Adeno-Associated Virus Expression of α-Synuclein as a Tool to Model Parkinson’s Disease: Current Understanding and Knowledge Gaps

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 · see citing works

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 · see citing works

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 3,151 · see citing works

Non-motor features of Parkinson disease

Schapira, A. H. V., Chaudhuri, K. R., & Jenner, P. (2017) · Nature Reviews Neuroscience · doi:10.1038/nrn.2017.62 · Cited by 2,053 · see citing works

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 · see citing works

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 1,763 · see citing works

In vivo demonstration that α-synuclein oligomers are toxic

Winner, B., Jappelli, R., Maji, S. K., Desplats, P., Boyer, L. F., Aigner, S., Hetzer, C., Loher, T., Vilar, M., Campioni, S., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100976108 · Cited by 1,487 · see citing works

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 1,469 · see citing works

Intravascular AAV9 preferentially targets neonatal neurons and adult astrocytes

Foust, K. D., Nurre, E., Montgomery, C. L., Hernandez, A., Chan, C. M., & Kaspar, B. K. (2009) · Nature Biotechnology · doi:10.1038/nbt.1515 · Cited by 1,456 · see citing works

Transneuronal Propagation of Pathologic α-Synuclein from the Gut to the Brain Models Parkinson’s Disease

Kim, S., Kwon, S.-H., Kam, T.-I., Panicker, N., Karuppagounder, S. S., Lee, S., Lee, J. H., Kim, W. R., Kook, M., Foss, C. A., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.05.035 · Cited by 1,397 · see citing works

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 · cited 1× · see citing works

α-Synuclein strains cause distinct synucleinopathies after local and systemic administration

Peelaerts, W., Bousset, L., Van der Perren, A., Moskalyuk, A., Pulizzi, R., Giugliano, M., Van den Haute, C., Melki, R., & Baekelandt, V. (2015) · Nature · doi:10.1038/nature14547 · Cited by 1,130 · see citing works

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 · see citing works

Structure and Dynamics of Micelle-bound Human α-Synuclein

Ulmer, T. S., Bax, A., Cole, N. B., & Nussbaum, R. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411805200 · Cited by 966 · see citing works

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

Tuttle, M. D., Comellas, G., Nieuwkoop, A. J., Covell, D. J., Berthold, D. A., Kloepper, K. D., Courtney, J. M., Kim, J. K., Barclay, A. M., Kendall, A. K., et al. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3194 · Cited by 951 · see citing works

Direct Transfer of α-Synuclein from Neuron to Astroglia Causes Inflammatory Responses in Synucleinopathies

Lee, H.-J., Suk, J.-E., Patrick, C., Bae, E.-J., Cho, J.-H., Rho, S., Hwang, D., Masliah, E., & Lee, S.-J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.081125 · Cited by 877 · see citing works

Astrocytes Control Synapse Formation, Function, and Elimination

Chung, W.-S., Allen, N. J., & Eroglu, C. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a020370 · Cited by 839 · see citing works

Recombinant AAV Viral Vectors Pseudotyped with Viral Capsids from Serotypes 1, 2, and 5 Display Differential Efficiency and Cell Tropism after Delivery to Different Regions of the Central Nervous System

Burger, C., Gorbatyuk, O. S., Velardo, M. J., Peden, C. S., Williams, P., Zolotukhin, S., Reier, P. J., Mandel, R. J., & Muzyczka, N. (2004) · Molecular Therapy · doi:10.1016/j.ymthe.2004.05.024 · Cited by 741 · see citing works

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

Kirik, D., Rosenblad, C., Bürger, C., Lundberg, C., Johansen, T. E., Muzyczka, N., Mandel, R. J., & Björklund, A. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-07-02780.2002 · Cited by 730 · see citing works

Extracellular vesicles round off communication in the nervous system

Budnik, V., Ruiz-Cañada, C., & Wendler, F. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.29 · Cited by 712 · see citing works

The process of Lewy body formation, rather than simply α-synuclein fibrillization, is one of the major drivers of neurodegeneration

Mahul-Mellier, A.-L., Burtscher, J., Maharjan, N., Weerens, L., Croisier, M., Kuttler, F., Leleu, M., Knott, G. W., & Lashuel, H. A. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1913904117 · Cited by 710 · see citing works

Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons

Guo, J. L., Covell, D. J., Daniels, J. P., Iba, M., Stieber, A., Zhang, B., Riddle, D. M., Kwong, L. K., Xu, Y., Trojanowski, J. Q., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.057 · Cited by 680 · see citing works

α-Synuclein misfolding and Parkinson's disease

Breydo, L., Wu, J., & Uversky, V. N. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.002 · Cited by 656 · see citing works

Amphipathic helix motif: Classes and properties

Segrest, J. P., Loof, H. D., Dohlman, J. G., Brouillette, C. G., & Anantharamaiah, G. M. (1990) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340080202 · Cited by 642 · see citing works

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) · Journal of Neuroscience · doi:10.1523/jneurosci.20-17-06365.2000 · Cited by 641 · see citing works

The Role of Astrocyte Dysfunction in Parkinson’s Disease Pathogenesis

Booth, H. D. E., Hirst, W. D., & Wade-Martins, R. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.04.001 · Cited by 633 · see citing works

Structure of the toxic core of α-synuclein from invisible crystals

Rodríguez, J. A., Ivanova, M. I., Sawaya, M. R., Cascio, D., Reyes, F. E., Shi, D., Sangwan, S., Guenther, E. L., Johnson, L. M., Zhang, M., et al. (2015) · Nature · doi:10.1038/nature15368 · Cited by 629 · see citing works

Rodent models in neuroscience research: is it a rat race?

Ellenbroek, B., & Youn, J. (2016) · Disease Models & Mechanisms · doi:10.1242/dmm.026120 · Cited by 627 · see citing works

Prions hijack tunnelling nanotubes for intercellular spread

Gousset, K., Schiff, E., Langevin, C., Marijanovic, Z., Caputo, A., Browman, D., Chenouard, N., de Chaumont, F., Martino, A., Enninga, J., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1841 · Cited by 616 · see citing works

Astrocyte Kir4.1 ion channel deficits contribute to neuronal dysfunction in Huntington's disease model mice

Tong, X., Ao, Y., Faas, G. C., Nwaobi, S. E., Xu, J., Haustein, M. D., Anderson, M. A., Mody, I., Olsen, M. L., Sofroniew, M. V., et al. (2014) · Nature Neuroscience · doi:10.1038/nn.3691 · Cited by 592 · see citing works

Cell Biology and Pathophysiology of α-SynucleinPreprint

Burré, J., Sharma, M., & Südhof, T. C. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024091 · Cited by 576 · see citing works

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. A., 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 565 · see citing works

α-Synucleinopathy and selective dopaminergic neuron loss in a rat lentiviral-based model of Parkinson's disease

Bianco, C. L., Ridet, J.-L., Schneider, B. L., Déglon, N., & Aebischer, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.152339799 · Cited by 533 · see citing works

Activation of the unfolded protein response in Parkinson’s disease

Hoozemans, J. J. M., van Haastert, E. S., Eikelenboom, P., de Vos, R. A. I., Rozemuller, J. M., & Scheper, W. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.01.043 · Cited by 525 · see citing works

Analysis of Transduction Efficiency, Tropism and Axonal Transport of AAV Serotypes 1, 2, 5, 6, 8 and 9 in the Mouse Brain

Aschauer, D. F., Kreuz, S., & Rumpel, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076310 · Cited by 522 · see citing works

Neuropathology in mice expressing human alpha-synuclein

van der Putten, H., Wiederhold, K., Probst, A., Barbieri, S., Mistl, C., Danner, S., Kauffmann, S., Hofele, K., Spooren, W. P. J. M., Rüegg, M. A., et al. (2000) · PubMed Central · doi:10.5451/unibas-ep2767 · Cited by 505 · see citing works

Structure of membrane-bound α-synuclein from site-directed spin labeling and computational refinement

