Parkinson's Disease

Dauer, William; Przedborski, Serge

doi:10.1016/s0896-6273(03)00568-3

Cited by 5,469Parkinson's Disease Mechanisms and TreatmentsNuclear Receptors and SignalingNeurological disorders and treatments

Parkinson's Disease

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Dauer, William, Przedborski, Serge·2003·Neuron

DOI 10.1016/s0896-6273(03)00568-3

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Abstract

Parkinson's disease (PD) results primarily from the death of dopaminergic neurons in the substantia nigra. Current PD medications treat symptoms; none halt or retard dopaminergic neuron degeneration. The main obstacle to developing neuroprotective therapies is a limited understanding of the key molecular events that provoke neurodegeneration. The discovery of PD genes has led to the hypothesis that misfolding of proteins and dysfunction of the ubiquitin-proteasome pathway are pivotal to PD pathogenesis. Previously implicated culprits in PD neurodegeneration, mitochondrial dysfunction and oxidative stress, may also act in part by causing the accumulation of misfolded proteins, in addition to producing other deleterious events in dopaminergic neurons. Neurotoxin-based models (particularly MPTP) have been important in elucidating the molecular cascade of cell death in dopaminergic neurons. PD models based on the manipulation of PD genes should prove valuable in elucidating important aspects of the disease, such as selective vulnerability of substantia nigra dopaminergic neurons to the degenerative process.

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The diagnosis of Parkinson's disease is reliant on clinical motor symptoms and neuroimaging; by symptom onset, an estimated 50-70% of substantia nigra pars compacta dopaminergic neurons have already been lost.
“The diagnosis of PD is reliant on clinical motor symptoms and neuroimaging; however, by the onset of symptoms, it is estimated that 50–70% of substantia nigra pars compacta dopaminergic neurons have already been lost [247, 248].”
From Extracellular vesicles as nanotheranostic platforms for targeted neurological disorder interventions (2024) · cites this paper as [248]
Neurotoxicants such as MPTP, paraquat, rotenone and 6-OHDA are commonly used to induce experimental PD models by disrupting mitochondria and increasing oxidative stress.
“Neurotoxicants, such as 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), paraquat, rotenone and 6-hydroxydopamine (6-OHDA), are commonly used to induce experimental PD models by disrupting mitochondria and increasing oxidative stress [9]”
From Healthy Human Fecal Microbiota Transplantation into Mice Attenuates MPTP-Induced Neurotoxicity via AMPK/SOD2 Pathway (2023) · cites this paper as [9]
PD is characterized by progressive loss of dopaminergic neurons in the substantia nigra pars compacta and nerve terminals in the striatum.
“PD is characterized by the progressive loss of dopaminergic neurons in the substantia nigra pars compacta and the nerve terminals in the striatum (Dauer and Przedborski, 2003).”
From The role of microglia in retinal neurodegeneration: Alzheimer’s disease, parkinson, and glaucoma. (2017) · cites this paper as Dauer and Przedborski, 2003
Genetic factors for PD include mutations in α-syn, while mitochondrial dysfunction and oxidative stress may also act by causing the accumulation of misfolded proteins.
“Genetic factors include mutations in α-syn (Olanow and Tatton, 1999; Pérez and Arancibia, 2007), while mitochondrial dysfunction and oxidative stress may also act by causing the accumulation of misfolded proteins (Dauer and Przedborski, 2003).”
From The role of microglia in retinal neurodegeneration: Alzheimer’s disease, parkinson, and glaucoma. (2017) · cites this paper as Dauer and Przedborski, 2003
Mitochondrial dysfunction is implicated in the pathophysiology of Parkinson's disease.
“Mitochondrial dysfunction is implicated in the pathophysiology of Parkinson′s disease (PD), a common age-associated neurodegenerative disease characterized by intraneuronal inclusions (Lewy bodies) and progressive degeneration of the nigrostriatal dopamine (DA) system.”
