The DOI matches its Crossref record; 243 of the 243 references it cites were found in a registry or an index.
Parkinson's Disease
Open accessAbstract
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.
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
“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]
In the citing paper
“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]
In the citing paper
“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
In the citing paper
“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
In the citing paper
“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]
In the citing paper
“In addition to mtDNA mutations, pathogenic mutations in several genes including α–synuclein, parkin, UCHL-1, DJ-1, PINK-1, LRRK-2, NURR-1, tau, and HtrA2 also directly or indirectly implicate a role of mitochondrial dysfunction in familial PD pathogenesis3, 28, 29.”
From Mitochondrial Approaches for Neuroprotection (2008) · cites this paper as [29]
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
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
Chronic Parkinsonism in Humans Due to a Product of Meperidine-Analog Synthesis
Langston, J. W., Ballard, P., Tetrud, J. W., & Irwin, I. (1983) · Science · doi:10.1126/science.6823561 · Cited by 4,914
Handbook of Chemical Neuroanatomy
Stern, C. D. (1986) · Neurochemistry International · doi:10.1016/0197-0186(86)90021-5 · Cited by 4,160
The Free Radical Theory of Aging Matures
BECKMAN, K. B., & AMES, B. N. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.2.547 · Cited by 3,879
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
Stereotaxic mapping of the monoamine pathways in the rat brain
Ungerstedt, U. (1971) · Acta Physiologica Scandinavica · doi:10.1111/j.1365-201x.1971.tb10998.x · Cited by 3,819
Chronic systemic pesticide exposure reproduces features of Parkinson's disease
Betarbet, R. S., Sherer, T., MacKenzie, G. M., Garcia‐Osuna, M., Panov, A. V., & Greenamyre, J. T. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,770
AGEING AND PARKINSON'S DISEASE: SUBSTANTIA NIGRA REGIONAL SELECTIVITY
FEARNLEY, J. M., & LEES, A. J. (1991) · Brain · doi:10.1093/brain/114.5.2283 · Cited by 3,529
The relevance of the Lewy body to the pathogenesis of idiopathic Parkinson's disease.
Gibb, W. R., & Lees, A. J. (1988) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp.51.6.745 · Cited by 3,481
Research works printed but not linked: 3
- Forno, 1993, Similarities and differences between MPTP-induced parkinsonism and Parkinson's disease, Adv. Neurol., 60, 600
- Irwin, 1993, MPTP and aging, Adv. Neurol., 60, 197
- Zecca, 2001, Substantia nigra neuromelanin, Mol. Pathol., 54, 414
Cited by
Sorted by citations
Items 101–153 of 153
The Therapeutic Role of Minocycline in Parkinson’s Disease
Cankaya, S., Cankaya, B., Kilic, U., Kilic, E., & Yulug, B. (2019) · Drugs in Context · doi:10.7573/dic.212553 · Cited by 93
BAX channel activity mediates lysosomal disruption linked to Parkinson disease
Bové, J., Martínez-Vicente, M., Dehay, B., Perier, C., Recasens, A., Bombrun, A., Antonsson, B., & Vila, M. (2014) · Autophagy · doi:10.4161/auto.28286 · Cited by 89
Hou, Y.-S., Guan, J.-J., Xu, H.-D., Wu, F., Sheng, R., & Qin, Z.-H. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00285-15 · Cited by 87
Neurotrophic factors in Parkinson’s disease are regulated by exercise: Evidence-based practice
da Silva, P. G. C., Domingues, D. D., de Carvalho, L. A., Allodi, S., & Correa, C. L. (2016) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2016.02.017 · Cited by 87
Rosa, A. I., Fonseca, I., Nunes, M. J., Moreira, S., Rodrigues, E., Carvalho, A. N., Rodrigues, C. M. P., Gama, M. J., & Castro-Caldas, M. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.06.004 · Cited by 82
van Hameren, G., Campbell, G., Deck, M., Berthelot, J., Gautier, B., Quintana, P., Chrast, R., & Tricaud, N. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0740-4 · Cited by 83
Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1
Nucifora, F. C., Nucifora, L. G., Ng, C.-H., Arbez, N., Guo, Y., Roby, E., Shani, V., Engelender, S., Wei, D., Wang, X.-F., et al. (2016) · Nature Communications · doi:10.1038/ncomms11792 · Cited by 82
Xie, Z., Zhang, M., Luo, Y., Jin, D., Guo, X., Yang, W., Zheng, J., Zhang, H., Zhang, L., Deng, C., et al. (2023) · Aging and disease · doi:10.14336/ad.2023.0309 · Cited by 80
“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].”
