Lewy Body-like α-Synuclein Aggregates Resist Degradation and Impair Macroautophagy

Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease

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LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.

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p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy

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Methods in Mammalian Autophagy Research

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α-Synuclein Locus Triplication Causes Parkinson's Disease

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Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice

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AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease

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Loss of autophagy in the central nervous system causes neurodegeneration in mice

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The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementia

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Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice

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Overexpression of alpha synuclein disrupts APP and Endolysosomal axonal trafficking in a mouse model of synucleinopathy

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Concomitant protein pathogenesis in Parkinson’s disease and perspective mechanisms

Han, Y., & He, Z. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1189809 · Cited by 18

Salidroside protects SH‑SY5Y from pathogenic α‑synuclein by promoting cell autophagy via mediation of mTOR/p70S6K signaling

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White and gray matter alterations in de novo PD patients: which matter most?

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Proteostasis defects: Medicinal challenges of imperfect aging & neurodegeneration

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Demystifying the Neuroprotective Role of Neuropeptides in Parkinson’s Disease: A Newfangled and Eloquent Therapeutic Perspective

Behl, T., Madaan, P., Sehgal, A., Singh, S., Makeen, H. A., Albratty, M., Alhazmi, H. A., Meraya, A. M., & BUNGAU, S. G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094565 · Cited by 19

Neonatal 6-hydroxydopamine lesioning of rats and dopaminergic neurotoxicity: proposed animal model of Parkinson’s disease

Kostrzewa, R. M. (2022) · Journal of Neural Transmission · doi:10.1007/s00702-022-02479-4 · Cited by 17

Perspectives of autophagy-tethering compounds (ATTECs) in drug discovery

Ding, Y., Xing, D., Fei, Y., Luo, S., & Lu, B. (2024) · Medicine Plus · doi:10.1016/j.medp.2023.100004 · Cited by 16

The E3 ubiquitin ligase seven in absentia homolog 1 may be a potential new therapeutic target for Parkinson′s disease

Cai, Z., Xu, J., Xue, S.-R., Liu, Y.-Y., Zhang, Y., Zhang, X.-Z., Wang, X., Wu, F., & Li, X. (2015) · Neural Regeneration Research · doi:10.4103/1673-5374.162763 · Cited by 15

C. elegans to model autophagy-related human disorders

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Deconvoluting the complexity of autophagy and Parkinson's disease for potential therapeutic purpose

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Associations of ATG7 rs1375206 polymorphism and elevated plasma ATG7 levels with late-onset sporadic Parkinson’s disease in a cohort of Han Chinese from southern China

Zhao, X., Chen, Y., Wang, L., Li, X., Chen, X., & Zhang, H. (2020) · International Journal of Neuroscience · doi:10.1080/00207454.2020.1731507 · Cited by 14

Fluorescent Protein-Based Autophagy Biosensors

Kim, H., & Seong, J. (2021) · Materials · doi:10.3390/ma14113019 · Cited by 15

A surge of cytosolic calcium dysregulates lysosomal function and impairs autophagy flux during cupric chloride–induced neuronal death

Kim, Y., Lee, Y., Choo, M., Yun, N., Cho, J. W., & Oh, Y. J. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105479 · Cited by 14

Association of ATG5 gene polymorphism with Parkinson’s disease in a Han Chinese population

Han, J., Feng, G., Wu, J., Zhang, Y., Long, Z., & Yao, X. (2021) · Acta Neurologica Belgica · doi:10.1007/s13760-021-01814-y · Cited by 13

The Impact of Paeoniflorin onα-Synuclein Degradation Pathway

Cai, Z., Zhang, X., Zhang, Y., Li, X.-M., Xu, J., & Li, X. (2015) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2015/182495 · Cited by 13

Desferrioxamine Ameliorates Lipopolysaccharide-Induced Lipocalin-2 Upregulation via Autophagy Activation in Primary Astrocytes

Cui, J., Yu, Y., Wang, J., Song, N., & Xie, J. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02687-1 · Cited by 12

MicroRNAs regulating autophagy: opportunities in treating neurodegenerative diseases

Mohseni, M., Behzad, G., Farhadi, A., Behroozi, J., Mohseni, H., & Valipour, B. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1397106 · Cited by 12