Jao, C. C., Hegde, B. G., Chen, J., Haworth, I. S., & Langen, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807826105 · Cited by 501 · see citing works

Ca2+ signaling in astrocytes from Ip3r2−/− mice in brain slices and during startle responses in vivo

Srinivasan, R., Huang, B. S., Venugopal, S., Johnston, A. D., Chai, H., Zeng, H., Golshani, P., & Khakh, B. S. (2015) · Nature Neuroscience · doi:10.1038/nn.4001 · Cited by 499 · see citing works

Selective induction of astrocytic gliosis generates deficits in neuronal inhibition

Ortinski, P. I., Dong, J., Mungenast, A., Yue, C., Takano, H., Watson, D. J., Haydon, P. G., & Coulter, D. A. (2010) · Nature Neuroscience · doi:10.1038/nn.2535 · Cited by 495 · see citing works

α-Synuclein Is Localized to Mitochondria-Associated ER Membranes

Guardia-Laguarta, C., Area-Gómez, E., Rüb, C., Liu, Y.-H., Magrané, J., Becker, D., Voos, W., Schon, E., & Przedborski, S. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.2507-13.2014 · Cited by 489 · see citing works

Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour

Fusco, G., Simone, A. D., Gopinath, T., Vostrikov, V. V., Vendruscolo, M., Dobson, C. M., & Veglia, G. (2014) · Nature Communications · doi:10.1038/ncomms4827 · Cited by 483 · see citing works

A soluble α-synuclein construct forms a dynamic tetramer

Wang, W., Perovic, I., Chittuluru, J., Kaganovich, A., Nguyen, L. T. T., Liao, J., Auclair, J. R., Johnson, D., Landeru, A., Simorellis, A. K., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113260108 · Cited by 478 · see citing works

Neuropathology in Mice Expressing Human α-Synuclein

van der Putten, H., Wiederhold, K., Probst, A., Barbieri, S., Mistl, C., Danner, S., Kauffmann, S., Hofele, K., Spooren, W. P. J. M., Rüegg, M. A., et al. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-16-06021.2000 · Cited by 478 · see citing works

Development of α-synuclein immunoreactive astrocytes in the forebrain parallels stages of intraneuronal pathology in sporadic Parkinson’s disease

Braak, H., Sastre, M., & Del Tredici, K. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0244-3 · Cited by 462 · see citing works

Modeling Parkinson’s Disease With the Alpha-Synuclein Protein

Gómez-Benito, M., Granado, N., García‐Sanz, P., Michel, A., Dumoulin, M., & Moratalla, R. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00356 · Cited by 445 · see citing works

New Transgenic Mouse Lines for Selectively Targeting Astrocytes and Studying Calcium Signals in Astrocyte Processes In Situ and In Vivo

Srinivasan, R., Lu, T.-Y., Chai, H., Xu, J., Huang, B. S., Golshani, P., Coppola, G., & Khakh, B. S. (2016) · Neuron · doi:10.1016/j.neuron.2016.11.030 · Cited by 443 · see citing works

Alpha-synuclein structure and Parkinson’s disease – lessons and emerging principles

Meade, R. M., Fairlie, D. P., & Mason, J. M. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0329-1 · Cited by 430 · see citing works

Astrocytes in Neurodegenerative Disease: Table 1.

Phatnani, H., & Maniatis, T. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a020628 · Cited by 420 · see citing works

Major Shifts in Glial Regional Identity Are a Transcriptional Hallmark of Human Brain Aging

Soreq, L., Rose, J., Soreq, E., Hardy, J., Trabzuni, D., Cookson, M. R., Smith, C., Ryten, M., Patani, R., & Ule, J. (2017) · Cell Reports · doi:10.1016/j.celrep.2016.12.011 · Cited by 419 · see citing works

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

Bussell, R., & Eliezer, D. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00520-5 · Cited by 418 · see citing works

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

Larsen, K. E., Schmitz, Y., Troyer, M. D., Mosharov, E. V., Dietrich, P., Quazi, A. Z., Savalle, M., Nemani, V. M., Chaudhry, F. A., Edwards, R. H., et al. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3821-06.2006 · Cited by 415 · see citing works

On Cell Loss and Selective Vulnerability of Neuronal Populations in Parkinson's Disease

Giguère, N., Burke, S., & Trudeau, L. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00455 · Cited by 415 · see citing works

Tunneling nanotubes spread fibrillar α-synuclein by intercellular trafficking of lysosomes

Abounit, S., Bousset, L., Loria, F., Zhu, S., de Chaumont, F., Pieri, L., Olivo‐Marin, J., Melki, R., & Zurzolo, C. (2016) · The EMBO Journal · doi:10.15252/embj.201593411 · Cited by 414 · see citing works

Transduction characteristics of adeno-associated virus vectors expressing cap serotypes 7, 8, 9, and Rh10 in the mouse brain

Cearley, C. N., & Wolfe, J. H. (2006) · Molecular Therapy · doi:10.1016/j.ymthe.2005.11.015 · Cited by 409 · see citing works

Gender differences in Parkinson's disease: Clinical characteristics and cognition

Miller, I. N., & Cronin‐Golomb, A. (2010) · Movement Disorders · doi:10.1002/mds.23388 · Cited by 405 · see citing works

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

Chu, Y., & Kordower, J. H. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.08.021 · Cited by 396 · see citing works

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 392 · see citing works

Widespread transneuronal propagation of α-synucleinopathy triggered in olfactory bulb mimics prodromal Parkinson’s disease

Rey, N. L., Steiner, J. A., Maroof, N., Luk, K. C., Madaj, Z., Trojanowski, J. Q., Lee, V. M. ‐., & Brundin, P. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20160368 · Cited by 389 · see citing works

Multiple Tight Phospholipid-Binding Modes of α-Synuclein Revealed by Solution NMR Spectroscopy

Bodner, C. R., Dobson, C. M., & Bax, A. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.05.066 · Cited by 370 · see citing works

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 367 · see citing works

Slow oscillatory activity and levodopa-induced dyskinesias in Parkinson's disease

Alonso‐Frech, F. (2006) · Brain · doi:10.1093/brain/awl103 · Cited by 360 · see citing works

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

Diao, J., Burré, J., Vivona, S., Cipriano, D. J., Sharma, M., Kyoung, M., Südhof, T. C., & Brünger, A. T. (2013) · eLife · doi:10.7554/elife.00592 · Cited by 351 · see citing works

Astrocytic expression of Parkinson's disease-related A53T α-synuclein causes neurodegeneration in mice

Gu, X., Long, C.-X., Sun, L., Xie, C., Lin, X. Z., & Cai, H. (2010) · Molecular Brain · doi:10.1186/1756-6606-3-12 · Cited by 341 · see citing works

Human Astrocytes Transfer Aggregated Alpha-Synuclein via Tunneling Nanotubes

Rostami, J., Holmqvist, S., Lindström, V., Sigvardson, J., Westermark, G. T., Ingelsson, M., Bergström, J., Roybon, L., & Erlandsson, A. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.0983-17.2017 · Cited by 339 · see citing works

Inoculation of α-synuclein preformed fibrils into the mouse gastrointestinal tract induces Lewy body-like aggregates in the brainstem via the vagus nerve

Uemura, N., Yagi, H., Uemura, M. T., Hatanaka, Y., Yamakado, H., & Takahashi, R. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0257-5 · Cited by 328 · see citing works

Lentiviral vector delivery of parkin prevents dopaminergic degeneration in an α-synuclein rat model of Parkinson's disease

Bianco, C. L., Schneider, B. L., Bauer, M., Sajadi, A., Brice, A., Iwatsubo, T., & Aebischer, P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405313101 · Cited by 322 · see citing works

Extensive graft-derived dopaminergic innervation is maintained 24 years after transplantation in the degenerating parkinsonian brain

Li, W., Englund, E., Widner, H., Mattsson, B., van Westen, D., Lätt, J., Rehncrona, S., Brundin, P., Björklund, A., Lindvall, O., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605245113 · Cited by 313 · see citing works

