Role of α-Synuclein in Inducing Innate and Adaptive Immunity in Parkinson Disease

Staging of brain pathology related to sporadic Parkinson’s disease

Braak, H., Tredici, K. D., Rüb, U., de Vos, R. A. I., Jansen Steur, E. N. H., & Braak, E. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00065-9 · Cited by 10,777

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

Macrophage activation and polarization: nomenclature and experimental guidelines

Murray, P. J., Allen, J. E., Biswas, S. K., Fisher, E. A., Gilroy, D. W., Goerdt, S., Gordon, S., Hamilton, J. A., Ivashkiv, L. B., Lawrence, T., et al. (2014) · Immunity · doi:10.1016/j.immuni.2014.06.008 · Cited by 6,337

Fate Mapping Analysis Reveals That Adult Microglia Derive from Primitive Macrophages

Ginhoux, F., Greter, M., Leboeuf, M., Nandi, S., See, P., Gokhan, S., Mehler, M. F., Conway, S. J., Ng, L. G., Stanley, E. R., et al. (2010) · Science · doi:10.1126/science.1194637 · Cited by 5,175

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

Reactive microglia are positive for HLA‐DR in the substantia nigra of Parkinson's and Alzheimer's disease brains

McGeer, P. L., Itagaki, S., Boyes, B. E., & McGeer, E. G. (1988) · Neurology · doi:10.1212/wnl.38.8.1285 · Cited by 2,990

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

A Lineage of Myeloid Cells Independent of Myb and Hematopoietic Stem Cells

Schulz, C., Perdiguero, E. G., Chorro, L., Szabo-Rogers, H., Cagnard, N., Kierdorf, K., Prinz, M., Wu, B., Jacobsen, S. E. W., Pollard, J. W., et al. (2012) · Science · doi:10.1126/science.1219179 · Cited by 2,578

Identification of a unique TGF-β–dependent molecular and functional signature in microglia

Butovsky, O., Jedrychowski, M. P., Moore, C. S., Cialic, R., Lanser, A. J., Gabriely, G., Koeglsperger, T., Dake, B., Wu, P. M., Doykan, C. E., et al. (2014) · Nature Neuroscience · doi:10.1038/nn.3599 · Cited by 2,543

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 2,174

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

Chartier-Harlin, M.-C., Kachergus, J., Roumier, C., Mouroux, V., Douay, X., Lincoln, S., Levecque, C., Larvor, L., Andrieux, J., Hulihan, M., et al. (2004) · The Lancet · doi:10.1016/s0140-6736(04)17103-1 · Cited by 2,029

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

Burré, J., Sharma, M., Tsetsenis, T., Buchman, V. L., Etherton, M. R., & Südhof, T. C. (2010) · Science · doi:10.1126/science.1195227 · Cited by 1,907

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

Masliah, E., Rockenstein, E. M., Veinbergs, I., Mallory, M. E., Hashimoto, M., Takeda, A., Sagara, Y., Sisk, A., & Mucke, L. (2000) · Science · doi:10.1126/science.287.5456.1265 · Cited by 1,779

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

Maroteaux, L., Campanelli, J., & Scheller, R. (1988) · Journal of Neuroscience · doi:10.1523/jneurosci.08-08-02804.1988 · Cited by 1,646

Local self-renewal can sustain CNS microglia maintenance and function throughout adult life

Ajami, B., Bennett, J. L., Krieger, C., Tetzlaff, W., & Rossi, F. M. V. (2007) · Nature Neuroscience · doi:10.1038/nn2014 · Cited by 1,643

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 1,622

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., & Lee, V. M. ‐. (2000) · Science · doi:10.1126/science.290.5493.985 · Cited by 1,567

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

Conway, K. A., Lee, S., Rochet, J., Ding, T. T., Williamson, R. E., & Lansbury, P. T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.571 · Cited by 1,559

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 1,524

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. D. M., Ihara, Y., & Saitoh, T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11282 · Cited by 1,502

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

Anderson, J. P., Walker, D., 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 1,452

Gastric α-synuclein immunoreactive inclusions in Meissner's and Auerbach's plexuses in cases staged for Parkinson's disease-related brain pathology

Braak, H., de Vos, R. A. I., Bohl, J., & Del Tredici, K. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2005.11.012 · Cited by 1,354

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

In vivo imaging of microglial activation with [11C](R)-PK11195 PET in idiopathic Parkinson's disease

Gerhard, A., Pavese, N., Hotton, G., Turkheimer, F., Es, M., Hammers, A., Eggert, K., Oertel, W., Banati, R. B., & Brooks, D. J. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.08.002 · Cited by 1,200

Infiltration of CD4+ lymphocytes into the brain contributes to neurodegeneration in a mouse model of Parkinson disease

Brochard, V., Combadière, B., Prigent, A., Laouar, Y., Perrin, A., Beray-Berthat, V., Bonduelle, O., Alvarez-Fischer, D., Callebert, J., Launay, J.-M., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci36470 · Cited by 1,172

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

A Hydrophobic Stretch of 12 Amino Acid Residues in the Middle of α-Synuclein Is Essential for Filament Assembly

Giasson, B. I., Murray, I. V. J., Trojanowski, J. Q., & Lee, V. M.-Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008919200 · 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

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 1,063

Tumor necrosis factor-α (TNF-α) increases both in the brain and in the cerebrospinal fluid from parkinsonian patients

Mogi, M., Harada, M., Riederer, P., Narabayashi, H., Fujita, K., & Nagatsu, T. (1994) · Neuroscience Letters · doi:10.1016/0304-3940(94)90746-3 · Cited by 986

Increased Intestinal Permeability Correlates with Sigmoid Mucosa alpha-Synuclein Staining and Endotoxin Exposure Markers in Early Parkinson's Disease

Forsyth, C. B., Shannon, K. M., Kordower, J. H., Voigt, R. M., Shaikh, M., Jaglin, J. A., Estes, J. D., Dodiya, H. B., & Keshavarzian, A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028032 · Cited by 974

Neuropathological assessment of Parkinson’s disease: refining the diagnostic criteria

Dickson, D. W., Braak, H., Duda, J. E., Duyckaerts, C., Gasser, T., Halliday, G. M., Hardy, J., Leverenz, J. B., Del Tredici, K., Wszolek, Z. K., et al. (2009) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70238-8 · Cited by 972

Structural and functional characterization of two alpha-synuclein strains

Bousset, L., Pieri, L., Ruiz-Arlandis, G., Gath, J., Jensen, P. H., Habenstein, B., Madiona, K., Oliéric, V., Böckmann, A., Meier, B. H., et al. (2013) · Nature Communications · doi:10.1038/ncomms3575 · Cited by 925

Multi-organ distribution of phosphorylated α-synuclein histopathology in subjects with Lewy body disorders