From Progressive parkinsonism in mice with respiratory-chain-deficient dopamine neurons (2007) · cites this paper as [2]

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Rapid ATP Loss Caused by 1‐Methyl‐4‐Phenyl‐1,2,3,6‐Tetrahydropyridine in Mouse Brain
Chan, P., DeLanney, L. E., Irwin, I., Langston, J. W., & Monte, D. A. D. (1991) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1991.tb02134.x · Cited by 241 · see citing works
Role of Cytochrome c as a Stimulator of α-Synuclein Aggregation in Lewy Body Disease
Hashimoto, M., Takeda, A., Hsu, L. J., Takenouchi, T., & Masliah, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.28849 · Cited by 236 · see citing works
MPTP Activates c‐Jun NH2‐Terminal Kinase (JNK) and Its Upstream Regulatory Kinase MKK4 in Nigrostriatal Neurons In Vivo
Saporito, M. S., Thomas, B. A., & Scott, R. W. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0751200.x · Cited by 233 · see citing works
Gene transfer of the JNK interacting protein-1 protects dopaminergic neurons in the MPTP model of Parkinson's disease
Xia, X., Harding, T. A., Weller, M., Bieneman, A., Uney, J. B., & Schulz, J. B. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181182298 · Cited by 232 · see citing works
Transgenic mice expressing human Bcl-2 in their neurons are resistant to 6-hydroxydopamine and 1-methyl-4-phenyl-1,2,3,6- tetrahydropyridine neurotoxicity
Offen, D., Beart, P. M., Cheung, N. S., Pascoe, C. J., Hochman, A., Gorodin, S., Melamed, E., Bernard, R., & Bernard, O. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.10.5789 · Cited by 229 · see citing works
Isoquinoline neurotoxins in the brain and Parkinson's disease
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Absence of MPTP-Induced Neuronal Death in Mice Lacking the Dopamine Transporter
Bézard, E., Gross, C. E., Fournier, M.-C., Doveró, S., Bloch, B., & Jaber, M. (1999) · Experimental Neurology · doi:10.1006/exnr.1998.6995 · Cited by 227 · see citing works
Oxy-radical toxicity in catecholamine neurons.
Cohen, G. (1984) · PubMed · Cited by 224 · see citing works
Case-control study of the ubiquitin carboxy-terminal hydrolase L1 gene in Parkinson’s disease
Maraganore, D. M., Farrer, M. J., Hardy, J., et al. (1999) · Neurology · doi:10.1212/wnl.53.8.1858 · Cited by 211 · see citing works
Threshold Effects and Control of Oxidative Phosphorylation in Nonsynaptic Rat Brain Mitochondria
Davey, G. P., & Clark, J. B. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66041617.x · Cited by 209 · see citing works
Similarities and differences between MPTP-induced parkinsonsim and Parkinson's disease. Neuropathologic considerations.
Forno, L. S., DeLanney, L. E., Irwin, I., & Langston, J. W. (1993) · PubMed · Cited by 207 · see citing works
A mechanism of paraquat toxicity involving nitric oxide synthase
Day, B. J., Patel, M., Calavetta, L., Chang, L.-Y., & Stamler, J. S. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.22.12760 · Cited by 206 · see citing works
Protection by Synergistic Effects of Adenovirus-Mediated X-Chromosome-Linked Inhibitor of Apoptosis and Glial Cell Line-Derived Neurotrophic Factor Gene Transfer in the 1-Methyl-4-Phenyl-1,2,3,6-Tetrahydropyridine Model of Parkinson's Disease
Eberhardt, O., von Coelln, R., Kügler, S., Lindenau, J. H., Rathke‐Hartlieb, S., Gerhardt, E., Haid, S., Isenmann, S., Gravel, C., Srinivasan, A. N., et al. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-24-09126.2000 · Cited by 206 · see citing works
Systemic administration of rotenone produces selective damage in the striatum and globus pallidus, but not in the substantia nigra
Ferrante, R. J., Schulz, J. B., Kowall, N. W., et al. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00008-5 · Cited by 204 · see citing works
p53 inhibitors preserve dopamine neurons and motor function in experimental parkinsonism
Duan, W., Zhu, X., Ladenheim, B., Yu, Q., Guo, Z., Oyler, J. M., Cutler, R. G., Cadet, J. L., Greig, N. H., & Mattson, M. P. (2002) · Annals of Neurology · doi:10.1002/ana.10350 · Cited by 204 · see citing works
Substantia nigra neuromelanin: structure, synthesis, and molecular behaviour.
