Novel insights into the antioxidant role of tauroursodeoxycholic acid in experimental models of Parkinson's disease

Parkinson's disease: clinical features and diagnosis

Jankovic, J. (2008) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp.2007.131045 · Cited by 5,720 · see citing works

Parkinson's Disease

Dauer, W., & Przedborski, S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00568-3 · Cited by 5,469 · see citing works

Chronic systemic pesticide exposure reproduces features of Parkinson's disease

Betarbet, R., Sherer, T., Mackenzie, G., Garcia-Osuna, M., Panov, A., & Greenamyre, J. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,797 · see citing works

PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin

Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944 · see citing works

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835 · see citing works

The pathways of mitophagy for quality control and clearance of mitochondria

Ashrafi, G., & Schwarz, T. L. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.81 · Cited by 1,900 · see citing works

Genetics of Parkinson's DiseasePreprint

Klein, C., & Westenberger, A. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a008888 · Cited by 1,370 · see citing works

MOLECULAR PATHOPHYSIOLOGY OF PARKINSON'S DISEASE

Moore, D. J., West, A. B., Dawson, V. L., & Dawson, T. M. (2005) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.28.061604.135718 · Cited by 1,274 · see citing works

PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65

Kondapalli, C., Kazlauskaite, A., Zhang, N., Woodroof, H. I., Campbell, D. G., Gourlay, R., Burchell, L., Walden, H., Macartney, T. J., Deak, M., et al. (2012) · Open Biology · doi:10.1098/rsob.120080 · Cited by 940 · see citing works

Compromised autophagy and neurodegenerative diseases

Menzies, F. M., Fleming, A., & Rubinsztein, D. C. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3961 · Cited by 851 · see citing works

Parkinson's disease

Thomas, B., & Beal, M. F. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm159 · Cited by 748 · see citing works

Deficiencies in Complex I subunits of the respiratory chain in Parkinson's disease

Mizuno, Y., Ohta, S., Tanaka, M., Takamiya, S., Suzuki, K., SATO, T. A., Oya, H., Ozawa, T., & Kagawa, Y. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)91141-8 · Cited by 735 · see citing works

Dopamine covalently modifies and functionally inactivates parkin

LaVoie, M. J., Ostaszewski, B. L., Weihofen, A., Schlossmacher, M. G., & Selkoe, D. J. (2005) · Nature Medicine · doi:10.1038/nm1314 · Cited by 722 · see citing works

Mitochondrial dysfunction in Parkinson's disease

Winklhofer, K. F., & Haass, C. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.08.013 · Cited by 688 · see citing works

Role of PINK1 Binding to the TOM Complex and Alternate Intracellular Membranes in Recruitment and Activation of the E3 Ligase Parkin

Lazarou, M., Jin, S. M., Kane, L. A., & Youle, R. J. (2012) · Developmental Cell · doi:10.1016/j.devcel.2011.12.014 · Cited by 670 · see citing works

Nitric oxide‐induced mitochondrial fission is regulated by dynamin‐related GTPases in neurons

Barsoum, M. J., Yuan, H., Gerencser, A. A., Liot, G., Kushnareva, Y., Gräber, S., Kovács, I., Lee, W. D., Waggoner, J., Cui, J., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601253 · Cited by 658 · see citing works

PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy

Shiba-Fukushima, K., Imai, Y., Yoshida, S., Ishihama, Y., Kanao, T., Sato, S., & Hattori, N. (2012) · Scientific Reports · doi:10.1038/srep01002 · Cited by 577 · see citing works

A novel role for ursodeoxycholic acid in inhibiting apoptosis by modulating mitochondrial membrane perturbation.

Rodrigues, C. M. P., Fan, G., Ma, X., Kren, B. T., & Steer, C. J. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1325 · Cited by 515 · see citing works

Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin

Ashrafi, G., Schlehe, J. S., LaVoie, M. J., & Schwarz, T. L. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201401070 · Cited by 502 · see citing works

Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism

Silvestri, L., Caputo, V., Bellacchio, E., Atorino, L., Dallapiccola, B., Valente, E. M., & Casari, G. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi377 · Cited by 449 · see citing works

Recent Advances in the Genetics of Parkinson's Disease

Martin, I., Dawson, V. L., & Dawson, T. M. (2011) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-082410-101440 · Cited by 438 · see citing works

Mitochondrial homeostasis: The interplay between mitophagy and mitochondrial biogenesis

Palikaras, K., & Tavernarakis, N. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.01.021 · Cited by 428 · see citing works

Current and experimental treatments of Parkinson disease: A guide for neuroscientists

Oertel, W. H., & Schulz, J. B. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13750 · Cited by 372 · see citing works

Impulse control disorders and levodopa-induced dyskinesias in Parkinson's disease: an update

Voon, V., Napier, T. C., Frank, M. J., Sgambato, V., Grace, A. A., Rodríguez‐Oroz, M., Obeso, J. A., Bézard, E., & Fernagut, P. (2017) · The Lancet Neurology · doi:10.1016/s1474-4422(17)30004-2 · Cited by 360 · see citing works

