The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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]
Citations
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
Sorted by citations
Dauer, W., & Przedborski, S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00568-3 · Cited by 5,469
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
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563
Pathological roles of MAPK signaling pathways in human diseases
Kim, E. K., & Choi, E.-J. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.12.009 · Cited by 2,472
Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024
Self-citationOxidative stress in neurodegeneration: Cause or consequence?
Andersen, J. K. (2004) · Nature Medicine · doi:10.1038/nrn1434 · Cited by 1,869
The Role of Oxidative Stress in Parkinson's Disease
Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845
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
The many faces of α-synuclein: from structure and toxicity to therapeutic target
Lashuel, H. A., Overk, C., Oueslati, A., & Masliah, E. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3406 · Cited by 1,684
Volpicelli-Daley, L. A., Luk, K. C., Patel, T. P., Tanik, S. A., Riddle, D. M., Stieber, A., Meaney, D. F., Trojanowski, J. Q., & Lee, V. M.-Y. (2011) · Neuron · doi:10.1016/j.neuron.2011.08.033 · Cited by 1,569
Unfolding the role of protein misfolding in neurodegenerative diseases
Soto, C. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1007 · Cited by 1,506
-Synuclein in Parkinson's Disease
Stefanis, L. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009399 · Cited by 1,446
α-Synuclein Is Degraded by Both Autophagy and the Proteasome
Webb, J. L., Ravikumar, B., Atkins, J., Skepper, J. N., & Rubinsztein, D. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300227200 · Cited by 1,429
Alpha-synuclein and neurodegenerative diseases
Goedert, M. (2001) · Nature reviews. Neuroscience · doi:10.1038/35081564 · Cited by 1,428
Genetics of Parkinson's DiseasePreprint
Klein, C., & Westenberger, A. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a008888 · Cited by 1,446
Neuronal α-Synucleinopathy with Severe Movement Disorder in Mice Expressing A53T Human α-Synuclein
Giasson, B. I., Duda, J. E., Quinn, S. M., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2002) · Neuron · doi:10.1016/s0896-6273(02)00682-7 · Cited by 1,266
Pathogenesis of parkinson's disease: dopamine, vesicles and α-synuclein
Lotharius, J., & Brundin, P. (2002) · Nature reviews. Neuroscience · doi:10.1038/nrn983 · Cited by 1,319
MOLECULAR PATHOPHYSIOLOGY OF PARKINSON'S DISEASE
Moore, D. J., West, A. B., Dawson, V. L., & Dawson, T. M. (2005) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.28.061604.135718 · Cited by 1,304
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
Blum, D. L., Torch, S., Lambeng, N., Nissou, M.-F., Benabid, A., Sadoul, R., & Verna, J. (2001) · Progress in Neurobiology · doi:10.1016/s0301-0082(01)00003-x · Cited by 1,269
Goedert, M., Spillantini, M. G., Del Tredici, K., & Braak, H. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.242 · Cited by 1,190
Luk, K. C., Kehm, V. M., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M. ‐. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20112457 · Cited by 1,136
Mitochondria in neuroplasticity and neurological disorders
Mattson, M. P., Gleichmann, M., & Cheng, A. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.010 · Cited by 1,081
Eliezer, D., Kutluay, E., Bussell, R., & Browne, G. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4538 · Cited by 1,110
Nemani, V. M., Lü, W., Berge‐Seidl, V., Nakamura, K., Onoa, B., Lee, M. K., Chaudhry, F. A., Nicoll, R. A., & Edwards, R. H. (2010) · Neuron · doi:10.1016/j.neuron.2009.12.023 · Cited by 1,094
Luk, K. C., Song, C., O'Brien, P., Stieber, A., Branch, J. R., Brunden, K. R., Trojanowski, J. Q., & Lee, V. M.-Y. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908005106 · Cited by 938
α-Synuclein Cooperates with CSPα in Preventing Neurodegeneration
Chandra, S. S., Gallardo, G., Fernández‐Chacón, R., Schlüter, O. M., & Südhof, T. C. (2005) · Cell · doi:10.1016/j.cell.2005.09.028 · Cited by 990
α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies
Wong, Y. C., & Krainc, D. (2017) · Nature Medicine · doi:10.1038/nm.4269 · Cited by 897
Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein
Cremades, N., Cohen, S. I. A., Deas, E., Abramov, A. Y., Chen, A. Y., Orte, A., Sandal, M., Clarke, R. W., Dunne, P., Aprile, F. A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.037 · Cited by 911