Zecca, L., Tampellini, D., Gerlach, M., Riederer, P. F., Fariello, R. G., & Sulzer, D. L. (2001) · Europe PMC (PubMed Central) · doi:10.1136/mp.54.6.414 · Cited by 200 · see citing works
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyride Neurotoxicity Is Attenuated in Mice Overexpressing Bcl-2
Yang, L., Matthews, R. T., Schulz, J. B., Klockgether, T., Liao, A., Martinou, J., Penney, J. B., Hyman, B. T., & Beal, M. F. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-20-08145.1998 · Cited by 199 · see citing works
Neurotoxicity of the meperidine analogue N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine on brain catecholamine neurons in the mouse
Hallman, H., Olson, L., & JONSSON, G. (1984) · European Journal of Pharmacology · doi:10.1016/0014-2999(84)90521-1 · Cited by 194 · see citing works
Association of Single-Nucleotide Polymorphisms of the Tau Gene With Late-Onset Parkinson Disease
Martin, E. R. (2001) · JAMA · doi:10.1001/jama.286.18.2245 · Cited by 191 · see citing works
Oxidative post‐translational modifications of α‐synuclein in the 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP) mouse model of Parkinson's disease
Przedborski, S., Chen, Q., Vila, M., Giasson, B. I., Djaldatti, R., Vukosavić, S., Souza, J. M., Jackson-Lewis, V. R., Lee, V. M. ‐., & Ischiropoulos, H. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00174.x · Cited by 190 · see citing works
Self-citation
Subsets of midbrain dopaminergic neurons in monkeys are distinguished by different levels of mRNA for the dopamine transporter: Comparison with the mRNA for the D2 receptor, tyrosine hydroxylase and calbindin immunoreactivity
Haber, S. N., Ryoo, H., Cox, C., & Lu, W. (1995) · The Journal of Comparative Neurology · doi:10.1002/cne.903620308 · Cited by 188 · see citing works
Selective retention of MPP+ within the monoaminergic systems of the primate brain following MPTP administration: An in vivo autoradiographic study
Herkenham, M. A., Little, M. D., Bankiewicz, K. S., Yang, S., Markey, S. P., & Johannessen, J. N. (1991) · Neuroscience · doi:10.1016/0306-4522(91)90180-v · Cited by 180 · see citing works
Programmed cell death and the control of cell survival
Raff, M. C., Barres, B. A., Burne, J. F., Coles, H. S. R., Ishizaki, Y., & Jacobson, M. D. (1994) · Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences · doi:10.1098/rstb.1994.0104 · Cited by 166 · see citing works
Differential vulnerability of primate caudate-putamen and striosome-matrix dopamine systems to the neurotoxic effects of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine.
Moratalla, R., Quinn, B., DeLanney, L. E., Irwin, I., Langston, J. W., & Graybiel, A. M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.9.3859 · Cited by 158 · see citing works
Effects of Pharmacological Agents upon a Transgenic Model of Parkinson’s Disease in Drosophila melanogaster
Pendleton, R. G., Parvez, F., SAYED, M. E. S., & Hillman, R. (2002) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.300.1.91 · Cited by 158 · see citing works
Selective lesion of central dopamine or noradrenaline neuron systems in the neonatal rat: motor behavior and monoamine alterations at adult stage
Luthman, J., Fredriksson, A., Sundström, E., JONSSON, G., & Archer, T. (1989) · Behavioural Brain Research · doi:10.1016/s0166-4328(89)80121-4 · Cited by 155 · see citing works
Is Bax a mitochondrial mediator in apoptotic death of dopaminergic neurons in Parkinson's disease?