Machado, V., Zöller, T., Attaai, A., & Spittau, B. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17020151 · Cited by 76
Dong, X.-L., Wang, X., Liu, F., Liu, X., Du, Z.-R., Li, R. W., Xue, C.-H., Wong, K.-H., Wong, W.-T., Zhao, Q., et al. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.07.180 · Cited by 75
Kawahata, I., & Fukunaga, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113779 · Cited by 71
The impact of base excision DNA repair in age-related neurodegenerative diseases
Leandro, G. S., Sykora, P., & Bohr, V. A. (2015) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/j.mrfmmm.2014.12.011 · Cited by 72
Morais, L. H., Hara, D. B., Bicca, M. A., Poli, A., & Takahashi, R. N. (2018) · Behavioural Pharmacology · doi:10.1097/fbp.0000000000000389 · Cited by 58
Yamamuro, A., Yoshioka, Y., Ogita, K., & Maeda, S. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9062-6 · Cited by 70
Loss of Parkin impairs mitochondrial function and leads to muscle atrophy
Peker, N., Donipadi, V., Sharma, M., McFarlane, C., & Kambadur, R. (2018) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00064.2017 · Cited by 68
Cronin, A., & Grealy, M. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.10.018 · Cited by 68
Zhong, Z., Chen, W., Gao, H., Che, N., Xu, M., Yang, L., Zhang, Y., & Ye, M. (2021) · Neurochemical Research · doi:10.1007/s11064-021-03411-0 · Cited by 66
Vulnerability of mesostriatal dopaminergic neurons in Parkinson’s disease
González-Hernández, T. (2010) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2010.00140 · Cited by 65
Dopamine selectively potentiates hippocampal mossy fiber to CA3 synaptic transmission
Kobayashi, K., & Suzuki, H. (2007) · Neuropharmacology · doi:10.1016/j.neuropharm.2006.08.026 · Cited by 63
Heng, N., Malek, N., Lawton, M. A., Nodehi, A., Pitz, V., Grosset, K. A., Ben‐Shlomo, Y., & Grosset, D. G. (2023) · Movement Disorders Clinical Practice · doi:10.1002/mdc3.13687 · Cited by 64
Recent progress in the role of autophagy in neurological diseases
Meng, T., Lin, S., Zhuang, H., Huang, H., He, Z., Hu, Y., Gong, Q., & Feng, D. (2019) · Cell Stress · doi:10.15698/cst2019.05.186 · Cited by 58
Xu, J., Chen, T.-Y., Tai, C.-H., & Hsu, S.-H. (2023) · Biomaterials Research · doi:10.1186/s40824-023-00347-0 · Cited by 57
Kawahata, I., Bousset, L., Melki, R., & Fukunaga, K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215358 · Cited by 56
Panayotis, N., Pratte, M., Borges-Correia, A., Ghata, A., Villard, L., & Roux, J.-C. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.10.006 · Cited by 54
Rangasamy, S. B., Dasarathi, S., Pahan, P., Jana, M., & Pahan, K. (2019) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-018-9808-3 · Cited by 49
Tobón-Velasco, J. C., Palafox-Sánchez, V., Mendieta, L., García, E., Santamaría, A., Chamorro-Cevallos, G., & Limón, I. D. (2013) · Journal of Neural Transmission · doi:10.1007/s00702-013-0976-2 · Cited by 47
Infiltration of circulating myeloid cells through CD95L contributes to neurodegeneration in mice
Gao, L., Brenner, D., Llorens-Bobadilla, E., Saiz-Castro, G., Frank, T., Wieghofer, P., Hill, O., Thiemann, M., Karray, S., Prinz, M., et al. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20132423 · Cited by 42
Yazdani, S., Mariosa, D., Hammar, N., Andersson, J., Ingre, C., Walldius, G., & Fang, F. (2019) · Annals of Neurology · doi:10.1002/ana.25614 · Cited by 42
Pradhan, P., Majhi, O., Biswas, A., Joshi, V. K., & Sinha, D. (2020) · Cell Death & Disease · doi:10.1038/s41419-020-02942-8 · Cited by 44
Relevance of chronic stress and the two faces of microglia in Parkinson's disease
Herrera, A. J., Espinosa-Oliva, A. M., Carrillo-Jiménez, A., Oliva-Martín, M. J., García-Revilla, J., García-Quintanilla, A., de Pablos, R. M., & Venero, J. L. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00312 · Cited by 42
Induction of a Unique Isoform of the NCOA7 Oxidation Resistance Gene by Interferon β-1b
Yu, L., Croze, E., Yamaguchi, K. D., Tran, T., Reder, A. T., Litvak, V., & Volkert, M. R. (2015) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2014.0115 · Cited by 41
Xie, W., Gao, J., Jiang, R., Liu, X., Lai, F., Tang, Y., Xiao, H., Jia, Y., & Bai, Q. (2020) · NeuroToxicology · doi:10.1016/j.neuro.2019.11.009 · Cited by 40
Male/female differences in neuroprotection and neuromodulation of brain dopamine
Bourque, M. (2011) · Frontiers in Endocrinology · doi:10.3389/fendo.2011.00035 · Cited by 40
Iyer, R., Ungless, M. A., & Faisal, A. A. (2017) · Scientific Reports · doi:10.1038/s41598-017-05578-5 · Cited by 41
