{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,20]],"date-time":"2026-07-20T11:42:12Z","timestamp":1784547732228,"version":"3.55.0"},"reference-count":206,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2025,3,26]],"date-time":"2025-03-26T00:00:00Z","timestamp":1742947200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32270739"],"award-info":[{"award-number":["32270739"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Neurodegenerative diseases (NDDs), including Alzheimer\u2019s disease (AD), Parkinson\u2019s disease (PD), amyotrophic lateral sclerosis (ALS), Huntington\u2019s disease (HD), and prion disease, represent a group of age-related disorders that pose a growing and formidable challenge to global health. Despite decades of extensive research that has uncovered key genetic factors and biochemical pathways, the precise molecular mechanisms underlying these diseases and effective therapeutic strategies remain elusive. Caenorhabditis elegans (C. elegans) has emerged as a powerful model organism for studying NDDs due to its unique biological features such as genetic tractability, conserved molecular pathways, and ease of high-throughput screening. This model provides an exceptional platform for identifying molecular targets associated with NDDs and developing novel therapeutic interventions. This review highlights the critical role of C. elegans in elucidating the complex molecular mechanisms of human NDDs, with a particular focus on recent advancements and its indispensable contributions to the discovery of molecular targets and therapeutic strategies for these NDDs.<\/jats:p>","DOI":"10.3390\/ijms26073030","type":"journal-article","created":{"date-parts":[[2025,3,26]],"date-time":"2025-03-26T09:13:26Z","timestamp":1742980406000},"page":"3030","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Unraveling Molecular Targets for Neurodegenerative Diseases Through Caenorhabditis elegans Models"],"prefix":"10.3390","volume":"26","author":[{"given":"Rongmei","family":"Xu","sequence":"first","affiliation":[{"name":"School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230002, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qiaoju","family":"Kang","sequence":"additional","affiliation":[{"name":"Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xuefei","family":"Yang","sequence":"additional","affiliation":[{"name":"School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230002, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6954-102X","authenticated-orcid":false,"given":"Ping","family":"Yi","sequence":"additional","affiliation":[{"name":"Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rongying","family":"Zhang","sequence":"additional","affiliation":[{"name":"Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,3,26]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Wu, Y., Chen, Y., Yu, X., Zhang, M., and Li, Z. (2023). Towards Understanding Neurodegenerative Diseases: Insights from Caenorhabditis elegans. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25010443"},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Cheslow, L., Snook, A.E., and Waldman, S.A. (2024). Biomarkers for Managing Neurodegenerative Diseases. Biomolecules, 14.","DOI":"10.20944\/preprints202403.0247.v1"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"2665","DOI":"10.1021\/acschemneuro.4c00184","article-title":"Polyglutamine (PolyQ) Diseases: Navigating the Landscape of Neurodegeneration","volume":"15","author":"Tenchov","year":"2024","journal-title":"ACS Chem. Neurosci."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1271","DOI":"10.1080\/14728222.2023.2199923","article-title":"Human prion disease: Molecular pathogenesis, and possible therapeutic targets and strategies","volume":"27","author":"Baiardi","year":"2023","journal-title":"Expert. Opin. Ther. Targets"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"25168657221135848","DOI":"10.1177\/25168657221135848","article-title":"The Neuroepigenetic Landscape of Vertebrate and Invertebrate Models of Neurodegenerative Diseases","volume":"15","author":"Sundaramoorthy","year":"2022","journal-title":"Epigenet. Insights"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"102036","DOI":"10.1016\/j.arr.2023.102036","article-title":"Caenorhabditis elegans: A transgenic model for studying age-associated neurodegenerative diseases","volume":"91","author":"Rani","year":"2023","journal-title":"Ageing Res. Rev."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1093\/genetics\/77.1.71","article-title":"The genetics of Caenorhabditis elegans","volume":"77","author":"Brenner","year":"1974","journal-title":"Genetics"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1101\/gr.10.5.703","article-title":"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics","volume":"10","author":"Lai","year":"2000","journal-title":"Genome Res."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1038\/s41586-019-1352-7","article-title":"Whole-animal connectomes of both Caenorhabditis elegans sexes","volume":"571","author":"Cook","year":"2019","journal-title":"Nature"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1098\/rstb.1986.0056","article-title":"The structure of the nervous system of the nematode Caenorhabditis elegans","volume":"314","author":"White","year":"1986","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Roussos, A., Kitopoulou, K., Borbolis, F., and Palikaras, K. (2023). Caenorhabditis elegans as a Model System to Study Human Neurodegenerative Disorders. Biomolecules, 13.","DOI":"10.3390\/biom13030478"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1016\/j.cell.2013.08.001","article-title":"Serotonin and the neuropeptide PDF initiate and extend opposing behavioral states in C. elegans","volume":"154","author":"Flavell","year":"2013","journal-title":"Cell"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1186\/s13065-015-0143-y","article-title":"Using C. elegans to discover therapeutic compounds for ageing-associated neurodegenerative diseases","volume":"9","author":"Chen","year":"2015","journal-title":"Chem. Cent. J."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Ikenaka, K., Tsukada, Y., Giles, A.C., Arai, T., Nakadera, Y., Nakano, S., Kawai, K., Mochizuki, H., Katsuno, M., and Sobue, G. (2019). A behavior-based drug screening system using a Caenorhabditis elegans model of motor neuron disease. Sci. Rep., 9.","DOI":"10.1038\/s41598-019-46642-6"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"119857","DOI":"10.1016\/j.cca.2024.119857","article-title":"Biomarkers in Alzheimer\u2019s disease","volume":"562","author":"Rajendran","year":"2024","journal-title":"Clin. Chim. Acta"},{"key":"ref_16","first-page":"1598","article-title":"Alzheimer\u2019s disease facts and figures","volume":"19","author":"Better","year":"2023","journal-title":"Alzheimer\u2019s Dement."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Andrade-Guerrero, J., Santiago-Balmaseda, A., Jeronimo-Aguilar, P., Vargas-Rodriguez, I., Cadena-Suarez, A.R., Sanchez-Garibay, C., Pozo-Molina, G., Mendez-Catala, C.F., Cardenas-Aguayo, M.D., and Diaz-Cintra, S. (2023). Alzheimer\u2019s Disease: An Updated Overview of Its Genetics. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24043754"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1016\/j.ijbiomac.2020.11.192","article-title":"Review on Alzheimer\u2019s disease: Inhibition of amyloid beta and tau tangle formation","volume":"167","author":"Ashrafian","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Alvarez, J., Alvarez-Illera, P., Santo-Domingo, J., Fonteriz, R.I., and Montero, M. (2022). Modeling Alzheimer\u2019s Disease in Caenorhabditis elegans. Biomedicines, 10.","DOI":"10.3390\/biomedicines10020288"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1074\/jbc.M112.419135","article-title":"Interplay between alpha-, beta-, and gamma-secretases determines biphasic amyloid-beta protein level in the presence of a gamma-secretase inhibitor","volume":"288","author":"Ortega","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1248\/yakushi.15-00189","article-title":"Molecular Pathogenesis of Sporadic Alzheimer\u2019s Disease (AD) and Pharmaceutical Research to Develop a Biomarker for AD Diagnosis","volume":"135","author":"Hata","year":"2015","journal-title":"Yakugaku Zasshi"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"2674","DOI":"10.1111\/febs.12813","article-title":"The coexistence of an equal amount of Alzheimer\u2019s amyloid-beta 40 and 42 forms structurally stable and toxic oligomers through a distinct pathway","volume":"281","author":"Chang","year":"2014","journal-title":"FEBS J."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"9368","DOI":"10.1073\/pnas.92.20.9368","article-title":"Expression of human beta-amyloid peptide in transgenic Caenorhabditis elegans","volume":"92","author":"Link","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.ejmech.2019.03.009","article-title":"Therapeutic potentials of plant iridoids in Alzheimer\u2019s and Parkinson\u2019s diseases: A review","volume":"169","author":"Dinda","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"17669","DOI":"10.1073\/pnas.1205748109","article-title":"O-GlcNAc cycling mutants modulate proteotoxicity in Caenorhabditis elegans models of human neurodegenerative diseases","volume":"109","author":"Wang","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1007\/s00401-016-1634-1","article-title":"eEF2K inhibition blocks Abeta42 neurotoxicity by promoting an NRF2 antioxidant response","volume":"133","author":"Jan","year":"2017","journal-title":"Acta Neuropathol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1074\/jbc.M703339200","article-title":"Suppression of in vivo beta-amyloid peptide toxicity by overexpression of the HSP-16.2 small chaperone protein","volume":"283","author":"Fonte","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1808","DOI":"10.1074\/jbc.M505581200","article-title":"Conversion of green fluorescent protein into a toxic, aggregation-prone protein by C-terminal addition of a short peptide","volume":"281","author":"Link","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.neurobiolaging.2023.09.015","article-title":"Role and molecular regulatory mechanisms of Hippo signaling pathway in Caenorhabditis elegans and mammalian cell models of Alzheimer\u2019s disease","volume":"134","author":"Zhu","year":"2024","journal-title":"Neurobiol. Aging"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"569","DOI":"10.4161\/auto.4776","article-title":"Decreased insulin-receptor signaling promotes the autophagic degradation of beta-amyloid peptide in C. elegans","volume":"3","author":"Hohsfield","year":"2007","journal-title":"Autophagy"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"9415","DOI":"10.1021\/bi952646n","article-title":"ptl-1, a Caenorhabditis elegans gene whose products are homologous to the tau microtubule-associated proteins","volume":"35","author":"McDermott","year":"1996","journal-title":"Biochemistry"},{"key":"ref_32","first-page":"2079","article-title":"PTL-1 regulates neuronal integrity and lifespan in C. elegans","volume":"126","author":"Chew","year":"2013","journal-title":"J. Cell Sci."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Natale, C., Barzago, M.M., and Diomede, L. (2020). Caenorhabditis elegans Models to Investigate the Mechanisms Underlying Tau Toxicity in Tauopathies. Brain Sci., 10.","DOI":"10.3390\/brainsci10110838"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"9980","DOI":"10.1073\/pnas.1533448100","article-title":"Neurodegeneration and defective neurotransmission in a Caenorhabditis elegans model of tauopathy","volume":"100","author":"Kraemer","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1016\/j.nbd.2005.03.017","article-title":"Progressive neurodegeneration in C. elegans model of tauopathy","volume":"20","author":"Miyasaka","year":"2005","journal-title":"Neurobiol. Dis."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.neurobiolaging.2007.05.011","article-title":"A Caenorhabditis elegans model of tau hyperphosphorylation: Induction of developmental defects by transgenic overexpression of Alzheimer\u2019s disease-like modified tau","volume":"30","author":"Brandt","year":"2009","journal-title":"Neurobiol. Aging"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"449","DOI":"10.2174\/156720506779025279","article-title":"The role of tau phosphorylation in the pathogenesis of Alzheimer\u2019s disease","volume":"3","author":"Mi","year":"2006","journal-title":"Curr. Alzheimer Res."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1038\/ncomms1255","article-title":"The acetylation of tau inhibits its function and promotes pathological tau aggregation","volume":"2","author":"Cohen","year":"2011","journal-title":"Nat. Commun."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1154","DOI":"10.1038\/nm.3951","article-title":"Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits","volume":"21","author":"Min","year":"2015","journal-title":"Nat. Med."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1007\/s004010100423","article-title":"Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer\u2019s disease","volume":"103","author":"Augustinack","year":"2002","journal-title":"Acta Neuropathol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1186\/s13024-020-00410-7","article-title":"Tauopathy-associated tau modifications selectively impact neurodegeneration and mitophagy in a novel C. elegans single-copy transgenic model","volume":"15","author":"Guha","year":"2020","journal-title":"Mol. Neurodegener."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"dmm050473","DOI":"10.1242\/dmm.050473","article-title":"Transgenic Dendra2::tau expression allows in vivo monitoring of tau proteostasis in Caenorhabditis elegans","volume":"17","author":"Han","year":"2024","journal-title":"Dis. Model. Mech."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/j.nbd.2017.10.003","article-title":"Human amyloid beta peptide and tau co-expression impairs behavior and causes specific gene expression changes in Caenorhabditis elegans","volume":"109","author":"Wang","year":"2018","journal-title":"Neurobiol. Dis."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1959","DOI":"10.1093\/hmg\/ddm143","article-title":"SUT-1 enables tau-induced neurotoxicity in C. elegans","volume":"16","author":"Kraemer","year":"2007","journal-title":"Hum. Mol. Genet."},{"key":"ref_45","unstructured":"Currey, H.N., Kraemer, B.C., and Liachko, N.F. (2023). sut-2 loss of function mutants protect against tau-driven shortened lifespan and hyperactive pharyngeal pumping in a C. elegans model of tau toxicity. MicroPubl. Biol., 2023."