Cited by 203Parkinson's Disease Mechanisms and TreatmentsNuclear Receptors and SignalingUbiquitin and proteasome pathways

The DOI matches its Crossref record; 94 of the 96 references it cites were found in a registry or an index.

Proteolytic stress: A unifying concept for the etiopathogenesis of Parkinson’s disease

McNaught, Kevin St. P., Olanow, C. Warren·2003·Annals of Neurology

DOI 10.1002/ana.10512

Open this paper in CoChat — free account

Abstract

The etiopathogenesis of Parkinson's disease (PD) has been elusive. Recently, several lines of evidence have converged to suggest that defects in the ubiquitin-proteasome system and proteolytic stress underlie nigral pathology in both familial and sporadic forms of the illness. In support of this concept, mutations in alpha-synuclein that cause the protein to misfold and resist proteasomal degradation cause familial PD. Similarly, mutations in two enzymes involved in the normal function of the ubiquitin-proteasome system, parkin and ubiquitin C-terminal hydrolase L1, are also associated with hereditary PD. Furthermore, structural and function defects in 26/20S proteasomes with accumulation and aggregation of potentially cytotoxic abnormal proteins have been identified in the substantia nigra pars compacta of patients with sporadic PD. Thus, a defect in protein handling appears to be a common factor in sporadic and the various familial forms of PD. This hypothesis may also account for the vulnerability of the substantia nigra pars compacta in PD, why the disorder is age related, and the nature of the Lewy body. It has also facilitated the development of experimental models that recapitulate the behavioral and pathological features of PD, and hopefully will lead to the development of novel neuroprotective therapies for the disorder.