Lewy body diseases and the gut

Sampson, T. R., Tansey, M. G., West, A. B., & Liddle, R. A. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00804-5 · Cited by 13

Neuroprotective Effects of a Novel Demeclocycline Derivative Lacking Antibiotic Activity: From a Hit to a Promising Lead Compound

Tomas‐Grau, R. H., González‐Lizárraga, F., Ploper, D., Ávila, C. L., Socías, S. B., Besnault, P., Tourville, A., Mella, R. M., Villacé, P., Salado, C., et al. (2022) · Cells · doi:10.3390/cells11172759 · Cited by 12

Aβ exacerbates α‐synuclein‐induced neurotoxicity through impaired insulin signaling in α‐synuclein‐overexpressed human SK‐N‐MC neuronal cells

Chang, C., Li, H., Chang, Y., Ho, Y., Hsieh, L., Chiu, P., Cheng, Y., Lin, C., & Lai, T. (2017) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12772 · Cited by 12

Suppression of α-synuclein propagation after intrastriatal injection in FABP3 null mice

Matsuo, K., Kawahata, K., Melki, R., Bousset, L., Owada, Y., & Fukunaga, K. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147383 · Cited by 13

Dysregulation of protein degradation and alteration of secretome in α-synuclein-exposed astrocytes: implications for dopaminergic neuronal dysfunction

Raj, A., Banerjee, R., Holla, V. V., Kamble, N. L., Yadav, R., Pal, P. K., & Datta, I. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01928-9 · Cited by 11

Converging pathologies in neurodegeneration: the mechanistic interplay between α-Synuclein and Tau in Alzheimer’s and Parkinson’s

Jeyabalan, J. B., Vignesh Pandi, A., Sankar, V., Sivasamy, R., Dhanasekaran, M., & Justin, A. (2025) · Neurological Sciences · doi:10.1007/s10072-025-08421-2 · Cited by 11

Exposure of α-Synuclein Aggregates to Organotypic Slice Cultures Recapitulates Key Molecular Features of Parkinson's Disease

Moudio, S., Rodin, F., Albargothy, N. J., Karlsson, U., Reyes, J. F., & Hallbeck, M. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.826102 · Cited by 11

Dysregulation of bcl-2 enhanced rotenone-induced α-synuclein aggregation associated with autophagic pathways

Chen, Y., Zhang, N., Ji, D., Hou, Y., Chen, C., Fu, Y., Ge, R., Zheng, Q., Chen, J., & Wang, H. (2018) · Neuroreport · doi:10.1097/wnr.0000000000001097 · Cited by 10

Modulation of autophagy in human diseases strategies to foster strengths and circumvent weaknesses

Xu, S., Sui, S., Zhang, X., Pang, B., Wan, L., & Pang, D. (2019) · Medicinal Research Reviews · doi:10.1002/med.21571 · Cited by 10

A First Order Phase Transition Underlies the Formation of Sub-Diffractive Protein Aggregates in Mammalian CellsPreprint

Narayanan, A., Meriin, A. B., Sherman, M. Y., & Cissé, I. I. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/148395 · Cited by 10

A splicing variant of TFEB negatively regulates the TFEB-autophagy pathway

Park, J.-Y., Sohn, H., Koh, Y. H., & Jo, C. (2021) · Scientific Reports · doi:10.1038/s41598-021-00613-y · Cited by 9

The role of autophagy in synucleinopathy: clearance versus spread of α-synuclein

Birnbaum, E., & Yue, Z. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2577406 · Cited by 10

Autophagy–NAD+ axis: emerging insights into neuronal homeostasis and neurodegenerative diseases

Koçak, G., Dimas, M. M., Silva, L., Silva-Amaral, D., Sun, C., Cruddas, S., Barrett, T. G., Martins‐de‐Souza, D., Cunha‐Neto, E., Brocardo, P. S., et al. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2025.1695486 · Cited by 8

Genetically encoded fluorescent reporters to visualize α-synuclein pathology in live brain

Zhang, L. I., Yu, M., Chen, G., Ge, S., Wang, M., Zhang, X., Zhao, M., Gu, H., Huang, M., Liu, A., et al. (2026) · Cell · doi:10.1016/j.cell.2026.01.035 · Cited by 10

