi, M., Golbe, L. I., Graves, C. L., Kotzbauer, P. T., Trojanowski, J. Q., & Lee, V. M.-Y. (2003) · Science · doi:10.1126/science.1082324 · Cited by 879

Structural disorder of monomeric α-synuclein persists in mammalian cells

Theillet, F.-X., Binolfi, A., Bekei, B., Martorana, A., Rose, H. M., Stuiver, M., Verzini, S., Lorenz, D., van Rossum, M., Goldfarb, D., et al. (2016) · Nature · doi:10.1038/nature16531 · Cited by 868

Prion-like spreading of pathological α-synuclein in brain

Masuda-Suzukake, M., Nonaka, T., Hosokawa, M., Oikawa, T., Arai, T., Akiyama, H., Mann, D. M. A., & Hasegawa, M. (2013) · Brain · doi:10.1093/brain/awt037 · Cited by 867

Synaptic Vesicle Depletion Correlates with Attenuated Synaptic Responses to Prolonged Repetitive Stimulation in Mice Lacking α-Synuclein

Cabin, D. E., Shimazu, K., Murphy, D., Cole, N. B., Gottschalk, W., McIlwain, K. L., Orrison, B., Chen, A., Ellis, C. E., Paylor, R., et al. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-20-08797.2002 · Cited by 865

Characterization of a novel protein regulated during the critical period for song learning in the zebra finch

George, J. M., Jin, H., Woods, W. S., & Clayton, D. F. (1995) · Neuron · doi:10.1016/0896-6273(95)90040-3 · Cited by 844

α-Synuclein impairs macroautophagy: implications for Parkinson’s disease

Winslow, A. R., Chen, C.-W., Corrochano, S., Acevedo-Arozena, A., Gordon, D. E., Peden, A. A., Lichtenberg, M., Menzies, F. M., Ravikumar, B., Imarisio, S., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201003122 · Cited by 825

α-Synuclein, Especially the Parkinson's Disease-associated Mutants, Forms Pore-like Annular and Tubular Protofibrils

Lashuel, H. A., Petre, B. M., Wall, J., Simon, M., Nowak, R. J., Walz, T., & Lansbury, P. T. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00735-0 · Cited by 805

Intravesicular Localization and Exocytosis of α-Synuclein and its Aggregates

Lee, H.-J., Patel, S., & Lee, S.-J. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.0692-05.2005 · Cited by 797

Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein

Bertoncini, C. W., Jung, Y.-S., Fernandez, C. O., Hoyer, W., Griesinger, C., Jovin, T. M., & Zweckstetter, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407146102 · Cited by 790

The UCH-L1 Gene Encodes Two Opposing Enzymatic Activities that Affect α-Synuclein Degradation and Parkinson's Disease Susceptibility

Liu, Y., Fallon, L., Lashuel, H. A., Liu, Z., & Lansbury, P. T. (2002) · Cell · doi:10.1016/s0092-8674(02)01012-7 · Cited by 785

The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and disease

Clayton, D. F., & George, J. M. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(97)01213-7 · Cited by 779

Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation

Serpell, L. C., Berriman, J., Jakes, R., Goedert, M., & Crowther, R. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.9.4897 · Cited by 748

Detection of oligomeric forms of α‐synuclein protein in human plasma as a potential biomarker for Parkinson's disease

El‐Agnaf, O. M. A., Salem, S. A., Paleologou, K. E., Curran, M. D., Gibson, M. J., Court, J. A., Schlossmacher, M. G., & Allsop, D. (2006) · The FASEB Journal · doi:10.1096/fj.03-1449com · Cited by 715

α-Synuclein Promotes Mitochondrial Deficit and Oxidative Stress

Hsu, L. J., Sagara, Y., Arroyo, A., Rockenstein, E., Sisk, A., Mallory, M., Wong, J., Takenouchi, T., Hashimoto, M., & Masliah, E. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64553-1 · Cited by 714