Gene therapy for neurological disorders: progress and prospects

Deverman, B. E., Ravina, B. M., Bankiewicz, K. S., Paul, S. M., & Sah, D. W. Y. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.110 · Cited by 306 · see citing works

Comparative Analysis of Adeno-Associated Viral Vector Serotypes 1, 2, 5, 7, And 8 in Mouse Brain

Taymans, J.-M., Vandenberghe, L. H., Haute, C. V. D., Thiry, I., Deroose, C. M., Mortelmans, L., Wilson, J. M., Debyser, Z., & Baekelandt, V. (2007) · Human Gene Therapy · doi:10.1089/hum.2006.178 · Cited by 305 · see citing works

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 294 · see citing works

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

Gosavi, N., Lee, H.-J., Lee, J. S., Patel, S. S., & Lee, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208194200 · Cited by 294 · see citing works

The Concept of Prodromal Parkinson’s Disease

Mahlknecht, P., Seppi, K., & Poewe, W. H. (2015) · Journal of Parkinson s Disease · doi:10.3233/jpd-150685 · Cited by 291 · see citing works

Progressive neurodegenerative and behavioural changes induced by AAV-mediated overexpression of α-synuclein in midbrain dopamine neurons

Decressac, M., Mattsson, B., Lundblad, M., Weikop, P., & Björklund, A. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.013 · Cited by 286 · see citing works

α-Synuclein transfer between neurons and astrocytes indicates that astrocytes play a role in degradation rather than in spreading

Loría, F., Vargas, J., Bousset, L., Syan, S., Salles, A., Melki, R., & Zurzolo, C. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1746-2 · Cited by 278 · see citing works

Overexpression of α‐synuclein in rat substantia nigra results in loss of dopaminergic neurons, phosphorylation of α‐synuclein and activation of caspase‐9: resemblance to pathogenetic changes in Parkinson's disease

YAMADA, M., Iwatsubo, T., Mizuno, Y., & Mochizuki, H. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02728.x · Cited by 270 · see citing works

The relevance of gender in Parkinson’s disease: a review

Picillo, M., Nicoletti, A. S. Q., Fetoni, V., Garavaglia, B., Barone, P., & Pellecchia, M. T. (2017) · Journal of Neurology · doi:10.1007/s00415-016-8384-9 · Cited by 261 · see citing works

Alterations in neuronal activity in basal ganglia-thalamocortical circuits in the parkinsonian state

Galván, A., Devergnas, A. D., & Wichmann, T. (2015) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2015.00005 · Cited by 250 · see citing works

Erratum: Gene therapy for neurological disorders: progress and prospects

Deverman, B. E., Ravina, B. M., Bankiewicz, K. S., Paul, S. M., & Sah, D. W. Y. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.158 · Cited by 248 · see citing works

Localization of α-synuclein to mitochondria within midbrain of mice

Li, W.-W., Yang, R., Guo, J.-C., Ren, H., Zha, X., Cheng, J.-S., & Cai, D. (2007) · Neuroreport · doi:10.1097/wnr.0b013e3282f03db4 · Cited by 245 · see citing works

CX3CL1 reduces neurotoxicity and microglial activation in a rat model of Parkinson’s disease

Pabon, M. M., Bachstetter, A. D., Hudson, C. E., Gemma, C., & Bickford, P. C. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-9 · Cited by 241 · see citing works

Degeneration in Different Parkinsonian Syndromes Relates to Astrocyte Type and Astrocyte Protein Expression

Song, Y. J. C., Halliday, G. M., Holton, J. L., Lashley, T., O’Sullivan, S. S., McCann, H., Lees, A. J., Ozawa, T., Williams, D. R., Lockhart, P. J., et al. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181b66f1b · Cited by 239 · see citing works

Animal models of α-synucleinopathy for Parkinson disease drug development

Koprich, J. B., Kalia, L. V., & Brotchie, J. M. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.75 · Cited by 235 · see citing works

Modeling Parkinson’s disease pathology by combination of fibril seeds and α-synuclein overexpression in the rat brain

Thakur, P. S., Breger, L. S., Lundblad, M., Wan, O. W., Mattsson, B., Luk, K. C., Lee, V. M. ‐., Trojanowski, J. Q., & Björklund, A. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1710442114 · Cited by 235 · see citing works

Extensive uptake of α-synuclein oligomers in astrocytes results in sustained intracellular deposits and mitochondrial damage

Lindström, V., Gustafsson, G., Sanders, L. H., Howlett, E. H., Sigvardson, J., Kasrayan, A., Ingelsson, M., Bergström, J., & Erlandsson, A. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.04.009 · Cited by 233 · cited 2× · see citing works

The synucleins.

George, J. M. (2001) · Genome biology · doi:10.1186/gb-2001-3-1-reviews3002 · Cited by 233 · see citing works

Astrocytic control of synaptic function

Papouin, T., Dunphy, J. M., Tolman, M., Foley, J., & Haydon, P. G. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0154 · Cited by 229 · see citing works

Astrocytes and Therapeutics for Parkinson's Disease

Rappold, P. M., & Tieu, K. (2010) · Neurotherapeutics · doi:10.1016/j.nurt.2010.07.001 · Cited by 228 · see citing works

Seeking a Mechanism for the Toxicity of Oligomeric α-Synuclein

Hall‐Roberts, H., & Brown, D. R. (2015) · Biomolecules · doi:10.3390/biom5020282 · Cited by 213 · see citing works

The Roles of Post-translational Modifications on α-Synuclein in the Pathogenesis of Parkinson’s Diseases

Zhang, J., Li, X., & Li, J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00381 · Cited by 213 · see citing works

Dopaminergic Cell Loss Induced by Human A30P α -Synuclein Gene Transfer to the Rat Substantia Nigra

Klein, R. L., King, M. A., Hamby, M. E., & Meyer, E. M. (2002) · Human Gene Therapy · doi:10.1089/10430340252837206 · Cited by 209 · see citing works

Evolving basic, pathological and clinical concepts in PD

Kalia, L. V., & Lang, A. E. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.249 · Cited by 208 · see citing works

A photostable fluorescent marker for the superresolution live imaging of the dynamic structure of the mitochondrial cristae

Wang, C., Taki, M., Sato, Y., Tamura, Y., Yaginuma, H., Okada, Y., & Yamaguchi, S. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1905924116 · Cited by 204 · see citing works

Glia and alpha-synuclein in neurodegeneration: A complex interaction

Brück, D., Wenning, G. K., Stefanova, N., & Fellner, L. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.03.003 · Cited by 202 · see citing works

Capsid Serotype and Timing of Injection Determines AAV Transduction in the Neonatal Mice Brain

Chakrabarty, P., Rosario, A. M., Cruz, P. E., Siemienski, Z. B., Ceballos‐Diaz, C., Crosby, K. W., Jansen, K. R., Borchelt, D., Kim, J., Jankowsky, J. L., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067680 · Cited by 201 · see citing works

rAAV2/7 vector-mediated overexpression of alpha-synuclein in mouse substantia nigra induces protein aggregation and progressive dose-dependent neurodegeneration

Oliveras-Salvá, M., Van der Perren, A., Casadei, N., Stroobants, S., Nuber, S., D’Hooge, R., Van den Haute, C., & Baekelandt, V. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-44 · Cited by 191 · see citing works

Phosphorylation Does Not Prompt, Nor Prevent, the Formation of -synuclein Toxic Species in a Rat Model of Parkinson's Disease

da Silveira, S. A., Schneider, B. L., Cifuentes-Díaz, C., Sage, D., Abbas‐Terki, T., Iwatsubo, T., Unser, M. A., & Aebischer, P. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn417 · Cited by 190 · see citing works

Adeno-associated Virus (AAV) Serotypes Have Distinctive Interactions with Domains of the Cellular AAV Receptor

Pillay, S., Zou, W., Cheng, F., Puschnik, A. S., Meyer, N., Ganaie, S. S., Deng, X., Wosen, J. E., Davulcu, O., Yan, Z., et al. (2017) · Journal of Virology · doi:10.1128/jvi.00391-17 · Cited by 190 · see citing works