Autoregulation of Parkin activity through its ubiquitin‐like domain

Chaugule, V. K., Burchell, L., Barber, K. R., Sidhu, A., Leslie, S. J., Shaw, G. S., & Walden, H. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.204 · Cited by 339 · see citing works

Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease

Keene, C. D., Rodrigues, C. M. P., Eich, T., Chhabra, M. S., Steer, C. J., & Low, W. C. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162362299 · Cited by 306 · see citing works

Oxidative and Inflammatory Pathways in Parkinson’s Disease

Miller, R. L., James-Kracke, M., Sun, G. Y., & Sun, A. Y. (2009) · Neurochemical Research · doi:10.1007/s11064-008-9656-2 · Cited by 306 · see citing works

Parkin enhances mitochondrial biogenesis in proliferating cells

Kuroda, Y., Mitsui, T., Kunishige, M., Shono, M., Akaike, M., Azuma, H., & Matsumoto, T. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl006 · Cited by 268 · see citing works

Similar Patterns of Mitochondrial Vulnerability and Rescue Induced by Genetic Modification of α-Synuclein, Parkin, and DJ-1 in Caenorhabditis elegans

Ved, R., Saha, S., Westlund, B., Perier, C., Griffin, L. B., Sluder, A. E., Hoener, M. C., Rodrigues, C. M. P., Alfonso, A., Steer, C. J., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505910200 · Cited by 256 · see citing works

Complex II inhibition by 3-NP causes mitochondrial fragmentation and neuronal cell death via an NMDA- and ROS-dependent pathway

Liot, G., Bossy, B., Lubitz, S., Kushnareva, Y., Sejbuk, N. E., & Bossy‐Wetzel, E. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.22 · Cited by 239 · see citing works

Tauroursodeoxycholic acid in the treatment of patients with amyotrophic lateral sclerosis

Elia, A. E., Lalli, S., Monsurrò, M. R., Sagnelli, A., Taiello, A. C., Reggiori, B., Bella, V. L., Tedeschi, G., & Albanese, A. (2015) · European Journal of Neurology · doi:10.1111/ene.12664 · Cited by 225 · see citing works

TUDCA, a Bile Acid, Attenuates Amyloid Precursor Protein Processing and Amyloid-β Deposition in APP/PS1 Mice

Nunes, A. F., Amaral, J. D., Lo, A. C., Fonseca, M. B., Viana, R. J. S., Callaerts-Vegh, Z., D’Hooge, R., & Rodrigues, C. M. P. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8256-y · Cited by 192 · see citing works

The hitchhiker’s guide to PGC-1α isoform structure and biological functions

Martínez-Redondo, V., Pettersson, A. T., & Ruas, J. (2015) · Diabetologia · doi:10.1007/s00125-015-3671-z · Cited by 191 · see citing works

Mitochondrial Dysfunction in Parkinson's Disease

Keane, P. C., Kurzawa‐Akanbi, M., Blain, P. G., & Morris, C. M. (2011) · Parkinson s Disease · doi:10.4061/2011/716871 · Cited by 177 · see citing works

Neuroprotection by a Bile Acid in an Acute Stroke Model in the Rat

Rodrigues, C. M. P., Spellman, S. R., Solá, S., Grande, A. W., Linehan-Stieers, C., Low, W. C., & Steer, C. J. (2002) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200204000-00010 · Cited by 160 · see citing works

Mitochondrial Dysfunction in Parkinson's Disease

Zhu, J., & Chu, C. T. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100363 · Cited by 158 · see citing works

Tauroursodeoxycholic acid prevents MPTP-induced dopaminergic cell death in a mouse model of Parkinson's disease

Castro-Caldas, M., Carvalho, A. N., Rodrigues, E., Henderson, C. J., Wolf, C. R., Rodrigues, C. M. P., & Gama, M. J. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8295-4 · Cited by 156 · see citing works

Mitochondrial alterations in Parkinson’s disease: new clues

Vila, M., Ramonet, D., & Perier, C. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05604.x · Cited by 131 · see citing works

UDCA exerts beneficial effect on mitochondrial dysfunction in <i>LRRK2</i> ^{<i>G2019S</i>} carriers and in vivo

Mortiboys, H., Furmston, R., Bronstad, G., Aasly, J., Elliott, C., & Bandmann, O. (2015) · Neurology · doi:10.1212/wnl.0000000000001905 · Cited by 131 · see citing works

Nrf2 activation by tauroursodeoxycholic acid in experimental models of Parkinson's disease

Moreira, S., Fonseca, I., Nunes, M. J., Rosa, A., Lemos, L., Rodrigues, E., Carvalho, A. N., Outeiro, T. F., Rodrigues, C. M. P., Gama, M. J., et al. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.05.009 · Cited by 112 · see citing works

Dysregulation of autophagy and mitochondrial function in Parkinson’s disease

Wang, B., Abraham, N. A., Gao, G., & Yang, Q. (2016) · Translational Neurodegeneration · doi:10.1186/s40035-016-0065-1 · Cited by 106 · see citing works

Tauroursodeoxycholic Acid Partially Prevents Apoptosis Induced by 3‐Nitropropionic Acid

Rodrigues, C. M. P., Linehan-Stieers, C., Keene, C. D., Ma, X., Kren, B. T., Low, W. C., & Steer, C. J. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0752368.x · Cited by 104 · see citing works