Both Familial Parkinson's Disease Mutations Accelerate α-Synuclein Aggregation

Narhi, L., Wood, S. J., Steavenson, S., Jiang, Y., Wu, G. M., Anafi, D., Kaufman, S. A., Martin, F., Sitney, K., Denis, P., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9843 · Cited by 710

Mitochondrial dysfunction in Parkinson's disease

Winklhofer, K. F., & Haass, C. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.08.013 · Cited by 688

Parkinson's Disease α-Synuclein Transgenic Mice Develop Neuronal Mitochondrial Degeneration and Cell Death

Martin, L. J., Pan, Y., Price, A. C., Sterling, W., Copeland, N. G., Jenkins, N. A., Price, D. L., & Lee, M. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4308-05.2006 · Cited by 684

The Herbicide Paraquat Causes Up-regulation and Aggregation of α-Synuclein in Mice

Manning-Bog, A. B., McCormack, A. L., Li, J., Uversky, V. N., Fink, A. L., & Di Monte, D. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c100560200 · Cited by 684

Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's Disease

Volles, M. J., Lee, S.-J., Rochet, J.-C., Shtilerman, M. D., Ding, T. T., Kessler, J. C., & Lansbury, P. T. (2001) · Biochemistry · doi:10.1021/bi0102398 · Cited by 682

Parkinson-Like Neurodegeneration Induced by Targeted Overexpression of α-Synuclein in the Nigrostriatal System

Kirik, D., Rosenblad, C., Burger, C., Lundberg, C., Johansen, T. E., Muzyczka, N., Mandel, R. J., & Björklund, A. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-07-02780.2002 · Cited by 649

Subcellular Localization of Wild-Type and Parkinson's Disease-Associated Mutant α-Synuclein in Human and Transgenic Mouse Brain

Kahle, P. J., Neumann, M., Ozmen, L., Müller, V., Jacobsen, H., Schindzielorz, A., Okochi, M., Leimer, U., van der Putten, H., Probst, A., et al. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-17-06365.2000 · Cited by 641

Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders

Jucker, M., & Walker, L. C. (2011) · Annals of Neurology · doi:10.1002/ana.22615 · Cited by 622

α-Synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease

Chen, L., & Feany, M. B. (2005) · Nature Neuroscience · doi:10.1038/nn1443 · Cited by 618

α-Synuclein Membrane Interactions and Lipid Specificity

Jo, E., McLaurin, J., Yip, C. M., St. George-Hyslop, P., & Fraser, P. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004345200 · Cited by 604

A Role for α-Synuclein in the Regulation of Dopamine Biosynthesis

Perez, R. G., Waymire, J. C., Lin, E., Liu, J. J., Guo, F., & Zigmond, M. J. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-08-03090.2002 · Cited by 598

Direct Membrane Association Drives Mitochondrial Fission by the Parkinson Disease-associated Protein α-Synuclein

Nakamura, K., Nemani, V. M., Azarbal, F., Skibinski, G., Levy, J. M., Egami, K., Munishkina, L., Zhang, J., Gardner, B., Wakabayashi, J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213538 · Cited by 596

α‐Synuclein implicated in Parkinson's disease is present in extracellular biological fluids, including human plasma

El-Agnaf, O. M. A., Salem, S. A., Paleologou, K. E., Cooper, L. J., Fullwood, N. J., Gibson, M. J., Curran, M. D., Court, J. A., Mann, D. M. A., Ikeda, S.-I., et al. (2003) · The FASEB Journal · doi:10.1096/fj.03-0098fje · Cited by 590

Prediction of “Aggregation-prone” and “Aggregation-susceptible” Regions in Proteins Associated with Neurodegenerative Diseases

Pawar, A. P., DuBay, K. F., Zurdo, J., Chiti, F., Vendruscolo, M., & Dobson, C. M. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.04.016 · Cited by 588

The mystery of nonclassical protein secretion: A current view on cargo proteins and potential export routes

Nickel, W. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03577.x · Cited by 586

Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation

Uversky, V. N. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04764.x · Cited by 567