Arizona Parkinson’s Disease Consortium, Beach, T. G., Adler, C. H., Sue, L. I., Vedders, L., Lue, L., White III, C. L., Akiyama, H., Caviness, J. N., Shill, H. A., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0664-3 · Cited by 911

Exosomal cell-to-cell transmission of alpha synuclein oligomers

Danzer, K. M., Kranich, L. R., Ruf, W. P., Cagsal‐Getkin, O., Winslow, A. R., Zhu, L., Vanderburg, C. R., & McLean, P. J. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-42 · Cited by 880

Microglial activation and dopamine terminal loss in early Parkinson's disease

Ouchi, Y., Yoshikawa, E., Sekine, Y., Futatsubashi, M., Kanno, T., Ogusu, T., & Torizuka, T. (2005) · Annals of Neurology · doi:10.1002/ana.20338 · Cited by 864

Differential roles of microglia and monocytes in the inflamed central nervous system

Yamasaki, R., Lu, H., Butovsky, O., Ohno, N., Rietsch, A. M., Cialic, R., Wu, P. M., Doykan, C. E., Lin, J., Cotleur, A. C., et al. (2014) · Journal of Experimental Medicine · doi:10.1084/jem.20132477 · Cited by 856

Neuron-released oligomeric α-synuclein is an endogenous agonist of TLR2 for paracrine activation of microglia

Kim, C., Ho, D.-H., Suk, J.-E., You, S., Michael, S., Kang, J., Joong Lee, S., Masliah, E., Hwang, D., Lee, H.-J., et al. (2013) · Nature Communications · doi:10.1038/ncomms2534 · Cited by 856

Interleukin-1β, interleukin-6, epidermal growth factor and transforming growth factor-α are elevated in the brain from parkinsonian patients

Mogi, M., Harada, M., Kondo, T., Riederer, P., Inagaki, H., Minami, M., & Nagatsu, T. (1994) · Neuroscience Letters · doi:10.1016/0304-3940(94)90508-8 · Cited by 855

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. S., Simon, M. N., Nowak, R. J., Walz, T., & Lansbury, P. T. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00735-0 · Cited by 819

Common genetic variation in the HLA region is associated with late-onset sporadic Parkinson's disease

Hamza, T. H., Zabetian, C. P., Tenesa, A., Laederach, A., Montimurro, J. S., Yearout, D., Kay, D. M., Doheny, K. F., Paschall, J. E., Pugh, E., et al. (2010) · Nature Genetics · doi:10.1038/ng.642 · Cited by 808

Interleukin-1β and interleukin-6 are elevated in the cerebrospinal fluid of Alzheimer's and de novo Parkinson's disease patients

Blum-Degena, D., Müller, T., Kuhn, W., Gerlach, M., Przuntek, H., & Riederer, P. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)12192-7 · Cited by 801

Minocycline Prevents Nigrostriatal Dopaminergic Neurodegeneration in the MPTP Model of Parkinson’s Disease

Du, Y., Ma, Z., Lin, S., Dodel, R. C., Gao, F., Bales, K. R., Triarhou, L. C., Chernet, E., Perry, K. W., Nelson, D. L. G., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251341998 · Cited by 789

Fibrils Formed in Vitro from α-Synuclein and Two Mutant Forms Linked to Parkinson's Disease are Typical Amyloid

Conway, K. A., Harper, J. D., & Lansbury, P. T. (2000) · Biochemistry · doi:10.1021/bi991447r · Cited by 786

Lysosomal dysfunction increases exosome-mediated alpha-synuclein release and transmission

Alvarez‐Erviti, L., Seow, Y., Schapira, A. H. V., Gardiner, C., Sargent, I. L., Wood, M. J. A., & Cooper, J. A. D. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.029 · Cited by 762

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

Serpell, L. C., Berriman, J. A., Jakes, R., Goedert, M., & Crowther, R. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.9.4897 · Cited by 755

G51D α‐synuclein mutation causes a novel Parkinsonian–pyramidal syndrome

Lesage, S., Anheim, M., Letournel, F., Bousset, L., Honoré, A., Rozas, N., Pieri, L., Madiona, K., Dürr, A., Melki, R., et al. (2013) · Annals of Neurology · doi:10.1002/ana.23894 · Cited by 741

Comparison of kindreds with parkinsonism and α‐synuclein genomic multiplications

Farrer, M. J., Kachergus, J. M., Forno, L. S., Lincoln, S., Wang, D., Hulihan, M., Maraganore, D. M., Gwinn, K. A., Wszołek, Z. K., Dickson, D. W., et al. (2004) · Annals of Neurology · doi:10.1002/ana.10846 · Cited by 711

Cutting Edge: The Conversion of Arginine to Citrulline Allows for a High-Affinity Peptide Interaction with the Rheumatoid Arthritis-Associated HLA-DRB1*0401 MHC Class II Molecule

Hill, J. A., Southwood, S., Sette, A., Jevnikar, A. M., Bell, D., & Cairns, E. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.2.538 · Cited by 711

Staging of the intracerebral inclusion body pathology associated with idiopathic Parkinson's disease (preclinical and clinical stages)

Braak, H., Tredici, K. D., Bratzke, H., Hamm-Clement, J., Sandmann-Keil, D., & Rüb, U. (2002) · Journal of Neurology · doi:10.1007/s00415-002-1301-4 · Cited by 710

Alpha‐synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease

Appel‐Cresswell, S., Vilariño‐Güell, C., Encarnacion, M. J., Sherman, H. E., Yu, I. S., Shah, B., Weir, D., Thompson, C., Szu‐Tu, C., Trinh, J., et al. (2013) · Movement Disorders · doi:10.1002/mds.25421 · Cited by 687

Plasma exosomal α-synuclein is likely CNS-derived and increased in Parkinson’s disease

Shi, M., Liu, C., Cook, T. J., Bullock, K. M., Zhao, Y., Ginghina, C., Li, Y., Aro, P., Dator, R., He, C., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1314-y · Cited by 676

Inflammation and neurodegeneration in Parkinson's disease

McGeer, P. L., & McGeer, E. G. (2004) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2004.01.005 · Cited by 632

Colonic inflammation in Parkinson's disease

Devos, D., Lebouvier, T., Lardeux, B., Biraud, M., Rouaud, T., Pouclet, H., Coron, E., Bruley des Varannes, S., Naveilhan, P., Nguyen, J.-M., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.09.007 · Cited by 627

Time course and morphology of dopaminergic neuronal death caused by the neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine

Jackson-Lewis, V. R., Jakowec, M. W., Burke, R. E., & Przedborski, S. (1995) · Neurodegeneration · doi:10.1016/1055-8330(95)90015-2 · Cited by 609

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 593

Triggering of inflammasome by aggregated α-synuclein, an inflammatory response in synucleinopathies

