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This dopamine deficiency gives rise to a spectrum of movement-related symptoms, including tremors, rigidity, and bradykinesia. While the precise etiology of Parkinson\u2019s disease remains elusive, genetic mutations, protein aggregation, inflammatory processes, and oxidative stress are believed to contribute to its development. In this context, fatty acid-binding proteins (FABPs) in the central nervous system, FABP3, FABP5, and FABP7, impact \u03b1-synuclein aggregation, neurotoxicity, and neuroinflammation. These FABPs accumulate in mitochondria during neurodegeneration, disrupting their membrane potential and homeostasis. In particular, FABP3, abundant in nigrostriatal dopaminergic neurons, is responsible for \u03b1-synuclein propagation into neurons and intracellular accumulation, affecting the loss of mesencephalic tyrosine hydroxylase protein, a rate-limiting enzyme of dopamine biosynthesis. This review summarizes the characteristics of FABP family proteins and delves into the pathogenic significance of FABPs in the pathogenesis of Parkinson\u2019s disease. Furthermore, it examines potential novel therapeutic targets and early diagnostic biomarkers for Parkinson\u2019s disease and related neurodegenerative disorders.<\/jats:p>","DOI":"10.3390\/ijms242317037","type":"journal-article","created":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T08:36:59Z","timestamp":1701419819000},"page":"17037","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["Pathogenic Impact of Fatty Acid-Binding Proteins in Parkinson\u2019s Disease\u2014Potential Biomarkers and Therapeutic Targets"],"prefix":"10.3390","volume":"24","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5916-7847","authenticated-orcid":false,"given":"Ichiro","family":"Kawahata","sequence":"first","affiliation":[{"name":"Department of CNS Drug Innovation, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai 980-8578, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8526-2824","authenticated-orcid":false,"given":"Kohji","family":"Fukunaga","sequence":"additional","affiliation":[{"name":"Department of CNS Drug Innovation, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai 980-8578, Japan"},{"name":"BRI Pharma Inc., Sendai 982-0804, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,12,1]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1074\/mcp.M300066-MCP200","article-title":"Fatty acid binding protein as a serum marker for the early diagnosis of stroke: A pilot study","volume":"3","author":"Burkhard","year":"2004","journal-title":"Mol. Cell. Proteom."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1159\/000105157","article-title":"Serum heart-type fatty acid-binding protein and cerebrospinal fluid tau: Marker candidates for dementia with Lewy bodies","volume":"4","author":"Mollenhauer","year":"2007","journal-title":"Neurodegener. Dis."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.jns.2007.08.018","article-title":"Serum heart-fatty acid binding protein levels in patients with Lewy body disease","volume":"266","author":"Imamura","year":"2008","journal-title":"J. Neurol. Sci."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1111\/j.1468-1331.2010.03273.x","article-title":"Brain-specific fatty acid-binding protein is elevated in serum of patients with dementia-related diseases","volume":"18","author":"Teunissen","year":"2011","journal-title":"Eur. J. Neurol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1097\/MCO.0000000000000600","article-title":"Fatty acid-binding proteins: Functional understanding and diagnostic implications","volume":"22","author":"Xu","year":"2019","journal-title":"Curr. Opin. Clin. Nutr. Metab. Care"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1126\/science.177.4043.56","article-title":"A binding protein for fatty acids in cytosol of intestinal mucosa, liver, myocardium, and other tissues","volume":"177","author":"Ockner","year":"1972","journal-title":"Science"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1079\/PNS19950035","article-title":"Fatty acid transport and fatty acid-binding proteins","volume":"54","author":"Veerkamp","year":"1995","journal-title":"Proc. Nutr. Soc."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/S0005-2760(97)00205-1","article-title":"Physiological properties and functions of intracellular fatty acid-binding proteins","volume":"1391","author":"Coe","year":"1998","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/S1388-1981(00)00046-9","article-title":"The fatty acid transport function of fatty acid-binding proteins","volume":"1486","author":"Storch","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1007\/BF03194597","article-title":"The multigene family of fatty acid-binding proteins (FABPs): Function, structure and polymorphism","volume":"47","year":"2006","journal-title":"J. Appl. Genet."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1186\/1479-7364-5-3-170","article-title":"The human fatty acid-binding protein family: Evolutionary divergences and functions","volume":"5","author":"Smathers","year":"2011","journal-title":"Hum. Genom."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1096","DOI":"10.1007\/s00018-002-8490-y","article-title":"New insights into the structure and function of fatty acid-binding proteins","volume":"59","author":"Zimmerman","year":"2002","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1016\/S1357-2725(01)00070-X","article-title":"Ligand specificity and conformational stability of human fatty acid-binding proteins","volume":"33","author":"Zimmerman","year":"2001","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1387\/ijdb.092976rl","article-title":"Fatty acid binding proteins in brain development and disease","volume":"54","author":"Liu","year":"2010","journal-title":"Int. J. Dev. Biol."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Xu, B., Chen, L., Zhan, Y., Marquez, K.N.S., Zhuo, L., Qi, S., Zhu, J., He, Y., Chen, X., and Zhang, H. (2022). The Biological Functions and Regulatory Mechanisms of Fatty Acid Binding Protein 5 in Various Diseases. Front. Cell Dev. Biol., 10.","DOI":"10.3389\/fcell.2022.857919"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1096\/fasebj.13.8.805","article-title":"Requirement for the heart-type fatty acid binding protein in cardiac fatty acid utilization","volume":"13","author":"Binas","year":"1999","journal-title":"FASEB J."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1161\/01.RES.85.4.329","article-title":"Impaired long-chain fatty acid utilization by cardiac myocytes isolated from mice lacking the heart-type fatty acid binding protein gene","volume":"85","author":"Schaap","year":"1999","journal-title":"Circ. Res."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/S0891-0618(96)00192-5","article-title":"Spatio-temporally differential expression of genes for three members of fatty acid binding proteins in developing and mature rat brains","volume":"12","author":"Owada","year":"1996","journal-title":"J. Chem. Neuroanat."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1620\/tjem.214.213","article-title":"Fatty acid binding protein: Localization and functional significance in the brain","volume":"214","author":"Owada","year":"2008","journal-title":"Tohoku J. Exp. Med."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1023\/A:1020502624234","article-title":"Insights into binding of fatty acids by fatty acid binding proteins","volume":"239","author":"Hanhoff","year":"2002","journal-title":"Mol. Cell. Biochem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"14941","DOI":"10.1074\/jbc.M113.514646","article-title":"Structural basis for ligand regulation of the fatty acid-binding protein 5, peroxisome proliferator-activated receptor beta\/delta (FABP5-PPARbeta\/delta) signaling pathway","volume":"289","author":"Armstrong","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"37005","DOI":"10.1074\/jbc.M110.170076","article-title":"Brain fatty acid-binding protein and omega-3\/omega-6 fatty acids: Mechanistic insight into malignant glioma cell migration","volume":"285","author":"Mita","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"41958","DOI":"10.1074\/jbc.M105022200","article-title":"Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins","volume":"276","author":"Perrin","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"9110","DOI":"10.1073\/pnas.171300598","article-title":"alpha-Synuclein occurs in lipid-rich high molecular weight complexes, binds fatty acids, and shows homology to the fatty acid-binding proteins","volume":"98","author":"Sharon","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1016\/S0896-6273(03)00024-2","article-title":"The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson\u2019s disease","volume":"37","author":"Sharon","year":"2003","journal-title":"Neuron"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1111\/j.1750-3639.2011.00530.x","article-title":"Alpha-synuclein neuropathology is controlled by nuclear hormone receptors and enhanced by docosahexaenoic acid in a mouse model for Parkinson\u2019s disease","volume":"22","author":"Yakunin","year":"2012","journal-title":"Brain Pathol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.jns.2009.09.021","article-title":"Dietary fat intake and risk of Parkinson\u2019s disease: A case-control study in Japan","volume":"288","author":"Miyake","year":"2010","journal-title":"J. Neurol. Sci."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1568","DOI":"10.1373\/clinchem.2003.030361","article-title":"Brain- and heart-type fatty acid-binding proteins in the brain: Tissue distribution and clinical utility","volume":"50","author":"Pelsers","year":"2004","journal-title":"Clin. Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"3943","DOI":"10.1002\/pmic.200400848","article-title":"Proteome analysis of human substantia nigra in Parkinson\u2019s disease","volume":"4","author":"Basso","year":"2004","journal-title":"Proteomics"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"648982","DOI":"10.3389\/fnagi.2021.648982","article-title":"Fatty Acid-Binding Protein 3 Expression in the Brain and Skin in Human Synucleinopathies","volume":"13","author":"Oizumi","year":"2021","journal-title":"Front. Aging Neurosci."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Kawahata, I., Sekimori, T., Oizumi, H., Takeda, A., and Fukunaga, K. (2023). Using Fatty Acid-Binding Proteins as Potential Biomarkers to Discriminate between Parkinson\u2019s Disease and Dementia with Lewy Bodies: Exploration of a Novel Technique. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241713267"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1001\/jamaneurol.2015.1449","article-title":"Cerebrospinal Fluid Patterns and the Risk of Future Dementia in Early, Incident Parkinson Disease","volume":"72","author":"Backstrom","year":"2015","journal-title":"JAMA Neurol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"7872","DOI":"10.1016\/S0021-9258(18)34463-6","article-title":"Fatty acid binding protein. Isolation from rat liver, characterization, and immunochemical quantification","volume":"257","author":"Ockner","year":"1982","journal-title":"J. Biol. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"3413","DOI":"10.1016\/S0021-9258(19)83637-2","article-title":"Human liver fatty acid binding protein. Isolation of a full length cDNA and comparative sequence analyses of orthologous and paralogous proteins","volume":"260","author":"Lowe","year":"1985","journal-title":"J. Biol. Chem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"5553","DOI":"10.1016\/S0021-9258(19)57250-7","article-title":"The nucleotide sequence of the rat liver fatty acid-binding protein gene. Evidence that exon 1 encodes an oligopeptide domain shared by a family of proteins which bind hydrophobic ligands","volume":"261","author":"Sweetser","year":"1986","journal-title":"J. Biol. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1073\/pnas.81.2.313","article-title":"Cloning of a cDNA encoding rat intestinal fatty acid binding protein","volume":"81","author":"Alpers","year":"1984","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"16060","DOI":"10.1016\/S0021-9258(18)47696-X","article-title":"The human and rodent intestinal fatty acid binding protein genes. A comparative analysis of their structure, expression, and linkage relationships","volume":"262","author":"Sweetser","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1089\/dna.1992.11.31","article-title":"The mouse intestinal fatty acid binding protein gene: Nucleotide sequence, pattern of developmental and regional expression, and proposed structure of its protein product","volume":"11","author":"Green","year":"1992","journal-title":"DNA Cell Biol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"8218","DOI":"10.1016\/S0021-9258(19)83898-X","article-title":"Rat heart fatty acid-binding protein is highly homologous to the murine adipocyte 422 protein and the P2 protein of peripheral nerve myelin","volume":"261","author":"Sacchettini","year":"1986","journal-title":"J. Biol. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"9709","DOI":"10.1016\/S0021-9258(18)47992-6","article-title":"Analysis of the tissue-specific expression, developmental regulation, and linkage relationships of a rodent gene encoding heart fatty acid binding protein","volume":"262","author":"Heuckeroth","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"2637","DOI":"10.1242\/dev.120.9.2637","article-title":"The expression pattern of a novel gene encoding brain-fatty acid binding protein correlates with neuronal and glial cell development","volume":"120","author":"Kurtz","year":"1994","journal-title":"Development"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0165-3806(95)00099-Y","article-title":"Developmental role of fatty acid-binding proteins in mouse brain","volume":"89","author":"Sellner","year":"1995","journal-title":"Brain Res. Dev. Brain Res."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1385\/JMN:16:2-3:133","article-title":"Fatty acid-binding proteins of nervous tissue","volume":"16","author":"Veerkamp","year":"2001","journal-title":"J. Mol. Neurosci."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"10083","DOI":"10.1016\/S0021-9258(17)44608-4","article-title":"Molecular cloning of mRNA from 3T3 adipocytes. Regulation of mRNA content for glycerophosphate dehydrogenase and other differentiation-dependent proteins during adipocyte development","volume":"258","author":"Spiegelman","year":"1983","journal-title":"J. Biol. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"5468","DOI":"10.1073\/pnas.81.17.5468","article-title":"Expression of specific mRNAs during adipose differentiation: Identification of an mRNA encoding a homologue of myelin P2 protein","volume":"81","author":"Bernlohr","year":"1984","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1449","DOI":"10.1016\/S0022-2275(20)41912-1","article-title":"Regulation of adipose cell differentiation. I. Fatty acids are inducers of the aP2 gene expression","volume":"32","author":"Amri","year":"1991","journal-title":"J. Lipid Res."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1007\/978-1-4757-2670-1_12","article-title":"Regulation of gene expression in adipose cells by polyunsaturated fatty acids","volume":"422","author":"Bernlohr","year":"1997","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1111\/1523-1747.ep12616641","article-title":"Molecular cloning and expression of a novel keratinocyte protein (psoriasis-associated fatty acid-binding protein [PA-FABP]) that is highly up-regulated in psoriatic skin and that shares similarity to fatty acid-binding proteins","volume":"99","author":"Madsen","year":"1992","journal-title":"J. Investig. Dermatol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"17362","DOI":"10.1016\/S0021-9258(19)85343-7","article-title":"Tumor-specific overexpression of a novel keratinocyte lipid-binding protein. Identification and characterization of a cloned sequence activated during multistage carcinogenesis in mouse skin","volume":"268","author":"Krieg","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/S0006-8993(99)02158-7","article-title":"In situ and immunocytochemical localization of E-FABP mRNA and protein during neuronal migration and differentiation in the rat brain","volume":"852","author":"Liu","year":"2000","journal-title":"Brain Res."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"4741","DOI":"10.1073\/pnas.91.11.4741","article-title":"Molecular cloning, tissue distribution, and expression of a 14-kDa bile acid-binding protein from rat ileal cytosol","volume":"91","author":"Gong","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1016\/0006-291X(91)90659-U","article-title":"Identification of the 14 kDa bile acid transport protein of rat ileal cytosol as gastrotropin","volume":"177","author":"Vodenlich","year":"1991","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"14189","DOI":"10.1016\/S0021-9258(18)68204-3","article-title":"The complete amino acid sequence of porcine gastrotropin, an ileal protein which stimulates gastric acid and pepsinogen secretion","volume":"263","author":"Walz","year":"1988","journal-title":"J. Biol. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"20248","DOI":"10.1016\/S0021-9258(19)47054-3","article-title":"Gastrotropin: Not an enterooxyntin but a member of a family of cytoplasmic hydrophobic ligand binding proteins","volume":"264","author":"Gantz","year":"1989","journal-title":"J. Biol. Chem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1016\/0896-6273(94)90341-7","article-title":"Brain lipid-binding protein (BLBP): A novel signaling system in the developing mammalian CNS","volume":"12","author":"Feng","year":"1994","journal-title":"Neuron"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/S0167-4781(97)00115-2","article-title":"Isolation and expression of a cDNA for human brain fatty acid-binding protein (B-FABP)","volume":"1354","author":"Shimizu","year":"1997","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1006\/dbio.1994.1310","article-title":"A novel testicular protein, with sequence similarities to a family of lipid binding proteins, is a major component of the rat sperm perinuclear theca","volume":"166","author":"Oko","year":"1994","journal-title":"Dev. Biol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1095\/biolreprod57.3.655","article-title":"Molecular cloning and structural analysis of the gene encoding PERF 15 protein present in the perinuclear theca of the rat spermatozoa","volume":"57","author":"Pouresmaeili","year":"1997","journal-title":"Biol. Reprod."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1016\/S1474-4422(06)70471-9","article-title":"Epidemiology of Parkinson\u2019s disease","volume":"5","author":"Breteler","year":"2006","journal-title":"Lancet Neurol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1159\/000445751","article-title":"The Incidence of Parkinson\u2019s Disease: A Systematic Review and Meta-Analysis","volume":"46","author":"Hirsch","year":"2016","journal-title":"Neuroepidemiology"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"728083","DOI":"10.3389\/fnins.2021.728083","article-title":"Comparative Efficacy and Safety of Dopamine Agonists in Advanced Parkinson\u2019s Disease With Motor Fluctuations: A Systematic Review and Network Meta-Analysis of Double-Blind Randomized Controlled Trials","volume":"15","author":"Ruan","year":"2021","journal-title":"Front. Neurosci."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1176\/jnp.14.2.223","article-title":"An essay on the shaking palsy. 1817","volume":"14","author":"Parkinson","year":"2002","journal-title":"J. Neuropsychiatry Clin. Neurosci."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1007\/s11940-023-00749-4","article-title":"Parkinson Disease Dementia Management: An Update of Current Evidence and Future Directions","volume":"25","author":"Phillips","year":"2023","journal-title":"Curr. Treat. Options Neurol."},{"key":"ref_64","first-page":"181","article-title":"Olfactory dysfunction and dementia in Parkinson\u2019s disease","volume":"4","author":"Takeda","year":"2014","journal-title":"J. Park. Dis."},{"key":"ref_65","first-page":"943","article-title":"How Useful is an Olfactory Test for Diagnosing Alzheimer\u2019s Syndrome?","volume":"75","author":"Takeda","year":"2023","journal-title":"Brain Nerve"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1016\/j.nbd.2016.12.013","article-title":"The olfactory bulb as the entry site for prion-like propagation in neurodegenerative diseases","volume":"109","author":"Rey","year":"2018","journal-title":"Neurobiol. Dis."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/42166","article-title":"Alpha-synuclein in Lewy bodies","volume":"388","author":"Spillantini","year":"1997","journal-title":"Nature"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"6469","DOI":"10.1073\/pnas.95.11.6469","article-title":"alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson\u2019s disease and dementia with lewy bodies","volume":"95","author":"Spillantini","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/S0304-3940(98)00504-7","article-title":"Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson\u2019s disease and dementia with Lewy bodies","volume":"251","author":"Spillantini","year":"1998","journal-title":"Neurosci. Lett."},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Shetty, A.S., Bhatia, K.P., and Lang, A.E. (2019). Dystonia and Parkinson\u2019s disease: What is the relationship?. Neurobiol. Dis., 132.","DOI":"10.1016\/j.nbd.2019.05.001"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1038\/nature03015","article-title":"Computational roles for dopamine in behavioural control","volume":"431","author":"Montague","year":"2004","journal-title":"Nature"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1146\/annurev.psych.56.091103.070229","article-title":"Behavioral theories and the neurophysiology of reward","volume":"57","author":"Schultz","year":"2006","journal-title":"Annu. Rev. Psychol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1124","DOI":"10.1111\/j.1460-9568.2012.07990.x","article-title":"From prediction error to incentive salience: Mesolimbic computation of reward motivation","volume":"35","author":"Berridge","year":"2012","journal-title":"Eur. J. Neurosci."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1093\/brain\/89.3.449","article-title":"The effects of lesions in the substantia nigra","volume":"89","author":"Stern","year":"1966","journal-title":"Brain"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1001\/archneurpsyc.1940.02280040091006","article-title":"Action Potentials of Muscles in Rigidity and Tremor","volume":"43","author":"Hoefer","year":"1940","journal-title":"Arch. Neurol. Psychiatry"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"388","DOI":"10.2183\/pjab.82.388","article-title":"The catecholamine system in health and disease -Relation to tyrosine 3-monooxygenase and other catecholamine-synthesizing enzymes","volume":"82","author":"Nagatsu","year":"2007","journal-title":"Proc. Jpn. Acad. Ser. B Phys. Biol. Sci."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1007\/s00702-016-1596-4","article-title":"Tyrosine hydroxylase (TH), its cofactor tetrahydrobiopterin (BH4), other catecholamine-related enzymes, and their human genes in relation to the drug and gene therapies of Parkinson\u2019s disease (PD): Historical overview and future prospects","volume":"123","author":"Nagatsu","year":"2016","journal-title":"J. Neural Transm."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Nagatsu, T. (2023). Catecholamines and Parkinson\u2019s disease: Tyrosine hydroxylase (TH) over tetrahydrobiopterin (BH4) and GTP cyclohydrolase I (GCH1) to cytokines, neuromelanin, and gene therapy: A historical overview. J. Neural Transm., ahead of print.","DOI":"10.1007\/s00702-023-02673-y"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"2910","DOI":"10.1016\/S0021-9258(18)93832-9","article-title":"Tyrosine Hydroxylase. The initial step in norepinephrine biosynthesis","volume":"239","author":"Nagatsu","year":"1964","journal-title":"J. Biol. Chem."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1007\/s10571-018-0632-3","article-title":"Dopamine: Functions, Signaling, and Association with Neurological Diseases","volume":"39","author":"Klein","year":"2019","journal-title":"Cell. Mol. Neurobiol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1007\/8904_2014_327","article-title":"Widening Phenotypic Spectrum of AADC Deficiency, a Disorder of Dopamine and Serotonin Synthesis","volume":"17","author":"Helman","year":"2014","journal-title":"JIMD Rep."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.ymgme.2015.04.008","article-title":"Aromatic L-amino acid decarboxylase deficiency diagnosed by clinical metabolomic profiling of plasma","volume":"115","author":"Atwal","year":"2015","journal-title":"Mol. Genet. Metab."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1038\/ng1194-236","article-title":"Hereditary progressive dystonia with marked diurnal fluctuation caused by mutations in the GTP cyclohydrolase I gene","volume":"8","author":"Ichinose","year":"1994","journal-title":"Nat. Genet."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1016\/B978-0-444-52014-2.00039-2","article-title":"Dopa-responsive dystonia","volume":"100","author":"Segawa","year":"2011","journal-title":"Handb. Clin. Neurol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"22358","DOI":"10.1016\/S0021-9258(18)45713-4","article-title":"Site-specific phosphorylation of tyrosine hydroxylase after KCl depolarization and nerve growth factor treatment of PC12 cells","volume":"265","author":"Mitchell","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"10489","DOI":"10.1016\/S0021-9258(18)67410-1","article-title":"Identification of four phosphorylation sites in the N-terminal region of tyrosine hydroxylase","volume":"261","author":"Campbell","year":"1986","journal-title":"J. Biol. Chem."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1111\/j.1471-4159.2004.02797.x","article-title":"Tyrosine hydroxylase phosphorylation: Regulation and consequences","volume":"91","author":"Dunkley","year":"2004","journal-title":"J. Neurochem."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.abb.2010.12.017","article-title":"Tyrosine hydroxylase and regulation of dopamine synthesis","volume":"508","author":"Daubner","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1023\/A:1014880403970","article-title":"Tyrosine hydroxylase dephosphorylation by protein phosphatase 2A in bovine adrenal chromaffin cells","volume":"27","author":"Leal","year":"2002","journal-title":"Neurochem. Res."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"30390","DOI":"10.1038\/srep30390","article-title":"Stable preparations of tyrosine hydroxylase provide the solution structure of the full-length enzyme","volume":"6","author":"Bezem","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1038\/s41467-021-27657-y","article-title":"Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation","volume":"13","author":"Flydal","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1093\/jb\/mvj073","article-title":"Molecular mechanism for pterin-mediated inactivation of tyrosine hydroxylase: Formation of insoluble aggregates of tyrosine hydroxylase","volume":"139","author":"Urano","year":"2006","journal-title":"J. Biochem."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"39488","DOI":"10.1038\/srep39488","article-title":"Tyrosine Hydroxylase Binding to Phospholipid Membranes Prompts Its Amyloid Aggregation and Compromises Bilayer Integrity","volume":"6","author":"Baumann","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/S0304-3940(02)00296-3","article-title":"Selective loss of 20S proteasome alpha-subunits in the substantia nigra pars compacta in Parkinson\u2019s disease","volume":"326","author":"McNaught","year":"2002","journal-title":"Neurosci. Lett."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/S0304-3940(00)01701-8","article-title":"Proteasomal function is impaired in substantia nigra in Parkinson\u2019s disease","volume":"297","author":"McNaught","year":"2001","journal-title":"Neurosci. Lett."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"20288","DOI":"10.1074\/jbc.M710560200","article-title":"alpha-Synuclein protofibrils inhibit 26 S proteasome-mediated protein degradation: Understanding the cytotoxicity of protein protofibrils in neurodegenerative disease pathogenesis","volume":"283","author":"Zhang","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1571","DOI":"10.1007\/s00702-009-0304-z","article-title":"Accumulation of phosphorylated tyrosine hydroxylase into insoluble protein aggregates by inhibition of an ubiquitin-proteasome system in PC12D cells","volume":"116","author":"Kawahata","year":"2009","journal-title":"J. Neural Transm."},{"key":"ref_98","first-page":"1","article-title":"Immunohistochemical analyses of the postmortem human brains from patients with Parkinson\u2019s disease with anti-tyrosine hydroxylase antibodies","volume":"23","author":"Kawahata","year":"2009","journal-title":"Biog. Amines"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.bbrc.2015.07.125","article-title":"Dopamine or biopterin deficiency potentiates phosphorylation at (40)Ser and ubiquitination of tyrosine hydroxylase to be degraded by the ubiquitin proteasome system","volume":"465","author":"Kawahata","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"1561","DOI":"10.1046\/j.1432-1033.2002.02808.x","article-title":"Ubiquitination of soluble and membrane-bound tyrosine hydroxylase and degradation of the soluble form","volume":"269","author":"Flatmark","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"ref_101","doi-asserted-by":"crossref","unstructured":"Kawahata, I., and Fukunaga, K. (2020). Degradation of Tyrosine Hydroxylase by the Ubiquitin-Proteasome System in the Pathogenesis of Parkinson\u2019s Disease and Dopa-Responsive Dystonia. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21113779"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.acthis.2009.07.007","article-title":"Phosphorylation of alpha-synuclein upregulates tyrosine hydroxylase activity in MN9D cells","volume":"113","author":"Wu","year":"2011","journal-title":"Acta Histochem."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"382","DOI":"10.3389\/fnins.2019.00382","article-title":"Differential Aggregation and Phosphorylation of Alpha Synuclein in Membrane Compartments Associated With Parkinson Disease","volume":"13","author":"Pereda","year":"2019","journal-title":"Front. Neurosci."},{"key":"ref_104","doi-asserted-by":"crossref","unstructured":"Kawahata, I., Bousset, L., Melki, R., and Fukunaga, K. (2019). Fatty Acid-Binding Protein 3 is Critical for alpha-Synuclein Uptake and MPP(+)-Induced Mitochondrial Dysfunction in Cultured Dopaminergic Neurons. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20215358"},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Kawahata, I., Sekimori, T., Wang, H., Wang, Y., Sasaoka, T., Bousset, L., Melki, R., Mizobata, T., Kawata, Y., and Fukunaga, K. (2021). Dopamine D2 Long Receptors Are Critical for Caveolae-Mediated alpha-Synuclein Uptake in Cultured Dopaminergic Neurons. Biomedicines, 9.","DOI":"10.3390\/biomedicines9010049"},{"key":"ref_106","doi-asserted-by":"crossref","unstructured":"Yabuki, Y., Matsuo, K., Kawahata, I., Fukui, N., Mizobata, T., Kawata, Y., Owada, Y., Shioda, N., and Fukunaga, K. (2020). Fatty Acid Binding Protein 3 Enhances the Spreading and Toxicity of alpha-Synuclein in Mouse Brain. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21062230"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"147383","DOI":"10.1016\/j.brainres.2021.147383","article-title":"Suppression of alpha-synuclein propagation after intrastriatal injection in FABP3 null mice","volume":"1760","author":"Matsuo","year":"2021","journal-title":"Brain Res."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"947785","DOI":"10.3389\/fphar.2022.947785","article-title":"Dopamine Receptors: Is It Possible to Become a Therapeutic Target for Depression?","volume":"13","author":"Zhao","year":"2022","journal-title":"Front. Pharmacol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1064","DOI":"10.1046\/j.1471-4159.2003.01763.x","article-title":"Differential subcellular localization of two dopamine D2 receptor isoforms in transfected NG108-15 cells","volume":"85","author":"Takeuchi","year":"2003","journal-title":"J. Neurochem."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"12554","DOI":"10.1074\/jbc.M112.443945","article-title":"Plasma membrane compartmentalization of D2 dopamine receptors","volume":"288","author":"Sharma","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1111\/j.1476-5381.2011.01787.x","article-title":"The N-terminal region of the dopamine D2 receptor, a rhodopsin-like GPCR, regulates correct integration into the plasma membrane and endocytic routes","volume":"166","author":"Cho","year":"2012","journal-title":"Br. J. Pharmacol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1126\/science.2867601","article-title":"Quantitative analysis of D2 dopamine receptor binding in the living human brain by PET","volume":"231","author":"Farde","year":"1986","journal-title":"Science"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.3389\/fphar.2020.01003","article-title":"Dopamine Receptor Subtypes, Physiology and Pharmacology: New Ligands and Concepts in Schizophrenia","volume":"11","author":"Martel","year":"2020","journal-title":"Front. Pharmacol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1260419","DOI":"10.1126\/science.1260419","article-title":"Proteomics. Tissue-based map of the human proteome","volume":"347","author":"Uhlen","year":"2015","journal-title":"Science"},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Fukui, N., Yamamoto, H., Miyabe, M., Aoyama, Y., Hongo, K., Mizobata, T., Kawahata, I., Yabuki, Y., Shinoda, Y., and Fukunaga, K. (2021). An alpha-synuclein decoy peptide prevents cytotoxic alpha-synuclein aggregation caused by fatty acid binding protein 3. J. Biol. Chem., 296.","DOI":"10.1016\/j.jbc.2021.100663"},{"key":"ref_116","first-page":"45","article-title":"Mitochondria and Parkinson\u2019s Disease: Clinical, Molecular, and Translational Aspects","volume":"11","author":"Borsche","year":"2021","journal-title":"J. Park. Dis."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1265","DOI":"10.1046\/j.1471-4159.2001.00183.x","article-title":"The parkinsonian toxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP): A technical review of its utility and safety","volume":"76","author":"Przedborski","year":"2001","journal-title":"J. Neurochem."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/0165-1781(79)90006-4","article-title":"Chronic Parkinsonism secondary to intravenous injection of meperidine analogues","volume":"1","author":"Davis","year":"1979","journal-title":"Psychiatry Res."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1126\/science.6823561","article-title":"Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis","volume":"219","author":"Langston","year":"1983","journal-title":"Science"},{"key":"ref_120","first-page":"11","article-title":"The actions of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine in animals as a model of Parkinson\u2019s disease","volume":"20","author":"Jenner","year":"1986","journal-title":"J. Neural Transm. Suppl."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/0304-3940(85)90580-4","article-title":"Dopaminergic toxicity of rotenone and the 1-methyl-4-phenylpyridinium ion after their stereotaxic administration to rats: Implication for the mechanism of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine toxicity","volume":"62","author":"Heikkila","year":"1985","journal-title":"Neurosci. Lett."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.neuro.2014.12.002","article-title":"An update on the rotenone models of Parkinson\u2019s disease: Their ability to reproduce the features of clinical disease and model gene-environment interactions","volume":"46","author":"Johnson","year":"2015","journal-title":"Neurotoxicology"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1021\/acs.chemrestox.0c00522","article-title":"Using Rotenone to Model Parkinson\u2019s Disease in Mice: A Review of the Role of Pharmacokinetics","volume":"34","author":"Innos","year":"2021","journal-title":"Chem. Res. Toxicol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"dmm049082","DOI":"10.1242\/dmm.049082","article-title":"The rat rotenone model reproduces the abnormal pattern of central catecholamine metabolism found in Parkinson\u2019s disease","volume":"15","author":"Landau","year":"2022","journal-title":"Dis. Model. Mech."},{"key":"ref_125","doi-asserted-by":"crossref","unstructured":"Haga, H., Yamada, R., Izumi, H., Shinoda, Y., Kawahata, I., Miyachi, H., and Fukunaga, K. (2020). Novel fatty acid-binding protein 3 ligand inhibits dopaminergic neuronal death and improves motor and cognitive impairments in Parkinson\u2019s disease model mice. Pharmacol. Biochem. Behav., 191.","DOI":"10.1016\/j.pbb.2020.172891"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.jphs.2023.02.008","article-title":"Novel FABP3 ligand, HY-11-9, ameliorates neuropathological deficits in MPTP-induced Parkinsonism in mice","volume":"152","author":"Wang","year":"2023","journal-title":"J. Pharmacol. Sci."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1186\/s13041-017-0340-9","article-title":"Oxidative stress and cellular pathologies in Parkinson\u2019s disease","volume":"10","author":"Puspita","year":"2017","journal-title":"Mol. Brain"},{"key":"ref_128","first-page":"461","article-title":"The role of oxidative stress in Parkinson\u2019s disease","volume":"3","author":"Dias","year":"2013","journal-title":"J. Park. Dis."},{"key":"ref_129","doi-asserted-by":"crossref","unstructured":"Wang, Y., Shinoda, Y., Cheng, A., Kawahata, I., and Fukunaga, K. (2021). Epidermal Fatty Acid-Binding Protein 5 (FABP5) Involvement in Alpha-Synuclein-Induced Mitochondrial Injury under Oxidative Stress. Biomedicines, 9.","DOI":"10.3390\/biomedicines9020110"},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Cheng, A., Kawahata, I., and Fukunaga, K. (2020). Fatty Acid Binding Protein 5 Mediates Cell Death by Psychosine Exposure through Mitochondrial Macropores Formation in Oligodendrocytes. Biomedicines, 8.","DOI":"10.3390\/biomedicines8120635"},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"Cheng, A., Jia, W., Kawahata, I., and Fukunaga, K. (2021). A novel fatty acid-binding protein 5 and 7 inhibitor ameliorates oligodendrocyte injury in multiple sclerosis mouse models. EBioMedicine, 72.","DOI":"10.1016\/j.ebiom.2021.103582"},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Guo, Q., Kawahata, I., Degawa, T., Ikeda-Matsuo, Y., Sun, M., Han, F., and Fukunaga, K. (2021). Fatty Acid-Binding Proteins Aggravate Cerebral Ischemia-Reperfusion Injury in Mice. Biomedicines, 9.","DOI":"10.3390\/biomedicines9050529"},{"key":"ref_133","doi-asserted-by":"crossref","unstructured":"Guo, Q., Kawahata, I., Cheng, A., Wang, H., Jia, W., Yoshino, H., and Fukunaga, K. (2023). Fatty acid-binding proteins 3 and 5 are involved in the initiation of mitochondrial damage in ischemic neurons. Redox Biol., 59.","DOI":"10.1016\/j.redox.2022.102547"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"1283","DOI":"10.1007\/s10571-020-01027-6","article-title":"Role of Microgliosis and NLRP3 Inflammasome in Parkinson\u2019s Disease Pathogenesis and Therapy","volume":"42","author":"Costa","year":"2022","journal-title":"Cell. Mol. Neurobiol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"666737","DOI":"10.3389\/fneur.2021.666737","article-title":"The Pathogenesis of Parkinson\u2019s Disease: A Complex Interplay Between Astrocytes, Microglia, and T Lymphocytes?","volume":"12","author":"McComish","year":"2021","journal-title":"Front. Neurol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1002\/hipo.20682","article-title":"Cellular localization of epidermal-type and brain-type fatty acid-binding proteins in adult hippocampus and their response to cerebral ischemia","volume":"20","author":"Ma","year":"2010","journal-title":"Hippocampus"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1002\/hipo.20732","article-title":"Expression of fatty acid-binding proteins in adult hippocampal neurogenic niche of postischemic monkeys","volume":"21","author":"Boneva","year":"2011","journal-title":"Hippocampus"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"1370","DOI":"10.1002\/cne.22282","article-title":"Regional heterogeneity in astrocyte responses following contusive spinal cord injury in mice","volume":"518","author":"White","year":"2010","journal-title":"J. Comp. Neurol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1002\/glia.20437","article-title":"Astrogliosis in EAE spinal cord: Derivation from radial glia, and relationships to oligodendroglia","volume":"55","author":"Bannerman","year":"2007","journal-title":"Glia"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1038\/s41401-021-00675-8","article-title":"Fatty acid-binding protein 7 triggers alpha-synuclein oligomerization in glial cells and oligodendrocytes associated with oxidative stress","volume":"43","author":"Cheng","year":"2022","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"3172","DOI":"10.1093\/brain\/awad137","article-title":"Epsin2, a novel target for multiple system atrophy therapy via alpha-synuclein\/FABP7 propagation","volume":"146","author":"Cheng","year":"2023","journal-title":"Brain"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1111\/cns.14120","article-title":"alpha-Synuclein decoy peptide protects mice against alpha-synuclein-induced memory loss","volume":"29","author":"Guo","year":"2023","journal-title":"CNS Neurosci. Ther."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Cheng, A., Jia, W., Finkelstein, D.I., Stefanova, N., Wang, H., Sasaki, T., Kawahata, I., and Fukunaga, K. (2023). Pharmacological inhibition of FABP7 by MF 6 counteracts cerebellum dysfunction in an experimental multiple system atrophy mouse model. Acta Pharmacol. Sin., ahead of print.","DOI":"10.1038\/s41401-023-01138-y"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/s10020-021-00279-2","article-title":"Novel targeted therapies for Parkinson\u2019s disease","volume":"27","author":"Ntetsika","year":"2021","journal-title":"Mol. Med."},{"key":"ref_145","doi-asserted-by":"crossref","unstructured":"Prasad, E.M., and Hung, S.Y. (2021). Current Therapies in Clinical Trials of Parkinson\u2019s Disease: A 2021 Update. Pharmaceuticals, 14.","DOI":"10.3390\/ph14080717"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/j.expneurol.2008.06.004","article-title":"Direct quantification of CSF alpha-synuclein by ELISA and first cross-sectional study in patients with neurodegeneration","volume":"213","author":"Mollenhauer","year":"2008","journal-title":"Exp. Neurol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1007\/s12035-021-02657-7","article-title":"Review of Metabolomics-Based Biomarker Research for Parkinson\u2019s Disease","volume":"59","author":"Li","year":"2022","journal-title":"Mol. Neurobiol."},{"key":"ref_148","unstructured":"Ma, Z.L., Wang, Z.L., Zhang, F.Y., Liu, H.X., Mao, L.H., and Yuan, L. (2023). Biomarkers of Parkinson\u2019s Disease: From Basic Research to Clinical Practice. Aging Dis., ahead of print."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"101771","DOI":"10.1016\/j.arr.2022.101771","article-title":"From protein biomarkers to proteomics in dementia with Lewy Bodies","volume":"83","author":"Tsamourgelis","year":"2023","journal-title":"Ageing Res. Rev."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1093\/brain\/awr321","article-title":"Severe olfactory dysfunction is a prodromal symptom of dementia associated with Parkinson\u2019s disease: A 3 year longitudinal study","volume":"135","author":"Baba","year":"2012","journal-title":"Brain"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.parkreldis.2017.02.017","article-title":"Olfactory dysfunction and dementia in newly diagnosed patients with Parkinson\u2019s disease","volume":"38","author":"Domellof","year":"2017","journal-title":"Park. Relat. Disord."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1007\/s12264-017-0170-x","article-title":"Olfactory Dysfunction as an Early Biomarker in Parkinson\u2019s Disease","volume":"33","author":"Fullard","year":"2017","journal-title":"Neurosci. Bull."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1186\/s13195-017-0276-4","article-title":"Differential role of CSF fatty acid binding protein 3, alpha-synuclein, and Alzheimer\u2019s disease core biomarkers in Lewy body disorders and Alzheimer\u2019s dementia","volume":"9","author":"Chiasserini","year":"2017","journal-title":"Alzheimers Res. Ther."},{"key":"ref_154","doi-asserted-by":"crossref","unstructured":"Jellinger, K.A., and Korczyn, A.D. (2018). Are dementia with Lewy bodies and Parkinson\u2019s disease dementia the same disease?. BMC Med., 16.","DOI":"10.1186\/s12916-018-1016-8"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"199","DOI":"10.2217\/fnl-2018-0003","article-title":"Role of FABP3 as biomarker in Alzheimer\u2019s disease and synucleinopathies","volume":"13","author":"Sepe","year":"2018","journal-title":"Future Neurol."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1055\/s-0039-1678579","article-title":"Parkinson\u2019s Disease Dementia and Lewy Body Disease","volume":"39","author":"Sezgin","year":"2019","journal-title":"Semin. Neurol."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1111\/jnc.14698","article-title":"Clinical and neuropathological differences between Parkinson\u2019s disease, Parkinson\u2019s disease dementia and dementia with Lewy bodies\u2014Current issues and future directions","volume":"150","author":"Walker","year":"2019","journal-title":"J. Neurochem."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1016\/S1474-4422(19)30024-9","article-title":"CSF and blood biomarkers for Parkinson\u2019s disease","volume":"18","author":"Parnetti","year":"2019","journal-title":"Lancet Neurol."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"1192","DOI":"10.1158\/1078-0432.CCR-21-3114","article-title":"Circulating Immune Bioenergetic, Metabolic, and Genetic Signatures Predict Melanoma Patients\u2019 Response to Anti-PD-1 Immune Checkpoint Blockade","volume":"28","author":"Triozzi","year":"2022","journal-title":"Clin. Cancer Res."},{"key":"ref_160","doi-asserted-by":"crossref","unstructured":"Lu, Z., Priya Rajan, S.A., Song, Q., Zhao, Y., Wan, M., Aleman, J., Skardal, A., Bishop, C., Atala, A., and Lu, B. (2021). 3D scaffold-free microlivers with drug metabolic function generated by lineage-reprogrammed hepatocytes from human fibroblasts. Biomaterials, 269.","DOI":"10.1016\/j.biomaterials.2021.120668"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1592","DOI":"10.1038\/s41467-021-21669-4","article-title":"Metabolomics of sebum reveals lipid dysregulation in Parkinson\u2019s disease","volume":"12","author":"Sinclair","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_162","doi-asserted-by":"crossref","unstructured":"Oizumi, H., Sugimura, Y., Totsune, T., Kawasaki, I., Ohshiro, S., Baba, T., Kimpara, T., Sakuma, H., Hasegawa, T., and Kawahata, I. (2022). Plasma sphingolipid abnormalities in neurodegenerative diseases. 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