Are ubiquitination pathways central to Parkinson’s disease?

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Discovering Endophenotypes for Major Depression

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Back to the Future with Ubiquitin

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Drug discovery in the ubiquitin–proteasome system

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Parkinson-like syndrome induced by continuous MPTP infusion: Convergent roles of the ubiquitin-proteasome system and α-synuclein

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Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity

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Honey Bee Nest Thermoregulation: Diversity Promotes Stability

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Clearance of α-Synuclein Oligomeric Intermediates via the Lysosomal Degradation Pathway

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Chronic Exposure to Rotenone Models Sporadic Parkinson's Disease in Drosophila melanogaster

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Toward constructing an endophenotype strategy for bipolar disorders

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Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

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Neuroinflammation, oxidative stress, and the pathogenesis of Parkinson’s disease

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Small Molecule Inhibitors of α-Synuclein Filament Assembly

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Post-translational Modifications and Their Biological Functions: Proteomic Analysis and Systematic Approaches

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Drosophila DJ-1 Mutants Are Selectively Sensitive to Environmental Toxins Associated with Parkinson’s Disease

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Loss of locus coeruleus neurons and reduced startle in parkin null mice

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Intersecting pathways to neurodegeneration in Parkinson's disease: Effects of the pesticide rotenone on DJ-1, α-synuclein, and the ubiquitin–proteasome system

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Metabotropic glutamate receptors in the basal ganglia motor circuit

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Armet, a UPR-upregulated protein, inhibits cell proliferation and ER stress-induced cell death

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UCHL1 (PGP 9.5): Neuronal biomarker and ubiquitin system protein

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Familial Parkinson's Disease-associated L166P Mutation Disrupts DJ-1 Protein Folding and Function

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Caught in the Act

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Chemoenzymatic Semisynthesis of Proteins

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Propagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies

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Ubiquitin–proteasome system and Parkinson's diseases

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An integrated bioinformatics platform for investigating the human E3 ubiquitin ligase-substrate interaction network

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α-Synuclein: Normal Function and Role in Neurodegenerative Diseases

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BAG5 Inhibits Parkin and Enhances Dopaminergic Neuron Degeneration

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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

More than just two peas in a pod: common amyloidogenic properties of tau and α-synuclein in neurodegenerative diseases

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Increased expression of p62 in expanded polyglutamine‐expressing cells and its association with polyglutamine inclusions

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Diverse Effects of Pathogenic Mutations of Parkin That Catalyze Multiple Monoubiquitylation in Vitro

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UBIQUITIN-DEPENDENT REGULATION OF THE SYNAPSE

DiAntonio, A., & Hicke, L. (2004) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.27.070203.144317 · Cited by 175

Microglial Activation and Antioxidant Responses Induced by the Parkinson’s Disease Protein α-Synuclein

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MALDI Imaging of Formalin-Fixed Paraffin-Embedded Tissues: Application to Model Animals of Parkinson Disease for Biomarker Hunting

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Regulation of Akt signaling activation by ubiquitination

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Oxidation of the cysteine-rich regions of parkin perturbs its E3 ligase activity and contributes to protein aggregation

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Mitochondrial associated metabolic proteins are selectively oxidized in A30P α-synuclein transgenic mice—a model of familial Parkinson's disease

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Does α‐synuclein modulate dopaminergic synaptic content and tone at the synapse?

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Snaring the Function of α-Synuclein

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Signaling Through Monoubiquitination

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Sulphated tyrosines mediate association of chemokines and Plasmodium vivax Duffy binding protein with the Duffy antigen/receptor for chemokines (DARC)

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Ubiquitin-specific protease 4 (USP4) targets TRAF2 and TRAF6 for deubiquitination and inhibits TNFα-induced cancer cell migration

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Degradation of BACE by the ubiquitin‐proteasome pathway

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A Drosophila Model of Mutant Human Parkin-Induced Toxicity Demonstrates Selective Loss of Dopaminergic Neurons and Dependence on Cellular Dopamine

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Hsp70 Gene Transfer by Adeno-associated Virus Inhibits MPTP-Induced Nigrostriatal Degeneration in the Mouse Model of Parkinson Disease

Dong, Z., Wolfer, D. P., Lipp, H., & Büeler, H. (2004) · Molecular Therapy · doi:10.1016/j.ymthe.2004.09.007 · Cited by 148

Divergent Roles in Arabidopsis thaliana Development and Defense of Two Homologous Genes, ABERRANT GROWTH AND DEATH2 and AGD2-LIKE DEFENSE RESPONSE PROTEIN1, Encoding Novel Aminotransferases

Song, J. T., Lu, H., & Greenberg, J. T. (2004) · The Plant Cell · doi:10.1105/tpc.019372 · Cited by 146

What causes cell death in Parkinson's disease?