Parkin functionally interacts with PGC-1α to preserve mitochondria and protect dopaminergic neurons

Zheng, L., Bernard‐Marissal, N., Moullan, N., D'Amico, D. F., Auwerx, J. H., Moore, D. J., Knott, G. W., Aebischer, P., & Schneider, B. L. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw418 · Cited by 84 · see citing works

Parkin Plays a Role in Sporadic Parkinson's Disease

Dawson, T. M., & Dawson, V. L. (2013) · Neurodegenerative Diseases · doi:10.1159/000354307 · Cited by 82 · see citing works

Peroxisome proliferator-activated receptor-γ (PPARγ) agonist is neuroprotective and stimulates PGC-1α expression and CREB phosphorylation in human dopaminergic neurons

Mäkelä, J., Tselykh, T. V., Kukkonen, J. P., Eriksson, O., Korhonen, L., & Lindholm, D. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.11.020 · Cited by 60 · see citing works

Post translational modification of Parkin

Chakraborty, J., Basso, V., & Ziviani, E. (2017) · Biology Direct · doi:10.1186/s13062-017-0176-3 · Cited by 58 · see citing works

Tauroursodeoxycholic Acid Protects Against Mitochondrial Dysfunction and Cell Death via Mitophagy in Human Neuroblastoma Cells

Fonseca, I., Gordino, G., Moreira, S., Nunes, M. J., Azevedo, C., Gama, M. J., Rodrigues, E., Rodrigues, C. M. P., & Castro‐Caldas, M. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0145-3 · Cited by 52 · see citing works

The E3 Ubiquitin Ligase Parkin Is Recruited to the 26 S Proteasome via the Proteasomal Ubiquitin Receptor Rpn13

Aguileta, M., Korać-Prlić, J., Durcan, T. M., Trempe, J., Haber, M., Gehring, K., Elsasser, S., Waidmann, O., Fon, E. A., & Husnjak, K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.614925 · Cited by 42 · see citing works

GSTpi Expression in MPTP-Induced Dopaminergic Neurodegeneration of C57BL/6 Mouse Midbrain and Striatum

Castro‐Caldas, M., Carvalho, A. N., Peixeiro, I., Rodrigues, E., Lechner, M. C., & Gama, M. J. (2008) · Journal of Molecular Neuroscience · doi:10.1007/s12031-008-9141-z · Cited by 34 · see citing works

Integrated pathways of parkin control over mitochondrial maintenance – relevance to Parkinson’s disease pathogenesis

Gawęda-Walerych, K., & Żekanowski, C. (2013) · Acta Neurobiologiae Experimentalis · doi:10.55782/ane-2013-1931 · Cited by 30 · see citing works

The role of gut dysbiosis in Parkinson’s disease: mechanistic insights and therapeutic options

Wang, Q., Luo, Y., Ray Chaudhuri, K., Reynolds, R., Tan, E.-K., & Pettersson, S. (2021) · Brain · doi:10.1093/brain/awab156 · Cited by 281 · see citing works

Tauroursodeoxycholate—Bile Acid with Chaperoning Activity: Molecular and Cellular Effects and Therapeutic Perspectives

Kusaczuk, M. (2019) · Cells · doi:10.3390/cells8121471 · Cited by 244 · see citing works

Bile acid metabolism is altered in multiple sclerosis and supplementation ameliorates neuroinflammation

Bhargava, P., Smith, M. D., Mische, L., Harrington, E., Fitzgerald, K. C., Martin, K. A., Kim, S., Reyes, A. A., Cardona, J. G., Volsko, C. M., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci129401 · Cited by 236 · see citing works

The biosynthesis, signaling, and neurological functions of bile acids

Kiriyama, Y., & Nochi, H. (2019) · Biomolecules · doi:10.3390/biom9060232 · Cited by 204 · see citing works

Tauroursodeoxycholic acid: a potential therapeutic tool in neurodegenerative diseases

Khalaf, K., Tornese, P., Cocco, A., & Albanese, A. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00307-z · Cited by 150 · see citing works

Bile acids: a communication channel in the gut-brain axis

Monteiro-Cardoso, V. F., Corlianò, M., & Singaraja, R. R. (2021) · NeuroMolecular Medicine · doi:10.1007/s12017-020-08625-z · Cited by 145 · see citing works

The bile acid TUDCA and neurodegenerative disorders: An overview

Zangerolamo, L., Vettorazzi, J. F., Rosa, L. R. D. O., Carneiro, E. M., & Barbosa, H. C. L. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119252 · Cited by 127 · see citing works

From dried bear bile to molecular investigation: A systematic review of the effect of bile acids on cell apoptosis, oxidative stress and inflammation in the brain, across pre-clinical models of neurological, neurodegenerative and neuropsychiatric disorders

Huang, F., Pariante, C. M., & Borsini, A. (2022) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2021.09.021 · Cited by 117 · see citing works

Roles of bile acids signaling in neuromodulation under physiological and pathological conditions

Chen, X., Huang, X., Wang, D., Yu, D., Hou, S., Cui, H., & Song, L. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-01053-z · Cited by 120 · see citing works