Codolo, G., Plotegher, N., Pozzobon, T., Brucale, M., Tessari, I., Bubacco, L., & de Bernard, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055375 · Cited by 585

Stress-Induced Recruitment of Bone Marrow-Derived Monocytes to the Brain Promotes Anxiety-Like Behavior

Wohleb, E. S., Powell, N. D., Godbout, J. P., & Sheridan, J. F. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.1671-13.2013 · Cited by 563

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. E. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.03.024 · Cited by 554

Peripheral cytokines profile in parkinson’s disease

Reale, M., Iarlori, C., Thomas, A., Gambi, D., Perfetti, B., Di Nicola, M., & Onofrj, M. (2009) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2008.07.003 · Cited by 547

Protein Nitration in Parkinsonʼs Disease

Good, P. F., Hsu, A., Werner, P., Perl, D. P., & Olanow, C. W. (1998) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199804000-00006 · Cited by 540

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

Okochi, M., Walter, J., Koyama, A., Nakajo, S., Baba, M., Iwatsubo, T., Meijer, L., Kahle, P. J., & Haass, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.390 · Cited by 535

Parkinson's disease: the presence of Lewy bodies in Auerbach's and Meissner's plexuses

Wakabayashi, K., Takahashi, H., Takeda, S., Ohama, E., & Ikuta, F. (1988) · Acta Neuropathologica · doi:10.1007/bf00687767 · Cited by 528

Collaborative Analysis of α-Synuclein Gene Promoter Variability and Parkinson Disease

Maraganore, D. M. (2006) · JAMA · doi:10.1001/jama.296.6.661 · Cited by 518

Mutant and Wild Type Human α-Synucleins Assemble into Elongated Filaments with Distinct Morphologies in Vitro

Giasson, B. I., Uryu, K., Trojanowski, J. Q., & Lee, V. M. ‐. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.7619 · Cited by 510

Modulating inflammatory monocytes with a unique microRNA gene signature ameliorates murine ALS

Butovsky, O., Siddiqui, S., Gabriely, G., Lanser, A. J., Dake, B., Murugaiyan, G., Doykan, C. E., Wu, P. M., Gali, R. R., Iyer, L. K., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci62636 · Cited by 481

Aggregation promoting C-terminal truncation of α-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations

Li, W., West, N. C., Colla, E., Pletniková, O., Troncoso, J. C., Marsh, L., Dawson, T. M., Jäkälä, P., Hartmann, T., Price, D. L., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406976102 · Cited by 479

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

Perrin, R. J., Woods, W. S., Clayton, D. F., & George, J. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004851200 · Cited by 444

Phosphorylated α-Synuclein Is Ubiquitinated in α-Synucleinopathy Lesions

Hasegawa, M., Fujiwara, H., Nonaka, T., Wakabayashi, K., Takahashi, H., Lee, V. M.-Y., Trojanowski, J. Q., Mann, D., & Iwatsubo, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208046200 · Cited by 428

Endoproteolytic Activity of the Proteasome

Liu, C.-W., Corboy, M. J., Demartino, G., & Thomas, P. (2003) · Science · doi:10.1126/science.1079293 · Cited by 422

Degradation of α-Synuclein by Proteasome

Bennett, M. C., Bishop, J. F., Leng, Y., Chock, P. B., Chase, T. N., & Mouradian, M. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.33855 · Cited by 417

Regulatory T Cells Attenuate Th17 Cell-Mediated Nigrostriatal Dopaminergic Neurodegeneration in a Model of Parkinson’s Disease

Reynolds, A. D., Stone, D. K., Hutter-Saunders, J. A. L., Benner, E. J., Mosley, R. L., & Gendelman, H. E. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0901852 · Cited by 417

Microglial inflammation in the parkinsonian substantia nigra: relationship to alpha-synuclein deposition

Croisier, E., Moran, L. B., Dexter, D. T., Pearce, R. K., & Graeber, M. B. (2005) · Journal of Neuroinflammation · doi:10.1186/1742-2094-2-14 · Cited by 414

Neuropathology of Autonomic Nervous System in Parkinson's Disease

Wakabayashi, K., & Takahashi, H. (2008) · European Neurology · doi:10.1159/000113469 · Cited by 407

MHCII Is Required for -Synuclein-Induced Activation of Microglia, CD4 T Cell Proliferation, and Dopaminergic Neurodegeneration

Harms, A. S., Cao, S., Rowse, A. L., Thome, A. D., Li, X., Mangieri, L. R., Cron, R. Q., Shacka, J. J., Raman, C., & Standaert, D. G. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5610-12.2013 · Cited by 406

Dynamic Changes in Presynaptic and Axonal Transport Proteins Combined with Striatal Neuroinflammation Precede Dopaminergic Neuronal Loss in a Rat Model of AAV α-Synucleinopathy

Chung, C. Y., Koprich, J. B., Siddiqi, H. K., & Ole Isacson, A. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.5427-08.2009 · Cited by 406

Presence of reactive microglia in monkey substantia nigra years after 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine administration

McGeer, P. L., Schwab, C., Parent, A., & Doudet, D. (2003) · Annals of Neurology · doi:10.1002/ana.10728 · Cited by 400

Nigral and Cortical Lewy Bodies and Dystrophic Nigral Neurites in Parkinsonʼs Disease and Cortical Lewy Body Disease Contain α-synuclein Immunoreactivity

Irizarry, M. C., Growdon, W., Gómez‐Isla, T., Newell, K. L., George, J. M., Clayton, D. F., & Hyman, B. T. (1998) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199804000-00005 · Cited by 394

Targeted Overexpression of Human α-Synuclein Triggers Microglial Activation and an Adaptive Immune Response in a Mouse Model of Parkinson Disease

Theodore, S., Cao, S., McLean, P. J., & Standaert, D. G. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31818e5e99 · Cited by 392

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

Murray, I. V. J., Giasson, B. I., Quinn, S. M., Koppaka, V., Axelsen, P. H., Ischiropoulos, H., Trojanowski, J. Q., & Lee, V. M. ‐. (2003) · Biochemistry · doi:10.1021/bi027363r · Cited by 372

Phosphorylation at Ser-129 but Not the Phosphomimics S129E/D Inhibits the Fibrillation of α-Synuclein

Paleologou, K. E., Schmid, A. W., Rospigliosi, C. C., Kim, H., Lamberto, G. R., Fredenburg, R. A., Lansbury, P. T., Fernández, C. O., Eliezer, D., Zweckstetter, M., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800747200 · Cited by 372

Nitrated α–Synuclein Immunity Accelerates Degeneration of Nigral Dopaminergic Neurons

Benner, E. J., Banerjee, R., Reynolds, A. D., Sherman, S., Писарев, В. М., Tsiperson, V., Nemachek, C., Ciborowski, P. S., Przedborski, S., Mosley, R. L., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001376 · Cited by 371

