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Lentiviral vector delivery of parkin prevents dopaminergic degeneration in an α-synuclein rat model of Parkinson's disease

Bianco, C. L., Schneider, B. L., Bauer, M., Sajadi, A., Brice, A., Iwatsubo, T., & Aebischer, P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405313101 · Cited by 322 · see citing works

α‐Synuclein and Parkinson's disease

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Parkin Binds to α/β Tubulin and Increases their Ubiquitination and Degradation

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RBR E3 ubiquitin ligases: new structures, new insights, new questions

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Lewy-body formation is an aggresome-related process: a hypothesis

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Molecular pathogenesis of Parkinson disease: insights from genetic studies

Gasser, T. (2009) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399409001148 · Cited by 289 · see citing works

Parkin Facilitates the Elimination of Expanded Polyglutamine Proteins and Leads to Preservation of Proteasome Function

Tsai, Y. C., Fishman, P. S., Thakor, N. V., & Oyler, G. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212235200 · Cited by 282 · see citing works

Aggresome‐related biogenesis of Lewy bodies

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DWA1 and DWA2, Two Arabidopsis DWD Protein Components of CUL4-Based E3 Ligases, Act Together as Negative Regulators in ABA Signal Transduction

Lee, J., Yoon, H., Terzaghi, W., Martínez, C., Dai, M., Li, J., Byun, M.-O., & Deng, X. W. (2010) · The Plant Cell · doi:10.1105/tpc.109.073783 · Cited by 269 · see citing works

Impaired dopamine storage resulting from alpha-synuclein mutations may contribute to the pathogenesis of Parkinson's disease

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-Synuclein Phosphorylation Enhances Eosinophilic Cytoplasmic Inclusion Formation in SH-SY5Y Cells

Smith, W. W. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0482-05.2005 · Cited by 264 · see citing works

Part II: α-synuclein and its molecular pathophysiological role in neurodegenerative disease

Dev, K. K. (2003) · Neuropharmacology · doi:10.1016/s0028-3908(03)00140-0 · Cited by 262 · see citing works

Parkin negatively regulates JNK pathway in the dopaminergic neurons of Drosophila

Cha, G., Kim, S., Park, J., Lee, E., Kim, M., Lee, S. B., Kim, J., Chung, J., & Cho, K. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500346102 · Cited by 261 · see citing works

The ubiquitin–proteasome pathway in Parkinson's disease and other neurodegenerative diseases

Ross, C. A., & Pickart, C. M. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.10.006 · Cited by 257 · see citing works

Accumulation of the Authentic Parkin Substrate Aminoacyl-tRNA Synthetase Cofactor, p38/JTV-1, Leads to Catecholaminergic Cell Death

Ko, H. S., von Coelln, R., Sriram, S. R., Kim, S. W., Chung, K. K. K., Pletniková, O., Troncoso, J. C., Johnson, B. L., Saffary, R., Goh, E. L. K., et al. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.2172-05.2005 · Cited by 247 · see citing works

Cooperation of molecular chaperones with the ubiquitin/proteasome system

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Ubiquitin–proteasome system and Parkinson's diseases

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Association of DJ-1 and parkin mediated by pathogenic DJ-1 mutations and oxidative stress

Moore, D. J., Zhang, L., Troncoso, J. C., Lee, M. K., Hattori, N., Mizuno, Y., Dawson, T. M., & Dawson, V. L. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddi007 · Cited by 245 · see citing works

Lewy body Parkinson's disease in a large pedigree with 77Parkin mutation carriers

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Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin‐like domain

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The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: linking protein biosynthesis and neurodegeneration

Corti, O. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg159 · Cited by 243 · see citing works

Parkin protects human dopaminergic neuroblastoma cells against dopamine-induced apoptosis

Jiang, H., Ren, Y., Zhao, J., & Feng, J. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh180 · Cited by 239 · see citing works

Rare genetic mutations shed light on the pathogenesis of Parkinson disease

Dawson, T. M., & Dawson, V. L. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17575 · Cited by 239 · see citing works

The Ubiquitin Proteasome System Acutely Regulates Presynaptic Protein Turnover and Synaptic Efficacy

Speese, S. D., Trotta, N., Rodesch, C. K., Aravamudan, B., & Broadie, K. S. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00338-5 · Cited by 236 · see citing works

Are ubiquitination pathways central to Parkinson’s disease?