Bendor, J. T., Logan, T. P., & Edwards, R. H. (2013) · Neuron · doi:10.1016/j.neuron.2013.09.004 · Cited by 825
Mitochondria in the aetiology and pathogenesis of Parkinson's disease
Schapira, A. H. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(07)70327-7 · Cited by 883
Cabin, D. E., Shimazu, K., Murphy, D., Cole, N. B., Gottschalk, W., McIlwain, K. L., Orrison, B., Chen, A., Ellis, C. E., Paylor, R., et al. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-20-08797.2002 · Cited by 865
Calabresi, P., Mechelli, A., Natale, G., Volpicelli‐Daley, L. A., Lazzaro, G. D., & Ghiglieri, V. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05672-9 · Cited by 930
Genetic Animal Models of Parkinson's Disease
Dawson, T. M., Ko, H. S., & Dawson, V. L. (2010) · Neuron · doi:10.1016/j.neuron.2010.04.034 · Cited by 866
Parkinson’s disease: genetics and pathogenesis
Shulman, J. M., De Jager, P. L., & Feany, M. B. (2011) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-011110-130242 · Cited by 801
Intravesicular Localization and Exocytosis of α-Synuclein and its Aggregates
Lee, H.-J., Patel, S. S., & Lee, S. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0692-05.2005 · Cited by 824
Murphy, D. D., Rueter, S. M., Trojanowski, J. Q., & Lee, V. M. ‐. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-09-03214.2000 · Cited by 927
Chung, K. K. K., Zhang, Y., Lim, K. L., Tanaka, Y., Huang, H., Gao, J., Ross, C. A., Dawson, V. L., & Dawson, T. M. (2001) · Nature Medicine · doi:10.1038/nm1001-1144 · Cited by 750
Oxidative stress and nitration in neurodegeneration: Cause, effect, or association?
Ischiropoulos, H., & Beckman, J. S. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200317638 · Cited by 759
Lee, M. K., Stirling, W., Xu, Y., Xu, X., Qui, D., Mandir, A. S., Dawson, T. M., Copeland, N. G., Jenkins, N. A., & Price, D. L. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.132197599 · Cited by 824
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
THE BIOCHEMISTRY OF PARKINSON'S DISEASE
Cookson, M. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133400 · Cited by 666
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
Galvagnion, C., Buell, A. K., Meisl, G., Michaels, T. C. T., Vendruscolo, M., Knowles, T. P. J., & Dobson, C. M. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1750 · Cited by 661
Diagnosis and treatment of Parkinson disease: molecules to medicine
Savitt, J. M. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29178 · Cited by 660
Exner, N., Lutz, A. K., Haass, C., & Winklhofer, K. F. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.170 · Cited by 677
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 642
Experimental models of Parkinson's disease
Beal, M. F. (2001) · Nature reviews. Neuroscience · doi:10.1038/35072550 · Cited by 645
Dopamine-modified α-synuclein blocks chaperone-mediated autophagy
Martínez‐Vicente, M., Tallóczy, Z., Kaushik, S., Massey, A. C., Mazzulli, J. R., Mosharov, E. V., Hodara, R., Fredenburg, R. A., Wu, D.-C., Follenzi, A., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32806 · Cited by 660
Self-citationRecasens, A., Dehay, B., Bové, J., Carballo‐Carbajal, I., Doveró, S., Pérez‐Villalba, A., Fernagut, P., Blesa, J., Parent, A., Perier, C., et al. (2013) · Annals of Neurology · doi:10.1002/ana.24066 · Cited by 670
Self-citationWhat Genetics Tells us About the Causes and Mechanisms of Parkinson's Disease
Corti, O., Lesage, S., & Brice, A. (2011) · Physiological Reviews · doi:10.1152/physrev.00022.2010 · Cited by 652
Cellular milieu imparts distinct pathological α-synuclein strains in α-synucleinopathies
Peng, C., Gathagan, R. J., Covell, D. J., Medellin, C., Stieber, A., Robinson, J. L., Zhang, B., Pitkin, R. M., Olufemi, M. F., Luk, K. C., et al. (2018) · Nature · doi:10.1038/s41586-018-0104-4 · Cited by 605
Understanding Dopaminergic Cell Death Pathways in Parkinson Disease
Michel, P. P., Hirsch, É. C., & Hunot, S. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.038 · Cited by 622
A Role for α-Synuclein in the Regulation of Dopamine Biosynthesis
Perez, R. G., Waymire, J. C., Lin, E., Liu, J. J., Guo, F., & Zigmond, M. J. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-08-03090.2002 · Cited by 598
El-Agnaf, O. M. A., Salem, S. A., Paleologou, K. E., Cooper, L. J., Fullwood, N. J., Gibson, M. J., Curran, M. D., Court, J. A., Mann, D. M. A., Ikeda, S.-I., et al. (2003) · The FASEB Journal · doi:10.1096/fj.03-0098fje · Cited by 590
DJ-1 Is a Redox-Dependent Molecular Chaperone That Inhibits α-Synuclein Aggregate Formation