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1825","DOI":"10.1093\/hmg\/ddp099","article-title":"SUT-2 potentiates tau-induced neurotoxicity in Caenorhabditis elegans","volume":"18","author":"Guthrie","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"2292","DOI":"10.1093\/hmg\/ddad049","article-title":"Sut-6\/NIPP1 modulates tau toxicity","volume":"32","author":"Kow","year":"2023","journal-title":"Hum. Mol. Genet."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1007\/s11357-022-00526-2","article-title":"Loss of aly\/ALYREF suppresses toxicity in both tau and TDP-43 models of neurodegeneration","volume":"44","author":"Kow","year":"2022","journal-title":"Geroscience"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"e2207250120","DOI":"10.1073\/pnas.2207250120","article-title":"SPOP loss of function protects against tauopathy","volume":"120","author":"Eck","year":"2023","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"10965","DOI":"10.1093\/nar\/gkae705","article-title":"Loss of DNA glycosylases improves health and cognitive function in a C. elegans model of human tauopathy","volume":"52","author":"Tiwari","year":"2024","journal-title":"Nucleic. Acids Res."},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Vidovic, M., and Rikalovic, M.G. (2022). Alpha-Synuclein Aggregation Pathway in Parkinson\u2019s Disease: Current Status and Novel Therapeutic Approaches. Cells, 11.","DOI":"10.3390\/cells11111732"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1146\/annurev-pathmechdis-031521-034145","article-title":"Genetics and Pathogenesis of Parkinson\u2019s Syndrome","volume":"18","author":"Ye","year":"2023","journal-title":"Annu. Rev. Pathol."},{"key":"ref_53","first-page":"1","article-title":"The clinical diagnosis of Parkinson\u2019s disease","volume":"82","author":"Munhoz","year":"2024","journal-title":"Arq. Neuropsiquiatr."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1007\/s12640-024-00686-3","article-title":"Exploring Caenorhabditis elegans as Parkinson\u2019s Disease Model: Neurotoxins and Genetic Implications","volume":"42","author":"Fernandes","year":"2024","journal-title":"Neurotox. Res."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"3033","DOI":"10.2174\/1381612828666220915103502","article-title":"Modelling Parkinson\u2019s Disease in C. elegans: Strengths and Limitations","volume":"28","author":"Ma","year":"2022","journal-title":"Curr. Pharm. Des."},{"key":"ref_56","first-page":"17","article-title":"Modeling Parkinson\u2019s Disease in C. elegans","volume":"8","author":"Cooper","year":"2018","journal-title":"J. Park. Dis."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Kawahata, I., Finkelstein, D.I., and Fukunaga, K. (2022). Pathogenic Impact of alpha-Synuclein Phosphorylation and Its Kinases in alpha-Synucleinopathies. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23116216"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"2308","DOI":"10.1021\/acschembio.8b00466","article-title":"Multistep Inhibition of alpha-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine","volume":"13","author":"Perni","year":"2018","journal-title":"ACS Chem. Biol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1038\/s41419-019-2092-1","article-title":"A split-GFP tool reveals differences in the sub-mitochondrial distribution of wt and mutant alpha-synuclein","volume":"10","author":"Vicario","year":"2019","journal-title":"Cell Death Dis."},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Asthana, J., and Shravage, B.V. (2022). Exploring therapeutic potential of mitophagy modulators using Drosophila models of Parkinson\u2019s disease. Front. Aging Neurosci., 14.","DOI":"10.3389\/fnagi.2022.986849"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1046\/j.1471-4159.2003.01809.x","article-title":"Dopaminergic neuronal loss and motor deficits in Caenorhabditis elegans overexpressing human alpha-synuclein","volume":"86","author":"Lakso","year":"2003","journal-title":"J. Neurochem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"728","DOI":"10.1073\/pnas.0711018105","article-title":"Hypothesis-based RNAi screening identifies neuroprotective genes in a Parkinson\u2019s disease model","volume":"105","author":"Hamamichi","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1126\/science.1129462","article-title":"Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson\u2019s models","volume":"313","author":"Cooper","year":"2006","journal-title":"Science"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/1756-6606-1-17","article-title":"Lysosomal enzyme cathepsin D protects against alpha-synuclein aggregation and toxicity","volume":"1","author":"Qiao","year":"2008","journal-title":"Mol. Brain"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"e2","DOI":"10.1038\/cddis.2009.4","article-title":"Differential neuroprotective effects of 14-3-3 proteins in models of Parkinson\u2019s disease","volume":"1","author":"Yacoubian","year":"2010","journal-title":"Cell Death Dis."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"7533","DOI":"10.1007\/s12035-018-0881-7","article-title":"The Small GTPase RAC1\/CED-10 Is Essential in Maintaining Dopaminergic Neuron Function and Survival Against alpha-Synuclein-Induced Toxicity","volume":"55","author":"Kim","year":"2018","journal-title":"Mol. Neurobiol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.cmet.2014.04.017","article-title":"The glycolytic enzyme, GPI, is a functionally conserved modifier of dopaminergic neurodegeneration in Parkinson\u2019s models","volume":"20","author":"Knight","year":"2014","journal-title":"Cell Metab."},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Cooper, J.F., Machiela, E., Dues, D.J., Spielbauer, K.K., Senchuk, M.M., and Van Raamsdonk, J.M. (2017). Activation of the mitochondrial unfolded protein response promotes longevity and dopamine neuron survival in Parkinson\u2019s disease models. Sci. Rep., 7.","DOI":"10.1038\/s41598-017-16637-2"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"11085","DOI":"10.1523\/JNEUROSCI.1294-17.2017","article-title":"Dysregulation of the Mitochondrial Unfolded Protein Response Induces Non-Apoptotic Dopaminergic Neurodegeneration in C. elegans Models of Parkinson\u2019s Disease","volume":"37","author":"Martinez","year":"2017","journal-title":"J. Neurosci."},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Gaeta, A.L., Caldwell, K.A., and Caldwell, G.A. (2019). Found in Translation: The Utility of C. elegans Alpha-Synuclein Models of Parkinson\u2019s Disease. Brain Sci., 9.","DOI":"10.3390\/brainsci9040073"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/S0002-9440(10)61700-2","article-title":"A close association of torsinA and alpha-synuclein in Lewy bodies: A fluorescence resonance energy transfer study","volume":"159","author":"Sharma","year":"2001","journal-title":"Am. J. Pathol."},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Tyson, T., Senchuk, M., Cooper, J.F., George, S., Van Raamsdonk, J.M., and Brundin, P. (2017). Novel animal model defines genetic contributions for neuron-to-neuron transfer of alpha-synuclein. Sci. Rep., 7.","DOI":"10.1038\/s41598-017-07383-6"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"16076","DOI":"10.1523\/JNEUROSCI.1945-14.2014","article-title":"RTCB-1 mediates neuroprotection via XBP-1 mRNA splicing in the unfolded protein response pathway","volume":"34","author":"Ray","year":"2014","journal-title":"J. Neurosci."