α-Synuclein in Central Nervous System and from Erythrocytes, Mammalian Cells, and Escherichia coli Exists Predominantly as Disordered Monomer

Fauvet, B., Mbefo, M. K., Fares, M.-B., Desobry, C., Michael, S., Ardah, M. T., Tsika, E., Coune, P., Prudent, M., Lion, N., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.318949 · Cited by 566

α-Synuclein Shares Physical and Functional Homology with 14-3-3 Proteins

Ostrerova, N., Petrucelli, L., Farrer, M., Mehta, N., Choi, P., Hardy, J., & Wolozin, B. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-14-05782.1999 · Cited by 564

Dityrosine Cross-linking Promotes Formation of Stable α-Synuclein Polymers

Souza, J. M., Giasson, B. I., Chen, Q., Lee, V. M.-Y., & Ischiropoulos, H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000206200 · Cited by 563

Chaperone-Mediated Autophagy Markers in Parkinson Disease Brains

Alvarez-Erviti, L., Rodriguez-Oroz, M. C., Cooper, J. M., Caballero, C., Ferrer, I., Obeso, J. A., & Schapira, A. H. V. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.198 · Cited by 554

A Broken α-Helix in Folded α-Synuclein

Chandra, S., Chen, X., Rizo, J., Jahn, R., & Südhof, T. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213128200 · Cited by 540

α-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity

Kontopoulos, E., Parvin, J. D., & Feany, M. B. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl243 · Cited by 537

A novel α-synuclein mutation A53E associated with atypical multiple system atrophy and Parkinson's disease-type pathology

Pasanen, P., Myllykangas, L., Siitonen, M., Raunio, A., Kaakkola, S., Lyytinen, J., Tienari, P. J., Pöyhönen, M., & Paetau, A. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.03.024 · Cited by 536

Detection of elevated levels of α-synuclein oligomers in CSF from patients with Parkinson disease

Tokuda, T., Qureshi, M. M., Ardah, M. T., Varghese, S., Shehab, S. A. S., Kasai, T., Ishigami, N., Tamaoka, A., Nakagawa, M., & El-Agnaf, O. M. A. (2010) · Neurology · doi:10.1212/wnl.0b013e3181fd613b · Cited by 527

Constitutive Phosphorylation of the Parkinson's Disease Associated α-Synuclein

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Lipid Rafts Mediate the Synaptic Localization of α-Synuclein

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Inhibition of mitochondrial fusion by α‐synuclein is rescued by PINK1, Parkin and DJ‐1

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A soluble α-synuclein construct forms a dynamic tetramer

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Evidence for long‐term survival and function of dopaminergic grafts in progressive Parkinson's disease

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Mitochondrial alpha-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo

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Clearance of α-Synuclein Oligomeric Intermediates via the Lysosomal Degradation Pathway

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Double-knockout mice for α- and β-synucleins: Effect on synaptic functions

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Interaction of Human α-Synuclein and Parkinson's Disease Variants with Phospholipids

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Regulation of Phospholipase D2: Selective Inhibition of Mammalian Phospholipase D Isoenzymes by α- and β-Synucleins

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Lipid Droplet Binding and Oligomerization Properties of the Parkinson's Disease Protein α-Synuclein

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Aggregated and Monomeric α-Synuclein Bind to the S6′ Proteasomal Protein and Inhibit Proteasomal Function

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A Structural and Functional Role for 11-mer Repeats in α-Synuclein and Other Exchangeable Lipid Binding Proteins

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Degradation of α-Synuclein by Proteasome

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Synthetic filaments assembled from C‐terminally truncated α‐synuclein

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α-Synuclein Overexpression in PC12 and Chromaffin Cells Impairs Catecholamine Release by Interfering with a Late Step in Exocytosis

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Proteasomal Inhibition by α-Synuclein Filaments and Oligomers

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Age-associated increases of α-synuclein in monkeys and humans are associated with nigrostriatal dopamine depletion: Is this the target for Parkinson's disease?

