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Mice Lacking α-Synuclein Display Functional Deficits in the Nigrostriatal Dopamine System
Open accessAbstract
alpha-Synuclein (alpha-Syn) is a 14 kDa protein of unknown function that has been implicated in the pathophysiology of Parkinson's disease (PD). Here, we show that alpha-Syn-/- mice are viable and fertile, exhibit intact brain architecture, and possess a normal complement of dopaminergic cell bodies, fibers, and synapses. Nigrostriatal terminals of alpha-Syn-/- mice display a standard pattern of dopamine (DA) discharge and reuptake in response to simple electrical stimulation. However, they exhibit an increased release with paired stimuli that can be mimicked by elevated Ca2+. Concurrent with the altered DA release, alpha-Syn-/- mice display a reduction in striatal DA and an attenuation of DA-dependent locomotor response to amphetamine. These findings support the hypothesis that alpha-Syn is an essential presynaptic, activity-dependent negative regulator of DA neurotransmission.
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“However, αSyn-KO, and α/β-Syn double-KO mice exhibited reduced brain dopamine levels compared to wild-type (wt) animals”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [155]
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Cites
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
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
Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., & Goedert, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6469 · Cited by 2,868
Aggregation of Huntingtin in Neuronal Intranuclear Inclusions and Dystrophic Neurites in Brain
DiFiglia, M., Sapp, E., Chase, K. O., Davies, S. W., Bates, G. P., Vonsattel, J. P., & Aronin, N. (1997) · Science · doi:10.1126/science.277.5334.1990 · Cited by 2,439
The synaptic vesicle cycle: a cascade of protein–protein interactions
Südhof, T. C. (1995) · Nature · doi:10.1038/375645a0 · Cited by 1,991
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
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
Modulation of memory fields by dopamine Dl receptors in prefrontal cortex
Williams, G. V., & Goldman-Rakic, P. S. (1995) · Nature · doi:10.1038/376572a0 · Cited by 1,593
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
Conway, K. A., Harper, J. D., & Lansbury, P. T. (1998) · Nature Medicine · doi:10.1038/3311 · Cited by 1,520
Research works printed but not linked: 1
- Starke, 1989, Modulation of presynaptic release by presynaptic autoreceptors, J. Neurochem., 2, 449
Cited by
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Items 501–600 of 1,003
Rappley, I., Myers, D. S., Milne, S. B., Ivanova, P. T., LaVoie, M. J., Brown, H. A., & Selkoe, D. J. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06290.x · Cited by 87
Kholodilov, N. G., Yarygina, O., Oo, T. F., Zhang, H., Sulzer, D. L., Dauer, W. T., & Burke, R. E. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.4506-03.2004 · Cited by 86
Self-citationOikawa, T., Nonaka, T., Terada, M., Tamaoka, A., Hisanaga, S., & Hasegawa, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.736355 · Cited by 87
Kahle, P. J., Haass, C., Kretzschmar, H. A., & Neumann, M. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01020.x · Cited by 86
Orth, M., & Tabrizi, S. J. (2003) · Movement Disorders · doi:10.1002/mds.10447 · Cited by 87
Transcriptomic signatures of brain regional vulnerability to Parkinson’s disease
Keo, A., Mahfouz, A. E., Ingrassia, A. M. T., Meneboo, J., Villenet, C., Mutez, E., Comptdaer, T., Lelieveldt, B. P. F., Figeac, M., Chartier‐Harlin, M., et al. (2020) · Communications Biology · doi:10.1038/s42003-020-0804-9 · Cited by 84
Limelight on Alpha-Synuclein: Pathological and Mechanistic Implications in Neurodegeneration
Wales, P., Pinho, R., Lázaro, D. F., & Outeiro, T. F. (2013) · Journal of Parkinson s Disease · doi:10.3233/jpd-130216 · Cited by 89
The significance of tau and α-synuclein inclusions in neurodegenerative diseases
Goedert, M. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00200-8 · Cited by 86
Alpha-synuclein dysfunction in Lewy body diseases
Tofaris, G. K., & Spillantini, M. G. (2005) · Movement Disorders · doi:10.1002/mds.20538 · Cited by 87