Integrity signals

Registry

Crossref · 10.1002/ana.10512

Cites

94 of 94 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

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
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
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
Mechanisms Underlying Ubiquitination
Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184
α-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies
Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., & Goedert, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6469 · Cited by 2,868
Impairment of the Ubiquitin-Proteasome System by Protein Aggregation
Bence, N., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,209
A Drosophila model of Parkinson's disease
Feany, M. Β., & Bender, W. W. (2000) · Nature · doi:10.1038/35006074 · Cited by 2,156
Aggresomes: A Cellular Response to Misfolded Proteins
Johnston, J. A., Ward, C. L., & Kopito, R. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.7.1883 · Cited by 2,148
Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024
Aggresomes, inclusion bodies and protein aggregation
Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,942
Dopaminergic Loss and Inclusion Body Formation in α-Synuclein Mice: Implications for Neurodegenerative Disorders
Masliah, E., Rockenstein, E. M., Veinbergs, I., Mallory, M. E., Hashimoto, M., Takeda, A., Sagara, Y., Sisk, A., & Mucke, L. (2000) · Science · doi:10.1126/science.287.5456.1265 · Cited by 1,779
Mice Lacking α-Synuclein Display Functional Deficits in the Nigrostriatal Dopamine System
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., et al. (2000) · Neuron · doi:10.1016/s0896-6273(00)80886-7 · Cited by 1,722
The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis
Voges, D., Zwickl, P., & Baumeister, W. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.1015 · Cited by 1,608
The ubiquitin pathway in Parkinson's disease
Leroy, E., Boyer, R., Auburger, G. W. J., Leube, B., Ulm, G., Mezey, É., Harta, G., Brownstein, M., Jonnalagada, S., Chernova, T., et al. (1998) · Nature · doi:10.1038/26652 · Cited by 1,599
Oxidative Damage Linked to Neurodegeneration by Selective α-Synuclein Nitration in Synucleinopathy Lesions
Giasson, B. I., Duda, J. E., Murray, I. V. J., Chen, Q., Souza, J. M., Hurtig, H. I., Ischiropoulos, H., Trojanowski, J. Q., & Lee, V. M. ‐. (2000) · Science · doi:10.1126/science.290.5493.985 · Cited by 1,567
Neuropathology of Parkinson's Disease
Forno, L. (1996) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199603000-00001 · Cited by 1,556
Alpha-synuclein and neurodegenerative diseases
Goedert, M. (2001) · Nature reviews. Neuroscience · doi:10.1038/35081564 · Cited by 1,428
ETIOLOGY AND PATHOGENESIS OF PARKINSON'S DISEASE
Olanow, C. W., & Tatton, W. G. (1999) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.22.1.123 · Cited by 1,409
Self-citation
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
Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease
Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227
Kinetic Stabilization of the α-Synuclein Protofibril by a Dopamine-α-Synuclein Adduct
Conway, K. A., Rochet, J.-C., Bieganski, R. M., & Lansbury, P. T. (2001) · Science · doi:10.1126/science.1063522 · Cited by 1,127
Ubiquitination of a new form of α-synuclein by parkin from human brain: implications for Parkinson's disease
Shimura, H., Schlossmacher, M. G., Hattori, N., Frosch, M. P., Trockenbacher, A., Schneider, R., Mizuno, Y., Kosik, K. S., & Selkoe, D. J. (2001) · Science · doi:10.1126/science.1060627 · Cited by 1,053
An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of parkin
Imai, Y., Soda, M., Inoue, H., Hattori, N., Mizuno, Y., & Takahashi, R. (2001) · Cell · doi:10.1016/s0092-8674(01)00407-x · Cited by 1,050
Cellular Defenses against Unfolded Proteins
Sherman, M. Y., & Goldberg, A. L. (2001) · Neuron · doi:10.1016/s0896-6273(01)00177-5 · Cited by 996
Parkin functions as an E2-dependent ubiquitin– protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
Zhang, Y., Gao, J., Chung, K. K. K., Huang, H., Dawson, V. L., & Dawson, T. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.240347797 · Cited by 982
Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease.
Yoritaka, A., Hattori, N., Uchida, K., Tanaka, M., Stadtman, E. R., & Mizuno, Y. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.2696 · Cited by 981
Degradation of oxidized proteins by the 20S proteasome
Davies, K. J. A. (2001) · Biochimie · doi:10.1016/s0300-9084(01)01250-0 · Cited by 849
Dopamine-dependent neurotoxicity of α-synuclein: A mechanism for selective neurodegeneration in Parkinson disease
Xu, J., Kao, S., Lee, F. J. S., Song, W., Jin, L., & Yankner, B. A. (2002) · Nature Medicine · doi:10.1038/nm0602-600 · Cited by 768
Parkin ubiquitinates the α-synuclein–interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease
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
Clinical and pathological features of a parkinsonian syndrome in a family with an Ala53Thr α‐synuclein mutation
Spira, P. J., Sharpe, D. M., Halliday, G. M., Cavanagh, J., & Nicholson, G. A. (2001) · Annals of Neurology · doi:10.1002/ana.67 · Cited by 691
Understanding cell death in parkinson's disease
Jenner, P., & Olanow, C. W. (1998) · Annals of Neurology · doi:10.1002/ana.410440712 · Cited by 686
Self-citation
Anatomic and Disease Specificity of NADH CoQ1 Reductase (Complex I) Deficiency in Parkinson's Disease
Schapira, A. H. V., Mann, V. M., Cooper, J. A. D., Dexter, D. T., Daniel, S. E., Jenner, P. G., Clark, J. B., & MARSDEN, C. D. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb05809.x · Cited by 673
Proteasomal function is impaired in substantia nigra in Parkinson’s disease
McNaught, K. S. P., & Jenner, P. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01701-8 · Cited by 653
Self-citation
Parkinson-Like Neurodegeneration Induced by Targeted Overexpression of α-Synuclein in the Nigrostriatal System
Kirik, D., Rosenblad, C., Burger, C., Lundberg, C., Johansen, T. E., Muzyczka, N., Mandel, R. J., & Björklund, A. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-07-02780.2002 · Cited by 649
Accumulation of Mutant Huntingtin Fragments in Aggresome-like Inclusion Bodies as a Result of Insufficient Protein Degradation
Waelter, S., Boeddrich, A., Lurz, R., Scherzinger, E., Lüder, G., Lehrach, H., & Wanker, E. E. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.5.1393 · Cited by 637
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
Expression of A53T Mutant But Not Wild-Type α-Synuclein in PC12 Cells Induces Alterations of the Ubiquitin-Dependent Degradation System, Loss of Dopamine Release, and Autophagic Cell Death
Stefanis, L., Larsen, K. E., Rideout, H. J., Sulzer, D., & Greene, L. A. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-24-09549.2001 · Cited by 584
Altered proteasomal function in sporadic Parkinson’s disease
St. P. McNaught, K., Belizaire, R., Isacson, O., Jenner, P., & Olanow, C. W. (2003) · Experimental Neurology · doi:10.1006/exnr.2002.8050 · Cited by 573
Self-citation
A Generalised Increase in Protein Carbonyls in the Brain in Parkinson's but Not Incidental Lewy Body Disease
Alam, Z. I., Daniel, S. E., Lees, A. J., Marsden, D. C., Jenner, P. G., & Halliwell, B. B. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69031326.x · Cited by 547
Protein Nitration in Parkinsonʼs Disease
Good, P. F., Hsu, A., Werner, P., Perl, D. P., & Olanow, C. W. (1998) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199804000-00006 · Cited by 540
Self-citation
Failure of the ubiquitin-proteasome system in Parkinson’s disease
McNaught, K. S. P., Olanow, C. W., Halliwell, B., Isacson, O., & Jenner, P. (2001) · Nature Reviews Neuroscience · doi:10.1038/35086067 · Cited by 519
Self-citation
Dynamic Association of Proteasomal Machinery with the Centrosome
Wigley, W. C., Fabunmi, R. P., Lee, M. G., Marino, C. R., Muallem, S., Demartino, G., & Thomas, P. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.3.481 · Cited by 513
Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice.
Cummings, C., Reinstein, E., Sun, Y., Antalffy, B. A., Jiang, Y.-H., Ciechanover, A., Orr, H., Beaudet, A., & Zoghbi, H. (1999) · Neuron · doi:10.1016/s0896-6273(00)81035-1 · Cited by 513
Ester Bond-containing Tea Polyphenols Potently Inhibit Proteasome Activity in Vitro and in Vivo
Nam, S., Smith, D. M., & Dou, Q. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m004209200 · Cited by 509
Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis
Tanaka, Y. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.9.919 · Cited by 504
Intragenic deletion in the gene encoding ubiquitin carboxy-terminal hydrolase in gad mice
Saigoh, K., Wang, Y., Suh, J., Yamanishi, T., Sakai, Y., Kiyosawa, H., Harada, T., Ichihara, N., Wakana, S., Kikuchi, T., et al. (1999) · Nature Genetics · doi:10.1038/12647 · Cited by 501
Lewy bodies and parkinsonism in families with parkin mutations
Farrer, M. J., Chan, P., Chen, R., Tan, L. C. S., Lincoln, S., Hernandez, D. G., Forno, L. S., Gwinn, K. A., Petrucelli, L., Hussey, J., et al. (2001) · Annals of Neurology · doi:10.1002/ana.1132 · Cited by 483
A large kindred with autosomal dominant Parkinson's disease
Golbe, L., Iorio, G. D., Bonavita, V., Miller, D. C., & Duvoisin, R. (1990) · Annals of Neurology · doi:10.1002/ana.410270309 · Cited by 463
Increased Protein Oxidation in Human Substantia Nigra Pars Compacta in Comparison with Basal Ganglia and Prefrontal Cortex Measured with an Improved Dinitrophenylhydrazine Assay
Floor, E., & Wetzel, M. G. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70010268.x · Cited by 452
Induction of α-Synuclein Aggregation by Intracellular Nitrative Insult