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α‐Synuclein Up‐Regulation in Substantia Nigra Dopaminergic Neurons Following Administration of the Parkinsonian Toxin MPTP

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Synucleins Are a Novel Class of Substrates for G Protein-coupled Receptor Kinases

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α-Synuclein Binds to Tau and Stimulates the Protein Kinase A-catalyzed Tau Phosphorylation of Serine Residues 262 and 356

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Effects of Curvature and Composition on α-Synuclein Binding to Lipid Vesicles

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The E46K Mutation in α-Synuclein Increases Amyloid Fibril Formation

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Role of α-Synuclein Carboxy-Terminus on Fibril Formation in Vitro

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Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity

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Full length α-synuclein is present in cerebrospinal fluid from Parkinson's disease and normal subjects

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α‐Synuclein metabolism and aggregation is linked to ubiquitin‐independent degradation by the proteasome

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Structure of membrane-bound α-synuclein studied by site-directed spin labeling

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Impact of the Acidic C-Terminal Region Comprising Amino Acids 109−140 on α-Synuclein Aggregation in Vitro

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Annular α-Synuclein Protofibrils Are Produced When Spherical Protofibrils Are Incubated in Solution or Bound to Brain-Derived Membranes

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Abberant α-Synuclein Confers Toxicity to Neurons in Part through Inhibition of Chaperone-Mediated Autophagy

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Native α-synuclein induces clustering of synaptic-vesicle mimics via binding to phospholipids and synaptobrevin-2/VAMP2

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Properties of native brain α-synuclein

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Copper(II)-induced self-oligomerization of α-synuclein

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NACP, a presynaptic protein, immunoreactivity in Lewy bodies in Parkinson's disease

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α-Synuclein occurs in lipid-rich high molecular weight complexes, binds fatty acids, and shows homology to the fatty acid-binding proteins

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Identification of a breast cancer-specific gene, BCSG1, by direct differential cDNA sequencing.

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Phosphorylation at S87 Is Enhanced in Synucleinopathies, Inhibits α-Synuclein Oligomerization, and Influences Synuclein-Membrane Interactions

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Synucleins Regulate the Kinetics of Synaptic Vesicle Endocytosis

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Membrane Curvature Induction and Tubulation Are Common Features of Synucleins and Apolipoproteins

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Role of α-Synuclein in Presynaptic Dopamine Recruitment

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Hyperphosphorylation and insolubility of α‐synuclein in transgenic mouse oligodendrocytes

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αβγ-Synuclein triple knockout mice reveal age-dependent neuronal dysfunction

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Cathepsin D Is the Main Lysosomal Enzyme Involved in the Degradation of α-Synuclein and Generation of Its Carboxy-Terminally Truncated Species

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Tandem mass spectrometry identifies many mouse brain O -GlcNAcylated proteins including EGF domain-specific O -GlcNAc transferase targets

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Golgi Fragmentation Occurs in the Cells with Prefibrillar α-Synuclein Aggregates and Precedes the Formation of Fibrillar Inclusion

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Transplanted dopaminergic neurons develop PD pathologic changes: A second case report

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Functional Consequences of α-Synuclein Tyrosine Nitration

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Membrane-Bound α-Synuclein Forms an Extended Helix: Long-Distance Pulsed ESR Measurements Using Vesicles, Bicelles, and Rodlike Micelles

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α-Synuclein Multimers Cluster Synaptic Vesicles and Attenuate Recycling

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Neural Activity Controls the Synaptic Accumulation of α-Synuclein

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A Precipitating Role for Truncated α-Synuclein and the Proteasome in α-Synuclein Aggregation

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Mutant A53T α-Synuclein Induces Neuronal Death by Increasing Mitochondrial Autophagy

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Enrichment and Site Mapping of O-Linked N-Acetylglucosamine by a Combination of Chemical/Enzymatic Tagging, Photochemical Cleavage, and Electron Transfer Dissociation Mass Spectrometry

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Mitochondrial Lipid Abnormality and Electron Transport Chain Impairment in Mice Lacking α-Synuclein