GHSR deficiency exacerbates Parkinson's disease pathology by impairing autophagy

Xiao, X., Tang, T., Bi, M., Liu, J., Liu, M., Jiao, Q., Chen, X., Yan, C., Du, X., & Jiang, H. F. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103322 · Cited by 8

Macroautophagy of Aggregation-Prone Proteins in Neurodegenerative Disease

Fox, L. M., & Yamamoto, A. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801043-3.00007-8 · Cited by 9

Shining a light on autophagy in neurodegenerative diseases

Chandran, A., & Rochet, J. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101437 · Cited by 8

Mesenchymal stem cell transplantation and aerobic exercise for Parkinson’s disease: therapeutic assets beyond the motor domain

Berrío Sánchez, J., Cucarian Hurtado, J., Barcos Nunes, R., & de Oliveira, A. A. (2019) · Reviews in the Neurosciences · doi:10.1515/revneuro-2018-0011 · Cited by 7

Characterization of pSer129-αSyn Pathology and Neurofilament Light-Chain Release across In Vivo, Ex Vivo, and In Vitro Models of Pre-Formed-Fibril-Induced αSyn Aggregation

Hansen, M. L., Ambjørn, M., Harndahl, M. N., Benned‐Jensen, T., Fog, K., Bjerregaard-Andersen, K., & Sotty, F. (2024) · Cells · doi:10.3390/cells13030253 · Cited by 7

Enhanced alpha-synuclein pathology and exacerbated motor dysfunction in alpha-synuclein transgenic mice with autophagy deficiency

Noda, S., Sato, S., Yamakado, H., Takahashi, R., & Hattori, N. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.151514 · Cited by 7

Alpha-synuclein inclusions reduced by PIKfyve inhibition in Parkinson disease cell models

Pozo, S. L. D., Uras, G., Fierli, F., Lentini, V., Koletsi, S., Lazaro-Hernandez, C., Chau, K., Hughes, D. A., & Schapira, A. H. V. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107053 · Cited by 7

Propagated but Topologically Distributed Forebrain Neurons Expressing Alpha-Synuclein in Aged Macaques

Kimura, K., Inoue, K., Kuroiwa, Y., Tanaka, F., & Takada, M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0166861 · Cited by 8

Alpha‐Synuclein oligomerization and aggregation: All models are useful but only if we know what they model

Lashuel, H. A. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15275 · Cited by 7

Adenosine A2A receptor antagonist KW6002 protects against A53T mutant alpha-synuclein-induced brain damage and neuronal apoptosis in Parkinson's disease mice by restoring autophagic flux

Hu, Q., Lingli, X., Liu, X., Wang, Y., & Yuan, J. (2023) · Neuroscience Letters · doi:10.1016/j.neulet.2023.137610 · Cited by 6

Early α-synuclein/synapsin III co-accumulation, nigrostriatal dopaminergic synaptopathy and denervation in the MPTPp mouse model of Parkinson's Disease

Serra, M., Faustini, G., Brembati, V., Casu, M. A., Pizzi, M., Morelli, M., Pinna, A., & Bellucci, A. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.115040 · Cited by 6

Mitochondrial-membrane association of α-synuclein: Pros and cons in consequence of Parkinson's disease pathophysiology

Pariary, R., Bhattacharyya, D., & Bhunia, A. (2019) · Gene Reports · doi:10.1016/j.genrep.2019.100423 · Cited by 6

Pathways of protein synthesis and degradation in PD pathogenesis

Langston, R. G., & Cookson, M. (2020) · Progress in brain research · doi:10.1016/bs.pbr.2020.01.002 · Cited by 7

FRET‐based assay for intracellular evaluation of α‐synuclein aggregation inhibitors

Galkin, M., Priss, A., Topcheva, O., Yushchenko, D. A., & Shvadchak, V. V. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15528 · Cited by 6

Structure-function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathies

Serdiuk, T., Redeker, V., Savistchenko, J., Neupane, S., Haenseler, W., Fleischmann, Y., Reber, V., Keller, S., Tiberi, C., Bachmann-Gagescu, R., et al. (2026) · Molecular Systems Biology · doi:10.1038/s44320-026-00199-5 · Cited by 5

Multiple tethers of organelle contact sites are involved in α-synuclein toxicity in yeast