Neuroprotection and dopamine agonists
Schapira, A. H. V. (2002) · Neurology · doi:10.1212/wnl.58.suppl_1.s9 · Cited by 86
A critical role for alpha-synuclein in development and function of T lymphocytes
Shameli, A., Xiao, W., Zheng, Y., Shyu, S., Sumodi, J., Meyerson, H. J., Harding, C. V., & Maitta, R. W. (2015) · Immunobiology · doi:10.1016/j.imbio.2015.10.002 · Cited by 86
Myopathy causing camptocormia in idiopathic Parkinson's disease: A multidisciplinary approach
Spuler, S., Krug, H., Klein, C., Medialdea, I. C., Jakob, W., Ebersbach, G., Gruber, D., Hoffmann, K., Trottenberg, T., & Kupsch, A. R. (2009) · Movement Disorders · doi:10.1002/mds.22913 · Cited by 85
Adult Hippocampal Neurogenesis in Parkinson’s Disease: Impact on Neuronal Survival and Plasticity
Regensburger, M., Prots, I., & Winner, B. (2014) · Neural Plasticity · doi:10.1155/2014/454696 · Cited by 90
Bogaerts, V., Theuns, J., & Broeckhoven, C. V. (2007) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2007.00342.x · Cited by 91
Dynamic structural flexibility of α-synuclein
Mor, D. E., Ugras, S. E., Daniels, M. J., & Ischiropoulos, H. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.12.018 · Cited by 85
Singh, B., Covelo, A., Martell-Martinez, H. A., Nanclares, C., Sherman, M. A., Okematti, E., Meints, J. P., Teravskis, P. J., Gallardo, C., Savonenko, A. V., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02032-w · Cited by 85
α-Synuclein interacts with the switch region of Rab8a in a Ser129 phosphorylation-dependent manner
Yin, G., da Fonseca, T. L., Eisbach, S. E., Anduaga, A. M., Breda, C., Orcellet, M. L., Szegő, É. M., Guerreiro, P. S., Lázaro, D. F., Braus, G. H., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.06.018 · Cited by 85
Immunohistochemical comparison of α- and β-synuclein in adult rat central nervous system
Mori, F., Tanji, K., Yoshimoto, M., Takahashi, H., & Wakabayashi, K. (2002) · Brain Research · doi:10.1016/s0006-8993(02)02643-4 · Cited by 84
α-Synuclein transgenic mice exhibit reduced anxiety-like behaviour
George, S., van den Buuse, M., Mok, S. S., Masters, C. L., Li, Q., & Culvenor, J. G. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2007.12.017 · Cited by 84
Alpha-synuclein modulates dopamine neurotransmission
Butler, B., Sambo, D. O., & Khoshbouei, H. (2016) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2016.06.001 · Cited by 90
Molecular Insights into Parkinson's Disease
Rochet, J., Hay, B. A., & Guo, M. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00011-4 · Cited by 87
Minakaki, G., Krainc, D., & Burbulla, L. F. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.580634 · Cited by 87
Subcellular localisation of recombinant α- and γ-synuclein
Specht, C. G., Tigaret, C. M., Rast, G. F., Thalhammer, A., Rudhard, Y., & Schoepfer, R. (2004) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2004.09.017 · Cited by 83
Woods, W. S., Boettcher, J. M., Zhou, D. H., Kloepper, K. D., Hartman, K. L., Ladror, D. T., Qi, Z., Rienstra, C. M., & George, J. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705283200 · Cited by 83
Pathogenic effects of α-synuclein aggregation
Lundvig, D. M. S., Lindersson, E., & Jensen, P. H. (2004) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.09.001 · Cited by 83
Hashimoto, M., Takenouchi, T., Rockenstein, E. M., & Masliah, E. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01791.x · Cited by 83
α-Synuclein and Parkinsonism: Updates and Future Perspectives
Rosborough, K., Patel, N., & Kalia, L. V. (2017) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-017-0737-y · Cited by 83
Marwarha, G., Rhen, T., Schommer, T., & Ghribi, O. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07497.x · Cited by 85
RetractedLysosomes and α-synuclein form a dangerous duet leading to neuronal cell death
Bourdenx, M., Bézard, E., & Dehay, B. (2014) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2014.00083 · Cited by 88
Vernier, P., Moret, F., Callier, S., Snapyan, M., Wersinger, C., & Sidhu, A. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1332.015 · Cited by 82
Doxycycline Inhibits α-Synuclein-Associated Pathologies in Vitro and in Vivo