Oxidative Stress Leads to β-Cell Dysfunction Through Loss of β-Cell Identity

Leenders, F., Gröen, N., de Graaf, N., Engelse, M. A., Rabelink, T. J., de Koning, E. J. P., & Carlotti, F. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.690379 · Cited by 114 · see citing works

Tauroursodeoxycholic acid improves motor symptoms in a mouse model of Parkinson's disease

Rosa, A. I., Duarte-Silva, S., Silva-Fernandes, A., Nunes, M. J., Carvalho, A. N., Rodrigues, E., Gama, M. J., Rodrigues, C. M. P., Maciel, P., & Castro-Caldas, M. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1062-4 · Cited by 94 · see citing works

Linking Glycation and Glycosylation With Inflammation and Mitochondrial Dysfunction in Parkinson’s Disease

Videira, P. A., & Castro‐Caldas, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00381 · Cited by 93 · see citing works

Inhibition of phosphodiesterase 4 by FCPR16 protects SH-SY5Y cells against MPP+-induced decline of mitochondrial membrane potential and oxidative stress

Zhong, J., Yu, H., Huang, C., Zhong, Q., Chen, Y., Xie, J., Zhou, Z., Xu, J., & Wang, H. (2018) · Redox Biology · doi:10.1016/j.redox.2018.02.008 · Cited by 79 · see citing works

Review: The bile acids urso- and tauroursodeoxycholic acid as neuroprotective therapies in retinal disease.

Daruich, A., Picard, É., Boatright, J. H., & Béhar‐Cohen, F. (2019) · PubMed Central · Cited by 73 · see citing works

The multi‐faceted role of mitochondria in the pathology of Parkinson’s disease

Trinh, D., Israwi, A. R., Arathoon, L. R., Gleave, J. A., & Nash, J. E. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15154 · Cited by 72 · see citing works

TUDCA attenuates intestinal injury and inhibits endoplasmic reticulum stress-mediated intestinal cell apoptosis in necrotizing enterocolitis

Li, P., Fu, D., Sheng, Q., Yu, S., Bao, X., & Lv, Z. (2019) · International Immunopharmacology · doi:10.1016/j.intimp.2019.05.050 · Cited by 51 · see citing works

Connecting the Gut Microbiota and Neurodegenerative Diseases: the Role of Bile Acids

Wang, S., Xu, C., Liu, H., Wei, W., Zhou, X., Qian, H., Zhou, L., Zhang, H., Wu, L. M., Chen, Z., et al. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03340-9 · Cited by 50 · see citing works

Unravelling the role of gut microbiota in Parkinson’s disease progression: Pathogenic and therapeutic implications

Rani, L., & Mondal, A. C. (2021) · Neuroscience Research · doi:10.1016/j.neures.2021.01.001 · Cited by 48 · see citing works

Complex Interaction between Resident Microbiota and Misfolded Proteins: Role in Neuroinflammation and Neurodegeneration

González-Sanmiguel, J., Schuh, C. M. A. P., Muñoz-Montesino, C., Contreras‐Kallens, P., Aguayo, L. G., & Aguayo, S. D. (2020) · Cells · doi:10.3390/cells9112476 · Cited by 48 · see citing works

Protective effects of lipoic acid against acrylamide-induced neurotoxicity: involvement of mitochondrial energy metabolism and autophagy

Song, G., Liu, Z., Wang, L., Shi, R., Chu, C., Xiang, M., Tian, Q., & Liu, X. (2017) · Food & Function · doi:10.1039/c7fo01429e · Cited by 46 · see citing works

Ablation of RIP3 protects from dopaminergic neurodegeneration in experimental Parkinson’s disease

Dionísio, P. A., Oliveira, S. R., Gaspar, M. M., Gama, M. J., Castro‐Caldas, M., Amaral, J. D., & Rodrigues, C. M. P. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2078-z · Cited by 40 · see citing works

Mitochondrial Dysfunction in Genetic and Non-Genetic Parkinson’s Disease

Lucchesi, M., Biso, L., Bonaso, M., Longoni, B., Buchignani, B., Battini, R., Santorelli, F. M., Doccini, S., & Scarselli, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26094451 · Cited by 39 · see citing works

A Low-Protein, High-Carbohydrate Diet Exerts a Neuroprotective Effect on Mice with 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine-Induced Parkinson’s Disease by Regulating the Microbiota-Metabolite–Brain Axis and Fibroblast Growth Factor 21

Chu, C., Li, T., Yu, L., Li, Y. H., Li, M., Guo, M., Zhao, J., Zhai, Q., Tian, F., & Chen, W. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c07606 · Cited by 38 · see citing works

Bruceine D elevates Nrf2 activation to restrain Parkinson’s disease in mice through suppressing oxidative stress and inflammatory response

Yang, Y. X., Kong, F., Ding, Q., Cai, Y., Hao, Y., & Tang, B. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.03.097 · Cited by 35 · see citing works

Eclalbasaponin I from Aralia elata (Miq.) Seem. reduces oxidative stress-induced neural cell death by autophagy activation

Wang, W., Yao, G., Shang, X., Gao, J.-C., Zhang, Y., & Song, S. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.10.106 · Cited by 34 · see citing works

Linking Nonalcoholic Fatty Liver Disease and Brain Disease: Focusing on Bile Acid Signaling

Ren, Z., Li, C.-X., Ma, C., Chen, D., Chen, J., Xu, W., Chen, C.-A., Cheng, F., & Wang, X. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113045 · Cited by 32 · see citing works

Emerging insights between gut microbiome dysbiosis and Parkinson’s disease: Pathogenic and clinical relevance

Bi, M., Feng, L., He, J., Liu, C., Wang, Y., Jiang, H., & Liu, S. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101759 · Cited by 32 · see citing works

Neurotoxic effects of MPTP on mouse cerebral cortex: Modulation of neuroinflammation as a neuroprotective strategy

Mendes, M. O., Rosa, A. I., Carvalho, A. N., Nunes, M. J., Dionísio, P., Rodrigues, E., Costa, D., Duarte-Silva, S., Maciel, P., Rodrigues, C. M. P., et al. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.01.003 · Cited by 31 · see citing works

Gut microbiota and Parkinson’s disease

Wang, L., Cui, Y., Han, B., Du, Y., Salewala, K. S., Wang, S., Zhao, W., Zhang, H., Wang, S., Xu, X., et al. (2024) · Chinese Medical Journal · doi:10.1097/cm9.0000000000003318 · Cited by 31 · see citing works

Treatment of in vitro-Matured Bovine Oocytes With Tauroursodeoxycholic Acid Modulates the Oxidative Stress Signaling Pathway

Pioltine, E. M., Costa, C. B., Latorraca, L. B., Franchi, F. F., dos Santos, P. H., Mingoti, G. Z., de Paula-Lopes, F. F., & Nogueira, M. F. G. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.623852 · Cited by 30 · see citing works

Emerging Roles of Bile Acids in Neuroinflammation

Butcher, E. L., & Arthur, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262311301 · Cited by 34 · see citing works

Role of the HSP70 Co-Chaperone SIL1 in Health and Disease

Ichhaporia, V. P., & Hendershot, L. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041564 · Cited by 29 · see citing works

Tauroursodeoxycholic acid ameliorates renal injury induced by COL4A3 mutation

Yu, S., Gu, X., Zheng, Q., Liu, Y., Suhas, T., Du, W., Xie, L., Fang, Z., Zhao, Y., Yang, M., et al. (2024) · Kidney International · doi:10.1016/j.kint.2024.04.015 · Cited by 28 · see citing works

Determination of free and conjugated bile acids in serum of Apoe(−/−) mice fed different lingonberry fractions by UHPLC-MS

Ghaffarzadegan, T., Essén, S., Verbrugghe, P., Marungruang, N., Hållenius, F. F., NYMAN, M. E., & Sandahl, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-40272-8 · Cited by 28 · see citing works

Ursodeoxycholic acid as a potential alternative therapeutic approach for neurodegenerative disorders: Effects on cell apoptosis, oxidative stress and inflammation in the brain

Huang, F. (2021) · Brain Behavior & Immunity - Health · doi:10.1016/j.bbih.2021.100348 · Cited by 27 · see citing works

Neuroprotective Effect of Tauroursodeoxycholic Acid (TUDCA) on In Vitro and In Vivo Models of Retinal Disorders: A Systematic Review

Li, J., Huang, Z., Yu, J., Liang, L., Li, Y., Xu, K., Zhou, W., & Li, X. (2023) · Current Neuropharmacology · doi:10.2174/1570159x21666230907152207 · Cited by 26 · see citing works

Palmitate and Nitric Oxide Regulate the Expression of Spexin and Galanin Receptors 2 and 3 in Hypothalamic Neurons

Tran, A., Loganathan, N., McIlwraith, E. K., & Belsham, D. D. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.10.028 · Cited by 26 · see citing works

Proteomic and metabolomic insights into the functions of the male reproductive system in fishes

Dietrich, M. A., Nynca, J., & Ciereszko, A. (2019) · Theriogenology · doi:10.1016/j.theriogenology.2019.04.018 · Cited by 26 · see citing works

Large-scale production of tauroursodeoxycholic acid products through fermentation optimization of engineered Escherichia coli cell factory

Xu, Y., Yang, L., Zhao, S., & Wang, Z. (2019) · Microbial Cell Factories · doi:10.1186/s12934-019-1076-2 · Cited by 25 · see citing works

Multidirectional associations between the gut microbiota and Parkinson’s disease, updated information from the perspectives of humoral pathway, cellular immune pathway and neuronal pathway

Jia, X., Chen, Q., Zhang, Y., & Asakawa, T. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2023.1296713 · Cited by 22 · see citing works

BPA Differentially Regulates NPY Expression in Hypothalamic Neurons Through a Mechanism Involving Oxidative Stress

Loganathan, N., McIlwraith, E. K., & Belsham, D. D. (2020) · Endocrinology · doi:10.1210/endocr/bqaa170 · Cited by 22 · see citing works

Targeting Mitochondria as a Therapeutic Approach for Parkinson’s Disease

Abrishamdar, M., Jalali, M. S., & Farbood, Y. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01265-w · Cited by 22 · see citing works

Systematic Review of the Therapeutic Role of Apoptotic Inhibitors in Neurodegeneration and Their Potential Use in Schizophrenia

Morén, C., Treder, N., Martínez-Pinteño, A., Rodríguez, N., Arbelo, N., Madero, S., Gómez, M., Mas, S., Gassó, P., & Parellada, E. (2022) · Antioxidants · doi:10.3390/antiox11112275 · Cited by 20 · see citing works

Co-delivery of glial cell–derived neurotrophic factor (GDNF) and tauroursodeoxycholic acid (TUDCA) from PLGA microspheres: potential combination therapy for retinal diseases

Arranz-Romera, A., Esteban-Pérez, S., Molina-Martínez, I. T., Bravo‐Osuna, I., & Herrero‐Vanrell, R. (2021) · Drug Delivery and Translational Research · doi:10.1007/s13346-021-00930-9 · Cited by 18 · see citing works

Tauroursodeoxycholic Acid Inhibited Apoptosis and Oxidative Stress in H2O2-Induced BMSC Death via Modulating the Nrf-2 Signaling Pathway: the Therapeutic Implications in a Rat Model of Spinal Cord Injury

Weng, J., Wang, L., Wang, K., Su, H., Luo, D., Yang, H., Wen, Y., Wu, Q., & Li, X. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03754-5 · Cited by 17 · see citing works

Novel insight into the etiology of ischemic stroke gained by integrative multiome-wide association study

Jung, J., Lu, Z., de Smith, A. D., & Mancuso, N. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddad174 · Cited by 16 · see citing works

Impairment of chaperone-mediated autophagy affects neuronal homeostasis through altered expression of DJ-1 and CRMP-2 proteins

Brekk, O. R., Makridakis, M., Mavroeidi, P., Vlahou, A., Xilouri, M., & Stefanis, L. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.12.006 · Cited by 16 · see citing works

Retinal Neurodegeneration in Euglycemic Hyperinsulinemia, Prediabetes, and Diabetes

Ebrahimi, M., Sivaprasad, S., Thompson, P. M., & Perry, G. L. (2022) · Ophthalmic Research · doi:10.1159/000528503 · Cited by 15 · see citing works

The effects of ursodeoxycholic acid on Parkinson’s disease, a mechanistic review of the recent evidence

Razavi, S. M., Esmaealzadeh, N., Ataei, M., Afshari, N., Saleh, M., Amini, Y., Hasrati, S., Hashemi, F. G., Mortazavi, A., Shalmani, L. M., et al. (2025) · Metabolic Brain Disease · doi:10.1007/s11011-025-01542-9 · Cited by 15 · see citing works

The role of gut microbiota–mitochondria crosstalk in neurodegeneration: Underlying mechanisms and potential therapies

Ju, T., Zhang, Y., Liu, L., Zhao, X., Li, X., Liu, C., Sun, S., & Wu, L. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-01419 · Cited by 16 · see citing works

Combination of tauroursodeoxycholic acid, co-enzyme Q10 and creatine demonstrates additive neuroprotective effects in in-vitro models of Parkinson’s disease

Shtilbans, A., Reintsch, W., Piscopo, V. E. C., Krahn, A. I., & Durcan, T. M. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1492028 · Cited by 10 · see citing works

Metabolic fingerprinting of carp and rainbow trout seminal plasma

Dietrich, M. A., Samczuk, P., Ciborowski, M., Nynca, J., Parfieniuk, E., Pietrowska, K., Kowalczyk, T., Kretowski, A. J., & Ciereszko, A. (2018) · Aquaculture · doi:10.1016/j.aquaculture.2018.11.017 · Cited by 10 · see citing works

Diagnostic Potential of Alternations of Bile Acid Profiles in the Plasma of Patients with Huntington’s Disease

Chiang, P.-I., Chang, K., Tang, H.-Y., Wu, Y., Cheng, M., & Chen, C. (2024) · Metabolites · doi:10.3390/metabo14070394 · Cited by 8 · see citing works

Postprandial Responses of Serum Bile Acids in Healthy Humans after Ingestion of Turmeric before Medium/High‐Fat Breakfasts

Ghaffarzadegan, T., Zanzer, Y. C., Östman, E. M., Hållenius, F. F., Essén, S., Sandahl, M., & NYMAN, M. E. (2019) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201900672 · Cited by 8 · see citing works

Antioxidant Therapy and Neurodegenerative Disorders: Lessons From Clinical Trials

Silva, C., Pinto, M., Fernandes, C., Benfeito, S., & Borges, F. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.11611-3 · Cited by 8 · see citing works

Pleiotropic immunoregulation by bile acids in pathophysiology

Lin, B.-S., Yin, M., Xie, S.-A., Li, P., & Li, X. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1719092 · Cited by 7 · see citing works

Modulation of Autophagy and Nitric Oxide Signaling via Glycyrrhizic Acid and 7-Nitroindazole in MPTP-induced Parkinson’s Disease Model

Kartik, S., Pal, R., Chaudhary, M. J., Nath, R., & Kumar, M. (2023) · Annals of Neurosciences · doi:10.1177/09727531231191661 · Cited by 6 · see citing works