},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Starr, L.A., McKay, L.E., Peter, K.N., Seyfarth, L.M., Berkowitz, L.A., Caldwell, K.A., and Caldwell, G.A. (2023). Attenuation of Dopaminergic Neurodegeneration in a C. elegans Parkinson\u2019s Model through Regulation of Xanthine Dehydrogenase (XDH-1) Expression by the RNA Editase, ADR-2. J. Dev. Biol., 11.","DOI":"10.20944\/preprints202303.0230.v1"},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Kumar, L., and Nazir, A. (2017). Modulation of Alpha-synuclein Expression and Associated Effects by MicroRNA Let-7 in Transgenic C. elegans. Front. Mol. Neurosci., 10.","DOI":"10.3389\/fnmol.2017.00328"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"243","DOI":"10.5483\/BMBRep.2015.48.5.032","article-title":"Function and dysfunction of leucine-rich repeat kinase 2 (LRRK2): Parkinson\u2019s disease and beyond","volume":"48","author":"Bae","year":"2015","journal-title":"BMB Rep."},{"key":"ref_77","doi-asserted-by":"crossref","unstructured":"Seegobin, S.P., Heaton, G.R., Liang, D., Choi, I., Blanca Ramirez, M., Tang, B., and Yue, Z. (2020). Progress in LRRK2-Associated Parkinson\u2019s Disease Animal Models. Front. Neurosci., 14.","DOI":"10.3389\/fnins.2020.00674"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1016\/j.cub.2007.01.074","article-title":"LRK-1, a C. elegans PARK8-related kinase, regulates axonal-dendritic polarity of SV proteins","volume":"17","author":"Meir","year":"2007","journal-title":"Curr. Biol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/B978-0-323-85555-6.00018-7","article-title":"LRRK2: Genetic mechanisms vs genetic subtypes","volume":"193","author":"Mata","year":"2023","journal-title":"Handb. Clin. Neurol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"16482","DOI":"10.1074\/jbc.M808255200","article-title":"Caenorhabditits elegans LRK-1 and PINK-1 act antagonistically in stress response and neurite outgrowth","volume":"284","author":"Samann","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.nbd.2010.04.002","article-title":"LRRK2-mediated neurodegeneration and dysfunction of dopaminergic neurons in a Caenorhabditis elegans model of Parkinson\u2019s disease","volume":"40","author":"Yao","year":"2010","journal-title":"Neurobiol. Dis."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1093\/hmg\/dds431","article-title":"Kinase inhibitors arrest neurodegeneration in cell and C. elegans models of LRRK2 toxicity","volume":"22","author":"Yao","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1186\/s13024-015-0022-y","article-title":"Mutations in LRRK2 potentiate age-related impairment of autophagic flux","volume":"10","author":"Saha","year":"2015","journal-title":"Mol. Neurodegener."},{"key":"ref_84","doi-asserted-by":"crossref","unstructured":"Chandler, R.J., Cogo, S., Lewis, P.A., and Kevei, E. (2021). Modelling the functional genomics of Parkinson\u2019s disease in Caenorhabditis elegans: LRRK2 and beyond. Biosci. Rep., 41.","DOI":"10.1042\/BSR20203672"},{"key":"ref_85","doi-asserted-by":"crossref","unstructured":"Senchuk, M.M., Van Raamsdonk, J.M., and Moore, D.J. (2021). Multiple genetic pathways regulating lifespan extension are neuroprotective in a G2019S LRRK2 nematode model of Parkinson\u2019s disease. Neurobiol. Dis., 151.","DOI":"10.1016\/j.nbd.2021.105267"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"3465","DOI":"10.1038\/s41467-018-05958-z","article-title":"LRRK2 kinase regulates alpha-synuclein propagation via RAB35 phosphorylation","volume":"9","author":"Bae","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"e984","DOI":"10.1038\/cddis.2013.513","article-title":"Mitochondrial dysfunction, oxidative stress, and neurodegeneration elicited by a bacterial metabolite in a C. elegans Parkinson\u2019s model","volume":"5","author":"Ray","year":"2014","journal-title":"Cell Death Dis."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1080\/15622975.2021.1925585","article-title":"14-3-3 proteins at the crossroads of neurodevelopment and schizophrenia","volume":"23","author":"Antunes","year":"2022","journal-title":"World J. Biol. Psychiatry"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.tcb.2008.10.003","article-title":"The 14-3-3 proteins: Integrators of diverse signaling cues that impact cell fate and cancer development","volume":"19","author":"Morrison","year":"2009","journal-title":"Trends Cell Biol."},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"Fan, X., Cui, L., Zeng, Y., Song, W., Gaur, U., and Yang, M. (2019). 14-3-3 Proteins Are on the Crossroads of Cancer, Aging, and Age-Related Neurodegenerative Disease. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20143518"},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Long, S., Guo, W., Hu, S., Su, F., Zeng, Y., Zeng, J., Tan, E.K., Ross, C.A., and Pei, Z. (2018). G2019S LRRK2 Increases Stress Susceptibility Through Inhibition of DAF-16 Nuclear Translocation in a 14-3-3 Associated-Manner in Caenorhabditis elegans. Front. Neurosci., 12.","DOI":"10.3389\/fnins.2018.00782"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1093\/hmg\/ddu542","article-title":"Glutaredoxin deficiency exacerbates neurodegeneration in C. elegans models of Parkinson\u2019s disease","volume":"24","author":"Johnson","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1016\/j.ijpara.2023.08.002","article-title":"microRNA silencing in a whole worm cestode model provides insight into miR-71 function","volume":"53","author":"Grecco","year":"2023","journal-title":"Int. J. Parasitol."},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Naidoo, D., and de Lencastre, A. (2024). Regulation of TIR-1\/SARM-1 by miR-71 Protects Dopaminergic Neurons in a C. elegans Model of LRRK2-Induced Parkinson\u2019s Disease. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25168795"},{"key":"ref_95","first-page":"533","article-title":"The 6-hydroxydopamine model and parkinsonian pathophysiology: Novel findings in an older model","volume":"32","year":"2017","journal-title":"Neurologia"},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Chia, S.J., Tan, E.K., and Chao, Y.X. (2020). Historical Perspective: Models of Parkinson\u2019s Disease. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21072464"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1282","DOI":"10.1002\/dvdy.22231","article-title":"C. elegans as a model organism to investigate molecular pathways involved with Parkinson\u2019s disease","volume":"239","author":"Harrington","year":"2010","journal-title":"Dev. Dyn."},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Hsu, Y.L., Hung, H.S., Tsai, C.W., Liu, S.P., Chiang, Y.T., Kuo, Y.H., Shyu, W.C., Lin, S.Z., and Fu, R.H. (2021). Peiminine Reduces ARTS-Mediated Degradation of XIAP by Modulating the PINK1\/Parkin Pathway to Ameliorate 6-Hydroxydopamine Toxicity and alpha-Synuclein Accumulation in Parkinson\u2019s Disease Models In Vivo and In Vitro. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms221910240"},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Offenburger, S.L., and Gartner, A. (2018). 6-hydroxydopamine (6-OHDA) Oxidative Stress Assay for Observing Dopaminergic Neuron Loss in Caenorhabditis elegans. Bio-Protocol, 8.","DOI":"10.21769\/BioProtoc.3025"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"176819","DOI":"10.1016\/j.ejphar.2024.176819","article-title":"Experimental models of Parkinson\u2019s disease: Challenges and Opportunities","volume":"980","author":"Lal","year":"2024","journal-title":"Eur. J. Pharmacol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1166","DOI":"10.1007\/s00044-021-02720-x","article-title":"Dual monoamine oxidase B and acetylcholine esterase inhibitors for treating movement and cognition deficits in a C. elegans model of Parkinson\u2019s disease","volume":"30","author":"Boos","year":"2021","journal-title":"Med. Chem. Res."},{"key":"ref_102","doi-asserted-by":"crossref","unstructured":"Offenburger, S.L., Jongsma, E., and Gartner, A. (2018). Mutations in Caenorhabditis elegans neuroligin-like glit-1, the apoptosis pathway and the calcium chaperone crt-1 increase dopaminergic neurodegeneration after 6-OHDA treatment. PLoS Genet., 14.","DOI":"10.1371\/journal.pgen.1007106"},{"key":"ref_103","doi-asserted-by":"crossref","unstructured":"Offenburger, S.L., Ho, X.Y., Tachie-Menson, T., Coakley, S., Hilliard, M.A., and Gartner, A. (2018). 6-OHDA-induced dopaminergic neurodegeneration in Caenorhabditis elegans is promoted by the engulfment pathway and inhibited by the transthyretin-related protein TTR-33. PLoS Genet., 14.","DOI":"10.1371\/journal.pgen.1007125"},{"key":"ref_104","doi-asserted-by":"crossref","unstructured":"Hu, K., Zhu, S., Wu, F., Zhang, Y., Li, M., Yuan, L., Huang, W., Zhang, Y., Wang, J., and Ren, J. (2024). Aureusidin ameliorates 6-OHDA-induced neurotoxicity via activating Nrf2\/HO-1 signaling pathway and preventing mitochondria-dependent apoptosis pathway in SH-SY5Y cells and Caenorhabditis elegans. Chem. Biol. Interact., 387.","DOI":"10.1016\/j.cbi.2023.110824"},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Chen, Q.X., Zhou, L., Long, T., Qin, D.L., Wang, Y.L., Ye, Y., Zhou, X.G., Wu, J.M., and Wu, A.G. (2022). Galangin Exhibits Neuroprotective Effects in 6-OHDA-Induced Models of Parkinson\u2019s Disease via the Nrf2\/Keap1 Pathway. Pharmaceuticals, 15.","DOI":"10.3390\/ph15081014"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"114617","DOI":"10.1016\/j.taap.2019.114617","article-title":"Tricetin protects against 6-OHDA-induced neurotoxicity in Parkinson\u2019s disease model by activating Nrf2\/HO-1 signaling pathway and preventing mitochondria-dependent apoptosis pathway","volume":"378","author":"Ren","year":"2019","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_107","doi-asserted-by":"crossref","unstructured":"Morton, K.S., Hartman, J.H., Heffernan, N., Ryde, I.T., Kenny-Ganzert, I.W., Meng, L., Sherwood, D.R., and Meyer, J.N. (2023). Chronic high-sugar diet in adulthood protects Caenorhabditis elegans from 6-OHDA-induced dopaminergic neurodegeneration. BMC Biol., 21.","DOI":"10.1186\/s12915-023-01733-9"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/j.jocn.2017.08.035","article-title":"Military service and the risk of amyotrophic lateral sclerosis: A meta-analysis","volume":"45","author":"Tai","year":"2017","journal-title":"J. Clin. Neurosci."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"2084","DOI":"10.1016\/S0140-6736(17)31287-4","article-title":"Amyotrophic lateral sclerosis","volume":"390","author":"Hardiman","year":"2017","journal-title":"Lancet"},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Eck, R.J., Stair, J.G., Kraemer, B.C., and Liachko, N.F. (2023). Simple models to understand complex disease: 10 years of progress from Caenorhabditis elegans models of amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Front. Neurosci., 17.","DOI":"10.3389\/fnins.2023.1300705"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"e669","DOI":"10.1212\/NXG.0000000000000669","article-title":"Progress in Amyotrophic Lateral Sclerosis Gene Discovery: Reflecting on Classic Approaches and Leveraging Emerging Technologies","volume":"8","author":"Smukowski","year":"2022","journal-title":"Neurol. Genet."},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Zhou, L., and Xu, R. (2024). Invertebrate genetic models of amyotrophic lateral sclerosis. Front. Mol. Neurosci., 17.","DOI":"10.3389\/fnmol.2024.1328578"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1038\/362059a0","article-title":"Mutations in Cu\/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis","volume":"362","author":"Rosen","year":"1993","journal-title":"Nature"},{"key":"ref_114","doi-asserted-by":"crossref","unstructured":"Bernard, E., Pegat, A., Svahn, J., Bouhour, F., Leblanc, P., Millecamps, S., Thobois, S., Guissart, C., Lumbroso, S., and Mouzat, K. (2020). Clinical and Molecular Landscape of ALS Patients with SOD1 Mutations: Novel Pathogenic Variants and Novel Phenotypes. A Single ALS Center Study. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21186807"},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Wei, Q., Zhou, Q., Chen, Y., Ou, R., Cao, B., Xu, Y., Yang, J., and Shang, H.F. (2017). Analysis of SOD1 mutations in a Chinese population with amyotrophic lateral sclerosis: A case-control study and literature review. Sci. Rep., 7.","DOI":"10.1038\/srep44606"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1136\/jmedgenet-2021-107965","article-title":"Role of genetics in amyotrophic lateral sclerosis: A large cohort study in Chinese mainland population","volume":"59","author":"Chen","year":"2022","journal-title":"J. Med. Genet."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/s40035-015-0036-y","article-title":"Genotype-phenotype relationship in hereditary amyotrophic lateral sclerosis","volume":"4","author":"Yamashita","year":"2015","journal-title":"Transl. Neurodegener."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"1196","DOI":"10.1016\/j.bbrc.2015.06.084","article-title":"Cysteine residues in Cu,Zn-superoxide dismutase are essential to toxicity in Caenorhabditis elegans model of amyotrophic lateral sclerosis","volume":"463","author":"Ogawa","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"2013","DOI":"10.1093\/hmg\/10.19.2013","article-title":"Oxidative stress causes abnormal accumulation of familial amyotrophic lateral sclerosis-related mutant SOD1 in transgenic Caenorhabditis elegans","volume":"10","author":"Oeda","year":"2001","journal-title":"Hum. Mol. Genet."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.freeradbiomed.2022.01.030","article-title":"Activation of autophagy attenuates motor deficits and extends lifespan in a C. elegans model of ALS","volume":"181","author":"Xu","year":"2022","journal-title":"Free. Radic. Biol. Med."},{"key":"ref_121","doi-asserted-by":"crossref","unstructured":"Boccitto, M., Lamitina, T., and Kalb, R.G. (2012). Daf-2 signaling modifies mutant SOD1 toxicity in C. elegans. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0033494"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1038\/aps.2012.190","article-title":"Establishing a novel C. elegans model to investigate the role of autophagy in amyotrophic lateral sclerosis","volume":"34","author":"Li","year":"2013","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1038\/cdd.2012.19","article-title":"Reduced expression of BTBD10, an Akt activator, leads to motor neuron death","volume":"19","author":"Nawa","year":"2012","journal-title":"Cell Death Differ."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"14286","DOI":"10.1523\/JNEUROSCI.0642-15.2015","article-title":"Loss of RAD-23 Protects Against Models of Motor Neuron Disease by Enhancing Mutant Protein Clearance","volume":"35","author":"Jablonski","year":"2015","journal-title":"J. Neurosci."