Paxinou, E., Chen, Q., Weisse, M., Giasson, B. I., Norris, E. H., Rueter, S. M., Trojanowski, J. Q., Lee, V. M. ‐., & Ischiropoulos, H. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-20-08053.2001 · Cited by 440
Degradation of α-Synuclein by Proteasome
Bennett, M. C., Bishop, J. F., Leng, Y., Chock, P. B., Chase, T. N., & Mouradian, M. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.33855 · Cited by 417
Pathology and Biology of the Lewy Body
Pollanen, M. S., Dickson, D. W., & Bergeron, C. (1993) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199305000-00001 · Cited by 396
Pathologic and biochemical studies of juvenile parkinsonism linked to chromosome 6q
Mori, H., Kondo, T., Yokochi, M., Matsumine, H., Nakagawa-Hattori, Y., Miyake, T., Suda, K., & Mizuno, Y. (1998) · Neurology · doi:10.1212/wnl.51.3.890 · Cited by 370
α‐Synuclein metabolism and aggregation is linked to ubiquitin‐independent degradation by the proteasome
Tofaris, G. K., Layfield, R., & Spillantini, M. G. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03115-5 · Cited by 363
Ubiquitin carboxyl‐terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases
Lowe, J. S., McDermott, H., Landon, M., Mayer, R. J., & Wilkinson, K. D. (1990) · The Journal of Pathology · doi:10.1002/path.1711610210 · Cited by 359
Oxidative Modification and Inactivation of the Proteasome during Coronary Occlusion/Reperfusion
Bulteau, A., Lundberg, K. C., Humphries, K. M., Sadek, H. A., Szweda, P. A., Friguet, B., & Szweda, L. I. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100142200 · Cited by 354
Clinical and pathological features of a Parkinsonian syndrome in a family with an Ala53Thr alpha-synuclein mutation.
Spira, P. J., Sharpe, D. M., Halliday, G. M., Cavanagh, J., & Nicholson, G. A. (2001) · PubMed · Cited by 343
Degradation of Oxidized Proteins in K562 Human Hematopoietic Cells by Proteasome
Grune, T., Reinheckel, T., & Davies, K. J. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.26.15504 · Cited by 328
Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation
Ma, J., & Lindquist, S. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.011578098 · Cited by 295
Proteasomal inhibition leads to formation of ubiquitin/α‐synuclein‐immunoreactive inclusions in PC12 cells
Rideout, H. J., Larsen, K. E., Sulzer, D., & Stefanis, L. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00474.x · Cited by 283
Lack of Nigral Pathology in Transgenic Mice Expressing Human α-Synuclein Driven by the Tyrosine Hydroxylase Promoter
Matsuoka, Y., Vila, M., Lincoln, S., McCormack, A., Picciano, M., LaFrancois, J., Yu, X., Dickson, D., Langston, W. J., McGowan, E., et al. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0392 · Cited by 281
Increased susceptibility to sporadic Parkinson's disease by a certain combined ?-synuclein/apolipoprotein E genotype
Krüger, R., Vieira-Saecker, A. M. M., Kuhn, W., Berg, D., M�ller, T., K�hnl, N., Fuchs, G., Storch, A., Hungs, M., Woitalla, D., et al. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199905)45:5 · Cited by 281
Aggresome‐related biogenesis of Lewy bodies
McNaught, K. S. P., Shashidharan, P., Perl, D. P., Jenner, P. G., & Olanow, C. W. (2002) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2002.02301.x · Cited by 279
Self-citation
Proteasome inhibition causes nigral degeneration with inclusion bodies in rats
McNaught, K. S. P., rklund, L. M. B., Belizaire, R., Ole Isacson, A., Jenner, P. G., & Olanow, C. W. (2002) · Neuroreport · doi:10.1097/00001756-200208070-00018 · Cited by 276
Self-citation
Concurrence of α-synuclein and tau brain pathology in the Contursi kindred
Duda, J. E., Giasson, B. I., Mabon, M. E., Miller, D. C., Golbe, L. I., Lee, V. M. ‐., & Trojanowski, J. Q. (2002) · Acta Neuropathologica · doi:10.1007/s00401-002-0563-3 · Cited by 274
Synphilin-1 is present in Lewy bodies in Parkinson's disease
Wakabayashi, K., Engelender, S., Yoshimoto, M., Tsuji, S., Ross, C. A., & Takahashi, H. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200004)47:4 · Cited by 269
α-Synuclein–enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons
McLean, P. J., Kawamata, H., & Hyman, B. T. (2001) · Neuroscience · doi:10.1016/s0306-4522(01)00113-0 · Cited by 235
Effect of the overexpression of wild‐type or mutant α‐synuclein on cell susceptibility to insult
Lee, M., Hyun, D., Halliwell, B. B., & Jenner, P. G. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00149.x · Cited by 233
Chaperone‐like activity of synucleins
Souza, J. M., Giasson, B. I., Lee, V. M. ‐., & Ischiropoulos, H. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01563-5 · Cited by 223
Immunocytochemical Co-localization of the Proteasome in Ubiquitinated Structures in Neurodegenerative Diseases and the Elderly
Ii, K., Ito, H., Tanaka, K., & Hirano, A. (1997) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199702000-00002 · Cited by 218