NPC1-like phenotype, with intracellular cholesterol accumulation and altered mTORC1 signaling in models of Parkinson's disease

Caria, I., Nunes, M. J., Ciraci, V., Carvalho, A. N., Ranito, C., Santos, S. G., Gama, M. J., Castro‐Caldas, M., Rodrigues, C. M. P., Ruas, J. L., et al. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166980 · Cited by 6 · see citing works

Altered expression of Sialyl Lewis X in experimental models of Parkinson’s disease

Nunes, M. J., Carvalho, A. N., Rosa, A. I., Videira, P. A., Gama, M. J., Rodrigues, E., & Castro‐Caldas, M. (2024) · Journal of Molecular Medicine · doi:10.1007/s00109-023-02415-3 · Cited by 6 · see citing works

Current neuroprotective therapies and future prospects for motor neuron disease

Evans, L. J., O’Brien, D., & Shaw, P. J. (2024) · International review of neurobiology · doi:10.1016/bs.irn.2024.04.003 · Cited by 5 · see citing works

Exploring the therapeutic potential of Chinese herbs on comorbid type 2 diabetes mellitus and Parkinson's disease: A mechanistic study

Wang, Y., Gao, P.-P., Wu, Z., Jiang, B., Wang, Y., He, Z., Zhao, B., Tian, X., Gao, H., Cai, L., et al. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.119095 · Cited by 5 · see citing works

Sustained PGC-1α2 or PGC-1α3 expression induces astrocyte dysfunction and degeneration

Nunes, M. J., Carvalho, A. N., Sá-Lemos, C., Colaço, M. L., Červenka, I., Ciraci, V., Santos, S. G., Ribeiro, M. M., Castanheira, M., Jannig, P. R., et al. (2023) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2023.151377 · Cited by 5 · see citing works

3-(Naphthalen-2-yl(propoxy)methyl)azetidine hydrochloride attenuates MPP＋-induced cytotoxicity by regulating oxidative stress and mitochondrial dysfunction in SH-SY5Y cells

Yang, S.-J., Yang, J. W., Na, J.-M., Ha, J. S., Choi, S. Y., & Cho, S. W. (2018) · BMB Reports · doi:10.5483/bmbrep.2018.51.11.123 · Cited by 4 · see citing works

Experimental Protocol for Detecting Mitochondrial Function in Hepatocytes Exposed to Organochlorine Pesticides

Liu, Q., Jiang, Z., & Gu, A. (2020) · Journal of Visualized Experiments · doi:10.3791/56800 · Cited by 4 · see citing works

Dietary tauroursodeoxycholic acid supports growth and gut health in spotted seabass (Lateolabrax maculatus) under thermal stress conditions

Liu, Y., Mao, X., Song, K., Wang, L., Li, X., Zhang, C., Lu, K., & Rahimnejad, S. (2025) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2025.110423 · Cited by 3 · see citing works

Combination Supplement Therapy: A New Frontier in Treatment of Neurodegenerative Diseases

Shtilbans, A. (2025) · Journal of Nutrition · doi:10.1016/j.tjnut.2025.07.004 · Cited by 3 · see citing works

Synthesis of TUDCA from chicken bile: immobilized dual-enzymatic system for producing artificial bear bile substitute

Shijing, T., Yinping, P., Yang, Q., Deshuai, L., Liancai, Z., Jun, T., Shaoyong, L., & Wang, B. (2024) · Microbial Cell Factories · doi:10.1186/s12934-024-02592-x · Cited by 3 · see citing works

Ursodeoxycholic and tauroursodeoxycholic acids as antiapoptotic agents: modulation of Parkinson's disease

Abdelkader, N. F. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815946-0.00037-5 · Cited by 3 · see citing works

Long-term benefits of TUDCA supplement in ARSACS zebrafish model

Naef, V., Vecchia, S. D., Giacich, M., Licitra, R., Bachetti, T., Vargas, G. C., Ponassi, M., & Santorelli, F. M. (2025) · Scientific Reports · doi:10.1038/s41598-025-10850-0 · Cited by 3 · see citing works

Classifying the risk of cognitive impairment in Parkinson’s disease using serum bile acid profiles and machine learning

Shen, T., Cui, C., Liu, R., Yin, X., Zu, J., Zhang, W., Dong, L., Xu, C., Lu, H., Cui, G., et al. (2025) · npj Parkinson s Disease · doi:10.1038/s41531-025-01229-z · Cited by 2 · see citing works

Metabolomic Biomarkers in Parkinson’s Disease

Shao, Y., Xu, X., Wang, N., Xu, G., & Le, W. (2021) · Neuromethods · doi:10.1007/978-1-0716-1712-0_8 · Cited by 2 · see citing works

Novel insight into the etiology of ischemic stroke gained by integrative transcriptome-wide association studyPreprint

Jung, J., Lu, Z., de Smith, A. J., & Mancuso, N. (2023) · medRxiv · doi:10.1101/2023.03.30.23287918 · Cited by 2 · see citing works

Modulation of the JNK/c-Jun/HSP27 pathway in cardiomyocytes under chronic stress-induced cardiac dysfunction: Therapeutic implications of Tauroursodeoxycholic acid

Zhou, H., Yuan, J., Chen, X., Li, Z., Wu, H., Shi, H., Wu, X., Huang, J. L., & Huang, F. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.10.292 · Cited by 1 · see citing works

Combination Disease‐Modifying Therapy for Neurodegenerative Diseases Using Repurposed Drugs

Shtilbans, A., & Lang, A. E. (2026) · Annals of Neurology · doi:10.1002/ana.78190 · Cited by 1 · see citing works

Modulation of Cell Fate by Tauroursodeoxycholic Acid: All Paths Lead to Mitochondria

Solá, S., Ribeiro, M. F., Genebra, T., & Rodrigues, C. M. P. (2018) · Springer eBooks · doi:10.1007/978-3-319-73344-9_19 · Cited by 1 · see citing works

Corrigendum to “Neurotoxic effects of MPTP on mouse cerebral cortex: Modulation of neuroinflammation as a neuroprotective strategy” [Mol. Cell. Neurosci., Volume 96, April 2019, Pages 1–9.]

Mendes, M. O., Rosa, A. I., Carvalho, A. N., Nunes, M. J., Dionísio, P. A., Rodrigues, E., Costa, D., Duarte‐Silva, S., Maciel, P., Rodrigues, C. M. P., et al. (2021) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2021.103626

Papel do ácido biliar TUDCA no metabolismo glicêmico e energético de camundongos modelo experimental da doença de Alzheimer

Zangerolamo, L. (2021) · doi:10.47749/t/unicamp.2021.1162174

Combined Treatment with Tauroursodeoxycholic Acid and SCD Probiotics Reduces Oxidative Stress in Lung Tissue of Aged Rats

Baba, B., & Allahverdi, H. (2024) · Bitlis Eren Üniversitesi Fen Bilimleri Dergisi · doi:10.17798/bitlisfen.1472539

Reduced cerebrospinal fluid taurine is associated with nigrostriatal dopaminergic deficits in drug-naïve Parkinson’s disease

Mimori, M., Umehara, T., Takatsu, H., Okumura, M., Masui, M., Kida, H., Ozawa, M., Motegi, H., Onda, A., Matsuno, H., et al. (2025) · Journal of Neural Transmission · doi:10.1007/s00702-025-03027-6

Exploring the complex role of protein glycosylation in the pathogenesis of Parkinson’s disease

Carvalho, A. N., Nunes, M. J., Gama, M. J., Rodrigues, E., Videira, P. A., & Castro‐Caldas, M. (2025) · Royal Society of Chemistry eBooks · doi:10.1039/9781837676101-00062

Tauroursodeoxycholic acid alleviates depression-like behavior induced by chronic unpredictable mild stress through amelioration of catecholamine imbalance

Spasojević, N., Stefanović, B., Ferizović, H., Janković, M., Virijević, K., Contos, A., & Dronjak, S. (2026) · Brain Research · doi:10.1016/j.brainres.2026.150188

Comparative Network Pharmacology and Molecular Docking Analysis of Ursodeoxycholic Acid and Tauroursodeoxycholic Acid in Alzheimer’s Disease-Associated Molecular Networks

Zhou, B., Zhong, Y., Meng, X., Xu, B., & Jia, L. (2026) · Pharmaceuticals · doi:10.3390/ph19101512

Tauroursodeoxycholic acid (TUDCA) is neuroprotective in a chronic mouse model of Parkinson’s disease

Cuevas, E., Burks, S., Raymick, J., Robinson, B., Gómez-Crisóstomo, N. P., Escudero-Lourdes, C., Lopez, A. G. G., Chigurupati, S., Hanig, J., Ferguson, S. A., et al. (2022) · Nutritional Neuroscience · doi:10.1080/1028415x.2020.1859729 · Cited by 57 · see citing works

Tauroursodeoxycholic acid prevents MPTP-induced dopaminergic cell death in a mouse model of Parkinson's disease

Castro-Caldas, M., Carvalho, A. N., Rodrigues, E., Henderson, C. J., Wolf, C. R., Rodrigues, C. M. P., & Gama, M. J. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8295-4 · Cited by 156 · see citing works

Tauroursodeoxycholic Acid Protects Against Mitochondrial Dysfunction and Cell Death via Mitophagy in Human Neuroblastoma Cells

Fonseca, I., Gordino, G., Moreira, S., Nunes, M. J., Azevedo, C., Gama, M. J., Rodrigues, E., Rodrigues, C. M. P., & Castro‐Caldas, M. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0145-3 · Cited by 52 · see citing works

Ursodeoxycholic acid protects dopaminergic neurons from oxidative stress via regulating mitochondrial function, autophagy, and apoptosis in MPTP/MPP+-induced Parkinson’s disease

Qi, H., Shen, D., Jiang, C., Wang, H., & Chang, M. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2020.135493 · Cited by 76 · see citing works

Tauroursodeoxycholic acid improves motor symptoms in a mouse model of Parkinson's disease

Rosa, A. I., Duarte-Silva, S., Silva-Fernandes, A., Nunes, M. J., Carvalho, A. N., Rodrigues, E., Gama, M. J., Rodrigues, C. M. P., Maciel, P., & Castro-Caldas, M. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1062-4 · Cited by 94 · see citing works