Chao, O. Y.-H., Pum, M. E., & Huston, J. P. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.01.003 · Cited by 39
Tai, C.-H., Bellesi, M., Chen, A.-C., Lin, C.-L., Li, H.-H., Lin, P.-J., Liao, W.-C., Hung, C.-S., Schwarting, R. K., & Ho, Y.-J. (2019) · Behavioural Brain Research · doi:10.1016/j.bbr.2019.02.020 · Cited by 34
Kakoty, V., K C, S., Dubey, S. K., Yang, C.-H., & Taliyan, R. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00144 · Cited by 33
Liu, D., Guo, J.-J., Su, J.-H., Svanbergsson, A., Yuan, L., Haikal, C., Li, W., Gouras, G., & Li, J.-Y. (2021) · Translational Neurodegeneration · doi:10.1186/s40035-021-00242-5 · Cited by 32
Huang, T., Shi, H., Xu, Y., & Ji, L. (2021) · Neuroreport · doi:10.1097/wnr.0000000000001585 · Cited by 36
Mendes, M. O., Rosa, A. I., Carvalho, A. N., Nunes, M. J., Dionísio, P., Rodrigues, E., Costa, D., Duarte-Silva, S., Maciel, P., Rodrigues, C. M. P., et al. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.01.003 · Cited by 31
Pando‐Naude, V., Matthews, T. E., Højlund, A., Jakobsen, S., Østergaard, K., Johnsen, E., Garza‐Villarreal, E. A., Witek, M. A. G., Penhune, V., & Vuust, P. (2024) · European Journal of Neuroscience · doi:10.1111/ejn.16128 · Cited by 29
Anwarullah, Aslam, M., Badshah, M., Abbasi, R., Sultan, A., Khan, K., Ahmad, N., & von Engelhardt, J. (2017) · Genes and Environment · doi:10.1186/s41021-017-0078-8 · Cited by 27
Extracellular vesicles as nanotheranostic platforms for targeted neurological disorder interventions
Choi, H. K., Chen, M., Goldston, L. L., & Lee, K.-B. (2024) · Nano Convergence · doi:10.1186/s40580-024-00426-5 · Cited by 26
Post-COVID-19 Parkinsonism and Parkinson’s Disease Pathogenesis: The Exosomal Cargo Hypothesis
Mysiris, D. S., Vavougios, G. D., Karamichali, E., Papoutsopoulou, S., Stavrou, V. T., Papayianni, E., Boutlas, S., Mavridis, T., Foka, P., Zarogiannis, S. G., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179739 · Cited by 25
Chan, D. G., Ventura, K., Villeneuve, A., Du Bois, P., & Holahan, M. R. (2022) · Journal of Parkinson's Disease · doi:10.3233/jpd-223461 · Cited by 24
Lai, C.-L., Lu, C.-C., Lin, H.-C., Sung, Y.-F., Wu, Y.-P., Hong, J.-S., & Peng, G.-S. (2019) · Journal of the Formosan Medical Association · doi:10.1016/j.jfma.2018.06.017 · Cited by 18
Emerging roles of leptin in Parkinson’s disease: Chronic inflammation, neuroprotection and more?
Regensburger, M., Rasul Chaudhry, S., Yasin, H., Zhao, Y., Stadlbauer, A., Buchfelder, M., & Kinfe, T. (2023) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2022.09.010 · Cited by 17
Prothrombin Kringle-2: a potential inflammatory pathogen in the parkinsonian dopaminergic system
Leem, E., Jeong, K. H., Won, S.-Y., Shin, W.-H., & Kim, S. R. (2016) · Experimental Neurobiology · doi:10.5607/en.2016.25.4.147 · Cited by 16
Makav, M., & Eroğlu, H. A. (2021) · Environmental Science and Pollution Research · doi:10.1007/s11356-020-11985-5 · Cited by 16
Tian, J., Du, G., Ye, L., Yu, X., Zhang, J., Wang, H., Yu, P., Fu, F., Liu, W., Li, Y., et al. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2012.11.010 · Cited by 15
Three-month subchronic intramuscular toxicity study of rotigotine-loaded microspheres in SD rats
Ye, L., Guan, X., Tian, J., Zhang, J., Du, G., Yu, X., Yu, P., Cen, X., Liu, W., & Li, Y. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.02.015 · Cited by 14
Pulcrano, S., De Gregorio, R., De Sanctis, C., Volpicelli, F., Piscitelli, R. M., Speranza, L., Perrone-Capano, C., di Porzio, U., Caiazzo, M., Martini, A., et al. (2023) · The Journal of Neuroscience · doi:10.1523/jneurosci.0431-23.2023 · Cited by 12
AI-enabled Parkinson's disease screening using smile videos
Adnan, T., Islam, M. S., Lee, S., Wasifur Rahman Chowdhury, E. M., Tithi, S. D., Noshin, K., Islam, M. R., Sarker, I., Rahman, M. S., Schneider, R. B., et al. (2025) · NEJM AI · doi:10.1056/aioa2400950 · Cited by 5
Metadata
- Authors
- Dauer, W., & Przedborski, S.
- Affiliations
- Columbia University (US)
- Corresponding author
- Przedborski, Serge
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2003-09
- Volume
- 39
- Issue
- 6
- Pages
- 889-909
- ISSN
- 0896-6273 (ISSN-L)
- 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
- 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 › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Health Sciences › Medicine › Clinical Neurology › Deep Brain Stimulation and Movement Disorders
- 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
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