Alpha-Synuclein Physiology and Pathology: A Perspective on Cellular Structures and Organelles

Bernal-Conde, L. D., Ramos-Acevedo, R., Reyes-Hernández, M. A., Balbuena-Olvera, A. J., Morales-Moreno, I. D., Argüero‐Sánchez, R., Schüle, B., & Guerra‐Crespo, M. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01399 · Cited by 188 · see citing works

Dopaminergic neuron loss and up‐regulation of chaperone protein mRNA induced by targeted over‐expression of alpha‐synuclein in mouse substantia nigra

Martin, J. L. S., Klucken, J., Outeiro, T. F., Nguyen, P. T., Keller-McGandy, C. E., Cantuti‐Castelvetri, I., Grammatopoulos, T. N., Standaert, D. G., Hyman, B. T., & McLean, P. J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04310.x · Cited by 184 · see citing works

Elevated tonic extracellular dopamine concentration and altered dopamine modulation of synaptic activity precede dopamine loss in the striatum of mice overexpressing human α‐synuclein

Lam, H. A., Wu, N., Cely, I., Kelly, R. L., Hean, S., Richter, F., Magen, I., Cepeda, C., Ackerson, L. C., Walwyn, W., et al. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22611 · Cited by 184 · see citing works

α-Synuclein fibrils recruit peripheral immune cells in the rat brain prior to neurodegeneration

Harms, A. S., Delic, V., Thome, A. D., Bryant, N., Liu, Z., Chandra, S., Jurkuvenaite, A., & West, A. B. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0494-9 · Cited by 181 · see citing works

α-Synuclein and astrocytes: tracing the pathways from homeostasis to neurodegeneration in Lewy body disease

Sorrentino, Z. A., Giasson, B. I., & Chakrabarty, P. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01977-2 · Cited by 181 · see citing works

Rodent models of Parkinson's disease: beyond the motor symptomatology

Campos, F. L., Carvalho, M. M., Cristóvão, A. C., Je, G., Baltazar, G., Salgado, A. J., Kim, Y., & Sousa, N. (2013) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2013.00175 · Cited by 179 · see citing works

Brain-to-stomach transfer of α-synuclein via vagal preganglionic projections

Ulusoy, A., Phillips, R. J., Helwig, M., Klinkenberg, M., Powley, T. L., & Di Monte, D. A. (2017) · Acta Neuropathologica · doi:10.1007/s00401-016-1661-y · Cited by 179 · see citing works

AAV1/2-induced overexpression of A53T-α-synuclein in the substantia nigra results in degeneration of the nigrostriatal system with Lewy-like pathology and motor impairment: a new mouse model for Parkinson’s disease

Ip, C. W., Klaus, L.-C., Karikari, A. A., Visanji, N. P., Brotchie, J. M., Lang, A. E., Volkmann, J., & Koprich, J. B. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0416-x · Cited by 173 · see citing works

Neuropathology in Mice Expressing Mouse Alpha-Synuclein

Rieker, C., Dev, K. K., Lehnhoff, K., Barbieri, S., Ksiazek, I., Kauffmann, S., Danner, S., Schell, H., Boden, C., Rüegg, M. A., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024834 · Cited by 168 · see citing works

Assessment of α-Synuclein Secretion in Mouse and Human Brain Parenchyma

Emmanouilidou, E., Elenis, D., Papasilekas, T., Stranjalis, G., Gerozissis, K., Ioannou, P. C., & Vekrellis, K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022225 · Cited by 163 · see citing works

Cellular selectivity of AAV serotypes for gene delivery in neurons and astrocytes by neonatal intracerebroventricular injection

Hammond, S. L., Leek, A. N., Richman, E. H., & Tjalkens, R. B. (2017) · PLoS ONE · doi:10.1371/journal.pone.0188830 · Cited by 161 · see citing works

Glial phagocytic clearance in Parkinson’s disease

Tremblay, M., Cookson, M., & Civiero, L. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0314-8 · Cited by 159 · see citing works

Animal models of the non-motor features of Parkinson's disease

McDowell, K. A., & Chesselet, M. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.040 · Cited by 158 · see citing works

α-synuclein transfer through tunneling nanotubes occurs in SH-SY5Y cells and primary brain pericytes from Parkinson’s disease patients

Dieriks, B. V., Park, T. I.-H., Fourie, C., Faull, R. L. M., Dragunow, M., & Curtis, M. A. (2017) · Scientific Reports · doi:10.1038/srep42984 · Cited by 158 · see citing works

Nigrostriatal overabundance of α-synuclein leads to decreased vesicle density and deficits in dopamine release that correlate with reduced motor activity

Gaugler, M. N. M., Genç, Ö., Bobela, W., Mohanna, S., Ardah, M. T., El‐Agnaf, O. M. A., Cantoni, M., Bensadoun, J., Schneggenburger, R., Knott, G. W., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0963-y · Cited by 150 · see citing works

Demonstration of α-Synuclein Immunoreactivity in Neuronal and Glial Cytoplasm in Normal Human Brain Tissue Using Proteinase K and Formic Acid Pretreatment

Mori, F., Tanji, K., Yoshimoto, M., Takahashi, H., & Wakabayashi, K. (2002) · Experimental Neurology · doi:10.1006/exnr.2002.7929 · Cited by 149 · see citing works

Next-generation AAV vectors—Do not judge a virus (only) by its cover

Domenger, C., & Grimm, D. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz148 · Cited by 147 · see citing works

Abrogating Native α-Synuclein Tetramers in Mice Causes a L-DOPA-Responsive Motor Syndrome Closely Resembling Parkinson’s Disease

Nuber, S., Rajsombath, M. M., Minakaki, G., Winkler, J., Müller, C. P., Ericsson, M., Caldarone, B. J., Dettmer, U., & Selkoe, D. J. (2018) · Neuron · doi:10.1016/j.neuron.2018.09.014 · Cited by 145 · see citing works

Comparison of the behavioural and histological characteristics of the 6-OHDA and α-synuclein rat models of Parkinson's disease

Decressac, M., Mattsson, B., & Björklund, A. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.02.012 · Cited by 144 · see citing works

Early-onset impairment of the ubiquitin-proteasome system in dopaminergic neurons caused by α-synuclein

McKinnon, C., de Snoo, M. L., Gondard, E., Neudorfer, C., Chau, H., Ngana, S. G., O’Hara, D. M., Brotchie, J. M., Koprich, J. B., Lozano, A. M., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-0894-0 · Cited by 144 · see citing works

Intrastriatal injection of preformed alpha-synuclein fibrils alters central and peripheral immune cell profiles in non-transgenic mice

Earls, R. H., Menees, K. B., Chung, J., Barber, J., Gutekunst, C.-A., Hazim, M. G., & Lee, J.-K. (2019) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1636-8 · Cited by 138 · see citing works

Extracellular aggregated alpha synuclein primarily triggers lysosomal dysfunction in neural cells prevented by trehalose

Hoffmann, A.-C., Minakaki, G., Menges, S., Salvi, R., Savitskiy, S., Kazman, A., Miranda, H. V., Mielenz, D., Klucken, J., Winkler, J., et al. (2019) · Scientific Reports · doi:10.1038/s41598-018-35811-8 · Cited by 133 · see citing works

Non-Motor Symptoms of Parkinson’s Disease and Their Impact on Quality of Life in a Cohort of Moroccan Patients

Tibar, H., Bayad, K. E., Bouhouche, A., Haddou, E. H. A. B., Benomar, A., Yahyaoui, M., Benazzouz, A., & Regragui, W. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00170 · Cited by 132 · see citing works

Lentiviral nigral delivery of GDNF does not prevent neurodegeneration in a genetic rat model of Parkinson's disease

Bianco, C. L., Déglon, N., Pralong, W. F., & Aebischer, P. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.06.008 · Cited by 129 · see citing works

Lack of additive role of ageing in nigrostriatal neurodegeneration triggered by α-synuclein overexpression

Bourdenx, M., Doveró, S., Engeln, M., Bido, S., Bastide, M. F., Dutheil, N., Vollenweider, I., Baud, L., Piron, C., Grouthier, V., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0222-2 · Cited by 125 · see citing works

α-Synuclein and Mitochondria: Partners in Crime?