Hartmann, A., Michel, P. P., Troadec, J., Prigent, A., Faucheux, B. A., Ruberg, M., Agid, Y., & Hirsch, É. C. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00160.x · Cited by 153 · see citing works
Dose-dependent destruction of the coeruleus-cortical and nigral-striatal projections by MPTP
Seniuk, N. A., Tatton, W. G., & Greenwood, C. E. (1990) · Brain Research · doi:10.1016/0006-8993(90)91055-l · Cited by 153 · see citing works
Evaluation of 50 probands with early-onset Parkinson’s disease for Parkin mutations
Hedrich, K., Marder, K. S., Harris, J. M., Kann, M., Lynch, T., Meija‐Santana, H., Pramstaller, P. P., SCHWINGER, E., Bressman, S., Fahn, S., et al. (2002) · Neurology · doi:10.1212/wnl.58.8.1239 · Cited by 152 · see citing works
Dopamine transporter messenger RNA in Parkinson's disease and control substantia nigra neurons
Uhl, G. R., Walther, D. M., Mash, D. C., Faucheux, B. A., & Javoy-Agid, F. (1994) · Annals of Neurology · doi:10.1002/ana.410350421 · Cited by 151 · see citing works
Role of α-synuclein in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced parkinsonism in mice
Schlüter, O. M., Fornai, F., Alessandri, M., TAKAMORI, S., Geppert, M., Jahn, R., & Südhof, T. C. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00036-8 · Cited by 145 · see citing works
Neuromelanin and Parkinson's disease.
MARSDEN, C. D. (1983) · PubMed · Cited by 143 · see citing works
Parkinson Disease Survival
Morgante, L., Salemi, G., Meneghini, F., Rosa, A. E. D., Epifanio, A., Grigoletto, F., Ragonese, P., Patti, F., Reggio, A., Perri, R. D., et al. (2000) · Archives of Neurology · doi:10.1001/archneur.57.4.507 · Cited by 143 · see citing works
In Vivo Labeling of Mitochondrial Complex I (NADH:UbiquinoneOxidoreductase) in Rat Brain Using [3H]Dihydrorotenone
Talpade, D. J., Greene, J. G., Higgins, D. S., & Greenamyre, J. T. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0752611.x · Cited by 142 · see citing works
Differences in Nigral Neuron Number and Sensitivity to 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine in C57/bl and CD-1 Mice
Muthane, U. B., Ramsay, K., Jiang, H., et al. (1994) · Experimental Neurology · doi:10.1006/exnr.1994.1058 · Cited by 140 · see citing works
Prevention of the Nigrostriatal Toxicity of 1‐Methyl‐4‐Phenyl‐1,2,3,6‐Tetrahydropyridine by Inhibitors of 3,4‐Dihydroxyphenylethylamine Transport
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Studies on species sensitivity to the dopaminergic neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine. Part 1: Systemic administration.
Giovanni, A., Sieber, B.-A., Heikkila, R. E., et al. (1994) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)22503-4 · Cited by 138 · see citing works
α-Synuclein Interacts with Phospholipase D Isozymes and Inhibits Pervanadate-induced Phospholipase D Activation in Human Embryonic Kidney-293 Cells
Ahn, B., Rhim, H., Kim, S. Y., Sung, Y., Lee, M., Choi, J., Wolozin, B. L., Chang, J., Lee, Y. H., Kwon, T. K., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110414200 · Cited by 136 · see citing works
Dopamine Neurons from Transgenic Mice with a Knockout of the p53 Gene Resist MPTP Neurotoxicity
Trimmer, P. A., Smith, T. S., Jung, A. B., et al. (1996) · Neurodegeneration · doi:10.1006/neur.1996.0031 · Cited by 134 · see citing works
Microtubule-associated Protein 1B Is a Component of Cortical Lewy Bodies and Binds α-Synuclein Filaments
Jensen, P. H., Islam, K., Kenney, J. M., Nielsen, M. S., Power, J., & Gai, W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000099200 · Cited by 133 · see citing works
Neurochemistry of Parkinson's disease: relation between striatal and limbic dopamine.