Dopaminergic Cell Loss Induced by Human A30P α -Synuclein Gene Transfer to the Rat Substantia Nigra
Klein, R. L., King, M. A., Hamby, M. E., & Meyer, E. M. (2002) · Human Gene Therapy · doi:10.1089/10430340252837206 · Cited by 212
Regulated trafficking of neurotransmitter transporters: common notes but different melodies
Robinson, M. B. (2001) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2001.00698.x · Cited by 204
Neuronal vulnerability in Parkinson’s disease
Hirsch, É. C., Faucheux, B. A., Damier, P., Prigent, A., & Agid, Y. (1997) · Journal of neural transmission. Supplementum · doi:10.1007/978-3-7091-6842-4_9 · Cited by 192
Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease
Hoffner, G., Kahlem, P., & Djian, P. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.5.941 · Cited by 182
Effect of Wild-type or Mutant Parkin on Oxidative Damage, Nitric Oxide, Antioxidant Defenses, and the Proteasome
Hyun, D.-H., Lee, M., Hattori, N., Kubo, S.-I., Mizuno, Y., Halliwell, B., & Jenner, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200666200 · Cited by 172
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
Mutation analysis and association studies of the UCHL1 gene in German Parkinsonʼs disease patients
Wintermeyer, P., Krüger, R., Kuhn, W., Müller, T. H., Woitalla, D., Berg, D., Becker, G., Leroy, E., Polymeropoulos, M. H., Berger, K., et al. (2000) · Neuroreport · doi:10.1097/00001756-200007140-00004 · Cited by 141
Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases
Wilkinson, K. D., Deshpande, S. S., & Larsen, C. N. (1992) · Biochemical Society Transactions · doi:10.1042/bst0200631 · Cited by 132
Genetics of Parkinson's disease
Gasser, T. (2001) · Journal of Neurology · doi:10.1007/s004150170066 · Cited by 124
Parkin and Parkinsonʼs disease
Mizuno, Y., Hattori, N., Mori, H., Suzuki, T., & Tanaka, K. (2001) · Current Opinion in Neurology · doi:10.1097/00019052-200108000-00008 · Cited by 123
THE PHYSIOLOGICAL RELATION OF PLANT CAROTINOIDS TO THE CAROTINOIDS OF THE COW, HORSE, SHEEP, GOAT, PIG, AND HEN
Palmer, L. S. (1916) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)86887-9 · Cited by 119
Genetics of Parkinson's disease.
Gasser, T. (2004) · Europe PMC (PubMed Central) · Cited by 111
TorsinA accumulation in Lewy bodies in sporadic Parkinson’s disease
Shashidharan, P., Good, P. F., Hsu, A., Perl, D. P., Brin, M. F., & Olanow, C. W. (2000) · Brain Research · doi:10.1016/s0006-8993(00)02702-5 · Cited by 105
Self-citation
Rat α‐Synuclein Interacts with Tat Binding Protein 1, a Component of the 26S Proteasomal Complex
Ghee, M., Fournier, A., & Mallet, J. J. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0752221.x · Cited by 95
Caretaker or undertaker? The role of the proteasome in aging
Gaczynska, M. E., Osmulski, P. A., & Ward, W. F. (2001) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(00)00246-3 · Cited by 83
Aggresome Formation in Liver Cells in Response to Different Toxic Mechanisms: Role of the Ubiquitin-Proteasome Pathway and the Frameshift Mutant of Ubiquitin
French, B. A., van Leeuwen, F. W., Riley, N. E., Yuan, Q. X., Bardag‐Gorce, F., Gaal, K. K., Lue, Y., Marceau, N., & French, S. W. (2001) · Experimental and Molecular Pathology · doi:10.1006/exmp.2001.2401 · Cited by 77
Association between a polymorphism of ubiquitin carboxy-terminal hydrolase L1 (UCH-L1) gene and sporadic Parkinson's disease
Zhang, J., Hattori, N., Leroy, E., Morris, H. R., Kubo, S., Kobayashi, T., Wood, N. W., Polymeropoulos, M. H., & Mizuno, Y. (2000) · Parkinsonism & Related Disorders · doi:10.1016/s1353-8020(00)00015-8 · Cited by 68
The expression of mRNAs for the proteasome complex is developmentally regulated in the rat mesencephalon
El‐Khodor, B. F., Kholodilov, N. G., Yarygina, O., & Burke, R. E. (2001) · Developmental Brain Research · doi:10.1016/s0165-3806(01)00181-x · Cited by 38
The parkin gene and its phenotype
Bonifati, V., Michele, G. D., L�cking, C. B., D�rr, A., Fabrizio, E., Ambrosio, G., Vanacore, N., Mari, M. D., Marconi, R., Capus, L., et al. (2001) · Neurological Sciences · doi:10.1007/s100720170042 · Cited by 35
Nuclear magnetic relaxation dispersion profiles of substantia nigra pars compacta in Parkinson’s disease patients are consistent with protein aggregation
Lopiano, L., Fasano, M., Giraudo, S., Digilio, G., Koenig, S. H., Torre, E., Bergamasco, B., & Aime, S. (2000) · Neurochemistry International · doi:10.1016/s0197-0186(00)00036-x · Cited by 30
Occurrence of glutamate receptor subunit 1–containing aggresome‐like structures during normal development of rat spinal cord interneurons
Serrando, M., Casanovas, A., & Esquerda, J. E. (2001) · The Journal of Comparative Neurology · doi:10.1002/cne.1419 · Cited by 16
Untitled work
Solano (2000) · doi:10.1002/1531-8249(200002)47:2 · Cited by 3
Untitled work
Mattson, M. (1999) · doi:10.1002/(sici)1097-4547(19991001)58:1