Giasson, B. I., & Lee, V. M.-Y. (2003) · Cell · doi:10.1016/s0092-8674(03)00509-9 · Cited by 234 · see citing works

Neurodegenerative Diseases: Regenerative Mechanisms and Novel Therapeutic Approaches

Hussain, R., Zubair, H., Sarah, P., & Shahab, M. (2018) · Brain Sciences · doi:10.3390/brainsci8090177 · Cited by 233 · see citing works

The synucleins.

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The mitochondrial protein BNIP3L is the substrate of PARK2 and mediates mitophagy in PINK1/PARK2 pathway

Gao, F., Dong, C., Si, J., Hu, Q., Qin, Z., Fang, M., & Wang, G. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv017 · Cited by 230 · see citing works

Aggresome Formation and Neurodegenerative Diseases: Therapeutic Implications

Chin, L., Olzmann, J. A., & Li, L. (2008) · Current Medicinal Chemistry · doi:10.2174/092986708783330692 · Cited by 227 · see citing works

Emerging Roles for Ubiquitin and Protein Degradation in Neuronal Function

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The role of the ubiquitin-proteasomal pathway in Parkinson's disease and other neurodegenerative disorders

Chung, K. K. K., Dawson, V. L., & Dawson, T. M. (2001) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)01998-6 · Cited by 223 · see citing works

Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin–protein ligase with monoubiquitylation capacity

Hampe, C., Ardila-Osorio, H., Fournier, M., Brice, A., & Corti, O. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl131 · Cited by 222 · see citing works

Familial-associated mutations differentially disrupt the solubility, localization, binding and ubiquitination properties of parkin

Sriram, S. R., Li, X., Ko, H. S., Chung, K. K. K., Wong, E. S. P., Lim, K. L., Dawson, V. L., & Dawson, T. M. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi292 · Cited by 221 · see citing works

Amyloid‐fibril formation

Žerovnik, E. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03024.x · Cited by 218 · see citing works

The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI

Huynh, D. P. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg269 · Cited by 215 · see citing works

Novel regulation of parkin function through c-Abl-mediated tyrosine phosphorylation: implications for Parkinson’s disease

Imam, S. Z., Zhou, Q., Yamamoto, A., Valente, A. J., Ali, S. F., Bains, M., Roberts, J. L., Kahle, P. J., Clark, R. A., & Li, S. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.1833-10.2011 · Cited by 214 · see citing works

Narrative Review: Protein Degradation and Human Diseases: The Ubiquitin Connection

Reinstein, E., & Ciechanover, A. J. (2006) · Annals of Internal Medicine · doi:10.7326/0003-4819-145-9-200611070-00010 · Cited by 213 · see citing works

Parkin targets HIF-1α for ubiquitination and degradation to inhibit breast tumor progression

Liu, J., Zhang, C., Zhao, Y., Yue, X., Wu, H., HUANG, S. H., Chen, J., Tomsky, K., Xie, H., Khella, C. A., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01947-w · Cited by 213 · see citing works

Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease

Tang, B., Xiong, H., Sun, P., Zhang, Y., Wang, D., Hu, Z., Zhu, Z.-H., Ma, H., Pan, Q., Xia, J., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl104 · Cited by 213 · see citing works

Transcriptional repression of p53 by parkin and impairment by mutations associated with autosomal recessive juvenile Parkinson's disease

da Costa, C. A., Sunyach, C., Giaime, E., West, A. B., Corti, O., Brice, A., Safe, S. H., Abou‐Sleiman, P. M., Wood, N. W., Takahashi, H., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1981 · Cited by 211 · see citing works

Drosophila DJ-1 mutants show oxidative stress-sensitive locomotive dysfunction

Park, J., Kim, S. Y., Cha, G., Lee, S. B., Kim, S., & Chung, J. (2005) · Gene · doi:10.1016/j.gene.2005.06.040 · Cited by 211 · see citing works

The E3 Ligase Parkin Maintains Mitochondrial Integrity by Increasing Linear Ubiquitination of NEMO

Müller-Rischart, A. K., Pilsl, A., Beaudette, P., Patra, M., Hadian, K., Funke, M., Peis, R., Deinlein, A., Schweimer, C., Kuhn, P., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.036 · Cited by 210 · see citing works

Dorfin Ubiquitylates Mutant SOD1 and Prevents Mutant SOD1-mediated Neurotoxicity

Niwa, J.-I., Ishigaki, S., Hishikawa, N., Yamamoto, M., Doyu, M., Murata, S., Tanaka, K., Taniguchi, N., & Sobue, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206559200 · Cited by 209 · see citing works

α-Synuclein structure, posttranslational modification and alternative splicing as aggregation enhancers

Beyer, K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0104-6 · Cited by 208 · see citing works

Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function

Wang, C., Ko, H. S., Thomas, B., Tsang, F., Chew, K. C. M., Tay, S.-P., Ho, M. W. L., Lim, T. M., Soong, T. W., Pletniková, O., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi413 · Cited by 206 · see citing works

Common fragile sites, extremely large genes, neural development and cancer

Smith, D. I., Zhu, Y., McAvoy, S., & Kuhn, R. M. (2005) · Cancer Letters · doi:10.1016/j.canlet.2005.06.049 · Cited by 205 · see citing works

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

McNaught, K. S. P., & Olanow, C. W. (2003) · Annals of Neurology · doi:10.1002/ana.10512 · Cited by 203 · see citing works

Dieldrin-Induced Neurotoxicity: Relevance to Parkinson's Disease Pathogenesis

Kanthasamy, A. G., Kitazawa, M., Kanthasamy, A., & Anantharam, V. (2004) · NeuroToxicology · doi:10.1016/j.neuro.2004.07.010 · Cited by 201 · see citing works

BAG5 Inhibits Parkin and Enhances Dopaminergic Neuron Degeneration

Kalia, S. K., Lee, S., Smith, P. D., Liu, L., Crocker, S. J., Thorarinsdottir, T., Glover, J. R., Fon, E. A., Park, D. S., & Lozano, A. M. (2004) · Neuron · doi:10.1016/j.neuron.2004.11.026 · Cited by 201 · see citing works

Genetic and genomic studies of Drosophila parkin mutants implicate oxidative stress and innate immune responses in pathogenesis

Greene, J. C., Whitworth, A. J., Andrews, L. A., Parker, T. J., & Pallanck, L. J. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi074 · Cited by 194 · see citing works

Ubiquitylation of synphilin-1 and α-synuclein by SIAH and its presence in cellular inclusions and Lewy bodies imply a role in Parkinson's disease

Liani, E., Eyal, A., Avraham, E., Shemer, R., Szargel, R., Berg, D., Bornemann, A., Rieß, O., Ross, C. A., Rott, R., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401081101 · Cited by 192 · see citing works

Cell death: protein misfolding and neurodegenerative diseases

Nakamura, T., & Lipton, S. A. (2009) · APOPTOSIS · doi:10.1007/s10495-008-0301-y · Cited by 191 · see citing works

Targets for neuroprotection in Parkinson's disease

Yacoubian, T. A., & Standaert, D. G. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.09.009 · Cited by 189 · see citing works

Parkin genetics: one model for Parkinson's disease

Mata, I. F. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh089 · Cited by 186 · see citing works

Role of nitric oxide in Parkinson's disease

Zhang, L., Dawson, V. L., & Dawson, T. M. (2005) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.05.007 · Cited by 184 · see citing works

Parkin Mediates Nonclassical, Proteasomal-Independent Ubiquitination of Synphilin-1: Implications for Lewy Body Formation

Lim, K. L., Chew, K. C. M., Tan, J. M. M., Wang, C., Chung, K. K. K., Zhang, Y., Tanaka, Y., Smith, W. W., Engelender, S., Ross, C. A., et al. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4474-04.2005 · Cited by 543 · see citing works

Ubiquitylation of synphilin-1 and α-synuclein by SIAH and its presence in cellular inclusions and Lewy bodies imply a role in Parkinson's disease

Liani, E., Eyal, A., Avraham, E., Shemer, R., Szargel, R., Berg, D., Bornemann, A., Rieß, O., Ross, C. A., Rott, R., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401081101 · Cited by 192 · see citing works

Linking ubiquitin, parkin and synphilin-1

Ciechanover, A. J. (2001) · Nature Medicine · doi:10.1038/nm1001-1108 · Cited by 30 · see citing works

Parkin and defective ubiquitination in Parkinson’s disease

Dawson, T. M. (2006) · Springer eBooks · doi:10.1007/978-3-211-45295-0_32 · Cited by 74 · see citing works

Interaction between parkin and alpha‐synuclein

Shimura, H., Schlossmacher, M. G., Hattori, N., Mizuno, Y., Kosik, K. S., & Selkoe, D. J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.81.s1.49_4.x