Blocking Soluble Tumor Necrosis Factor Signaling with Dominant-Negative Tumor Necrosis Factor Inhibitor Attenuates Loss of Dopaminergic Neurons in Models of Parkinson's Disease

McCoy, M. K., Martinez, T. N., Ruhn, K. A., Szymkowski, D. E., Smith, C. G., Botterman, B. R., Tansey, K. E., & Tansey, M. G. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1504-06.2006 · Cited by 370

A possible role for humoral immunity in the pathogenesis of Parkinson's disease

Orr, C., Rowe, D. B., Mizuno, Y., Mori, H., & Halliday, G. M. (2005) · Brain · doi:10.1093/brain/awh625 · Cited by 367

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

Tofaris, G. K., Layfield, R., & Spillantini, M. G. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03115-5 · Cited by 363

Factors regulating microglia activation

Kierdorf, K., & Prinz, M. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00044 · Cited by 360

α-Synuclein in blood and brain from familial Parkinson disease with SNCA locus triplication

Miller, D. W., Hague, S., Clarimón, J., Baptista, M., Gwinn, K. A., Cookson, M., & Singleton, A. (2004) · Neurology · doi:10.1212/01.wnl.0000127517.33208.f4 · Cited by 356

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

Ding, T. T., Lee, S., Rochet, J., & Lansbury, P. T. (2002) · Biochemistry · doi:10.1021/bi020139h · Cited by 356

Annular Protofibrils Are a Structurally and Functionally Distinct Type of Amyloid Oligomer

Kayed, R., Pensalfini, A., Margol, L., Sokolov, Y., Sarsoza, F. M., Head, E., Hall, J. E., & Glabe, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808591200 · Cited by 356

Minocycline inhibits microglial activation and protects nigral cells after 6-hydroxydopamine injection into mouse striatum

He, Y., Appel, S. H., & Le, W. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02681-6 · Cited by 350

Properties of native brain α-synuclein

Burré, J., Vivona, S., Diao, J., Sharma, M., Brünger, A. T., & Südhof, T. C. (2013) · Nature · doi:10.1038/nature12125 · Cited by 340

Use of ibuprofen and risk of Parkinson disease

Gao, X., Chen, H., Schwarzschild, M. A., & Ascherio, A. (2011) · Neurology · doi:10.1212/wnl.0b013e31820f2d79 · Cited by 339

CD4+ Regulatory and Effector/Memory T Cell Subsets Profile Motor Dysfunction in Parkinson’s Disease

Hutter-Saunders, J. A. L., Estes, K. A., Kosloski, L. M., Allen, H. E., Dempsey, K., Torres‐Russotto, D. R., Meza, J. L., Santamaria, P. M., Bertoni, J. M., Murman, D. L., et al. (2012) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-012-9402-z · Cited by 339

MHC-I expression renders catecholaminergic neurons susceptible to T-cell-mediated degeneration

Cebrián, C., Zucca, F. A., Mauri, P., Steinbeck, J. A., Studer, L., Scherzer, C. R., Kanter, E., Budhu, S., Mandelbaum, J., Vonsattel, J. P., et al. (2014) · Nature Communications · doi:10.1038/ncomms4633 · Cited by 338

Alterations of T-lymphocyte populations in Parkinson disease

Baba, Y., Kuroiwa, A., Uitti, R. J., Wszolek, Z. K., & Yamada, T. (2005) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2005.07.005 · Cited by 336

Pathological Changes in Dopaminergic Nerve Cells of the Substantia Nigra and Olfactory Bulb in Mice Transgenic for Truncated Human α-Synuclein(1–120): Implications for Lewy Body Disorders

Tofaris, G. K., Garcia-Reitboeck, P., Humby, T., Lambourne, S. L., O’Connell, M. T., Ghetti, B. F., Gossage, H., Emson, P. C., Wilkinson, L. S., Goedert, M., et al. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.4965-05.2006 · Cited by 335

Involvement of Interferon-γ in Microglial-Mediated Loss of Dopaminergic Neurons

Mount, M. P., Lira, A., Grimes, D., Smith, P. D., Faucher, S., Slack, R. S., Anisman, H., Hayley, S. P., & Park, D. S. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.5321-06.2007 · Cited by 331

Reducing C-Terminal-Truncated Alpha-Synuclein by Immunotherapy Attenuates Neurodegeneration and Propagation in Parkinson's Disease-Like Models

Games, D., Valera, E., Spencer, B. J., Rockenstein, E. M., Mante, M., Adame, A., Patrick, C., Ubhi, K. K., Nuber, S., Sacayon, P., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.5314-13.2014 · Cited by 329

Anti-inflammatory drugs and risk of Parkinson disease

Gagne, J. J., & Power, M. C. (2010) · Neurology · doi:10.1212/wnl.0b013e3181d5a4a3 · Cited by 323

Selective microglial activation in the rat rotenone model of Parkinson's disease

Sherer, T., Betarbet, R. S., Kim, J.-H., & Greenamyre, J. T. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00172-1 · Cited by 317

Serum interleukin (IL-2, IL-10, IL-6, IL-4), TNFα, and INFγ concentrations are elevated in patients with atypical and idiopathic parkinsonism

Brodacki, B., Staszewski, J., Toczyłowska, B., Kozłowska, E., Drela, N., Chalimoniuk, M., & Stępien, A. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.06.040 · Cited by 316

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

Sevlever, D., Jiang, P., & Yen, S.-H. C. (2008) · Biochemistry · doi:10.1021/bi800699v · Cited by 305

Aggregated α-Synuclein Mediates Dopaminergic Neurotoxicity In Vivo

Periquet, M., Fulga, T. A., Myllykangas, L., Schlossmacher, M. G., & Feany, M. Β. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0285-07.2007 · Cited by 299

The phosphorylation state of Ser-129 in human α-synuclein determines neurodegeneration in a rat model of Parkinson disease

Gorbatyuk, O. S., Li, S., Sullivan, L. F., Chen, W., Kondrikova, G., Manfredsson, F. P., Mandel, R. J., & Muzyczka, N. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711053105 · Cited by 299

How T cells 'see' antigen

Krogsgaard, M., & Davis, M. M. (2005) · Nature Immunology · doi:10.1038/ni1173 · Cited by 294

Widespread Nitration of Pathological Inclusions in Neurodegenerative Synucleinopathies

Duda, J. E., Giasson, B. I., Chen, Q., Gur, T., Hurtig, H. I., Stern, M. B., Gollomp, S. M., Ischiropoulos, H., Lee, V. M. ‐., & Trojanowski, J. Q. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64781-5 · Cited by 276

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

Liu, C.-W., Giasson, B. I., Lewis, K. A., Lee, V. M., Demartino, G., & Thomas, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501508200 · Cited by 270

3-Nitrotyrosine: A biomarker of nitrogen free radical species modified proteins in systemic autoimmunogenic conditions