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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

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NMR of α‐synuclein–polyamine complexes elucidates the mechanism and kinetics of induced aggregation

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Sumoylation inhibits α-synuclein aggregation and toxicity

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α-Synuclein Has a High Affinity for Packing Defects in a Bilayer Membrane

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α-Synuclein activation of protein phosphatase 2A reduces tyrosine hydroxylase phosphorylation in dopaminergic cells

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Phosphorylation of Synucleins by Members of the Polo-like Kinase Family

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Localization of α-synuclein to mitochondria within midbrain of mice

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α-Synuclein Inhibits Intersynaptic Vesicle Mobility and Maintains Recycling-Pool Homeostasis

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The plasma alpha-synuclein levels in patients with Parkinson’s disease and multiple system atrophy

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Calpain-Cleavage of α-Synuclein

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The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of -synuclein, and enhances its secretion and nuclear localization in cells

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Polo-like Kinase 2 (PLK2) Phosphorylates α-Synuclein at Serine 129 in Central Nervous System

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Proteolytic Cleavage of Extracellular Secreted α-Synuclein via Matrix Metalloproteinases

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α-Synuclein–enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons

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Delayed localization of synelfin (synuclein, NACP) to presynaptic terminals in cultured rat hippocampal neurons

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Defective membrane interactions of familial Parkinson’s disease mutant A30P α-synuclein 1 1Edited by I. B. Holland

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Crosslinking of α-synuclein by advanced glycation endproducts — an early pathophysiological step in Lewy body formation?

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Multiple-system atrophy: a new α-synuclein disease?

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α-Synuclein Delays Endoplasmic Reticulum (ER)-to-Golgi Transport in Mammalian Cells by Antagonizing ER/Golgi SNAREs

Thayanidhi, N., Helm, J. R., Nycz, D. C., Bentley, M., Liang, Y., & Hay, J. C. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-09-0801 · Cited by 229

The Impact of the E46K Mutation on the Properties of α-Synuclein in Its Monomeric and Oligomeric States

Fredenburg, R. A., Rospigliosi, C., Meray, R. K., Kessler, J. C., Lashuel, H. A., Eliezer, D., & Lansbury, P. T. (2007) · Biochemistry · doi:10.1021/bi7000246 · Cited by 227

The solubility of α‐synuclein in multiple system atrophy differs from that of dementia with Lewy bodies and Parkinson's disease

Campbell, B. C. V., McLean, C. A., Culvenor, J. G., Gai, W. P., Blumbergs, P. C., Jäkälä, P., Beyreuther, K., Masters, C. L., & Li, Q. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00021.x · Cited by 225

Untitled work

(2002) · doi:10.1016/s0304-3940(02)00016-2 · Cited by 225

Interaction of the Molecular Chaperone αB-Crystallin with α-Synuclein: Effects on Amyloid Fibril Formation and Chaperone Activity

Rekas, A., Adda, C. G., Andrew Aquilina, J., Barnham, K. J., Sunde, M., Galatis, D., Williamson, N. A., Masters, C. L., Anders, R. F., Robinson, C. V., et al. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.054 · Cited by 223

Inhibition of Fibrillization and Accumulation of Prefibrillar Oligomers in Mixtures of Human and Mouse α-Synuclein

Rochet, J.-C., Conway, K. A., & Lansbury, P. T. (2000) · Biochemistry · doi:10.1021/bi001315u · Cited by 222

Accelerated Oligomerization by Parkinson's Disease Linked α‐Synuclein Mutants

CONWAY, K. A., LEE, S. ‐., ROCHET, J. ‐., DING, T. T., HARPER, J. D., WILLIAMSON, R. E., & LANSBURY, P. T. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06903.x · Cited by 222

Cell-produced α-synuclein oligomers are targeted to, and impair, the 26S proteasome

Emmanouilidou, E., Stefanis, L., & Vekrellis, K. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.07.008 · Cited by 221

Impact of N-Terminal Acetylation of α-Synuclein on Its Random Coil and Lipid Binding Properties