Nakamura, K. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0182-9 · Cited by 123 · see citing works

Region specific mitochondrial impairment in mice with widespread overexpression of alpha-synuclein

Subramaniam, S., Vergnes, L., Franich, N. R., Reue, K., & Chesselet, M. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.06.017 · Cited by 119 · see citing works

Neuropathology and Neurodegeneration in Rodent Brain Induced by Lentiviral Vectormediated Overexpression of α‐Synuclein

Lauwers, E., Debyser, Z., Dorpe, J. V., Strooper, B. D., Nuttin, B., & Baekelandt, V. (2003) · Brain Pathology · doi:10.1111/j.1750-3639.2003.tb00035.x · Cited by 116 · see citing works

Astrocytes Protect Human Dopaminergic Neurons from α-Synuclein Accumulation and Propagation

Tsunemi, T., Ishiguro, Y., Yoroisaka, A., Valdez, C., Miyamoto, K., Ishikawa, K., Saiki, S., Akamatsu, W., Hattori, N., & Krainc, D. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.0954-20.2020 · Cited by 115 · see citing works

Progressive Neurodegeneration or Endogenous Compensation in an Animal Model of Parkinson's Disease Produced by Decreasing Doses of Alpha-Synuclein

Koprich, J. B., Johnston, T. H., Huot, P., Reyes, M. G., Espinosa, M. C., & Brotchie, J. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017698 · Cited by 113 · see citing works

Alpha-Synuclein Produces Early Behavioral Alterations via Striatal Cholinergic Synaptic Dysfunction by Interacting With GluN2D N -Methyl-D-Aspartate Receptor Subunit

Tozzi, A., de Iure, A., Bagetta, V., Tantucci, M., Durante, V., Quiroga‐Varela, A., Costa, C., Filippo, M. D., Ghiglieri, V., Latagliata, E. C., et al. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2015.08.013 · Cited by 112 · see citing works

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 · see citing works

How can rAAV ‐α‐synuclein and the fibril α‐synuclein models advance our understanding of Parkinson's disease?

Volpicelli‐Daley, L. A., Kirik, D., Stoyka, L. E., Standaert, D. G., & Harms, A. S. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13627 · Cited by 110 · see citing works

Prodromal non-motor symptoms of Parkinson's disease

Pellicano, C., Benincasa, D., Pisani, V., Buttarelli, F. R., Giovannelli, M., & Pontieri, F. E. (2007) · Neuropsychiatric Disease and Treatment · doi:10.2147/nedt.2007.3.1.145 · Cited by 102 · see citing works

Lentiviral vectors as tools to understand central nervous system biology in mammalian model organisms

Parr-Brownlie, L., Bosch-Bouju, C., Schoderboeck, L., Sizemore, R. J., Abraham, W., & Hughes, S. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00014 · Cited by 101 · see citing works

Aggregation of αSynuclein promotes progressive in vivo neurotoxicity in adult rat dopaminergic neurons

Taschenberger, G., Garrido, M., Tereshchenko, Y., Bähr, M., Zweckstetter, M., & Kügler, S. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0926-8 · Cited by 100 · see citing works

Longitudinal follow-up and characterization of a robust rat model for Parkinson's disease based on overexpression of alpha-synuclein with adeno-associated viral vectors.

der Perren, A. V., Toelen, J., Casteels, C., Macchi, F., Rompuy, A. V., Sarre, S., Casadei, N., Nuber, S., Himmelreich, U., Garcia, M. I. O., et al. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.11.015 · Cited by 95 · see citing works

Modulation of the trafficking of the human serotonin transporter by human alpha‐synuclein

Wersinger, C., Rusnak, M., & Sidhu, A. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.04900.x · Cited by 93 · see citing works

Comparison of transduction efficiency of recombinant AAV serotypes 1, 2, 5, and 8 in the rat nigrostriatal system

McFarland, N. R., Lee, J., Hyman, B. T., & McLean, P. J. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06010.x · Cited by 91 · see citing works

Morphological and Behavioral Impact of AAV2/5-Mediated Overexpression of Human Wildtype Alpha-Synuclein in the Rat Nigrostriatal System

Gombash, S. E., Manfredsson, F. P., Kemp, C. J., Kuhn, N. C., Fleming, S. M., Egan, A. E., Grant, L. M., Ciucci, M. R., MacKeigan, J. P., & Sortwell, C. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081426 · Cited by 91 · see citing works

Neuron-to-neuron α-synuclein propagation in vivo is independent of neuronal injury

Ulusoy, A., Musgrove, R. E., Rusconi, R., Klinkenberg, M., Helwig, M., Schneider, A., & Monte, D. A. D. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0198-y · Cited by 91 · see citing works

Uptake and mitochondrial dysfunction of alpha-synuclein in human astrocytes, cortical neurons and fibroblasts

Braidy, N., Gai, W.-P., Xu, Y. H., Sachdev, P., Guillemin, G. J., Jiang, X.-M., Ballard, J. W. O., Horan, M. P., Fang, Z. M., Chong, B. H., et al. (2013) · Translational Neurodegeneration · doi:10.1186/2047-9158-2-20 · Cited by 91 · see citing works

Angiotensin Type 1 Receptor Antagonists Protect Against Alpha-Synuclein-Induced Neuroinflammation and Dopaminergic Neuron Death

Rodriguez-Perez, A. I., Sucunza, D., Pedrosa, M. A., Garrido‐Gil, P., Kulisevsky, J., Lanciego, J. L., & Labandeira-García, J. L. (2018) · Neurotherapeutics · doi:10.1007/s13311-018-0646-z · Cited by 91 · see citing works

Genetic mouse models for Parkinson's disease display severe pathology in glial cell mitochondria

Schmidt, S., Linnartz‐Gerlach, B., Mendritzki, S., Sczepan, T., Lübbert, M., Stichel, C. C., & Lübbert, H. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddq564 · Cited by 88 · see citing works

α-Synuclein Stimulates a Dopamine Transporter-dependent Chloride Current and Modulates the Activity of the Transporter*

Swant, J., Goodwin, J., North, A., Ali, A. A., Gamble-George, J., Chirwa, S., & Khoshbouei, H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.241232 · Cited by 85 · see citing works

Alpha Synuclein Connects the Gut-Brain Axis in Parkinson’s Disease Patients – A View on Clinical Aspects, Cellular Pathology and Analytical Methodology

Schaeffer, E., Kluge, A., Bottner, M. B., Zunke, F., Cossais, F., Berg, D., & Arnold, P. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.573696 · Cited by 84 · see citing works

Impact of monomeric, oligomeric and fibrillar alpha-synuclein on astrocyte reactivity and toxicity to neurons

Chavarría, C., Rodríguez-Bottero, S., Quijano, C., Cassina, P., & Souza, J. M. (2018) · Biochemical Journal · doi:10.1042/bcj20180297 · Cited by 82 · see citing works

Transcription factor EB overexpression prevents neurodegeneration in experimental synucleinopathies

Arotçarena, M.-L., Bourdenx, M., Dutheil, N., Thiolat, M.-L., Doudnikoff, É., Doveró, S., Ballabio, A., Fernagut, P., Meissner, W. G., Bézard, E., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.129719 · Cited by 82 · see citing works

Subthalamic nucleus neuronal firing rate increases with Parkinson's disease progression

Remple, M. S., Bradenham, C. H., Kao, C., Charles, D. P., Neimat, J. S., & Konrad, P. E. (2011) · Movement Disorders · doi:10.1002/mds.23708 · Cited by 81 · see citing works

Seeding and transgenic overexpression of alpha‐synuclein triggers dendritic spine pathology in the neocortex

Blumenstock, S., Rodrigues, E. F., Peters, F., Blázquez‐Llorca, L., Schmidt, F., Giese, A., & Herms, J. W. (2017) · EMBO Molecular Medicine · doi:10.15252/emmm.201607305 · Cited by 77 · see citing works

Subcellular localization of alpha-synuclein aggregates and their interaction with membranes

Colla, E., Miraglia, F., Ricci, A., & Rota, L. (2018) · Neural Regeneration Research · doi:10.4103/1673-5374.235013 · Cited by 74 · see citing works

The hidden side of Parkinson’s disease: Studying pain, anxiety and depression in animal models

Faivre, F., Joshi, A., Bézard, E., & Barrot, M. (2018) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2018.10.004 · Cited by 73 · see citing works

Intracellular delivery of Parkin rescues neurons from accumulation of damaged mitochondria and pathological α-synuclein

chung, E., Choi, Y., Park, J., Nah, W., Park, J.-H., Jung, Y., Lee, J., Lee, H., Park, S., Hwang, S., et al. (2020) · Science Advances · doi:10.1126/sciadv.aba1193 · Cited by 68 · see citing works

Depressive-like phenotype induced by AAV-mediated overexpression of human α-synuclein in midbrain dopaminergic neurons

Caudal, D., Alvarsson, A., Björklund, A., & Svenningsson, P. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.09.002 · Cited by 67 · see citing works

AAV Vector-Mediated Gene Delivery to Substantia Nigra Dopamine Neurons: Implications for Gene Therapy and Disease Models

Albert, K., Voutilainen, M. H., Domanskyi, A., & Airavaara, M. (2017) · Genes · doi:10.3390/genes8020063 · Cited by 66 · see citing works

Functional correlates of exaggerated oscillatory activity in basal ganglia output in hemiparkinsonian rats

Brazhnik, E. S., Novikov, N., McCoy, A. J., Cruz, A. V., & Walters, J. R. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.07.010 · Cited by 63 · see citing works

The Assembly-Activating Protein Promotes Stability and Interactions between AAV’s Viral Proteins to Nucleate Capsid Assembly

Maurer, A. C., Pacouret, S., Diaz, A. K. C., Blake, J., Andrés‐Mateos, E., & Vandenberghe, L. H. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.026 · Cited by 62 · see citing works

Viral Vector-Based Models of Parkinson’s Disease

der Perren, A. V., den Haute, C. V., & Baekelandt, V. (2014) · Current topics in behavioral neurosciences · doi:10.1007/7854_2014_310 · Cited by 61 · see citing works

Are rodent models of Parkinson’s disease behaving as they should?

Vingill, S., Connor‐Robson, N., & Wade‐Martins, R. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.10.021 · Cited by 60 · see citing works

α-Synuclein and Glia in Parkinson’s Disease: A Beneficial or a Detrimental Duet for the Endo-Lysosomal System?

Filippini, A., Gennarelli, M., & Russo, I. (2019) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-019-00649-9 · Cited by 58 · see citing works

Dysregulated dopamine storage increases the vulnerability to α-synuclein in nigral neurons

Ulusoy, A., Björklund, T., Buck, K., & Kirik, D. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.05.012 · Cited by 57 · see citing works

Erythrocytic α-synuclein contained in microvesicles regulates astrocytic glutamate homeostasis: a new perspective on Parkinson’s disease pathogenesis

Sheng, L., Stewart, T., Yang, D., Thorland, E., Soltys, D., Aro, P., Khrisat, T., Xie, Z., Li, N., Liu, Z., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00983-w · Cited by 56 · see citing works

Non-invasive imaging of neuropathology in a rat model of α-synuclein overexpression

Lauwers, E., Beque, D., Laere, K. V., Nuyts, J. L., Bormans, G. M., Mortelmans, L. A., Casteels, C., Vercammen, L., Bockstael, O., Nuttin, B., et al. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.12.005 · Cited by 52 · see citing works

Ser129D mutant alpha-synuclein induces earlier motor dysfunction while S129A results in distinctive pathology in a rat model of Parkinson's disease

Febbraro, F., Şahin, G., Farran, A., Soares, S., Jensen, P. H., Kirik, D., & Romero‐Ramos, M. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.03.014 · Cited by 52 · see citing works

The Mitochondrial Ca2+ Uniporter: Structure, Function, and Pharmacology

Mishra, J., Jhun, B. S., Hurst, S., O‐Uchi, J., Csordás, G., & Sheu, S. (2017) · Handbook of experimental pharmacology · doi:10.1007/164_2017_1 · Cited by 51 · see citing works

Relationship Between Mitochondria and α-Synuclein

Reeve, A. K. (2012) · Archives of Neurology · doi:10.1001/archneurol.2011.2675 · Cited by 49 · see citing works

Alpha-synuclein-based models of Parkinson's disease

Dehay, B., & Fernagut, P. (2016) · Revue Neurologique · doi:10.1016/j.neurol.2016.04.003 · Cited by 49 · see citing works

Structural and Functional Brain Patterns of Non-Motor Syndromes in Parkinson’s Disease

Prell, T. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00138 · Cited by 48 · see citing works

Targeted Overexpression of α-Synuclein by rAAV2/1 Vectors Induces Progressive Nigrostriatal Degeneration and Increases Vulnerability to MPTP in Mouse

Song, L.-K., Ma, K., Yuan, Y., Mu, Z., Song, X., Niu, F., Han, N., & Chen, N. (2015) · PLoS ONE · doi:10.1371/journal.pone.0131281 · Cited by 45 · see citing works

α‑synuclein induces apoptosis of astrocytes by causing dysfunction of the endoplasmic reticulum‑Golgi compartment

Liu, M., Qin, L., Wang, L., Tan, J., Zhang, H., Tang, J., Shen, X., Tan, L., & Wang, C. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.9002 · Cited by 45 · see citing works

Viral vectors for in vivo gene transfer in Parkinson's disease: Properties and clinical grade production

Mandel, R. J., Bürger, C., & Snyder, R. O. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.08.008 · Cited by 44 · see citing works

Decreased α-synuclein expression in the aging mouse substantia nigra

Mak, S. K., McCormack, A. L., Langston, J. W., Kordower, J. H., & Monte, D. A. D. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.09.021 · Cited by 44 · see citing works

Vibrational Circular Dichroism Reveals Supramolecular Chirality Inversion of α-Synuclein Peptide Assemblies upon Interactions with Anionic Membranes

Martial, B., Lefèvre, T., Buffeteau, T., & Auger, M. (2019) · ACS Nano · doi:10.1021/acsnano.8b08932 · Cited by 44 · see citing works

Novel Immunotherapeutic Approaches to Target Alpha-Synuclein and Related Neuroinflammation in Parkinson’s Disease

Zella, M. A. S., Metzdorf, J., Ostendorf, F., Maass, F., Muhlack, S., Gold, R., Haghikia, A., & Tönges, L. (2019) · Cells · doi:10.3390/cells8020105 · Cited by 43 · see citing works

Transduction efficiency of neurons and glial cells by AAV-1, -5, -9, -rh10 and -hu11 serotypes in rat spinal cord following contusion injury

Petrosyan, H. A., Alessi, V., Singh, V., Hunanyan, A. S., Levine, J. M., & Arvanian, V. L. (2014) · Gene Therapy · doi:10.1038/gt.2014.74 · Cited by 42 · see citing works

α-Synuclein-induced dopaminergic neurodegeneration in a rat model of Parkinson's disease occurs independent of ATP13A2 (PARK9)

Daniel, G., Musso, A., Tsika, E., Fiser, A., Glauser, L., Pletniková, O., Schneider, B. L., & Moore, D. J. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.10.007 · Cited by 39 · see citing works

Heme and hemoglobin suppress amyloid β–mediated inflammatory activation of mouse astrocytes

Sankar, S. B., Donegan, R. K., Shah, K. J., Reddi, A. R., & Wood, L. B. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001050 · Cited by 38 · see citing works

Visualization of Altered Hippocampal Connectivity in an Animal Model of Alzheimer’s Disease

Jeon, S. G., Kim, Y. J., Kim, K. A., Mook‐Jung, I., & Moon, M. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0918-y · Cited by 34 · see citing works

Modeling Parkinson’s Disease Neuropathology and Symptoms by Intranigral Inoculation of Preformed Human α-Synuclein Oligomers

Boi, L., Pisanu, A., Palmas, M. F., Fusco, G., Carboni, E., Casu, M. A., Satta, V., Scherma, M., Janda, E., Mocci, I., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228535 · Cited by 33 · see citing works

Seeding of protein aggregation causes cognitive impairment in rat model of cortical synucleinopathy

Espa, E., Clemensson, E. K. H., Luk, K. C., Heuer, A., Björklund, T., & Cenci, M. A. (2019) · Movement Disorders · doi:10.1002/mds.27810 · Cited by 32 · see citing works

Astrocytic mitochondria in adult mouse brain slices show spontaneous calcium influx events with unique properties

Huntington, T. E., & Srinivasan, R. (2021) · Cell Calcium · doi:10.1016/j.ceca.2021.102383 · Cited by 31 · see citing works

Fasudil Promotes α-Synuclein Clearance in an AAV-Mediated α-Synuclein Rat Model of Parkinson’s Disease by Autophagy Activation

Yang, Y., Bu, L.-L., Shen, C., Ge, J., He, S.-J., Yu, H., Tang, Y., Zhao, J., Sun, Y., Yu, W., et al. (2020) · Journal of Parkinson s Disease · doi:10.3233/jpd-191909 · Cited by 30 · see citing works

Neonatal AAV delivery of alpha-synuclein induces pathology in the adult mouse brain

Delenclos, M., Faroqi, A. H., Yue, M., Kurti, A., Castanedes‐Casey, M., Rousseau, L., Phillips, V. R., Dickson, D. W., Fryer, J. D., & McLean, P. J. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0455-3 · Cited by 29 · see citing works

Developmental Changes in Dendritic Spine Morphology in the Striatum and Their Alteration in an A53T α-Synuclein Transgenic Mouse Model of Parkinson’s Disease

Parajuli, L. K., Wako, K., Maruo, S., Kakuta, S., Taguchi, T., Ikuno, M., Yamakado, H., Takahashi, R., & Koike, M. (2020) · eNeuro · doi:10.1523/eneuro.0072-20.2020 · Cited by 29 · see citing works

Genetic targeting of astrocytes to combat neurodegenerative disease

Kirschen, G., Kéry, R., & Chen, A. F. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.265541 · Cited by 28 · see citing works

Advances in modelling alpha-synuclein-induced Parkinson’s diseases in rodents: Virus-based models versus inoculation of exogenous preformed toxic species

Carta, A. R., Boi, L., Pisanu, A., Palmas, M. F., Carboni, E., & Simone, A. D. (2020) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2020.108685 · Cited by 25 · see citing works

Viral Vector-Based Modeling of Neurodegenerative Disorders: Parkinson’s Disease

Fischer, D. L., Gombash, S. E., Kemp, C. J., Manfredsson, F. P., Polinski, N. K., Duffy, M. F., & Sortwell, C. E. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-3271-9_26 · Cited by 24 · see citing works

Recombinant Adeno-Associated Virus Serotype 6 (rAAV6) Potently and Preferentially Transduces Rat Astrocytes In vitro and In vivo

Schober, A. L., Gagarkin, D. A., Chen, Y., Gao, G., Jacobson, L., & Mongin, A. A. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00262 · Cited by 19 · see citing works

A New Synuclein-Transgenic Mouse Model for Early Parkinson’s Reveals Molecular Features of Preclinical Disease

Hendrickx, D. M., Garcia, P., Ashrafi, A., Sciortino, A., Schmit, K. J., Kollmus, H., Nicot, N., Kaoma, T., Vallar, L., Buttini, M., et al. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02085-z · Cited by 10 · see citing works

The development of flexible lentiviral vectors for gene transfer in the CNS

Manfredsson, F. P., & Mandel, R. J. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.03.013 · Cited by 9 · see citing works

Long-Term Exposure to PFE-360 in the AAV-α-Synuclein Rat Model: Findings and Implications

Andersen, M. A., Sotty, F., Jensen, P. H., Badolo, L., Jeggo, R., Smith, G. P., & Christensen, K. V. (2019) · eNeuro · doi:10.1523/eneuro.0453-18.2019 · Cited by 8 · see citing works

Alpha-Synuclein and Mitochondrial Dysfunction in Parkinson’s Disease

Долгачева, Л. П., Fedotova, E. I., Abramov, A. Y., & Berezhnov, A. V. (2018) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s1990747818010038 · Cited by 7 · see citing works

Long-term exposure to PFE-360 in the AAV-α-synuclein rat model: findings and implicationsPreprint

Andersen, M. A., Sotty, F., Jensen, P. H., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/465567 · Cited by 3 · see citing works

Animal models of Parkinson’s disease: bridging the gap between disease hallmarks and research questions

Dovonou, A., Bolduc, C., Linan, V. S., Gora, C., Peralta, M. R., & Lévesque, M. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00368-8 · Cited by 202 · see citing works

The role of tyrosine hydroxylase–dopamine pathway in Parkinson’s disease pathogenesis

Zhou, Z., Saw, W. T., Ho, P., Zhang, Z. W., Zeng, L., Chang, Y. Y., Sun, A. X., Ma, D. R., Wang, H. Y., Zhou, L., et al. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04574-x · Cited by 60 · see citing works

Advances in AAV technology for delivering genetically encoded cargo to the nonhuman primate nervous system

Campos, L., Arokiaraj, C. M., Chuapoco, M. R., Chen, X., Goeden, N., Gradinaru, V., & Fox, A. S. (2023) · Current Research in Neurobiology · doi:10.1016/j.crneur.2023.100086 · Cited by 41 · see citing works

Impact of aging on animal models of Parkinson's disease

Klæstrup, I. H., Just, M. K., Holm, K. L., Alstrup, A. K. O., Romero‐Ramos, M., Borghammer, P., & Berge, N. V. D. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.909273 · Cited by 42 · see citing works

The AAV-α-Synuclein Model of Parkinson’s Disease: An Update

Björklund, A., & Mattsson, B. (2024) · Journal of Parkinson s Disease · doi:10.3233/jpd-240207 · Cited by 27 · see citing works

Neurological and Neurodegenerative Disorders: Novel Concepts and Treatment

Kirmani, B. F., Shapiro, L. A., & Shetty, A. K. (2021) · Aging and Disease · doi:10.14336/ad.2021.0530 · Cited by 26 · see citing works

A Focus on Astrocyte Contribution to Parkinson’s Disease Etiology

Prunell, G., & Olivera‐Bravo, S. (2022) · Biomolecules · doi:10.3390/biom12121745 · Cited by 26 · see citing works

Intercellular transmission of alpha-synuclein

Wu, S., & Schekman, R. W. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1470171 · Cited by 24 · see citing works

Revolution of AAV in Drug Discovery: From Delivery System to Clinical Application

Yin, L., He, H., Zhang, H., Shang, Y., Fu, C., Wu, S., & Jin, T. (2025) · Journal of Medical Virology · doi:10.1002/jmv.70447 · Cited by 22 · see citing works

QEEG Signatures are Associated with Nonmotor Dysfunctions in Parkinson's Disease and Atypical Parkinsonism: An Integrative Analysis

Liu, H., Huang, Z., Deng, B., Chang, Z., Yang, X., Guo, X., Yuan, F., Yang, Q., Wang, L., Zou, H., et al. (2023) · Aging and disease · doi:10.14336/ad.2022.0514 · Cited by 20 · see citing works

Efficacy and mechanism study of Baichanting compound, a combination of Acanthopanax senticosus (Rupr. and Maxim.) Harms, Paeonia lactiflora Pall and Uncaria rhynchophylla (Miq.) Miq. ex Havil, on Parkinson's disease based on metagenomics and metabolomics