Ahsan, H. (2013) · Human Immunology · doi:10.1016/j.humimm.2013.06.009 · Cited by 269

α-Synuclein Activates Microglia by Inducing the Expressions of Matrix Metalloproteinases and the Subsequent Activation of Protease-Activated Receptor-1

Lee, E.-J., Woo, M.-S., Moon, P., Baek, M., Choi, I.-Y., Kim, W.-K., Junn, E., & Kim, H.-S. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903480 · Cited by 267

Microglia Acquire Distinct Activation Profiles Depending on the Degree of α-Synuclein Neuropathology in a rAAV Based Model of Parkinson's Disease

Sanchez-Guajardo, V., Febbraro, F., Kirik, D., & Romero-Ramos, M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008784 · Cited by 256

Regionally-specific microglial activation in young mice over-expressing human wildtype alpha-synuclein

Watson, M. B., Richter, F., Lee, S., Gabby, L. C., Wu, J. E., Masliah, E., Effros, R. B., & Chesselet, M. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.06.025 · Cited by 254

Genetic variability in the SNCA gene influences α‐synuclein levels in the blood and brain

Fuchs, J., Tichopád, A., Golub, Y., Munz, M., Schweitzer, K. J., Wolf, B., Berg, D., Mueller, J. C., & Gasser, T. (2007) · The FASEB Journal · doi:10.1096/fj.07-9348com · Cited by 254

Nitrated alpha‐synuclein‐activated microglial profiling for Parkinson’s disease

Reynolds, A. D., Glanzer, J. G., Kadiu, I., Ricardo-Dukelow, M., Chaudhuri, A., Ciborowski, P. S., Cerny, R. L., Gelman, B. B., Thomas, M. P., Mosley, R. L., et al. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05087.x · Cited by 247

Involvement of inducible nitric oxide synthase in inflammation-induced dopaminergic neurodegeneration.

Iravani, M. M., Kashefi, K., Mander, P., Rose, S., & Jenner, P. (2002) · Neuroscience · doi:10.1016/s0306-4522(01)00562-0 · Cited by 247

The synucleins.

George, J. M. (2001) · Genome biology · doi:10.1186/gb-2001-3-1-reviews3002 · Cited by 244

Extensive axonal Lewy neurites in Parkinson's disease: a novel pathological feature revealed by α-synuclein immunocytochemistry

Braak, H., Sandmann-Keil, D., Gai, W., & Braak, E. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00208-6 · Cited by 243

Lewy bodies in Parkinson's disease are recognized by antibodies to complement proteins

Yamada, T., McGeer, P. L., & McGeer, E. G. (1992) · Acta Neuropathologica · doi:10.1007/bf00427222 · Cited by 231

α-Synuclein activates stress signaling protein kinases in THP-1 cells and microglia

Klegeris, A., Pelech, S., Giasson, B. I., Maguire, J., Zhang, H., McGeer, E. G., & McGeer, P. L. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.11.013 · 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., Culvenor, J. G., Gai, W., Blumbergs, P. C., Jäkälä, P., Beyreuther, K. T., Masters, C. L., & Li, Q. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00021.x · Cited by 226

Proteomic Identification of Novel Proteins in Cortical Lewy Bodies

Leverenz, J. B., Umar, I., Wang, Q., Montine, T. J., McMillan, P. J., Tsuang, D. W., Jin, J., Pan, C., Shin, J., Zhu, D. C., et al. (2007) · Brain Pathology · doi:10.1111/j.1750-3639.2007.00048.x · Cited by 225

Chaperone‐like activity of synucleins

Souza, J. M., Giasson, B. I., Lee, V. M. ‐., & Ischiropoulos, H. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01563-5 · Cited by 223

Proteins Phosphorylated during Stress-induced Apoptosis Are Common Targets for Autoantibody Production in Patients with Systemic Lupus Erythematosus

Utz, P. J., Foley, M. H., Schur, P. H., & Anderson, P. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.185.5.843 · Cited by 219

High-resolution intravital imaging reveals that blood-derived macrophages but not resident microglia facilitate secondary axonal dieback in traumatic spinal cord injury

Evans, T. A., Barkauskas, D. S., Myers, J., Hare, E. G., You, J., Ransohoff, R. M., Huang, A. Y.-C., & Silver, J. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.01.013 · Cited by 217

Levels of cerebrospinal fluid α-synuclein oligomers are increased in Parkinson’s disease with dementia and dementia with Lewy bodies compared to Alzheimer’s disease

Hansson, O., Hall, S., Öhrfelt, A., Zetterberg, H., Blennow, K., Minthon, L., Nägga, K., Londos, E., Varghese, S., Majbour, N. K., et al. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt255 · Cited by 214

IFN-γ signaling, with the synergistic contribution of TNF-α, mediates cell specific microglial and astroglial activation in experimental models of Parkinson's disease

Barcia, C., Ros, C. M., Annese, V, Gómez, A., Ros-Bernal, F., Aguado-Llera, D., Martínez-Pagán, M. E., de Pablos, V, Fernandez-Villalba, E., & Herrero, M. T. (2011) · Cell Death & Disease · doi:10.1038/cddis.2011.17 · Cited by 203

Reduced T helper and B lymphocytes in Parkinson's disease

Stevens, C. H., Rowe, D. B., Morel‐Kopp, M., Orr, C., Russell, T., Ranola, M., Wård, C., & Halliday, G. M. (2012) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2012.07.015 · Cited by 200

Enhanced Phosphatase Activity Attenuates α-Synucleinopathy in a Mouse Model

Lee, K.-W., Chen, W. W., Junn, E., Im, J., Grosso, H., Sonsalla, P. K., Feng, X., Ray, N., Fernandez, J. R., Chao, Y., et al. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6513-10.2011 · Cited by 194

Association of Parkinson Disease with Structural and Regulatory Variants in the HLA Region

Wissemann, W. T., Hill-Burns, E. M., Zabetian, C. P., Factor, S. A., Patsopoulos, N., Hoglund, B., Holcomb, C., Donahue, R. J., Thomson, G., Erlich, H., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.10.009 · Cited by 189

Complement component C3 and complement receptor type 3 contribute to the phagocytosis and clearance of fibrillar Aβ by microglia

Fu, H., Liu, B., Frost, J. L., Hong, S., Jin, M., Ostaszewski, B., Shankar, G. M., Costantino, I. M., Carroll, M. C., Mayadas, T. N., et al. (2012) · Glia · doi:10.1002/glia.22331 · Cited by 180

Post-translational modifications of self antigens: implications for autoimmunity

Anderton, S. M. (2004) · Current Opinion in Immunology · doi:10.1016/j.coi.2004.09.001 · Cited by 171

The role of mitochondrial dysfunction and neuronal nitric oxide in animal models of neurodegenerative diseases