Dominguez-Meijide, A., Parrales, V., Vasili, E., González-Lizárraga, F., König, A., Lázaro, D. F., Lannuzel, A., Haik, S., Del Bel, E., Chehín, R., et al. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105256 · Cited by 81
Mitochondrial Dysfunction in Parkinson's Disease: Pathogenesis and Neuroprotection
Mounsey, R. B., & Teismann, P. (2010) · Parkinson s Disease · doi:10.4061/2011/617472 · Cited by 86
Xu, Y., Deng, Y., & Qing, H. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13234 · Cited by 87
Proteomics in animal models of Alzheimer's and Parkinson's diseases
Robinson, R. A. S., Owen, J. B., & Butterfield, D. A. (2008) · Ageing Research Reviews · doi:10.1016/j.arr.2008.07.003 · Cited by 81
123I-meta-iodobenzylguanidine (MIBG) cardiac scintigraphy in α-synucleinopathies
Orimo, S., Yogo, M., Nakamura, T., Suzuki, M., & Watanabe, H. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.01.001 · Cited by 83
Intrinsically disordered proteins in synaptic vesicle trafficking and release
Snead, D., & Eliezer, D. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.006493 · Cited by 79
α-Synuclein Budding Yeast Model: Toxicity Enhanced by Impaired Proteasome and Oxidative Stress
Sharma, N., Brandis, K. A., Herrera, S., Johnson, B. E., Vaidya, T., Shrestha, R., & DebBurman, S. K. (2006) · Journal of Molecular Neuroscience · doi:10.1385/jmn:28:2:161 · Cited by 78
Galli, S., Lopes, D. M., Ammari, R., Kopra, J. J., Millar, S. E., Gibb, A. J., & Salinas, P. C. (2014) · Nature Communications · doi:10.1038/ncomms5992 · Cited by 79
Synucleins: New Data on Misfolding, Aggregation and Role in Diseases
Surguchov, A. P., & Surguchev, A. A. (2022) · Biomedicines · doi:10.3390/biomedicines10123241 · Cited by 82
A Specific Survival Response in Dopamine Neurons at Most Risk in Parkinson's Disease
Murase, S., & McKay, R. D. G. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2745-06.2006 · Cited by 80
Zhou, W., & Freed, C. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307563200 · Cited by 80
Aggregation and neurotoxicity of recombinant α-synuclein aggregates initiated by dimerization
Roostaee, A., Beaudoin, S., Staskevicius, A., & Roucou, X. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-5 · Cited by 80
The effect of α‐synuclein knockdown on MPP+ toxicity in models of human neurons
Fountaine, T. M., Venda, L. L., Warrick, N., Christian, H., Brundin, P., Channon, K. M., & Wade‐Martins, R. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06527.x · Cited by 78
Hashimoto, M., & Masliah, E. (2003) · Neurochemical Research · doi:10.1023/a:1026073324672 · Cited by 78
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 80
Sekar, S., Ranju, V., Kalaivani, P., Priya, R. J., Sumathy, H., Sunil, A. G., & Chidambaram, S. B. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.05.025 · Cited by 78
Uemura, N., Koike, M., Ansai, S., Kinoshita, M., Ishikawa‐Fujiwara, T., Matsui, H., Naruse, K., Sakamoto, N., Uchiyama, Y., Todo, T., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005065 · Cited by 82
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Butler, Y. R., Liu, Y., Kumbhar, R., Zhao, P., Gadhave, K., Wang, N., Li, Y., Mao, X., & Wang, W. (2022) · Nature Communications · doi:10.1038/s41467-022-31787-2 · Cited by 80
Dopamine agonists and neuroprotection in Parkinson's disease
Schapira, A. H. V. (2002) · European Journal of Neurology · doi:10.1046/j.1468-1331.9.s3.9.x · Cited by 77
Endogenous alpha-synuclein influences the number of dopaminergic neurons in mouse substantia nigra
Garcia-Reitboeck, P., Anichtchik, O. V., Dalley, J. W., Ninkina, N. N., Tofaris, G. K., Buchman, V. L., & Spillantini, M. G. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.07.015 · Cited by 76
α-Synuclein knockout mice have cognitive impairments
Kokhan, V. S., Afanasyeva, M., & Van’kin, G. I. (2012) · Behavioural Brain Research · doi:10.1016/j.bbr.2012.03.026 · Cited by 76
Αlpha-Synuclein as a Mediator in the Interplay between Aging and Parkinson’s Disease
Bobela, W., Aebischer, P., & Schneider, B. L. (2015) · Biomolecules · doi:10.3390/biom5042675 · Cited by 75
Ninkina, N., Papachroni, K., Robertson, D. C., Schmidt, O., Delaney, L., O'Neill, F., Court, F., Rosenthal, A., Fleetwood-Walker, S. M., Davies, A. M., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8233-8245.2003 · Cited by 75