Maltsev, A. S., Ying, J., & Bax, A. (2012) · Biochemistry · doi:10.1021/bi300642h · Cited by 219

Tyrosine and serine phosphorylation of α-synuclein have opposing effects on neurotoxicity and soluble oligomer formation

Chen, L., Periquet, M., Wang, X., Negro, A., McLean, P. J., Hyman, B. T., & Feany, M. B. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39088 · Cited by 215

Wild-type but Not Parkinson's Disease-related Ala-53 → Thr Mutant α-Synuclein Protects Neuronal Cells from Apoptotic Stimuli

da Costa, C. A., Ancolio, K., & Checler, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002413200 · Cited by 213

α-Synuclein Binds Large Unilamellar Vesicles as an Extended Helix

Trexler, A. J., & Rhoades, E. (2009) · Biochemistry · doi:10.1021/bi900114z · Cited by 212

Optical Reporters for the Conformation of α-Synuclein Reveal a Specific Interaction with Mitochondria

Nakamura, K., Nemani, V. M., Wallender, E. K., Kaehlcke, K., Ott, M., & Edwards, R. H. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3088-08.2008 · Cited by 210

Specificity and Regulation of Casein Kinase-Mediated Phosphorylation of α-Synuclein

Waxman, E. A., & Giasson, B. I. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3186fc995 · Cited by 209

α-Synuclein Senses Lipid Packing Defects and Induces Lateral Expansion of Lipids Leading to Membrane Remodeling

Ouberai, M. M., Wang, J., Swann, M. J., Galvagnion, C., Guilliams, T., Dobson, C. M., & Welland, M. E. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.478297 · Cited by 208

Definition of a Molecular Pathway Mediating α-Synuclein Neurotoxicity

Burré, J., Sharma, M., & Südhof, T. C. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.4650-14.2015 · Cited by 202

α-Synuclein is differentially expressed in mitochondria from different rat brain regions and dose-dependently down-regulates complex I activity

Liu, G., Zhang, C., Yin, J., Li, X., Cheng, F., Li, Y., Yang, H., Uéda, K., Chan, P., & Yu, S. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.02.056 · Cited by 201

Functional Alterations to the Nigrostriatal System in Mice Lacking All Three Members of the Synuclein Family

Anwar, S., Peters, O., Millership, S., Ninkina, N., Doig, N., Connor-Robson, N., Threlfell, S., Kooner, G., Deacon, R. M., Bannerman, D. M., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.6194-10.2011 · Cited by 200

Tubulin Seeds α-Synuclein Fibril Formation

Alim, M. A., Hossain, M. S., Arima, K., Takeda, K., Izumiyama, Y., Nakamura, M., Kaji, H., Shinoda, T., Hisanaga, S., & Uéda, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m102981200 · Cited by 200

Induction of Neuronal Cell Death by Rab5A-dependent Endocytosis of α-Synuclein

Sung, J. Y., Kim, J., Paik, S. R., Park, J. H., Ahn, Y. S., & Chung, K. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101318200 · Cited by 200

Monomeric Synucleins Generate Membrane Curvature

Westphal, C. H., & Chandra, S. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.418871 · Cited by 199

α‐Synuclein produces a long‐lasting increase in neurotransmitter release

Liu, S., Ninan, I., Antonova, I., Battaglia, F., Trinchese, F., Narasanna, A., Kolodilov, N., Dauer, W., Hawkins, R. D., & Arancio, O. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600451 · Cited by 198

N‐terminal acetylation of α‐synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer

Kang, L., Moriarty, G. M., Woods, L. A., Ashcroft, A. E., Radford, S. E., & Baum, J. (2012) · Protein Science · doi:10.1002/pro.2088 · Cited by 195

Extensive nuclear localization of α-synuclein in normal rat brain neurons revealed by a novel monoclonal antibody

Yu, S., Li, X., Liu, G., Han, J., Zhang, C., Li, Y., Xu, S., Liu, C., Gao, Y., Yang, H., et al. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2006.12.028 · Cited by 194