Schulz, J. B., Matthews, R. T., Klockgether, T., DICHGANS, J., & Beal, M. F. (1997) · Springer eBooks · doi:10.1007/978-1-4615-6111-8_30 · Cited by 170

Microglial response to 6-hydroxydopamine-induced substantia nigra lesions

Akiyama, H., & McGeer, P. L. (1989) · Brain Research · doi:10.1016/0006-8993(89)90857-3 · Cited by 169

Levels of alpha‐synuclein mRNA in sporadic Parkinson disease patients

Chiba‐Falek, O., Lopez, G. J., & Nussbaum, R. L. (2006) · Movement Disorders · doi:10.1002/mds.21007 · Cited by 166

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 165

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

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

NSAID Use and the Risk of Parkinsonʼs Disease

Samii, A., Etminan, M., Wiens, M. O., & Jafari, S. (2009) · Drugs & Aging · doi:10.2165/11316780-000000000-00000 · Cited by 161

Effects of nitration on the structure and aggregation of α-synuclein

Uversky, V. N., Yamin, G., Munishkina, L. A., Karymov, M. A., Millett, I. S., Doniach, S., Lyubchenko, Y. L., & Fink, A. L. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.11.014 · Cited by 160

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 158

Selective loss of nigral dopamine neurons induced by overexpression of truncated human α-synuclein in mice

Wakamatsu, M., Ishii, A., Iwata, S., Sakagami, J., Ukai, Y., Ono, M., Kambe, D., Muramatsu, S., Kobayashi, K., Iwatsubo, T., et al. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.11.017 · Cited by 157

The acute inflammatory response to intranigral α-synuclein differs significantly from intranigral lipopolysaccharide and is exacerbated by peripheral inflammation

Couch, Y., Alvarez-Erviti, L., Sibson, N. R., Wood, M. J., & Anthony, D. C. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-166 · Cited by 155

Lewy bodies in the visceral autonomic nervous system in Parkinson's disease.

Wakabayashi, K., Takahashi, H. E., Ohama, E., Takeda, S., & Ikuta, F. (1993) · PubMed · Cited by 154

Complement activation in the Parkinson's disease substantia nigra: an immunocytochemical study.

Loeffler, D. A., Camp, D. M., & Conant, S. B. (2006) · Journal of Neuroinflammation · doi:10.1186/1742-2094-3-29 · Cited by 150

α-Synuclein Expression Modulates Microglial Activation Phenotype

Austin, S. A., Floden, A. M., Murphy, E. J., & Combs, C. K. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1799-06.2006 · Cited by 150

Ontogeny and Functions of Central Nervous System Macrophages

Katsumoto, A., Lu, H., Miranda, A. S., & Ransohoff, R. M. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1400716 · Cited by 149

Inflammatory Cytokine Gene Polymorphisms and Increased Risk of Parkinson Disease

Wahner, A. D., Sinsheimer, J. S., Bronstein, J. M., & Ritz, B. R. (2007) · Archives of Neurology · doi:10.1001/archneur.64.6.836 · Cited by 143

A pathway-based analysis provides additional support for an immune-related genetic susceptibility to Parkinson's disease

Holmans, P., Moskvina, V., Jones, L., Sharma, M., Vedernikov, A., Büchel, F., Sadd, M., Brás, J., Bettella, F., Nicolaou, N., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds492 · Cited by 142

Microtubule-associated Protein 1B Is a Component of Cortical Lewy Bodies and Binds α-Synuclein Filaments

Jensen, P. H., Islam, K., Kenney, J. M., Nielsen, M. S., Power, J., & Gai, W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000099200 · Cited by 133

The regulation of synaptic function by α-synuclein

Bellani, S., Sousa, V. L., Ronzitti, G., Valtorta, F., Meldolesi, J., & Chieregatti, E. (2010) · Communicative & Integrative Biology · doi:10.4161/cib.3.2.10964 · Cited by 133

Effects of peripheral lymphocyte subpopulations and the clinical correlation with Parkinson's disease

Niwa, F., Kuriyama, N., Nakagawa, M., & Imanishi, J. (2011) · Geriatrics and gerontology international/Geriatrics & gerontology international · doi:10.1111/j.1447-0594.2011.00740.x · Cited by 128

Association between Parkinson's disease and the HLA‐DRB1 locus

Ahmed, I., Tamouza, R., Delord, M., Krishnamoorthy, R., Tzourio, C., Mulot, C., Nacfer, M., Lambert, J., Beaune, P. H., Laurent‐Puig, P., et al. (2012) · Movement Disorders · doi:10.1002/mds.25035 · Cited by 124

Role of Matrix Metalloproteinase 3-mediated α-Synuclein Cleavage in Dopaminergic Cell Death

Choi, D.-H., Kim, Y.-J., Kim, Y.-G., Joh, T. H., Beal, M. F., & Kim, Y.-S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.222430 · Cited by 123

Distinct Roles of the N-terminal-binding Domain and the C-terminal-solubilizing Domain of α-Synuclein, a Molecular Chaperone

Park, S. M., Jung, H. Y., Kim, T. D., Park, J. H., Yang, C., & Kim, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111971200 · Cited by 123

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 122

Intranigral Lentiviral Delivery of Dominant-negative TNF Attenuates Neurodegeneration and Behavioral Deficits in Hemiparkinsonian rats

McCoy, M. K., Ruhn, K. A., Martinez, T. N., McAlpine, F. E., Blesch, A., & Tansey, M. G. (2008) · Molecular Therapy · doi:10.1038/mt.2008.146 · Cited by 121

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

Oueslati, A., Paleologou, K. E., Schneider, B. L., Aebischer, P., & Lashuel, H. A. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.3784-11.2012 · Cited by 121

Delayed Dominant-Negative TNF Gene Therapy Halts Progressive Loss of Nigral Dopaminergic Neurons in a Rat Model of Parkinson's Disease

Harms, A. S., Barnum, C. J., Ruhn, K. A., Varghese, S., Treviño, I., Blesch, A., & Tansey, M. G. (2010) · Molecular Therapy · doi:10.1038/mt.2010.217 · Cited by 120

Cleavage of α-Synuclein by Calpain: Potential Role in Degradation of Fibrillized and Nitrated Species of α-Synuclein

Mishizen-Eberz, A. J., Norris, E. H., Giasson, B. I., Hodara, R., Ischiropoulos, H., Lee, V. M. ‐., Trojanowski, J. Q., & Lynch, D. R. (2005) · Biochemistry · doi:10.1021/bi047846q · Cited by 119

Activation of microglia induces symptoms of Parkinson’s disease in wild-type, but not in IL-1 knockout mice

Tanaka, S., Ishii, A., Ohtaki, H., Shioda, S., Yoshida, T., & Numazawa, S. (2013) · Journal of Neuroinflammation · doi:10.1186/1742-2094-10-143 · Cited by 118

Association of interleukin-1β polymorphisms with idiopathic Parkinson's disease

McGeer, P. L., Yasojima, K., & McGeer, E. G. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(02)00300-2 · Cited by 118

Cutting Edge: Granzyme B Proteolysis of a Neuronal Glutamate Receptor Generates an Autoantigen and Is Modulated by Glycosylation

Gahring, L. C., Carlson, N. G., Meyer, E. L., & Rogers, S. W. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.3.1433 · Cited by 118

Experimental Destruction of Substantia Nigra Initiated by Parkinson Disease Immunoglobulins

Chen, S., Le, W.-D., Xie, W., Alexianu, M. E., Engelhardt, J. I., Siklós, L., & Appel, S. H. (1998) · Archives of Neurology · doi:10.1001/archneur.55.8.1075 · Cited by 118

The gamma chain subunit of Fc receptors is required for alpha-synuclein-induced pro-inflammatory signaling in microglia

Cao, S., Standaert, D. G., & Harms, A. S. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-259 · Cited by 115

MHC class II positive microglia and lymphocytic infiltration are present in the substantia nigra and striatum in mouse model of Parkinson's disease.

Kurkowska-Jastrzębska, I., Wrońska, A., Kohutnicka, M., Członkowski, A., & Członkowska, A. (1999) · Acta Neurobiologiae Experimentalis · doi:10.55782/ane-1999-1289 · Cited by 114

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 113

Co‐expression of C‐terminal truncated alpha‐synuclein enhances full‐length alpha‐synuclein‐induced pathology

Ulusoy, A., Febbraro, F., Jensen, P. H., Kirik, D., & Romero‐Ramos, M. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07284.x · Cited by 111

Semisynthetic, Site-Specific Ubiquitin Modification of α-Synuclein Reveals Differential Effects on Aggregation

Meier, F., Abeywardana, T., Dhall, A., Marotta, N. P., Varkey, J., Langen, R., Chatterjee, C., & Pratt, M. R. (2012) · Journal of the American Chemical Society · doi:10.1021/ja300094r · Cited by 111

γδ+ T cells are increased in patients with Parkinson's disease

Fiszer, U., Mix, E., Fredrikson, S., Kostulas, V., Olsson, T. P., & Link, H. (1994) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(94)90154-6 · Cited by 108

Nitrated α-Synuclein Induces the Loss of Dopaminergic Neurons in the Substantia Nigra of Rats

Yu, Z., Xu, X., Xiang, Z., Zhou, J., Zhang, Z., Hu, C., & He, C. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009956 · Cited by 108

Influence of interleukin-1β gene polymorphisms on age-at-onset of sporadic Parkinson's disease

Nishimura, M., Mizuta, I., Mizuta, E., Yamasaki, S., Ohta, M., & Kuno, S. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)00991-5 · Cited by 104

Polymorphisms in the interleukin-1 alpha and beta genes and the risk for Parkinson's disease

Schulte, T., Schöls, L. J., Müller, T. H., Woitalla, D., Berger, K., & Krüger, R. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(02)00301-4 · Cited by 104

Conserved C-Terminal Charge Exerts a Profound Influence on the Aggregation Rate of α-Synuclein

Levitan, K., Chéreau, D., Cohen, S. I. A., Knowles, T. P. J., Dobson, C. M., Fink, A. L., Anderson, J. P., Goldstein, J. M., & Millhauser, G. L. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.05.046 · Cited by 103

Alteration in α‐synuclein mRNA expression in Parkinson's disease

Kingsbury, A. E., Daniel, S. E., Sangha, H., Eisen, S., Lees, A. J., & Foster, O. J. F. (2003) · Movement Disorders · doi:10.1002/mds.10683 · Cited by 102

Preconditioning of Microglia by α-Synuclein Strongly Affects the Response Induced by Toll-like Receptor (TLR) Stimulation

Roodveldt, C., Labrador‐Garrido, A., González‐Rey, E., Lachaud, C. C., Guilliams, T., Fernández-Montesinos, R., Benitez-Rondan, A., Robledo, G., Hmadcha, A., Delgado, M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079160 · Cited by 99

Axonopathy in an α-Synuclein Transgenic Model of Lewy Body Disease Is Associated with Extensive Accumulation of C-Terminal–Truncated α-Synuclein

Games, D., Seubert, P. A., Rockenstein, E. M., Patrick, C., Trejo, M., Ubhi, K. K., Ettle, B., Ghassemiam, M., Barbour, R., Schenk, D., et al. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.11.018 · Cited by 97

Tumor necrosis factor gene polymorphisms in patients with sporadic Parkinson's disease

Nishimura, M., Mizuta, I., Mizuta, E., Yamasaki, S., Ohta, M., Kaji, R., & Kuno, S. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)02111-5 · Cited by 95

Conditional transgenic mice expressing C-terminally truncated human α-synuclein (αSyn119) exhibit reduced striatal dopamine without loss of nigrostriatal pathway dopaminergic neurons

Daher, J. P. L., Ying, M., Banerjee, R., McDonald, R. S., Hahn, M. D., Yang, L., Beal, M. F., Thomas, B., Dawson, V. L., Dawson, T. M., et al. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-34 · Cited by 95

Genetic analysis of immunomodulating factors in sporadic Parkinson's disease

Krüger, R., Hardt, C., Tschentscher, F., Jäckel, S., Kuhn, W., Müller, T., Werner, J., Woitalla, D., Berg, D., Kühnl, N., et al. (2000) · Journal of Neural Transmission · doi:10.1007/s007020070078 · Cited by 93

Enhanced ubiquitin-dependent degradation by Nedd4 protects against α-synuclein accumulation and toxicity in animal models of Parkinson's disease

Davies, S. E. W., Hallett, P. J., Moens, T. G., Smith, G. A., Mangano, E. N., Kim, H. T., Goldberg, A. L., Liu, J., Ole Isacson, A., & Tofaris, G. K. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.12.011 · Cited by 92

Fcγ receptors are required for NF-κB signaling, microglial activation and dopaminergic neurodegeneration in an AAV-synuclein mouse model of Parkinson's disease

Cao, S., Theodore, S., & Standaert, D. G. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-42 · Cited by 91

Possible Involvement of Complement Factor C1q in the Clearance of Extracellular Neuromelanin From the Substantia Nigra in Parkinson Disease

Depboylu, C., Schafer, M. K.-H., Arias-Carrión, Ó., Oertel, W. H., Weihe, E., & Höglinger, G. U. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31820805b9 · Cited by 91

Bone Marrow-Derived Microglia Infiltrate into the Paraventricular Nucleus of Chronic Psychological Stress-Loaded Mice

Ataka, K., Asakawa, A., Nagaishi, K., Kaimoto, K., Sawada, A., Hayakawa, Y., Tatezawa, R., Inui, A., & Fujimiya, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081744 · Cited by 89

Exosomes-associated neurodegeneration and progression of Parkinson's disease.