Self-citationMechanisms of alpha-synuclein toxicity: An update and outlook
Brás, I. C., Xylaki, M., & Outeiro, T. F. (2019) · Progress in brain research · doi:10.1016/bs.pbr.2019.10.005 · Cited by 78
Uversky, V. N. (2010) · Chemical Reviews · doi:10.1021/cr100186d · Cited by 75
Roy, B., & Jackson, G. R. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu011 · Cited by 75
GABA transmission via ATP-dependent K + channels regulates α-synuclein secretion in mouse striatum
Emmanouilidou, E., Minakaki, G., Keramioti, M. V., Xylaki, M., Balafas, E., Chrysanthou‐Piterou, M., Kloukina, I., & Vekrellis, K. (2016) · Brain · doi:10.1093/brain/awv403 · Cited by 77
Differential expression of α‐synuclein isoforms in dementia with Lewy bodies
Beyer, K., Lao, J. I., Carrato, C., Mate, J. L., López, D., Ferrer, I., & Ariza, A. (2004) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2004.00572.x · Cited by 75
Alpha‐synuclein and Parkinson's disease: Implications from the screening of more than 1,900 patients
Berg, D., Niwar, M., Maaß, S., Zimprich, A. A., Möller, J. C., Wüllner, U., Schmitz‐Hübsch, T., Klein, C., Tan, E., Schöls, L. J., et al. (2005) · Movement Disorders · doi:10.1002/mds.20504 · Cited by 75
The pathology roadmap in Parkinson disease
Surmeier, D. J., & Sulzer, D. (2013) · Prion · doi:10.4161/pri.23582 · Cited by 74
Self-citationGangliosides, α-Synuclein, and Parkinson's Disease
Ledeen, R. W., & Wu, G. (2018) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.12.009 · Cited by 73
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 78
Wu, Q., Shaikh, M., Meymand, E. S., Zhang, B., Luk, K. C., Trojanowski, J. Q., & Lee, V. M. ‐. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02227-6 · Cited by 71
Hsp70 molecular chaperones and Parkinson's disease
Witt, S. N. (2009) · Biopolymers · doi:10.1002/bip.21302 · Cited by 75
Kuwahara, T., Tonegawa‐Kuji, R., Ito, G., Mitani, S., & Iwatsubo, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.237131 · Cited by 74
Luth, E. S., Bartels, T., Dettmer, U., Kim, N. C., & Selkoe, D. J. (2014) · Biochemistry · doi:10.1021/bi501188a · Cited by 77
Chu, Y., Goldman, J. G., Kelly, L. P., He, Y., Waliczek, T., & Kordower, J. H. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.05.003 · Cited by 71
Bisaglia, M., Tessari, I., Mammi, S., & Bubacco, L. (2009) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8082-1 · Cited by 74
Synaptic Vesicle-Recycling Machinery Components as Potential Therapeutic Targets
Li, Y. C., & Kavalali, E. T. (2017) · Pharmacological Reviews · doi:10.1124/pr.116.013342 · Cited by 74
Parkinson’s disease: a rethink of rodent models
Melrose, H. L., Lincoln, S. J., Tyndall, G. M., & Farrer, M. J. (2006) · Experimental Brain Research · doi:10.1007/s00221-006-0461-3 · Cited by 74
Parkin is linked to the ubiquitin pathway
Tanaka, K., Suzuki, T., Chiba, T., Shimura, H., Hattori, N., & Mizuno, Y. (2001) · Journal of Molecular Medicine · doi:10.1007/s001090100242 · Cited by 74
Su, C., Yang, X., & Lou, J. (2016) · Brain Research · doi:10.1016/j.brainres.2016.05.011 · Cited by 73
Li, W., Hoffman, P. N., Stirling, W. L. H., Price, D. L., & Lee, M. K. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02166.x · Cited by 73
Soper, J. H., Kehm, V. M., Burd, C. G., Bankaitis, V. A., & Lee, V. M. ‐. (2010) · Journal of Molecular Neuroscience · doi:10.1007/s12031-010-9455-5 · Cited by 77
Wang, T., & Hay, J. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00433 · Cited by 74
Zhang, S., Eitan, E., Wu, T.-Y., & Mattson, M. P. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.09.016 · Cited by 76
Zhang, J., Culp, M. L., Craver, J., & Darley-Usmar, V. M. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14308 · Cited by 74
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Machida, Y., Chiba, T., Takayanagi, A., Tanaka, Y., Asanuma, M., Ogawa, N., Koyama, A., Iwatsubo, T., Ito, S., Jansen, P. H., et al. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.04.124 · Cited by 73
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Tarutani, A., Adachi, T., Akatsu, H., Hashizume, Y., Hasegawa, K., Saito, Y., Robinson, A., Mann, D. M. A., Yoshida, M., Murayama, S., et al. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02426-3 · Cited by 74
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Phung, N. V., Rong, F., Xia, W.-Y., Fan, Y., Li, X. Y., Wang, S. A., & Li, F. (2023) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2023.2203753 · Cited by 81
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Saha, S., Ash, P. E. A., Gowda, V., Liu‐Yesucevitz, L., Shirihai, O. S., & Wolozin, B. L. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0022-y · Cited by 72
Alpha‐synuclein overexpression in mice alters synaptic communication in the corticostriatal pathway
Wu, N., Joshi, P. R., Cepeda, C., Masliah, E., & Levine, M. S. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22327 · Cited by 74
Yavich, L., Jäkälä, P., & Tanila, H. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04098.x · Cited by 72
Schneider, B. L., Seehus, C. R., Capowski, E. E., Aebischer, P., Zhang, S., & Svendsen, C. N. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm008 · Cited by 73
Genetically engineered mouse models of Parkinson's disease
Crabtree, D., & Zhang, J. (2011) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2011.07.019 · Cited by 73
α-Synuclein aggregation and neurodegenerative diseases
Ma, Q., Chan, P., Yoshii, M., & Uéda, K. (2003) · Journal of Alzheimer s Disease · doi:10.3233/jad-2003-5208 · Cited by 72
Fecchio, C., Palazzi, L., & de Laureto, P. P. (2018) · Molecules · doi:10.3390/molecules23071531 · Cited by 74
Alpha-Synuclein Contribution to Neuronal and Glial Damage in Parkinson’s Disease
Saramowicz, K., Siwecka, N., Galita, G., Kucharska-Lusina, A., Rozpędek‐Kamińska, W., & Majsterek, I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010360 · Cited by 79
Feng, L., Federoff, H. J., Vicini, S., & Maguire‐Zeiss, K. A. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07266.x · Cited by 72
α-Synuclein, Parkinson's disease, and Alzheimer's disease
Kim, S., Seo, J., & Suh, Y. (2004) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2003.11.005 · Cited by 70
SUN, F., KANTHASAMY, A. G., ANANTHARAM, V., & KANTHASAMY, A. G. (2007) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2007.04.001 · Cited by 69
Kaul, S., Anantharam, V., Kanthasamy, A., & Kanthasamy, A. G. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2005.05.022 · Cited by 70
Mechanisms in dominant parkinsonism: The toxic triangle of LRRK2, α‐synuclein, and tau
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Metadata
- Authors
- Abeliovich, A., Schmitz, Y., Fariñas, I., Choi-Lundberg, D., Ho, W.-H., Castillo, P. E., Shinsky, N., Verdugo, J. M. G., Armanini, M., Ryan, A., Hynes, M., Phillips, H., Sulzer, D., & Rosenthal, A.
- Affiliations
- University of California, San Francisco (US)
- New York State Psychiatric Institute (US)
- Universitat de València (ES)
- Genentech (US)
- Stanford Medicine (US)
- Corresponding author
- Rosenthal, Arnon
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2000-01
- Volume
- 25
- Issue
- 1
- Pages
- 239-252
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2171281715
- Cited by
- 1,722
- References
- 51
- Citations by year
- 2026: 39 · 2025: 41 · 2024: 53 · 2023: 50 · 2022: 67 · 2021: 61 · 2020: 65 · 2019: 68 · 2018: 61 · 2017: 70 · 2016: 61 · 2015: 75 · 2014: 82 · 2013: 71 · 2012: 77
- FWCI
- 39.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- eCite Digital Repository (University of Tasmania) (submittedVersion)
- Figshare (submittedVersion)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neurotransmitter Receptor Influence on Behavior
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- alpha-synuclein, Parkinson's disease, nigrostriatal dopamine system, dopamine release, presynaptic modulation, paired-pulse facilitation, calcium-dependent release, striatal dopamine, dopamine reuptake, dopamine signaling
- MeSH terms
- Amphetamine, Animals, Calcium, Corpus Striatum, Dopamine, Female, Hippocampus, Locomotion, Male, Mice, Inbred C57BL, Motor Activity, Nerve Tissue Proteins, Synaptic Transmission, Neurons, Substantia Nigra, Dopamine Agents, Gene Expression, Autoreceptors, Presynaptic Terminals, Long-Term Potentiation, Mice, Knockout, Glutamic Acid, rab3A GTP-Binding Protein, Mice, Synucleins, alpha-Synuclein, Calbindins, S100 Calcium Binding Protein G
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