Price, K. S., Farley, I. J., & Hornykiewicz, O. (1978) · PubMed · Cited by 130 · see citing works
Apoptosis in substantia nigra following developmental striatal excitotoxic injury.
Macaya, A., Munell, F., Gubits, R. M., & Burke, R. E. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.17.8117 · Cited by 129 · see citing works
Specificity of dopaminergic neuronal degeneration induced by intracerebral injection of 6-hydroxydopamine in the nigrostriatal dopamine system
Javoy‐Agid, F., Sotelo, C., Herbet, A., et al. (1976) · Brain Research · doi:10.1016/0006-8993(76)90877-5 · Cited by 128 · see citing works
Increased susceptibility to MPTP toxicity in middle-aged rhesus monkeys
Ovadia, A., Zhang, Z., & Gash, D. M. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)02012-8 · Cited by 127 · see citing works
Epidemiology of Parkinson’s Disease
Tanner, C. M. (1992) · Neurologic Clinics · doi:10.1016/s0733-8619(18)30212-3 · Cited by 127 · see citing works
Gene transfer of a reserpine-sensitive mechanism of resistance to N-methyl-4-phenylpyridinium.
Liu, Y., Roghani, A., & Edwards, R. H. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.19.9074 · Cited by 124 · see citing works

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Neurodegenerative diseases and oxidative stress
Barnham, K. J., Masters, C. L., & Bush, A. I. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1330 · Cited by 3,683 · see citing works
Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1
Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481 · see citing works
Differential Roles of M1 and M2 Microglia in Neurodegenerative Diseases
Tang, Y., & Le, W. (2016) · Molecular Neurobiology · doi:10.1007/s12035-014-9070-5 · Cited by 2,190 · see citing works
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 · see citing works
PINK1-dependent recruitment of Parkin to mitochondria in mitophagy
Vives-Bauza, C., Zhou, C., Huang, Y., Cui, M., de Vries, R. L. A., Kim, J., May, J., Tocilescu, M. A., Liu, W., Ko, H. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911187107 · Cited by 1,616 · see citing works
Self-citation
Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein
Desplats, P., Lee, H.-J., Bae, E.-J., Patrick, C., Rockenstein, E., Crews, L., Spencer, B., Masliah, E., & Lee, S.-J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903691106 · Cited by 1,485 · see citing works
Molecular mechanisms of excitotoxicity and their relevance to pathogenesis of neurodegenerative diseases
Dong, X.-X., Wang, Y., & Qin, Z.-H. (2009) · Acta Pharmacologica Sinica · doi:10.1038/aps.2009.24 · Cited by 1,297 · see citing works
13 reasons why the brain is susceptible to oxidative stress
Cobley, J. N., Fiorello, M. L., & Bailey, D. M. (2018) · Redox Biology · doi:10.1016/j.redox.2018.01.008 · Cited by 1,215 · see citing works
Dopamine: Functions, Signaling, and Association with Neurological Diseases
Klein, M. O., Battagello, D. S., Cardoso, A. R., Hauser, D. N., Bittencourt, J. C., & Correa, R. G. (2019) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-018-0632-3 · Cited by 1,073 · see citing works
Clinical progression in Parkinson disease and the neurobiology of axons
Cheng, H., Ulane, C. M., & Burke, R. E. (2010) · Annals of Neurology · doi:10.1002/ana.21995 · Cited by 1,012 · 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
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 · see citing works
Neuroprotective effects of fecal microbiota transplantation on MPTP-induced Parkinson's disease mice: gut microbiota, glial reaction and TLR4/TNF-α signaling pathway