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Brain Injection of α-Synuclein Induces Multiple Proteinopathies, Gliosis, and a Neuronal Injury Marker

Sacino, A. N., Brooks, M., McKinney, A. B., Thomas, M. A., Shaw, G., Golde, T. E., & Giasson, B. I. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.2102-14.2014 · Cited by 141

Ashwagandha leaf extract: A potential agent in treating oxidative damage and physiological abnormalities seen in a mouse model of Parkinson's disease

Rajasankar, S., Manivasagam, T., & Surendran, S. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.02.044 · Cited by 140

Parkin-mediated Monoubiquitination of the PDZ Protein PICK1 Regulates the Activity of Acid-sensing Ion Channels

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Parkin-associated Parkinson’s disease

von Coelln, R., Dawson, V. L., & Dawson, T. M. (2004) · Cell and Tissue Research · doi:10.1007/s00441-004-0924-4 · Cited by 131

Rapid Ca 2+ -dependent decrease of protein ubiquitination at synapses

Chen, H., Polo, S., Fiore, P. P. D., & Camilli, P. V. D. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2136625100 · Cited by 121

Accumulation of NEDD8 in neuronal and glial inclusions of neurodegenerative disorders

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Ubiquitin, proteasome and parkin

Tanaka, K., Suzuki, T., Hattori, N., & Mizuno, Y. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.026 · Cited by 119

Phosphorylated and ubiquitinated TDP‐43 pathological inclusions in ALS and FTLD‐U are recapitulated in SH‐SY5Y cells

Nonaka, T., Arai, T., Buratti, E., Baralle, F. E., Akiyama, H., & Hasegawa, M. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.12.031 · Cited by 118

Metal-catalyzed Oxidation of α-Synuclein

Cole, N. B., Murphy, D. D., Lebowitz, J., Noto, L. D., Levine, R. L., & Nussbaum, R. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409946200 · Cited by 119

Parkin and relatives: the RBR family of ubiquitin ligases

Marı́n, I., Lucas‐Lledó, J. I., Gradilla, A., & Ferrús, A. (2004) · Physiological Genomics · doi:10.1152/physiolgenomics.00226.2003 · Cited by 124

A critical evaluation of the ubiquitin–proteasome system in Parkinson's disease

Cook, C. N., & Petrucelli, L. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.01.012 · Cited by 119

The Role of α‐Synuclein in Both Neuroprotection and Neurodegeneration

Sidhu, A., Wersinger, C., Moussa, C., & Vernier, P. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1332.016 · Cited by 110

Semisynthetic, Site-Specific Ubiquitin Modification of α-Synuclein Reveals Differential Effects on Aggregation

Meier, F., Abeywardana, T., Dhall, A., Marotta, N. P., Varkey, J., Langen, R., Chatterjee, C., & Pratt, M. R. (2012) · Journal of the American Chemical Society · doi:10.1021/ja300094r · Cited by 111

K63-Linked Ubiquitination in Kinase Activation and Cancer

Wang, G., Gao, Y., Li, L., Jin, G., Cai, Z., Chao, J. I., & Lin, H.-K. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00005 · Cited by 114

Interactions of Amyloidogenic Proteins

Giasson, B. I., Lee, V. M. ‐., & Trojanowski, J. Q. (2003) · NeuroMolecular Medicine · doi:10.1385/nmm:4:1-2:49 · Cited by 106

Potential Neuroprotective Activity of Ginseng in Parkinson’s Disease: A Review

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Characterization of Hydrophobic Residue Requirements for α-Synuclein Fibrillization

Waxman, E. A., Mazzulli, J. R., & Giasson, B. I. (2009) · Biochemistry · doi:10.1021/bi900539p · Cited by 110

The control of growth

Nijhout, H. F. (2003) · Development · doi:10.1242/dev.00902 · Cited by 103

Emerging role of Lys-63 ubiquitination in protein kinase and phosphatase activation and cancer development

Yang, W.-L., Zhang, X., & Lin, H.-K. (2010) · Oncogene · doi:10.1038/onc.2010.190 · Cited by 103

Neuroproteomics: Expression Profiling of the Brain's Proteomes in Health and Disease

Kim, S. I., Voshol, H., van Oostrum, J., Hastings, T. G., Cascio, M., & Glucksman, M. (2004) · Neurochemical Research · doi:10.1023/b:nere.0000023618.35579.7c · Cited by 104

Identification of post‐mortem cerebrospinal fluid proteins as potential biomarkers of ischemia and neurodegeneration

Lescuyer, P., Allard, L., Zimmermann‐Ivol, C. G., Burgess, J., Frutiger, S., Burkhard, P. R., Sanchez, J., & Hochstrasser, D. F. (2004) · PROTEOMICS · doi:10.1002/pmic.200300822 · Cited by 96

Drosophila DJ-1 mutants are sensitive to oxidative stress and show reduced lifespan and motor deficits

Lavara-Culebras, E., & Paricio, N. (2007) · Gene · doi:10.1016/j.gene.2007.06.013 · Cited by 92

Molecular chaperones and Parkinson's disease

Hu, S., Tan, J., Qin, L., Lv, L., Yan, W., Zhang, H., Tang, B., & Wang, C. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105527 · Cited by 90

Prolyl-isomerase Pin1 Accumulates in Lewy Bodies of Parkinson Disease and Facilitates Formation of α-Synuclein Inclusions

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S-Nitrosylation of parkin as a novel regulator of p53-mediated neuronal cell death in sporadic Parkinson’s disease

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Neurodegenerative models in Drosophila: Polyglutamine disorders, Parkinson disease, and amyotrophic lateral sclerosis

Ambegaokar, S. S., Roy, B., & Jackson, G. R. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.05.026 · Cited by 80

The Degeneration of Dopamine Neurons in Parkinson's Disease: Insights from Embryology and Evolution of the Mesostriatocortical System

Vernier, P., Moret, F., Callier, S., Snapyan, M., Wersinger, C., & Sidhu, A. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1332.015 · Cited by 82

Characterization of antibodies that selectively detect α-synuclein in pathological inclusions

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Changes in interfacial properties of α-synuclein preceding its aggregation

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Spatial transcriptomics reveals molecular dysfunction associated with cortical Lewy pathology

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Region-Specific Protein Abundance Changes in the Brain of MPTP-Induced Parkinson’s Disease Mouse Model

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Degradation of Tyrosine Hydroxylase by the Ubiquitin-Proteasome System in the Pathogenesis of Parkinson’s Disease and Dopa-Responsive Dystonia

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Pro‐apoptotic protein glyceraldehyde‐3‐phosphate dehydrogenase promotes the formation of Lewy body‐like inclusions

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G2019S LRRK2 mutation facilitates α-synuclein neuropathology in aged mice

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Genetic structure of nest aggregations and drone congregations of the southeast Asian stingless beeTrigona collina

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Genetic evidence for ubiquitin-specific proteasesUSP24andUSP40as candidate genes for late-onset Parkinson disease

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SUMO-1 marks subdomains within glial cytoplasmic inclusions of multiple system atrophy

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Intrapallidal lipopolysaccharide injection increases iron and ferritin levels in glia of the rat substantia nigra and induces locomotor deficits

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Late Domain-Dependent Inhibition of Equine Infectious Anemia Virus Budding

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Caspases‐2, ‐3, and ‐7 are involved in thapsigargin‐induced apoptosis of SH‐SY5Y neuroblastoma cells

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Role of the ubiquitin proteasome system in Parkinson's disease

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BMC Biochemistry BioMed Central Review Role of the ubiquitin proteasome system in Parkinson's disease

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Mechanism of Parkinson's disease resulted from ubiquitin-proteasome system dysfunction

Li, Y. (2009) · International Journal of Pathology and Clinical Medicine

Ubiquitin–proteasome system and Parkinson's diseases

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