Flagged first, then by citations

2 of the 96 references couldn’t be matched to a known paper.

Research works printed but not linked: 1

Lee, 2001, J Biol Chem, 27, 27

Sorted by citations

Molecular Pathways of Neurodegeneration in Parkinson's Disease
Dawson, T. M., & Dawson, V. L. (2003) · Science · doi:10.1126/science.1087753 · Cited by 1,674
Epidemiology and etiology of Parkinson's disease: a review of the evidence
Wirdefeldt, K., Adami, H.-O., Cole, P., Trichopoulos, D., & Mandel, J. (2011) · European Journal of Epidemiology · doi:10.1007/s10654-011-9581-6 · Cited by 1,199
The Ubiquitin Proteasome System in Neurodegenerative Diseases
Ciechanover, A. J., & Brundin, P. (2003) · Neuron · doi:10.1016/s0896-6273(03)00606-8 · Cited by 1,000
Oxidative Stress and Neurotoxicity
Sayre, L. M., Perry, G. L., & Smith, M. A. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700210j · Cited by 884
Biology of Parkinson's disease: pathogenesis and pathophysiology of a multisystem neurodegenerative disorder
Alexander, G. E. (2004) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2004.6.3/galexander · Cited by 530

See all 203

Authors: McNaught, K. S. P., & Olanow, C. W.
Affiliations: Icahn School of Medicine at Mount Sinai (US)
Corresponding author: Olanow, C. Warren
ORCID: Olanow, C. Warren
Venue: Annals of Neurology
Publisher: Wiley
Published: 2003
Volume: 53
Issue: S3
Pages: S73-S86
ISSN: 0364-5134 (ISSN-L)
1531-8249
DOI: 10.1002/ana.10512
OpenAlex: W2135387829
Cited by: 203
References: 96
Citations by year: 2026: 2 · 2025: 1 · 2024: 3 · 2023: 2 · 2021: 2 · 2020: 7 · 2019: 1 · 2018: 5 · 2017: 3 · 2016: 3 · 2015: 5 · 2014: 5 · 2013: 3 · 2012: 6
FWCI: 3.60
Type: journal article
Language: en
Open access: closed
Licence: doi.wiley.com/10.1002/tdm_license_1.1 (tdm, 4626 d)
Locations: Annals of Neurology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01ns033772-09)
National Institute of Neurological Disorders and Stroke (NS 33772)
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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: Parkinson's disease, ubiquitin-proteasome system, alpha-synuclein, Parkin, UCHL1, substantia nigra pars compacta, Lewy bodies, familial Parkinson's disease, sporadic Parkinson's disease, protein aggregation, neuroprotection
MeSH terms: Cysteine Endopeptidases, Humans, Ligases, Multienzyme Complexes, Nerve Degeneration, Nerve Tissue Proteins, Parkinson Disease, Peptide Hydrolases, Substantia Nigra, Thiolester Hydrolases, Lewy Bodies, Point Mutation, Ubiquitin Thiolesterase, Ubiquitin-Protein Ligases, Proteasome Endopeptidase Complex, Synucleins, alpha-Synuclein

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

Proteolytic stress: A unifying concept for the etiopathogenesis of Parkinson’s disease

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks