Fatty Acid Binding Protein 3 Enhances the Spreading and Toxicity of α-Synuclein in Mouse Brain
Open accessAbstract
Oligomerization and/or aggregation of α-synuclein (α-Syn) triggers α-synucleinopathies such as Parkinson’s disease and dementia with Lewy bodies. It is known that α-Syn can spread in the brain like prions; however, the mechanism remains unclear. We demonstrated that fatty acid binding protein 3 (FABP3) promotes propagation of α-Syn in mouse brain. Animals were injected with mouse or human α-Syn pre-formed fibrils (PFF) into the bilateral substantia nigra pars compacta (SNpc). Two weeks after injection of mouse α-Syn PFF, wild-type (WT) mice exhibited motor and cognitive deficits, whereas FABP3 knock-out (Fabp3−/−) mice did not. The number of phosphorylated α-Syn (Ser-129)-positive cells was significantly decreased in Fabp3−/− mouse brain compared to that in WT mice. The SNpc was unilaterally infected with AAV-GFP/FABP3 in Fabp3−/− mice to confirm the involvement of FABP3 in the development of α-Syn PFF toxicity. The number of tyrosine hydroxylase (TH)- and phosphorylated α-Syn (Ser-129)-positive cells following α-Syn PFF injection significantly decreased in Fabp3−/− mice and markedly increased by AAV-GFP/FABP3 infection. Finally, we confirmed that the novel FABP3 inhibitor MF1 significantly antagonized motor and cognitive impairments by preventing α-Syn spreading following α-Syn PFF injection. Overall, FABP3 enhances α-Syn spreading in the brain following α-Syn PFF injection, and the FABP3 ligand MF1 represents an attractive therapeutic candidate for α-synucleinopathy.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
FABP3 is critical for α-synuclein uptake into dopaminergic neurons and enhances α-synuclein spreading.
“Very recently, we showed that fatty acid-binding protein 3 (FABP3) is critical for α-synuclein uptake into dopaminergic neurons [144] and enhancement of α-synuclein spreading [145].”
From Degradation of Tyrosine Hydroxylase by the Ubiquitin-Proteasome System in the Pathogenesis of Parkinson’s Disease and Dopa-Responsive Dystonia (2020) · cites this paper as [145]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
1 retracted
RETRACTED ARTICLE: LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation
Bae, E.-J., Kim, D.-K., Kim, C., Mante, M., Adame, A., Rockenstein, E., Ulusoy, A., Klinkenberg, M., Jeong, G. R., Bae, J. R., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05958-z · Cited by 149 · see citing works
RetractedStaging of brain pathology related to sporadic Parkinson’s disease
Braak, H., Tredici, K. D., Rüb, U., de Vos, R. A. I., Jansen Steur, E. N. H., & Braak, E. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00065-9 · Cited by 10,777 · see citing works
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382 · see citing works
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 · see citing works
α-Synuclein Locus Triplication Causes Parkinson's Disease
Singleton, A. B., Farrer, M., Johnson, J., Singleton, A., Hague, S., Kachergus, J., Hulihan, M., Peuralinna, T., Dutra, A., Nussbaum, R., et al. (2003) · Science · doi:10.1126/science.1090278 · Cited by 4,383 · see citing works
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 · see citing works
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 3,151 · see citing works
The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementia
Zarranz, J. J., Alegre, J., Gómez‐Esteban, J. C., Lezcano, E., Ros, R., Ampuero, I., Vidal, L., Hoenicka, J., Rodriguez, O., Atarés, B., et al. (2004) · Annals of Neurology · doi:10.1002/ana.10795 · Cited by 2,737 · see citing works
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563 · see citing works
α-Synuclein is phosphorylated in synucleinopathy lesions
Fujiwara, H., Hasegawa, M., Dohmae, N., Kawashima, A., Masliah, E., Goldberg, M., Shen, J., Takio, K., & Iwatsubo, T. (2002) · Nature Cell Biology · doi:10.1038/ncb748 · Cited by 1,906 · see citing works
Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845 · see citing works
Fatty acid-binding proteins: role in metabolic diseases and potential as drug targets
Furuhashi, M., & Hotamışlıgil, G. S. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2589 · Cited by 1,790 · see citing works
Lewy body–like pathology in long-term embryonic nigral transplants in Parkinson's disease
Kordower, J. H., Chu, Y., Hauser, R. A., Freeman, T. B., & Olanow, C. W. (2008) · Nature Medicine · doi:10.1038/nm1747 · Cited by 1,722 · see citing works
Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
Maroteaux, L., Campanelli, J., & Scheller, R. (1988) · Journal of Neuroscience · doi:10.1523/jneurosci.08-08-02804.1988 · Cited by 1,646 · see citing works
Conway, K. A., Harper, J. D., & Lansbury, P. T. (1998) · Nature Medicine · doi:10.1038/3311 · Cited by 1,501 · see citing works
Luk, K. C., Kehm, V. M., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M. ‐. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20112457 · Cited by 1,087 · see citing works
Causal relation between α-synuclein locus duplication as a cause of familial Parkinson's disease
Ibáñez, P., Bonnet, A. M., Débarges, B., Lohmann, E., Tison, F., Agid, Y., Dürr, A., Brice, A., & Pollak, P. (2004) · The Lancet · doi:10.1016/s0140-6736(04)17104-3 · Cited by 1,042 · see citing works
Prion-like spreading of pathological α-synuclein in brain
Masuda-Suzukake, M., Nonaka, T., Hosokawa, M., Oikawa, T., Arai, T., Akiyama, H., Mann, D. M. A., & Hasegawa, M. (2013) · Brain · doi:10.1093/brain/awt037 · Cited by 867 · see citing works
Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3
Mao, X., Ou, M. T., Karuppagounder, S. S., Kam, T., Yin, X., Xiong, Y., Ge, P., Umanah, G. K. E., Brahmachari, S., Shin, J., et al. (2016) · Science · doi:10.1126/science.aah3374 · Cited by 739 · see citing works
Volpicelli-Daley, L. A., Luk, K. C., & Lee, V. M.-Y. (2014) · Nature Protocols · doi:10.1038/nprot.2014.143 · Cited by 731 · see citing works
Sharon, R., Bar-Joseph, I., Frosch, M. P., Walsh, D. M., Hamilton, J. A., & Selkoe, D. J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00024-2 · Cited by 562 · see citing works
Tunneling nanotubes spread fibrillar α-synuclein by intercellular trafficking of lysosomes
Abounit, S., Bousset, L., Loria, F., Zhu, S., de Chaumont, F., Pieri, L., Olivo‐Marin, J., Melki, R., & Zurzolo, C. (2016) · The EMBO Journal · doi:10.15252/embj.201593411 · Cited by 414 · see citing works
Rey, N. L., Steiner, J. A., Maroof, N., Luk, K. C., Madaj, Z., Trojanowski, J. Q., Lee, V. M. ‐., & Brundin, P. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20160368 · Cited by 389 · see citing works
Alpha-synuclein biology in Lewy body diseases
Kim, W. S., Kågedal, K., & Halliday, G. M. (2014) · Alzheimer s Research & Therapy · doi:10.1186/s13195-014-0073-2 · Cited by 376 · see citing works
Oueslati, A. (2016) · Journal of Parkinson s Disease · doi:10.3233/jpd-160779 · Cited by 375 · see citing works
Physiological properties and functions of intracellular fatty acid-binding proteins
Coe, N. R., & Bernlohr, D. (1998) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/s0005-2760(97)00205-1 · Cited by 329 · see citing works
Sharon, R., Goldberg, M. S., Bar-Josef, I., Betensky, R. A., Shen, J., & Selkoe, D. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171300598 · Cited by 329 · see citing works
Sacino, A. N., Brooks, M., Thomas, M. A., McKinney, A. B., Lee, S., Regenhardt, R. W., McGarvey, N. H., Ayers, J. I., Notterpek, L. M., Borchelt, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321785111 · Cited by 328 · see citing works
Flagmeier, P., Meisl, G., Vendruscolo, M., Knowles, T. P. J., Dobson, C. M., Buell, A. K., & Galvagnion, C. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604645113 · Cited by 323 · see citing works
Exposure to Long Chain Polyunsaturated Fatty Acids Triggers Rapid Multimerization of Synucleins
Perrin, R. J., Woods, W. S., Clayton, D. F., & George, J. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105022200 · Cited by 280 · see citing works
The prion hypothesis in Parkinson's disease: braak to the future
Visanji, N. P., Brooks, P. L., Hazrati, L.-N., & Lang, A. E. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-2 · Cited by 278 · see citing works
Proteome analysis of human substantia nigra in Parkinson's disease
Basso, M., Giraudo, S., Corpillo, D., Bergamasco, B., Lopiano, L., & Fasano, M. (2004) · PROTEOMICS · doi:10.1002/pmic.200400848 · Cited by 271 · see citing works
Pathological alpha-synuclein propagates through neural networks
Masuda‐Suzukake, M., Nonaka, T., Hosokawa, M., Kubo, M., Shimozawa, A., Akiyama, H., & Hasegawa, M. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0088-8 · Cited by 249 · see citing works
Grassi, D., Howard, S., Zhou, M., Diaz-Perez, N., Urban, N. T., Guerrero-Given, D., Kamasawa, N., Volpicelli-Daley, L. A., LoGrasso, P., & Lasmézas, C. I. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1713849115 · Cited by 228 · see citing works
Owada, Y., Yoshimoto, T., & Kondo, H. (1996) · Journal of Chemical Neuroanatomy · doi:10.1016/s0891-0618(96)00192-5 · Cited by 218 · see citing works
Self-citationRey, N. L., George, S., Steiner, J. A., Madaj, Z., Luk, K. C., Trojanowski, J. Q., Lee, V. M.-Y., & Brundin, P. (2018) · Acta Neuropathologica · doi:10.1007/s00401-017-1792-9 · Cited by 215 · see citing works
Schaap, F. G., Binas, B., Danneberg, H., Vusse, G. J., & Glatz, J. F. C. (1999) · Circulation Research · doi:10.1161/01.res.85.4.329 · Cited by 208 · see citing works
Sharon, R., Bar-Joseph, I., Mirick, G. E., Serhan, C. N., & Selkoe, D. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309127200 · Cited by 187 · see citing works
Fasudil attenuates aggregation of α-synuclein in models of Parkinson’s disease
Tatenhorst, L., Eckermann, K., Dambeck, V., Fonseca-Ornelas, L., Walle, H., Lopes da Fonseca, T., Koch, J. C., Becker, S., Tönges, L., Bähr, M., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0310-y · Cited by 158 · see citing works
Increased Oxidative Stress Exacerbates α-Synuclein Aggregation In Vivo
Scudamore, O., & Ciossek, T. (2018) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nly024 · Cited by 158 · see citing works
Liu, R., Li, X., & Godbout, R. (2008) · Genomics · doi:10.1016/j.ygeno.2008.08.003 · Cited by 139 · see citing works
Dietary Intakes of Fat and Risk of Parkinson's Disease
Chen, H. (2003) · American Journal of Epidemiology · doi:10.1093/aje/kwg073 · Cited by 126 · see citing works
Fatty Acid Binding Protein: Localization and Functional Significance in the Brain
Owada, Y. (2008) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.214.213 · Cited by 122 · see citing works
Self-citationCavaliere, F., Cerf, L., Dehay, B., Ramos‐Gonzalez, P., Giorgi, F. D., Bourdenx, M., Bessede, A., Obeso, J. A., Matute, C., Ichas, F., et al. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.04.011 · Cited by 119 · see citing works
Nobiletin treatment improves motor and cognitive deficits seen in MPTP-induced Parkinson model mice
Yabuki, Y., Ohizumi, Y., Yokosuka, A., Mimaki, Y., & Fukunaga, K. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.11.051 · Cited by 118 · see citing works
Self-citationJulien, C., Berthiaume, L., Tahar, A. H., Rajput, A. H., Bédard, P. J., Paolo, T. D., Julien, P., & Calon, F. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2005.12.002 · Cited by 114 · see citing works
Amyloid Fibril Formation of α-Synuclein Is Accelerated by Preformed Amyloid Seeds of Other Proteins
Yagi, H., Kusaka, E., Hongo, K., Mizobata, T., & Kawata, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508623200 · Cited by 111 · see citing works
Self-citationNutrition and cognitive function
Gordon, N. S. (1997) · Brain and Development · doi:10.1016/s0387-7604(96)00560-8 · Cited by 109 · see citing works
Polyunsaturated Fatty Acids Induce α-Synuclein-Related Pathogenic Changes in Neuronal Cells
Assayag, K., Yakunin, E., Loeb, V., Selkoe, D. J., & Sharon, R. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070373 · Cited by 106 · see citing works
Heart-Type Fatty Acid Binding Protein Regulates Dopamine D2Receptor Function in Mouse Brain
Shioda, N., Yamamoto, Y., Watanabe, M., Binas, B., Owada, Y., & Fukunaga, K. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.4140-09.2010 · Cited by 101 · see citing works
Self-citationShioda, N., Yabuki, Y., Kobayashi, Y., Onozato, M., Owada, Y., & Fukunaga, K. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.527341 · Cited by 95 · see citing works
Self-citationImport and Export of Misfolded α-Synuclein
Rodriguez, L., Marano, M. M., & Tandon, A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00344 · Cited by 93 · see citing works
Mollenhauer, B., Steinacker, P., Bahn, E., Bibl, M., Brechlin, P., Schlossmacher, M. G., Locascio, J. J., Wiltfang, J., Kretzschmar, H. A., Poser, S., et al. (2007) · Neurodegenerative Diseases · doi:10.1159/000105157 · Cited by 81 · see citing works
Sakayori, N., Kikkawa, T., Tokuda, H., Kiryu, E., Yoshizaki, K., Kawashima, H., Yamada, T., Arai, H., Kang, J. X., Katagiri, H., et al. (2015) · Stem Cells · doi:10.1002/stem.2246 · Cited by 74 · see citing works
Lue, L., Walker, D. G., Adler, C., Shill, H. A., Tran, H., Akiyama, H., Sue, L., Caviness, J., Sabbagh, M. N., & Beach, T. G. (2012) · Brain Pathology · doi:10.1111/j.1750-3639.2012.00585.x · Cited by 65 · see citing works
Kawahata, I., Bousset, L., Melki, R., & Fukunaga, K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215358 · Cited by 56 · see citing works
Self-citationDevelopment of FABP3 ligands that inhibit arachidonic acid-induced α-synuclein oligomerization
Cheng, A., Shinoda, Y., Yamamoto, T., Miyachi, H., & Fukunaga, K. (2019) · Brain Research · doi:10.1016/j.brainres.2018.11.036 · Cited by 50 · see citing works
Self-citationPharmacological properties of SAK3, a novel T-type voltage-gated Ca2+ channel enhancer
Yabuki, Y., Matsuo, K., Izumi, H., Haga, H., Yoshida, T., Wakamori, M., Kakei, A., Sakimura, K., Fukuda, T., & Fukunaga, K. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.01.011 · Cited by 48 · see citing works
Self-citationMatsuo, K., Cheng, A., Yabuki, Y., Takahata, I., Miyachi, H., & Fukunaga, K. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.03.029 · Cited by 43 · see citing works
Self-citationSerum heart-fatty acid binding protein levels in patients with Lewy body disease
Wada‐Isoe, K., Imamura, K., Michio, K., Kowa, H., & Nakashima, K. (2007) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2007.08.018 · Cited by 42 · see citing works
Wang, R., Wang, Y., Qu, L., Chen, B., Jiang, H. F., Song, N., & Xie, J. (2019) · Neurochemistry International · doi:10.1016/j.neuint.2019.02.016 · Cited by 40 · see citing works
Beniyama, Y., Matsuno, K., & Miyachi, H. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.01.054 · Cited by 31 · see citing works
Yabuki, Y., Takahata, I., Matsuo, K., Owada, Y., & Fukunaga, K. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0587-2 · Cited by 31 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- [64]Paxinos G. Franklin K.B.J. The Mouse Brain in Stereotaxic Coordinates Academic Press San Diego, CA, USA 2001
Cited by
Sorted by citations
RNA G-quadruplexes form scaffolds that promote neuropathological α-synuclein aggregation
Matsuo, K., Asamitsu, S., Maeda, K., Suzuki, H., Kawakubo, K., Komiya, G., Kudo, K., Sakai, Y., Hori, K., Ikenoshita, S., et al. (2024) · Cell · doi:10.1016/j.cell.2024.09.037 · Cited by 82 · see citing works
Self-citationKawahata, I., & Fukunaga, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113779 · Cited by 71 · see citing works
Self-citationKawahata, I., Bousset, L., Melki, R., & Fukunaga, K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215358 · Cited by 56 · see citing works
Self-citationBrain regions susceptible to alpha-synuclein spreading
Guo, Y., Xiong, H., Chen, K., Zou, J.-J., & Lei, P. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01296-7 · Cited by 53 · see citing works
Kawahata, K., Sekimori, T., Wang, H., Wang, Y., Sasaoka, T., Bousset, L., Melki, R., Mizobata, T., Kawata, Y., & Fukunaga, K. (2021) · Biomedicines · doi:10.3390/biomedicines9010049 · Cited by 32 · see citing works
Self-citationFatty Acid-Binding Proteins: Their Roles in Ischemic Stroke and Potential as Drug Targets
Guo, Q., Kawahata, K., Cheng, A., Jia, W., Wang, H., & Fukunaga, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179648 · Cited by 27 · see citing works
Self-citationEndocytic pathways of pathogenic protein aggregates in neurodegenerative diseases
Hivare, P., Mujmer, K., Swarup, G., Gupta, S. K., & Bhatia, D. D. (2023) · Traffic · doi:10.1111/tra.12906 · Cited by 22 · see citing works
Impact of fatty acid-binding proteins and dopamine receptors on α-synucleinopathy
Kawahata, K., & Fukunaga, K. (2021) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2021.12.003 · Cited by 20 · see citing works
Self-citationKawahata, K., & Fukunaga, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242317037 · Cited by 18 · see citing works
Self-citationFukui, N., Yamamoto, H., Miyabe, M., Aoyama, Y., Hongo, K., Mizobata, T., Kawahata, K., Yabuki, Y., Shinoda, Y., Fukunaga, K., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100663 · Cited by 17 · see citing works
Self-citationFrom protein biomarkers to proteomics in dementia with Lewy Bodies
Tsamourgelis, A., Swann, P., Chouliaras, L., & O'Brien, J. T. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101771 · Cited by 18 · see citing works
Kawahata, K., Sekimori, T., Oizumi, H., Takeda, A., & Fukunaga, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713267 · Cited by 17 · see citing works
Self-citationPotential safety implications of fatty acid-binding protein inhibition
Warren, W. G., Osborn, M., Duffy, P., Yates, A., & O’Sullivan, S. E. (2024) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2024.117079 · Cited by 17 · see citing works
Possible involvement of fatty acid binding proteins in psychiatric disorders
Yamamoto, Y., & Owada, Y. (2021) · Anatomical Science International · doi:10.1007/s12565-020-00598-0 · Cited by 16 · see citing works
Self-citationYabuki, Y., Matsuo, K., Yu, M., Xu, J., Sakimura, K., Shioda, N., & Fukunaga, K. (2021) · Acta Physiologica · doi:10.1111/apha.13613 · Cited by 14 · see citing works
Self-citationGuo, M., Liu, W., Luo, H., Shao, Q., Li, Y., Gu, Y., Guan, Y., Ma, W., Chen, M., Yang, H., et al. (2022) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14055 · Cited by 14 · see citing works
Parkinson disease is a fatty acidopathy
Fanning, S., & Selkoe, D. J. (2025) · Nature Reviews Neurology · doi:10.1038/s41582-025-01142-2 · Cited by 13 · see citing works
Modulating α-synuclein propagation and decomposition: Implications in Parkinson's disease therapy
Li, B., Xiao, X., Bi, M., Jiao, Q., Chen, X., Yan, C., Du, X., & Jiang, H. F. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102319 · Cited by 13 · see citing works
Jia, W., Kawahata, K., Cheng, A., Sasaki, T., Sasaoka, T., & Fukunaga, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076644 · Cited by 12 · see citing works
Self-citationSuppression of α-synuclein propagation after intrastriatal injection in FABP3 null mice
Matsuo, K., Kawahata, K., Melki, R., Bousset, L., Owada, Y., & Fukunaga, K. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147383 · Cited by 12 · see citing works
Self-citationXu, J., Kawahata, K., Izumi, H., & Fukunaga, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126185 · Cited by 12 · see citing works
Self-citationPeptide Profile of Zebrafish Brain in a 6-OHDA-Induced Parkinson Model
Fiametti, L. O., Correa, C. N., & de Castro, L. M. (2021) · Zebrafish · doi:10.1089/zeb.2020.1945 · Cited by 11 · see citing works
Degawa, T., Kawahata, K., Izumi, H., Shinoda, Y., & Fukunaga, K. (2021) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2021.02.006 · Cited by 9 · see citing works
Self-citationEndocytosis of dopamine receptor: Signaling in brain
Kawahata, K., & Fukunaga, K. (2022) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2022.09.005 · Cited by 9 · see citing works
Self-citationWang, H., Fukunaga, K., Cheng, A., Wang, Y., Arimura, N., Yoshino, H., Sasaki, T., & Kawahata, K. (2023) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2023.02.008 · Cited by 9 · see citing works
Self-citationFABP2 is Involved in Intestinal α-Synuclein Pathologies
Sekimori, T., Fukunaga, K., Oizumi, H., Baba, T., Totsune, T., Takeda, A., Sasaki, T., & Kawahata, K. (2024) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2302044 · Cited by 8 · see citing works
Self-citationThe emerging role of fatty acid-binding protein 3 (FABP3) in cancer
Warren, W. G., Osborn, M., Yates, A., & O’Sullivan, S. E. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104504 · Cited by 8 · see citing works
Yabuki, Y., Liu, J., Kawahata, K., Izumi, H., Shinoda, Y., Koga, K., Ueno, S., Shioda, N., & Fukunaga, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155525 · Cited by 9 · see citing works
Self-citationα‐Synuclein decoy peptide protects mice against α‐synuclein‐induced memory loss
Guo, Q., Kawahata, K., Jia, W., Wang, H., Cheng, A., Yabuki, Y., Shioda, N., & Fukunaga, K. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14120 · Cited by 7 · see citing works
Self-citationThe Role of Fatty Acid Binding Proteins in Neuropsychiatric Diseases: A Narrative Review
Powell, A., Yamaguchi, N., Lu, H., Pareek, O., Elman, I., Gold, M. S., Pinhasov, A., Blum, K., & Thanos, P. K. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl26812 · Cited by 5 · see citing works
Matsuo, K., Yabuki, Y., Melki, R., Bousset, L., Owada, Y., & Fukunaga, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22010400 · Cited by 5 · see citing works
Self-citationRecent Advances on Small-Molecule Inhibitors of Lipocalin-like Proteins
Chen, S., Pan, Z., Liu, M., Guo, L., Jiang, X. L., & He, G. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00086 · Cited by 4 · see citing works
Associations among blood biomarkers, clinical subtypes, and prognosis in Parkinson’s disease
Oizumi, H., Hasegawa, T., Kawahata, K., Sekimori, T., Totsune, T., Sugimura, Y., Baba, T., Fukunaga, K., & Takeda, A. (2025) · Clinical Parkinsonism & Related Disorders · doi:10.1016/j.prdoa.2025.100313 · Cited by 3 · see citing works
Self-citationLiang, Y.-L., Yang, F.-G., & Tang, Q. (2026) · Journal of Neurology · doi:10.1007/s00415-026-13900-3 · Cited by 3 · see citing works
Fu, Y., Wang, Z.-T., Huang, L., Tan, C., Cao, X., & Tan, L. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1008780 · Cited by 2 · see citing works
Tawfeeq, H. R., Lackey, A. I., Zhou, Y., Diolintzi, A., Zacharisen, S. M., Lau, Y. H., Quadro, L., & Storch, J. (2025) · Nutrients · doi:10.3390/nu17050753 · Cited by 2 · see citing works
Jia, W., He, X., Cheng, A., He, Y., Zhao, F., Fukunaga, K., & Zhao, W. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05963-0 · Cited by 1 · see citing works
Self-citationMcDermott, L., & Storch, J. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00173-0 · Cited by 1 · see citing works
Alpha-synuclein spreading mechanisms in Parkinson's disease: The role of membrane receptors
Brás, I. C., & Outeiro, T. F. (2021) · International review of movement disorders · doi:10.1016/bs.irmvd.2021.08.002
Fear Memory in Experimental Models of Parkinson’s Disease
Timofeeva, E., Dubrovina, N. I., Tikhonova, M. A., & Amstislavskaya, T. G. (2024) · Advances in Gerontology · doi:10.1134/s207905702460040x
Fatty acid-binding proteins as therapeutic targets in different diseases
Duttaroy, A. K. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95700-7.00004-8
Iqbal, M. S., Duan, X., Attia, K. A., Nabi, G., Peng, K., Sardar, N., Gu, D., Zeng, G., & Al-Theyab, N. S. (2025) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-025-05448-z
Blood-based biomarkers for dementia with Lewy bodies
Acquaviva, J., Delic, V., Bellacicco, N., & Choi, Y. (2026) · Journal of Alzheimer s Disease · doi:10.1177/13872877261456317
Mhatre, A., Prasad, A., & Naqvi, S. (2026) · ASPET Discovery · doi:10.1016/j.aspetd.2026.100033
Fatty Acid-Binding Proteins and Substance Use Disorders: From Lipid Signaling to Therapeutic Targets
Powell, A., Yamaguchi, N., Delgado, M., Blum, K., Pinhasov, A., Elman, I., & Thanos, P. K. (2026) · Genes · doi:10.3390/genes17091000
Venko, K., & Žerovnik, E. (2026) · Biomolecules · doi:10.3390/biom16091286
Zaharija, B., Stanivuk, I., Kršanac, M., Juković, M., Radonja, A. P., & Bradshaw, N. J. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-34176-2.00009-2
BindingDB Entry 50021299: Recent Advances on Small-Molecule Inhibitors of Lipocalin-like Proteins.
BindingDB (2025) · UC San Diego · doi:10.7270/q2x3533h
- Authors
- Yabuki, Y., Matsuo, K., Kawahata, I., Fukui, N., Mizobata, T., Kawata, Y., Owada, Y., Shioda, N., & Fukunaga, K.
- Affiliations
- Tohoku University (JP)
- Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Miyagi 980-8578, Japan
- Tottori University (JP)
- Institute of Molecular Embryology and Genetics, Kumamoto University (JP)
- Corresponding author
- Fukunaga, Kohji
- ORCID
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2020-03-23
- Volume
- 21
- Issue
- 6
- Pages
- 2230
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC7139546
- OpenAlex
- W3012697258
- Cited by
- 49
- References
- 63
- Citations by year
- 2026: 7 · 2025: 7 · 2024: 7 · 2023: 6 · 2022: 5 · 2021: 13 · 2020: 3 · 2019: 1
- FWCI
- 2.92
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Japan Agency for Medical Research and Development (JP17dm0107071, JP19dm0107071, JP18dm0107071)
- Ono Medical Research Foundation
- Japan Society for the Promotion of Science (20H03393, 15H06036, 20K21400, 19K07097, 20K11609, 16H05219, 18J20651)
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- fatty acid binding protein 3, alpha-synuclein, synucleinopathies, Parkinson's disease, dementia with Lewy bodies, preformed fibrils, prion-like propagation, substantia nigra pars compacta, alpha-synuclein phosphorylation, tyrosine hydroxylase, AAV gene transfer, motor impairment, cognitive impairment, therapeutic target
- MeSH terms
- Fatty Acid Binding Protein 3, Synucleinopathies, Animals, Brain, Cognition, Disease Models, Animal, Fluorescent Antibody Technique, Humans, Immunohistochemistry, Neurons, Phosphorylation, Tyrosine 3-Monooxygenase, Mice, Knockout, Mice, 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