Shendelman, S., Jonason, A. S., Martinat, C., Leete, T., & Abeliovich, A. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020362 · Cited by 610
Self-citationCell 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 626
Resistance of α-synuclein null mice to the parkinsonian neurotoxin MPTP
Dauer, W. T., Kholodilov, N. G., Vila, M., Trillat, A., Goodchild, R. E., Larsen, K. E., Staal, R. G. W., Tieu, K., Schmitz, Y., Yuan, C. A., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172514599 · Cited by 595
Self-citationThe Synaptic Function of α-Synuclein
Burré, J. (2015) · Journal of Parkinson s Disease · doi:10.3233/jpd-150642 · Cited by 610
The Synucleinopathies: Twenty Years On
Goedert, M., Jakes, R., & Spillantini, M. G. (2017) · Journal of Parkinson s Disease · doi:10.3233/jpd-179005 · Cited by 590
Nuytemans, K., Theuns, J., Cruts, M., & Broeckhoven, C. V. (2010) · Human Mutation · doi:10.1002/humu.21277 · Cited by 583
Sharon, R., Bar-Joseph, I., Frosch, M. P., Walsh, D. M., Hamilton, J. A., & Selkoe, D. J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00024-2 · Cited by 572
α-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity
Kontopoulos, E., Parvin, J. D., & Feany, M. Β. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl243 · Cited by 553
Mosharov, E. V., Larsen, K. E., Kanter, E., Phillips, K. A., Wilson, K., Schmitz, Y., Krantz, D. E., Kobayashi, K., Edwards, R. H., & Sulzer, D. (2009) · Neuron · doi:10.1016/j.neuron.2009.01.033 · Cited by 548
Self-citationLo Bianco, C., 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 482
The Parkinson's disease protein α-synuclein disrupts cellular Rab homeostasis
Gitler, A. D., Bevis, B. J., Shorter, J., Strathearn, K. E., Hamamichi, S., Su, L. J., Caldwell, K. A., Caldwell, G. A., Rochet, J., McCaffery, J. M., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710685105 · Cited by 535
RAB7L1 Interacts with LRRK2 to Modify Intraneuronal Protein Sorting and Parkinson’s Disease Risk
MacLeod, D. A., Rhinn, H., Kuwahara, T., Zolin, A., Di Paolo, G., McCabe, B. D., Marder, K. S., Honig, L. S., Clark, L. N., Small, S. A., et al. (2013) · Neuron · doi:10.1016/j.neuron.2012.11.033 · Cited by 516
Self-citationα-Synuclein: Membrane Interactions and Toxicity in Parkinson's Disease
Auluck, P. K., Caraveo, G., & Lindquist, S. L. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.042308.113313 · Cited by 537
Lipid Rafts Mediate the Synaptic Localization of α-Synuclein
Fortin, D. L., Troyer, M. D., Nakamura, K., Kubo, S., Anthony, M. D., & Edwards, R. H. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1594-04.2004 · Cited by 540
Systemic exosomal siRNA delivery reduced alpha‐synuclein aggregates in brains of transgenic mice
Cooper, J. A. D., Wiklander, O. P. B., Nordin, J. Z., Al‐Shawi, R., Wood, M. J. A., Vithlani, M., Schapira, A. H. V., Simons, J. P., Andaloussi, S. E., & Alvarez‐Erviti, L. (2014) · Movement Disorders · doi:10.1002/mds.25978 · Cited by 521
Parkin gene inactivation alters behaviour and dopamine neurotransmission in the mouse
Itier, J. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg239 · Cited by 523
Classic and New Animal Models of Parkinson's Disease
Blesa, J., Phani, S., Jackson-Lewis, V. R., & Przedborski, S. (2012) · BioMed Research International · doi:10.1155/2012/845618 · Cited by 533
α-Synuclein misfolding and aggregation: Implications in Parkinson’s disease pathogenesis
Mehra, S., Sahay, S., & Maji, S. K. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.03.001 · Cited by 536
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
Oxidative stress and cellular pathologies in Parkinson’s disease
Puspita, L., Chung, S. Y., & Shim, J. (2017) · Molecular Brain · doi:10.1186/s13041-017-0340-9 · Cited by 507
Inhibition of mitochondrial fusion by α‐synuclein is rescued by PINK1, Parkin and DJ‐1
Kamp, F., Exner, N., Lutz, A. K., Wender, N., Hegermann, J., Brunner, B., Nuscher, B., Bartels, T., Giese, A., Beyer, K., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.223 · Cited by 504
Shults, C. W. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509567103 · Cited by 495
Autophagy and neurodegeneration: when the cleaning crew goes on strike
Martínez‐Vicente, M., & Cuervo, A. M. (2007) · The Lancet Neurology · doi:10.1016/s1474-4422(07)70076-5 · Cited by 495
Suh, Y.-H., & Checler, F. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.469 · Cited by 476
Orimo, S., Uchihara, T., Nakamura, A., Mori, F., Kakita, A., Wakabayashi, K., & Takahashi, H. (2007) · Brain · doi:10.1093/brain/awm302 · Cited by 469
Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson’s disease?