Vecchio, M. D., Amado, L., Cogan, A. P., Meert, E. M. K., Rosseels, J., Franssens, V., Govers, S. K., Winderickx, J., & Montoro, A. G. (2023) · Molecular Biology of the Cell · doi:10.1091/mbc.e23-01-0029 · Cited by 4

Effects of caloric restriction on retinal aging and neurodegeneration

Adornetto, A., Morrone, L. A., Satriano, A., Laganà, M. L., Licastro, E., Nucci, C., Corasaniti, M. T., Tonin, P., Bagetta, G., & Russo, R. (2020) · Progress in brain research · doi:10.1016/bs.pbr.2020.07.005 · Cited by 6

Inhibition of Phosphorylated Alpha-Synuclein Aggregation by Synthetic Protein Mimetics and Foldamers

Oldani, E. G., Stillman, N. H., Dohoney, R. A., Baysah, C. Z., & Kumar, S. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00546 · Cited by 5

Programmed Cell Death and Its Therapeutic Implications in Parkinson's Disease: A Review of Apoptosis, Autophagy, Ferroptosis, and Necroptosis

Erekat, N. S. (2025) · Clinical Anatomy · doi:10.1002/ca.70057 · Cited by 4

Modeling Parkinson’s pathology in human iPSC dopaminergic neurons uncovers key mechanisms of Lewy body formation and heterogeneity

Mahul‐Mellier, A., van den Heuvel, L., Teixeira, M., Boussouf, M. L. N., Oudinot, G., Thonet, A., Speri, D., Jasiqi, Y., Ulrich, C. H., Sheta, R., et al. (2026) · Science Advances · doi:10.1126/sciadv.aed8851 · Cited by 4

The effect of AKT inhibition in α-synuclein-dependent neurodegeneration

Ranxhi, B., Bangash, Z. R., Chbihi, Z. M., Todi, S. V., LeWitt, P. A., & Tsou, W. (2025) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2025.1524044 · Cited by 4

From protective enzyme to facilitator of amyloid propagation: Cathepsin D-mediated amyloid fibril fragmentation

Sulatsky, M. I., Stepanenko, O. V., Stepanenko, O. V., Mikhailova, E. V., & Sulatskaya, A. I. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.140971 · Cited by 4

Quantitative Proteomic and Phosphoproteomic Analyses Reveal a Role of Death-Associated Protein Kinase 1 in Regulating Hippocampal Synapse

Tian, Y., Zheng, X., Li, R., Li, H., Shui, X., Wang, L., Chen, D., Lee, T. H., & Zhang, T. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03674-4 · Cited by 4

FABP5-binding lipids regulate autophagy in differentiated SH-SY5Y cells

Soto-Avellaneda, A., Oxford, A. E., Halla, F., Vasquez, P., Oe, E., Pugel, A. D., Schoenfeld, A. M., Tillman, M. C., Cuevas, A. R., Ortlund, E. A., et al. (2024) · PLoS ONE · doi:10.1371/journal.pone.0300168 · Cited by 4

Analysis of the Neuroproteome Associated With Cell Therapy After Intranigral Grafting in a Mouse Model of Parkinson Disease

Dakik, H., Mantash, S., Nehme, A., Kobeissy, F. H., Zabet‐Moghaddam, M., Mirzaei, P., Mechref, Y. S., Gaillard, A., Prestoz, L., & Zibara, K. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.621121 · Cited by 4

Dissecting the differential role of C-terminal truncations in the regulation of aSyn pathology formation and the biogenesis of Lewy bodiesPreprint

Mahul‐Mellier, A., Altay, M. F., Maharjan, N., Ait‐Bouziad, N., Chiki, A., Jagannath, S., Limorenko, G., Novello, S., Ricci, J., Vingill, S., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.29.625993 · Cited by 4

The emerging role and therapeutic targeting of autophagy-lysosome pathway in the pathogenesis of Parkinson’s disease

Shimizu, T., Isik, S., Kamath, N., & Yue, Z. (2026) · Translational Neurodegeneration · doi:10.1186/s40035-026-00555-3 · Cited by 3

Coronin1A Regulates the Trafficking of Alpha Synuclein in Microglia

Biggs, K. E., Fikse, E. N., Anderson, F. L., Kettenbach, A. N., & Havrda, M. C. (2025) · Journal of Neuroscience · doi:10.1523/jneurosci.1337-24.2025 · Cited by 4