Sun, M.-F., Zhu, Y.-L., Zhou, Z.-L., Jia, X.-B., Xu, Y.-D., Yang, Q., Cui, C., & Shen, Y.-Q. (2018) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2018.02.005 · Cited by 736 · see citing works
Mitochondrial dysfunction in Parkinson's disease
Winklhofer, K. F., & Haass, C. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.08.013 · Cited by 688 · see citing works
The mitochondrial energy transduction system and the aging process
Navarro, A., & Boveris, A. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00213.2006 · Cited by 646 · see citing works
Mutations in the Glucocerebrosidase Gene and Parkinson's Disease in Ashkenazi Jews
Aharon-Peretz, J., Rosenbaum, H., & Gershoni-Baruch, R. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa033277 · Cited by 597 · see citing works
Progressive parkinsonism in mice with respiratory-chain-deficient dopamine neurons
Ekstrand, M. I., Terzioglu, M., Galter, D., Zhu, S., Hofstetter, C., Lindqvist, E., Thams, S., Bergstrand, A., Hansson, F. S., Trifunovic, A., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605208103 · Cited by 605 · see citing works
Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export
Lei, P., Ayton, S., Finkelstein, D. I., Spoerri, L., Ciccotosto, G. D., Wright, D. K., Wong, B. X. W., Adlard, P. A., Cherny, R. A., Lam, L. Q., et al. (2012) · Nature Medicine · doi:10.1038/nm.2613 · Cited by 594 · see citing works
Nrf2-mediated neuroprotection in the MPTP mouse model of Parkinson’s disease: Critical role for the astrocyte
Chen, P.-C., Vargas, M. R., Pani, A. K., Smeyne, R. J., Johnson, D. A., Kan, Y. W., & Johnson, J. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813361106 · Cited by 579 · see citing works
The role of methionine on metabolism, oxidative stress, and diseases
Martínez, Y., Li, X., Liu, G., Bin, P., Yan, W., Más, D., Valdivié, M., Hu, C.-A. A., Ren, W., & Yin, Y. (2017) · Amino Acids · doi:10.1007/s00726-017-2494-2 · Cited by 583 · see citing works
Microglia in Neuroinflammation and Neurodegeneration: From Understanding to Therapy
Muzio, L., Viotti, A., & Martino, G. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.742065 · Cited by 581 · see citing works
Disorders of lysosomal acidification—The emerging role of v-ATPase in aging and neurodegenerative disease
Colacurcio, D. J., & Nixon, R. A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.004 · Cited by 548 · see citing works
Peripheral cytokines profile in parkinson’s disease
Reale, M., Iarlori, C., Thomas, A., Gambi, D., Perfetti, B., Di Nicola, M., & Onofrj, M. (2009) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2008.07.003 · Cited by 547 · see citing works
Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction
Tai, H.-C., & Schuman, E. M. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2499 · Cited by 532 · see citing works
Lipopolysaccharide-induced neuroinflammation as a bridge to understand neurodegeneration
Batista, C. R. A., Gomes, G. F., Candelario-Jalil, E., Fiebich, B. L., & de Oliveira, A. C. P. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092293 · Cited by 529 · see citing works
Towards an immuno-precipitated neurodevelopmental animal model of schizophrenia
Meyer, U., Feldon, J., Schedlowski, M., & Yee, B. K. (2005) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2004.10.012 · Cited by 494 · see citing works
A Guide to Neurotoxic Animal Models of Parkinson's Disease
Tieu, K. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009316 · Cited by 483 · see citing works
The role of microglia in retinal neurodegeneration: Alzheimer’s disease, parkinson, and glaucoma.