Goldberg, M. S., & Lansbury, P. T. (2000) · Nature Cell Biology · doi:10.1038/35017124 · Cited by 459
Lee, F. J. S., Liu, F., Pristupa, Z. B., & Niznik, H. B. (2001) · The FASEB Journal · doi:10.1096/fj.00-0334com · Cited by 463
Lee, H.-J., Choi, C., & Lee, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107045200 · Cited by 462
Defects in trafficking bridge Parkinson’s disease pathology and genetics
Abeliovich, A., & Gitler, A. D. (2016) · Nature · doi:10.1038/nature20414 · Cited by 462
Self-citationModification of Brain Aging and Neurodegenerative Disorders by Genes, Diet, and Behavior
Mattson, M. P., Chan, S. L., & Duan, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00004.2002 · Cited by 440
Double-knockout mice for α- and β-synucleins: Effect on synaptic functions
Chandra, S., Fornai, F., Kwon, H.-B., Yazdani, U., Atasoy, D., Liu, X., Hammer, R. E., Battaglia, G., German, D. C., Castillo, P. E., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406283101 · Cited by 438
Self-citationNeuroinflammation and Oxidation/Nitration of α-Synuclein Linked to Dopaminergic Neurodegeneration
Gao, H., Kotzbauer, P. T., Uryu, K., Leight, S., Trojanowski, J. Q., & Lee, V. M. ‐. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0143-07.2008 · Cited by 453
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
α-Synuclein and neuronal cell death
Cookson, M. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-9 · Cited by 440
Bussell, R., & Eliezer, D. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00520-5 · Cited by 437
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 424
Self-citationOxidative Stress and Genetics in the Pathogenesis of Parkinson's Disease
Zhang, Y., Dawson, V. L., & Dawson, T. M. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0319 · Cited by 408
Interplay of α-synuclein binding and conformational switching probed by single-molecule fluorescence
Ferreon, A. C. M., Gambin, Y., Lemke, E. A., & Deniz, A. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809232106 · Cited by 407
Genetic and environmental factors in the cause of Parkinson's disease
Warner, T. T., & Schapira, A. H. V. (2003) · Annals of Neurology · doi:10.1002/ana.10487 · Cited by 406
Synucleins Are a Novel Class of Substrates for G Protein-coupled Receptor Kinases
Pronin, A. N., Morris, A. J., Surguchov, A. P., & Benovic, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003542200 · Cited by 395
Striatal dopamine neurotransmission: Regulation of release and uptake
Sulzer, D., Cragg, S. J., & Rice, M. E. (2016) · Basal Ganglia · doi:10.1016/j.baga.2016.02.001 · Cited by 382
Self-citationMollenhauer, B., Cullen, V., Kahn, I., Krastins, B., Outeiro, T. F., Pepivani, I., Ng, J., Schulz-Schaeffer, W., Kretzschmar, H. A., McLean, P. J., et al. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2008.06.004 · Cited by 382
Mechanisms of α-Synuclein Induced Synaptopathy in Parkinson's Disease
Bridi, J. C., & Hirth, F. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00080 · Cited by 396
Gene Expression in Human Alcoholism: Microarray Analysis of Frontal Cortex
Lewohl, J. M., Wang, L., Miles, M. F., Zhang, L., Dodd, P. R., & Harris, R. A. (2000) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2000.tb01993.x · Cited by 379
Behavioral characterization of a unilateral 6-OHDA-lesion model of Parkinson's disease in mice
Ferfoglia, R. I., Mohapel, P., Brundin, P., & Paul, G. (2005) · Behavioural Brain Research · doi:10.1016/j.bbr.2005.02.023 · Cited by 387
Effects of Curvature and Composition on α-Synuclein Binding to Lipid Vesicles
Middleton, E. R., & Rhoades, E. R. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.07.056 · Cited by 392
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review