Lu, Y., Gao, X., Mohammed, S. A. D., Wang, T., Fu, J., Yang, N., Yang, N., Liu, S., & Liu, S. (2023) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.117182 · Cited by 19 · see citing works

Fucoidan ameliorates rotenone-induced Parkinsonism in mice by regulating the microbiota-gut-brain axis

Yang, X., Zhang, X., Ma, Y., Li, S., Wang, Q., Hong, J., Yu, G., Qi, B., Wang, J., Liu, C., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.137373 · Cited by 18 · see citing works

Adeno-Associated Viruses for Modeling Neurological Diseases in Animals: Achievements and Prospects

Lunev, E. A., Karan, A. A., Egorova, T. V., & Bardina, M. V. (2022) · Biomedicines · doi:10.3390/biomedicines10051140 · Cited by 16 · see citing works

Chronic stress induces depression-like behaviors and Parkinsonism via upregulating α-synuclein

Xia, D., Xiong, M., Yang, Y., Wang, X., Chen, Q., Li, S., Meng, L., & Zhang, Z. (2025) · npj Parkinson's Disease · doi:10.1038/s41531-025-00998-x · Cited by 15 · see citing works

Clearance Pathways for α‐Synuclein in Parkinson's Disease

Ho, M. S.-C. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70124 · Cited by 13 · see citing works

Neuroinflammation, immune response and α-synuclein pathology: how animal models are helping us to connect dots

Balzano, T., Esteban-García, N., & Blesa, J. (2022) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2023.2160440 · Cited by 10 · see citing works

Gastrointestinal dysmotility in rodent models of Parkinson’s disease

Pellegrini, C., & Travagli, R. A. (2024) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00225.2023 · Cited by 8 · see citing works

Cognitive dysfunction in animal models of human lewy-body dementia

Haikal, C., Winston, G. M., & Kaplitt, M. G. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1369733 · Cited by 7 · see citing works

TFE3-mediated neuroprotection: Clearance of aggregated α-synuclein and accumulated mitochondria in the AAV-α-synuclein model of Parkinson's disease

He, X., Chen, M., Fan, Y., Wu, B., & Dong, Z. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2024.101429 · Cited by 4 · see citing works

Evaluating alpha-synuclein proteinopathy and consequences for birdsong in zebra finch basal ganglia area X

Bjork, R. T., Patel, F., Daly, M. S., & Miller, J. E. (2025) · Behavioural Brain Research · doi:10.1016/j.bbr.2025.115698 · Cited by 2 · see citing works

Mechanisms mediating dynamic changes in neural responses during deep brain stimulation

Dale, J., Schmidt, S. L., Mitchell, K. T., Peters, J. J., Turner, D. A., & Grill, W. M. (2025) · Brain stimulation · doi:10.1016/j.brs.2025.103002 · Cited by 1 · see citing works

Advancing personalized medicine for Parkinson’s disease: transforming treatment and therapeutic outcomes

Swathi, M., Bedadakota, S. S., Animish, A., Suthindhiran, K., & Jayasri, M. A. (2026) · 3 Biotech · doi:10.1007/s13205-025-04674-y · Cited by 1 · see citing works

Potential Therapeutic Approach using Aromatic l-amino Acid Decarboxylase and Glial-derived Neurotrophic Factor Therapy Targeting Putamen in Parkinson's Disease

Tripathi, R. K., Goyal, L., & Singh, S. (2024) · Current Gene Therapy · doi:10.2174/0115665232283842240102073002 · Cited by 1 · see citing works

Evaluating Alpha-Synuclein Neuropathy and Consequences for Birdsong in Zebra Finch Basal Ganglia Area XPreprint

Bjork, R. T., Patel, F., Daly, M. S., & Miller, J. E. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5136982

A holistic rat model to investigate therapeutic interventions in Parkinson’s disease: viral induction of a slow-progressing motor phenotype, dopaminergic degeneration and early microglia neuroinflammation

Kefalakes, E., Mewes, F., Peristich, D., Plötner, C., Shcherbatyy, V., Schipke, J., Schneider, F., Käufer, C., & Rumpel, R. (2025) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2025.111464 · Cited by 1 · see citing works

Expression of human A53T alpha-synuclein without endogenous rat alpha-synuclein fails to elicit Parkinson’s disease-related phenotypes in a novel humanized rat model

Polinski, N. K., Puoliväli, J. T., Rauhala, L., Stenius, T.-K., Bragge, T., Parkkari, T., Penttinen, A., Chen, Y., Mabrouk, O. S., Glajch, K. E., et al. (2025) · PLoS ONE · doi:10.1371/journal.pone.0329823

A One-Step Mouse Model of Parkinson’s Disease Combining rAAV-α-Synuclein and Preformed Fibrils of α-Synuclein

Subramanya, S., Singh, D. N., & Thakur, P. S. (2025) · BIO-PROTOCOL · doi:10.21769/bioprotoc.5525

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Bhamare, U. U., Talpade, A., Pingili, R. B., & Palkar, M. B. (2025) · European Journal of Neuroscience · doi:10.1111/ejn.70343

Selective vulnerability of monoaminergic neurons and network spread of alpha-synuclein jointly explain pathology progression in Parkinson’s disease models

Teshome, S., Torok, J., Mezias, C., Gupta, A., & Raj, A. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107403

Construct optimization for AAV-mediated human α-syn overexpression, and validation across research settings: Development of a shared tool for the research community

Pardo, J., Mudannayake, J. M., Bernal-Conde, L. D., Sandoval, I. M., Dong, R. B., Avallone, M., Marmion, D. J., Gralen, A. R., Waite, L., Heuer, A., et al. (2026) · Journal of Parkinson s Disease · doi:10.1177/1877718x261447105

Adeno-Associated Virus as a Frontier Vector for Gene Therapy: From Basic Research to Clinical Translation

Yin, L. (2026) · IntechOpen eBooks · doi:10.5772/intechopen.1016169

Rodent models and accompanying in vitro strategies for studying the etiology and therapy of Parkinson's disease

Lau, K., Outeiro, T. F., & Richter, F. (2026) · Journal of Parkinson s Disease · doi:10.1177/1877718x261463389

Enavogliflozin alleviates motor deficits in rotenone-induced Parkinson's disease mice via attenuation of oxidative stress and neuroinflammation as well as activation of the SIRT1/PINK1/Parkin pathway

Liang, T., Pang, X., Liu, Q., Sun, S., Wang, L., & Yan, H. (2026) · Neuropharmacology · doi:10.1016/j.neuropharm.2026.111111

From dosage alteration to amplification strategies: mechanistically defined alpha-synuclein mouse models for Parkinson’s disease therapy development

Nuber, S., Fanning, S., & Dettmer, U. (2026) · Acta Neuropathologica · doi:10.1007/s00401-026-03112-4

Viral vector-mediated overexpression of α-synuclein as a progressive model of Parkinson’s disease

Ulusoy, A., Decressac, M., Kirik, D., & Björklund, A. (2010) · Progress in brain research · doi:10.1016/s0079-6123(10)84005-1 · Cited by 130 · see citing works

Progressive neurodegenerative and behavioural changes induced by AAV-mediated overexpression of α-synuclein in midbrain dopamine neurons

Decressac, M., Mattsson, B., Lundblad, M., Weikop, P., & Björklund, A. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.013 · Cited by 286 · see citing works

Parkinson pathology propagation and long-distance transport in neurons

Domingues, J. M. P. (2014) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)

The AAV-α-Synuclein Model of Parkinson’s Disease: An Update

Björklund, A., & Mattsson, B. (2024) · Journal of Parkinson s Disease · doi:10.3233/jpd-240207 · Cited by 27 · see citing works

Synaptic loss predominates neuronal loss in a PD model of AAV-mediated alpha-synuclein overexpression in hippocampus and striatum

Çınar, E., Çakmaklı, G. Y., Ulusoy, A., Saka, E., Elibol, B., & Tel, B. C. (2018) · Proceedings for Annual Meeting of The Japanese Pharmacological Society · doi:10.1254/jpssuppl.wcp2018.0_po2-1-42