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1126\/science.1134108","article-title":"Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis","volume":"314","author":"Neumann","year":"2006","journal-title":"Science"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1016\/j.bbrc.2006.10.093","article-title":"TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis","volume":"351","author":"Arai","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"2947","DOI":"10.15252\/embj.201488740","article-title":"TDP-1, the Caenorhabditis elegans ortholog of TDP-43, limits the accumulation of double-stranded RNA","volume":"33","author":"Saldi","year":"2014","journal-title":"EMBO J."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"4696","DOI":"10.1073\/pnas.1818415116","article-title":"Motor neuron disease-associated loss of nuclear TDP-43 is linked to DNA double-strand break repair defects","volume":"116","author":"Mitra","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_129","unstructured":"Koopman, M., Gungordu, L., Seinstra, R.I., and Nollen, E.A.A. (2023). Neuronal overexpression of hTDP-43 in Caenorhabditis elegans impairs motor function. MicroPubl. Biol., 2023."},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Liachko, N.F., Saxton, A.D., McMillan, P.J., Strovas, T.J., Keene, C.D., Bird, T.D., and Kraemer, B.C. (2019). Genome wide analysis reveals heparan sulfate epimerase modulates TDP-43 proteinopathy. PLoS Genet., 15.","DOI":"10.1371\/journal.pgen.1008526"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"8371","DOI":"10.1074\/jbc.M111.311977","article-title":"Caenorhabditis elegans RNA-processing protein TDP-1 regulates protein homeostasis and life span","volume":"287","author":"Zhang","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"7319","DOI":"10.1038\/ncomms8319","article-title":"Neurodegeneration in C. elegans models of ALS requires TIR-1\/Sarm1 immune pathway activation in neurons","volume":"6","author":"Veriepe","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"12093","DOI":"10.1523\/JNEUROSCI.2495-13.2014","article-title":"TDP-43 toxicity proceeds via calcium dysregulation and necrosis in aging Caenorhabditis elegans motor neurons","volume":"34","author":"Aggad","year":"2014","journal-title":"J. Neurosci."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1002\/ana.23870","article-title":"CDC7 inhibition blocks pathological TDP-43 phosphorylation and neurodegeneration","volume":"74","author":"Liachko","year":"2013","journal-title":"Ann. Neurol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"112968","DOI":"10.1016\/j.ejmech.2020.112968","article-title":"Targeting nuclear protein TDP-43 by cell division cycle kinase 7 inhibitors: A new therapeutic approach for amyotrophic lateral sclerosis","volume":"210","author":"Liachko","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"2434","DOI":"10.1111\/febs.14866","article-title":"Tau tubulin kinases in proteinopathy","volume":"286","author":"Taylor","year":"2019","journal-title":"FEBS J."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.nbd.2018.06.013","article-title":"alpha-Methyl-alpha-phenylsuccinimide ameliorates neurodegeneration in a C. elegans model of TDP-43 proteinopathy","volume":"118","author":"Wong","year":"2018","journal-title":"Neurobiol. Dis."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"1951","DOI":"10.1016\/j.bbadis.2014.01.015","article-title":"Genetic screens in Caenorhabditis elegans models for neurodegenerative diseases","volume":"1842","author":"Sin","year":"2014","journal-title":"Biochim. Biophys. Acta."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1038\/s43587-023-00383-4","article-title":"Cold temperature extends longevity and prevents disease-related protein aggregation through PA28gamma-induced proteasomes","volume":"3","author":"Lee","year":"2023","journal-title":"Nat. Aging"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"1952","DOI":"10.1093\/hmg\/ddr076","article-title":"TDP-43 neurotoxicity and protein aggregation modulated by heat shock factor and insulin\/IGF-1 signaling","volume":"20","author":"Zhang","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"ref_141","doi-asserted-by":"crossref","unstructured":"Tseng, Y.L., Lu, P.C., Lee, C.C., He, R.Y., Huang, Y.A., Tseng, Y.C., Cheng, T.R., Huang, J.J., and Fang, J.M. (2023). Degradation of neurodegenerative disease-associated TDP-43 aggregates and oligomers via a proteolysis-targeting chimera. J. Biomed. Sci., 30.","DOI":"10.1186\/s12929-023-00921-7"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"2128","DOI":"10.1007\/s13311-021-01061-2","article-title":"Correction to: The Novel Small Molecule TRVA242 Stabilizes Neuromuscular Junction Defects in Multiple Animal Models of Amyotrophic Lateral Sclerosis","volume":"18","author":"Bose","year":"2021","journal-title":"Neurotherapeutics"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"1656","DOI":"10.15252\/embj.201694401","article-title":"The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate initiation of autophagy","volume":"35","author":"Webster","year":"2016","journal-title":"EMBO J."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1080\/21541248.2016.1240495","article-title":"C9orf72 plays a central role in Rab GTPase-dependent regulation of autophagy","volume":"9","author":"Webster","year":"2018","journal-title":"Small GTPases"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1093\/brain\/awx024","article-title":"C9orf72 and RAB7L1 regulate vesicle trafficking in amyotrophic lateral sclerosis and frontotemporal dementia","volume":"140","author":"Aoki","year":"2017","journal-title":"Brain"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.neuron.2011.09.011","article-title":"Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS","volume":"72","author":"Mackenzie","year":"2011","journal-title":"Neuron"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"2528.e7","DOI":"10.1016\/j.neurobiolaging.2012.06.008","article-title":"C9ORF72 repeat expansion in a large Italian ALS cohort: Evidence of a founder effect","volume":"33","author":"Ratti","year":"2012","journal-title":"Neurobiol. Aging"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.neuron.2011.09.010","article-title":"A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD","volume":"72","author":"Renton","year":"2011","journal-title":"Neuron"},{"key":"ref_149","doi-asserted-by":"crossref","unstructured":"Wang, X., Hao, L., Saur, T., Joyal, K., Zhao, Y., Zhai, D., Li, J., Pribadi, M., Coppola, G., and Cohen, B.M. (2016). Forward Genetic Screen in Caenorhabditis elegans Suggests F57A10.2 and acp-4 As Suppressors of C9ORF72 Related Phenotypes. Front. Mol. Neurosci., 9.","DOI":"10.3389\/fnmol.2016.00113"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"1522","DOI":"10.1016\/j.cub.2018.03.063","article-title":"A C9orf72 ALS\/FTD Ortholog Acts in Endolysosomal Degradation and Lysosomal Homeostasis","volume":"28","author":"Corrionero","year":"2018","journal-title":"Curr. Biol."},{"key":"ref_151","doi-asserted-by":"crossref","unstructured":"Therrien, M., Rouleau, G.A., Dion, P.A., and Parker, J.A. (2013). Deletion of C9ORF72 results in motor neuron degeneration and stress sensitivity in C. elegans. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0083450"},{"key":"ref_152","doi-asserted-by":"crossref","unstructured":"Ji, Y.J., Ugolino, J., Zhang, T., Lu, J., Kim, D., and Wang, J. (2020). C9orf72\/ALFA-1 controls TFEB\/HLH-30-dependent metabolism through dynamic regulation of Rag GTPases. PLoS Genet., 16.","DOI":"10.1371\/journal.pgen.1008738"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"2102","DOI":"10.1080\/15548627.2024.2340415","article-title":"Toxic gain-of-function mechanisms in C9orf72 ALS-FTD neurons drive autophagy and lysosome dysfunction","volume":"20","author":"Beckers","year":"2024","journal-title":"Autophagy"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1038\/s41586-020-2288-7","article-title":"C9orf72 suppresses systemic and neural inflammation induced by gut bacteria","volume":"582","author":"Burberry","year":"2020","journal-title":"Nature"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"e2104664118","DOI":"10.1073\/pnas.2104664118","article-title":"The nuclear ubiquitin ligase adaptor SPOP is a conserved regulator of C9orf72 dipeptide toxicity","volume":"118","author":"Snoznik","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"6025","DOI":"10.1038\/s41467-021-26303-x","article-title":"A C. elegans model of C9orf72-associated ALS\/FTD uncovers a conserved role for eIF2D in RAN translation","volume":"12","author":"Sonobe","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1038\/s41593-019-0384-5","article-title":"L3MBTL1 regulates ALS\/FTD-associated proteotoxicity and quality control","volume":"22","author":"Lu","year":"2019","journal-title":"Nat. Neurosci."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1016\/j.cell.2009.03.006","article-title":"Rethinking ALS: The FUS about TDP-43","volume":"136","author":"Cleveland","year":"2009","journal-title":"Cell"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"2690","DOI":"10.1101\/gad.204602.112","article-title":"FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2","volume":"26","author":"Schwartz","year":"2012","journal-title":"Genes Dev."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"6030","DOI":"10.1073\/pnas.1203028109","article-title":"TLS\/FUS (translocated in liposarcoma\/fused in sarcoma) regulates target gene transcription via single-stranded DNA response elements","volume":"109","author":"Tan","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1093\/hmg\/ddr417","article-title":"ALS mutations in FUS cause neuronal dysfunction and death in Caenorhabditis elegans by a dominant gain-of-function mechanism","volume":"21","author":"Murakami","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"2781","DOI":"10.1093\/nar\/gkq1162","article-title":"Intracellular localization and splicing regulation of FUS\/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations","volume":"39","author":"Kino","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"ref_163","doi-asserted-by":"crossref","unstructured":"Lorenzo-Betancor, O., Ogaki, K., Soto-Ortolaza, A., Labbe, C., Vilarino-Guell, C., Rajput, A., Rajput, A.H., Pastor, P., Ortega, S., and Lorenzo, E. (2014). Analysis of nuclear export sequence regions of FUS-Related RNA-binding proteins in essential tremor. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0111989"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"2572","DOI":"10.1093\/brain\/awz217","article-title":"Widespread FUS mislocalization is a molecular hallmark of amyotrophic lateral sclerosis","volume":"142","author":"Tyzack","year":"2019","journal-title":"Brain"},{"key":"ref_165","doi-asserted-by":"crossref","unstructured":"Ishigaki, S., and Sobue, G. (2018). Importance of Functional Loss of FUS in FTLD\/ALS. Front. Mol. Biosci., 5.","DOI":"10.3389\/fmolb.2018.00044"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.semcdb.2019.05.023","article-title":"Cytoplasmic functions of TDP-43 and FUS and their role in ALS","volume":"99","author":"Birsa","year":"2020","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/21678421.2023.2272170","article-title":"FUS gene mutation in amyotrophic lateral sclerosis: A new case report and systematic review","volume":"25","author":"Xiao","year":"2024","journal-title":"Amyotroph. Lateral Scler. Front. Degener."},{"key":"ref_168","unstructured":"Labarre, A., Tossing, G., Maios, C., Doyle, J.J., and Parker, J.A. (2021). A single copy transgenic mutant FUS strain reproduces age-dependent ALS phenotypes in C. elegans. MicroPubl. Biol., 2021."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1007\/s11910-016-0658-1","article-title":"ALS: Recent Developments from Genetics Studies","volume":"16","author":"Therrien","year":"2016","journal-title":"Curr. Neurol. Neurosci. Rep."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1016\/j.molcel.2018.02.001","article-title":"FUS Regulates Activity of MicroRNA-Mediated Gene Silencing","volume":"69","author":"Zhang","year":"2018","journal-title":"Mol. Cell"},{"key":"ref_171","first-page":"9610","article-title":"TDP-1 and FUST-1 co-inhibit exon inclusion and control fertility together with transcriptional regulation","volume":"51","author":"Taylor","year":"2023","journal-title":"bioRxiv"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"110195","DOI":"10.1016\/j.celrep.2021.110195","article-title":"Disrupted autophagy and neuronal dysfunction in C. elegans knockin models of FUS amyotrophic lateral sclerosis","volume":"38","author":"Baskoylu","year":"2022","journal-title":"Cell Rep."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/j.freeradbiomed.2023.11.015","article-title":"Fused in sarcoma regulates glutamate signaling and oxidative stress response","volume":"210","author":"Wong","year":"2024","journal-title":"Free. Radic. Biol. Med."},{"key":"ref_174","doi-asserted-by":"crossref","unstructured":"Markert, S.M., Skoruppa, M., Yu, B., Mulcahy, B., Zhen, M., Gao, S., Sendtner, M., and Stigloher, C. (2020). Overexpression of an ALS-associated FUS mutation in C. elegans disrupts NMJ morphology and leads to defective neuromuscular transmission. Biol. Open, 9.","DOI":"10.1242\/bio.055129"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"114626","DOI":"10.1016\/j.celrep.2024.114626","article-title":"ALS-FUS mutations cause abnormal PARylation and histone H1.2 interaction, leading to pathological changes","volume":"43","author":"Alirzayeva","year":"2024","journal-title":"Cell Rep."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"e009070","DOI":"10.1136\/bmjopen-2015-009070","article-title":"Incidence of adult Huntington\u2019s disease in the UK: A UK-based primary care study and a systematic review","volume":"6","author":"Wexler","year":"2016","journal-title":"BMJ Open"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"2642","DOI":"10.1007\/s00018-006-6242-0","article-title":"Huntington\u2019s disease: From huntingtin function and dysfunction to therapeutic strategies","volume":"63","author":"Zala","year":"2006","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_178","unstructured":"Ajitkumar, A., and De Jesus, O. (2024). Huntington Disease. StatPearls, StatPearls."},{"key":"ref_179","doi-asserted-by":"crossref","unstructured":"Jiang, A., Handley, R.R., Lehnert, K., and Snell, R.G. (2023). From Pathogenesis to Therapeutics: A Review of 150 Years of Huntington\u2019s Disease Research. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241613021"},{"key":"ref_180","doi-asserted-by":"crossref","unstructured":"Rudich, P., Watkins, S., and Lamitina, T. (2020). PolyQ-independent toxicity associated with novel translational products from CAG repeat expansions. PLoS ONE, 15.","DOI":"10.1371\/journal.pone.0227464"},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1073\/pnas.96.1.179","article-title":"Polyglutamine-mediated dysfunction and apoptotic death of a Caenorhabditis elegans sensory neuron","volume":"96","author":"Faber","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_182","doi-asserted-by":"crossref","unstructured":"Koyuncu, S., Fatima, A., Gutierrez-Garcia, R., and Vilchez, D. (2017). Proteostasis of Huntingtin in Health and Disease. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18071568"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1007\/5584_2022_742","article-title":"HSF1 and Its Role in Huntington\u2019s Disease Pathology","volume":"1410","author":"Kim","year":"2023","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1007\/978-3-030-40204-4_4","article-title":"Challenging Proteostasis: Role of the Chaperone Network to Control Aggregation-Prone Proteins in Human Disease","volume":"1243","author":"Sinnige","year":"2020","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"21","DOI":"10.4161\/auto.3528","article-title":"Autophagy genes protect against disease caused by polyglutamine expansion proteins in Caenorhabditis elegans","volume":"3","author":"Jia","year":"2007","journal-title":"Autophagy"},{"key":"ref_186","doi-asserted-by":"crossref","unstructured":"Farina, F., Lambert, E., Commeau, L., Lejeune, F.X., Roudier, N., Fonte, C., Parker, J.A., Boddaert, J., Verny, M., and Baulieu, E.E. (2017). The stress response factor daf-16\/FOXO is required for multiple compound families to prolong the function of neurons with Huntington\u2019s disease. Sci. Rep., 7.","DOI":"10.1038\/s41598-017-04256-w"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"7927","DOI":"10.1073\/pnas.1002924107","article-title":"SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis","volume":"107","author":"Taylor","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1007\/s40263-013-0055-0","article-title":"Targeting sirtuin-1 in Huntington\u2019s disease: Rationale and current status","volume":"27","author":"Duan","year":"2013","journal-title":"CNS Drugs"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1096\/fj.14-252189","article-title":"20S proteasome activation promotes life span extension and resistance to proteotoxicity in Caenorhabditis elegans","volume":"29","author":"Chondrogianni","year":"2015","journal-title":"FASEB J."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"2886","DOI":"10.1038\/s41467-018-05320-3","article-title":"The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington\u2019s disease patients","volume":"9","author":"Koyuncu","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1093\/hmg\/ddv513","article-title":"AMPK activation protects from neuronal dysfunction and vulnerability across nematode, cellular and mouse models of Huntington\u2019s disease","volume":"25","author":"Farina","year":"2016","journal-title":"Hum. Mol. Genet."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"e104671","DOI":"10.15252\/embj.2020104671","article-title":"TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington\u2019s disease models","volume":"39","author":"Hegde","year":"2020","journal-title":"EMBO J."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"1753","DOI":"10.14336\/AD.2021.0404","article-title":"Targeting Mitochondrial Network Disorganization is Protective in C. elegans Models of Huntington\u2019s Disease","volume":"12","author":"Machiela","year":"2021","journal-title":"Aging Dis."},{"key":"ref_194","doi-asserted-by":"crossref","unstructured":"Traa, A., Machiela, E., Rudich, P.D., Soo, S.K., Senchuk, M.M., and Van Raamsdonk, J.M. (2021). Identification of Novel Therapeutic Targets for Polyglutamine Diseases That Target Mitochondrial Fragmentation. Int. J. Mol. Sci., 22.","DOI":"10.1101\/2021.10.19.465059"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1186\/s13024-021-00428-5","article-title":"Mammalian\/mechanistic target of rapamycin (mTOR) complexes in neurodegeneration","volume":"16","author":"Querfurth","year":"2021","journal-title":"Mol. Neurodegener."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"1471","DOI":"10.1126\/science.1124514","article-title":"Progressive disruption of cellular protein folding in models of polyglutamine diseases","volume":"311","author":"Gidalevitz","year":"2006","journal-title":"Science"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1126\/science.1067389","article-title":"Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson\u2019s disease","volume":"295","author":"Auluck","year":"2002","journal-title":"Science"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/B978-0-444-63233-3.00017-8","article-title":"Huntington disease","volume":"147","author":"Ghosh","year":"2018","journal-title":"Handb. Clin. Neurol."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1038\/ng1362","article-title":"Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease","volume":"36","author":"Ravikumar","year":"2004","journal-title":"Nat. Genet."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1016\/j.bbrc.2008.05.132","article-title":"Cytoplasmic expression of mouse prion protein causes severe toxicity in Caenorhabditis elegans","volume":"372","author":"Park","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_201","doi-asserted-by":"crossref","unstructured":"Sandhof, C.A., Hoppe, S.O., Tittelmeier, J., and Nussbaum-Krammer, C. (2020). C. elegans Models to Study the Propagation of Prions and Prion-Like Proteins. Biomolecules, 10.","DOI":"10.3390\/biom10081188"},{"key":"ref_202","doi-asserted-by":"crossref","unstructured":"Nussbaum-Krammer, C.I., Park, K.W., Li, L., Melki, R., and Morimoto, R.I. (2013). Spreading of a prion domain from cell-to-cell by vesicular transport in Caenorhabditis elegans. PLoS Genet., 9.","DOI":"10.1371\/journal.pgen.1003351"},{"key":"ref_203","doi-asserted-by":"crossref","unstructured":"Lackie, R.E., Maciejewski, A., Ostapchenko, V.G., Marques-Lopes, J., Choy, W.Y., Duennwald, M.L., Prado, V.F., and Prado, M.A.M. (2017). The Hsp70\/Hsp90 Chaperone Machinery in Neurodegenerative Diseases. Front. Neurosci., 11.","DOI":"10.3389\/fnins.2017.00254"},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1080\/19336896.2019.1670928","article-title":"Combining autophagy stimulators and cellulose ethers for therapy against prion disease","volume":"13","author":"Abdulrahman","year":"2019","journal-title":"Prion"},{"key":"ref_205","doi-asserted-by":"crossref","unstructured":"Donnelly, K.M., Coleman, C.M., Fuller, M.L., Reed, V.L., Smerina, D., Tomlinson, D.S., and Pearce, M.M.P. (2022). Hunting for the cause: Evidence for prion-like mechanisms in Huntington\u2019s disease. Front. Neurosci., 16.","DOI":"10.3389\/fnins.2022.946822"},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"69","DOI":"10.2174\/1871526510909010069","article-title":"LRP\/LR as an alternative promising target in therapy of prion diseases, Alzheimer\u2019s disease and cancer","volume":"9","author":"Vana","year":"2009","journal-title":"Infect. Disord. Drug Targets"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/7\/3030\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T17:00:38Z","timestamp":1760029238000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/7\/3030"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,3,26]]},"references-count":206,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2025,4]]}},"alternative-id":["ijms26073030"],"URL":"https:\/\/doi.org\/10.3390\/ijms26073030","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,3,26]]}}}