Ubiquitylation of synphilin-1 and α-synuclein by SIAH and its presence in cellular inclusions and Lewy bodies imply a role in Parkinson's disease

Liani, E., Eyal, A., Avraham, E., Shemer, R., Szargel, R., Berg, D., Bornemann, A., Riess, O., Ross, C. A., Rott, R., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401081101 · Cited by 193

N-terminal Acetylation Stabilizes N-terminal Helicity in Lipid- and Micelle-bound α-Synuclein and Increases Its Affinity for Physiological Membranes

Dikiy, I., & Eliezer, D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.512459 · Cited by 188

Dopamine induces autophagic cell death and α‐synuclein increase in human neuroblastoma SH‐SY5Y cells

Gómez‐Santos, C., Ferrer, I., Santidrián, A. F., Barrachina, M., Gil, J., & Ambrosio, S. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10663 · Cited by 188

Mitochondrial translocation of α-synuclein is promoted by intracellular acidification

Cole, N. B., DiEuliis, D., Leo, P., Mitchell, D. C., & Nussbaum, R. L. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.03.012 · Cited by 185

Effects of Oxidative and Nitrative Challenges on α-Synuclein Fibrillogenesis Involve Distinct Mechanisms of Protein Modifications

Norris, E. H., Giasson, B. I., Ischiropoulos, H., & Lee, V. M.-Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212436200 · Cited by 181

Identification, localization and characterization of the human γ-synuclein gene

Lavedan, C., Leroy, E., Dehejia, A., Buchholtz, S., Dutra, A., Nussbaum, R. L., & Polymeropoulos, M. H. (1998) · Human Genetics · doi:10.1007/s004390050792 · Cited by 179

Mono- and double-mutant mouse models of Parkinson's disease display severe mitochondrial damage

Stichel, C. C., Zhu, X.-R., Bader, V., Linnartz, B., Schmidt, S., & Lubbert, H. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm083 · Cited by 179

Systematic Mutagenesis of α-Synuclein Reveals Distinct Sequence Requirements for Physiological and Pathological Activities

Burré, J., Sharma, M., & Südhof, T. C. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.3545-12.2012 · Cited by 178

Ca2+ Binding to α-Synuclein Regulates Ligand Binding and Oligomerization

Nielsen, M. S., Vorum, H., Lindersson, E., & Jensen, P. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101181200 · Cited by 176

Parkinson Disease Epidemiology, Pathology, Genetics, and Pathophysiology

Simon, D. K., Tanner, C. M., & Brundin, P. (2020) · Clinics in Geriatric Medicine · doi:10.1016/j.cger.2019.08.002 · Cited by 1,114

Advanced Glycation End-Products (AGEs): Formation, Chemistry, Classification, Receptors, and Diseases Related to AGEs

Twarda-Clapa, A., Olczak, A., Białkowska, A. M., & Koziołkiewicz, M. (2022) · Cells · doi:10.3390/cells11081312 · Cited by 746

Neuropathology and molecular diagnosis of Synucleinopathies

Koga, S., Sekiya, H., Kondru, N., Ross, O. A., & Dickson, D. W. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00501-z · Cited by 347

Tau accelerates α-synuclein aggregation and spreading in Parkinson’s disease

Pan, L., Li, C., Meng, L., Tian, Y., He, M., Yuan, X., Zhang, G., Zhang, Z., Xiong, J., Chen, G., et al. (2022) · Brain · doi:10.1093/brain/awac171 · Cited by 154

Short-Chain Fatty Acid-Producing Gut Microbiota Is Decreased in Parkinson’s Disease but Not in Rapid-Eye-Movement Sleep Behavior Disorder

Nishiwaki, H., Hamaguchi, T., Ito, M., Ishida, T., Maeda, T., Kashihara, K., Tsuboi, Y., Ueyama, J., Shimamura, T., Mori, H., et al. (2020) · mSystems · doi:10.1128/msystems.00797-20 · Cited by 133