Ramirez, A. I., de Hoz, R., Salobrar-Garcia, E., Salazar, J. J., Rojas, B., Ajoy, D., López-Cuenca, I., Rojas, P., Triviño, A., & Ramírez, J. M. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00214 · Cited by 466 · see citing works
Mitochondrial respiratory complex I: Structure, function and implication in human diseases
Sharma, L., Lu, J., & Bai, Y. (2009) · Current Medicinal Chemistry · doi:10.2174/092986709787846578 · Cited by 438 · see citing works
Adenosine receptors and brain diseases: neuroprotection and neurodegeneration
Gomes, C. V., Kaster, M. P., Tomé, A. R., Agostinho, P. M., & Cunha, R. A. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.12.001 · Cited by 419 · see citing works
The Role of Mitochondria in Neurodegenerative Diseases: the Lesson from Alzheimer’s Disease and Parkinson’s Disease
Monzio Compagnoni, G., Di Fonzo, A., Corti, S., Comi, G. P., Bresolin, N., & Masliah, E. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01926-1 · Cited by 378 · see citing works
Neuroprotective effects of hydrogen sulfide on Parkinson’s disease rat models
Hu, L., Lu, M., Tiong, C. X., Dawe, G. S., Hu, G., & Bian, J. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2009.00543.x · Cited by 365 · see citing works
Cellular Specificity of NF-κB Function in the Nervous System
Dresselhaus, E. C., & Meffert, M. K. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01043 · Cited by 345 · see citing works
Pathogenesis of Parkinson's disease
Hirsch, E. C., Jenner, P., & Przedborski, S. (2013) · Movement Disorders · doi:10.1002/mds.25032 · Cited by 336 · see citing works
Self-citation
Spontaneous eye blink rate as predictor of dopamine-related cognitive function—A review
Jongkees, B. J., & Colzato, L. S. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.08.020 · Cited by 300 · see citing works
Endogenous Parkin Preserves Dopaminergic Substantia Nigral Neurons following Mitochondrial DNA Mutagenic Stress
Pickrell, A. M., Huang, C.-H., Kennedy, S. R., Ordureau, A., Sideris, D. P., Hoekstra, J. G., Harper, J. W., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2015.06.034 · Cited by 327 · see citing works
Disrupted Autophagy Leads to Dopaminergic Axon and Dendrite Degeneration and Promotes Presynaptic Accumulation of α-Synuclein and LRRK2 in the Brain
Friedman, L. G., Lachenmayer, M. L., Wang, J., He, L., Poulose, S. M., Komatsu, M., Holstein, G. R., & Yue, Z. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5809-11.2012 · Cited by 303 · see citing works
Mitochondrial Approaches for Neuroprotection
Chaturvedi, R. K., & Beal, M. F. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.027 · Cited by 294 · see citing works
Ghrelin promotes and protects nigrostriatal dopamine function via a UCP2-dependent mitochondrial mechanism
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Authors: Dauer, W., & Przedborski, S.
Affiliations: Columbia University (US)
Corresponding author: Przedborski, Serge
ORCID: Dauer, William
Przedborski, Serge
Venue: Neuron
Publisher: Elsevier BV
Published: 2003-09
Volume: 39
Issue: 6
Pages: 889-909
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/s0896-6273(03)00568-3
OpenAlex: W62603772
Cited by: 5,469
References: 243
Citations by year: 2026: 167 · 2025: 250 · 2024: 287 · 2023: 288 · 2022: 309 · 2021: 301 · 2020: 312 · 2019: 294 · 2018: 328 · 2017: 329 · 2016: 276 · 2015: 267 · 2014: 273 · 2013: 268 · 2012: 229
FWCI: 13.26
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3607 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of Neurological Disorders and Stroke (NS 38586, R01NS042269, R01NS038586, NS11766-27A1, P50NS038370, NS 42269, NS38370)
Topics: Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
Health Sciences › Medicine › Neurology › Neurological disorders and treatments
Keywords: Parkinson's disease, dopaminergic neuron loss, substantia nigra, neurodegeneration, protein misfolding, ubiquitin-proteasome system, mitochondrial dysfunction, oxidative stress, MPTP-induced neurotoxicity, neuroprotective therapy, disease models
MeSH terms: Animals, Disease Models, Animal, Humans, Neurons, Parkinson Disease

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