Russo, I., Bubacco, L., & Greggio, E. (2012) · Europe PMC (PubMed Central) · Cited by 85

INTERFERON γ GENE EXPRESSION IN RAT CENTRAL NERVOUS SYSTEM GLIAL CELLS

Simone, R. D., Levi, G., & Aloisi, F. (1998) · Cytokine · doi:10.1006/cyto.1997.0314 · Cited by 83

Association of an interleukin 1B gene polymorphism (−511) with Parkinson's disease in Finnish patients

Mattila, K. M., Rinne, J. O., Lehtimäki, T. J., Röyttä, M., Ahonen, J.-P., & Hurme, M. (2002) · Journal of Medical Genetics · doi:10.1136/jmg.39.6.400 · Cited by 81

Late stages of hematopoiesis and B cell lymphopoiesis are regulated by α-synuclein, a key player in Parkinson's disease

Xiao, W., Shameli, A., Harding, C. V., Meyerson, H. J., & Maitta, R. W. (2014) · Immunobiology · doi:10.1016/j.imbio.2014.07.014 · Cited by 78

Cleavage of normal and pathological forms of α-synuclein by neurosin in vitro

Kasai, T., Tokuda, T., Yamaguchi, N., Watanabe, Y., Kametani, F., Nakagawa, M., & Mizuno, T. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.02.057 · Cited by 76

Gammadelta T Cells: Innately Adaptive Immune Cells?

Ferreira, L. M. R. (2013) · International Reviews of Immunology · doi:10.3109/08830185.2013.783831 · Cited by 73

Evidence for More than One Parkinson's Disease-Associated Variant within the HLA Region

Hill‐Burns, E. M., Factor, S. A., Zabetian, C. P., Thomson, G. J., & Payami, H. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027109 · Cited by 71

Functional promoter region polymorphism of the proinflammatory chemokine IL-8 gene associates with Parkinson's disease in the Irish

Ross, O. A., O'Neill, C. M., Rea, I. M., Lynch, T., Gosal, D. Y., Wallace, A., Curran, M. D., Middleton, D., & Gibson, J. M. (2004) · Human Immunology · doi:10.1016/j.humimm.2004.01.015 · Cited by 68

Chemokines (RANTES and MCP-1) and chemokine-receptors (CCR2 and CCR5) gene polymorphisms in Alzheimer's and Parkinson's disease

Huerta, C., Álvarez, V., Mata, I. F., Coto, E., Ribacoba, R., Martínez, C., Estrada, M. B., Guisasola, L. M., Salvador, C., Lahoz, C. H., et al. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.08.016 · Cited by 67

Erratum: IFN-γ signaling, with the synergistic contribution of TNF-α, mediates cell specific microglial and astroglial activation in experimental models of Parkinson’s disease

Barcia, C., Ros, C. M., Annese, V., Gómez, A. M., Ros‐Bernal, F., Aguado‐Llera, D., Martínez-Pagán, M. E., de Pablos, V., Fernández‐Villalba, E., & Herrero, M. T. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.123 · Cited by 67

Loss of CD4 T-cell–dependent tolerance to proteins with modified amino acids

Gauba, V., Grünewald, J., Gorney, V., Deaton, L. M., Kang, M., Bursulaya, B. D., Ou, W., Lerner, R. A., Schmedt, C., Geierstanger, B. H., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110042108 · Cited by 63

T cells discriminate between differentially phosphorylated forms of alphaB-crystallin, a major central nervous system myelin antigen

van Stipdonk, M. J. B. (1998) · International Immunology · doi:10.1093/intimm/10.7.943 · Cited by 62

Interleukin-10 (IL10) and tumor necrosis factor α (TNF) gene polymorphisms in Parkinson's disease patients

Białecka, M. A., Kłodowska-Duda, G. A., Kurzawski, M., Sławek, J. W., Gorzkowska, A., Opala, G., Białecki, P., Sagan, L. M., & Droździk, M. (2008) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2008.02.001 · Cited by 58

Alpha-Synuclein and Chaperones in Dementia With Lewy Bodies

Cantuti‐Castelvetri, I., Klucken, J., Ingelsson, M., Ramasamy, K., McLean, P. J., Frosch, M. P., Hyman, B. T., & Standaert, D. G. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000190063.90440.69 · Cited by 58

The JAK/STAT signaling pathway: from bench to clinic

Hu, X., li, J., Fu, M., Zhao, X., & Wang, W. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00791-1 · Cited by 2,633

Microglia in neurodegenerative diseases: mechanism and potential therapeutic targets

Gao, C., Jiang, J., Tan, Y., & Chen, S. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01588-0 · Cited by 1,616

Block of A1 astrocyte conversion by microglia is neuroprotective in models of Parkinson’s disease

Yun, S. P., Kam, T.-I., Panicker, N., Kim, S., Oh, Y., Park, J.-S., Kwon, S.-H., Park, Y. J., Karuppagounder, S. S., Park, H., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0051-5 · Cited by 1,123

Exposure to the functional bacterial amyloid protein curli enhances alpha-synuclein aggregation in aged Fischer 344 rats and Caenorhabditis elegans

Chen, S. G., Stribinskis, V., Rane, M. J., Demuth, D. R., Gozal, E., Roberts, A. M., Jagadapillai, R., Liu, R., Choe, K., Shivakumar, B., et al. (2016) · Scientific Reports · doi:10.1038/srep34477 · Cited by 463

Self-assembling dipeptide antibacterial nanostructures with membrane disrupting activity

Schnaider, L., Brahmachari, S., Schmidt, N. W., Mensa, B., Shaham‐Niv, S., Bychenko, D., Adler‐Abramovich, L., Shimon, L. J. W., Kolusheva, S., DeGrado, W. F., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01447-x · Cited by 411

Upregulation of α-synuclein following immune activation: Possible trigger of Parkinson's disease

Kasen, A., Houck, C., Burmeister, A. R., Sha, Q., Brundin, L., & Brundin, P. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105654 · Cited by 78

Alpha-synuclein and neuroinflammation in Parkinson's disease

Varanita, T., & Bubacco, L. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815950-7.00027-8 · Cited by 2

Mechanisms of innate and adaptive immune function in Parkinson disease

Allen, H. E. (n.d.) · ProQuest Demo Repository

Alpha-Synuclein and the Immune Response in Parkinson’s Disease

Roodveldt, C., Labrador‐Garrido, A., Izquierdo, G., & Pozo, D. (2011) · InTech eBooks · doi:10.5772/17417 · Cited by 3

Is α-synuclein the culprit of the Parkinsonian neurodegeneration?

Kirik, D., Gai, W., & Jensen, P. H. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2007.12.007 · Cited by 2