Pathological α-synuclein elicits granulovacuolar degeneration independent of tau

Dues, D. J., Erb, M. L., Kasen, A., Vatsa, N., Williams, E. T., Nguyen, A. P. T., Henderson, M. X., & Moore, D. J. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00494-5 · Cited by 3

Age-related pathological impairments in induced neurons derived from patients with idiopathic Parkinson’s diseasePreprint

Drouin‐Ouellet, J., Pircs, K., Legault, E. M., Birtele, M., Nilsson, F., Shrigley, S., Pereira, M., Storm, P., Sharma, Y., Vuono, R., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.23.441070 · Cited by 3

A novel mutation (E83Q) unlocks the pathogenicity of human alpha-synuclein fibrils and recapitulates its pathological diversityPreprint

Kumar, S. T., Mahul‐Mellier, A., Hegde, R. N., Moons, R., Magalhães, P., de Opakua, A. I., Rivière, G., Rostami, I., Donzelli, S., Zweckstetter, M., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.11.21.469421 · Cited by 3

Structure-function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathiesPreprint

Serdiuk, T., Redeker, V., Savistchenko, J., Neupane, S., Haenseler, W., Fleischmann, Y., Reber, V., Keller, S., Tiberi, C., Bachmann‐Gagescu, R., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.13.682210 · Cited by 3

Recapitulating Parkinson’s pathology in human iPSC dopaminergic neurons reveals new mechanistic insights into Lewy body formation and heterogeneityPreprint

Mahul‐Mellier, A., van den Heuvel, L., Teixeira, M., Boussouf, M. L. N., Oudinot, G., Thonet, A., Speri, D., Jasiqi, Y., Ulrich, C. H., Sheta, R., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.26.684610 · Cited by 3

Silencing of Tctex1 impairs autophagy lysosomal degradation of α-synuclein and cell viability

Zhang, Y., Dong, S., Liu, Z., Ming, J., Sun, Z., Li, X., Cai, Z., & Li, X. (2018) · Neuroreport · doi:10.1097/wnr.0000000000000979 · Cited by 2

Unraveling the mystery: How autophagy deficiency in dopaminergic neurons drives human Parkinson’s disease

Noda, S., & Hattori, N. (2025) · Molecular Brain · doi:10.1186/s13041-025-01235-5 · Cited by 2

Autophagy dysfunction in iPSCs-derived neurons and midbrain organoids carrying a SNCA triplication

Serra-Almeida, C., Jarazo, J., Gomez‐Giro, G., Rosety, I., Žagare, A., Ferrante, D., Saraiva, C., Frangenberg, D., Modamio, J., Zuccoli, E., et al. (2026) · npj Parkinson s Disease · doi:10.1038/s41531-026-01330-x · Cited by 4

FAM48A mediates compensatory autophagy induced by proteasome impairment

Arata, Y., Watanabe, A., Motosugi, R., Iemura, S., Natsume, T., Mukai, K., Taguchi, T., Hirayama, S., Hamazaki, J., & Murata, S. (2019) · Genes to Cells · doi:10.1111/gtc.12708 · Cited by 2

Autophagy and Parkinson’s Disease

Ryan, L., Rob, M., He, J., & Rubinsztein, D. C. (2022) · Springer eBooks · doi:10.1007/978-3-031-15080-7_242 · Cited by 2

Protein aggregation in health and disease: A looking glass of two faces

de Andrade, G. C., Mota, M. F., Moreira-Ferreira, D. N., Silva, J. L., de Oliveira, G. A. P., & Marques, M. A. (2024) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2024.09.010 · Cited by 2

Immunotherapies for Movement Disorders: Parkinson’s Disease and Amyotrophic Lateral Sclerosis

Schutt, C. R., Gendelman, H. E., & Mosley, R. L. (2016) · Springer eBooks · doi:10.1007/978-3-319-44022-4_46 · Cited by 2

Structural brain changes in Ser129-phosphorylated alpha-synuclein rats based on voxel-based morphometry

Wang, J., Tan, Y., Peng, Q., Zeng, W., Yang, X., Chen, C., Wu, Y., Xu, Y., & Cao, X. (2020) · Behavioural Brain Research · doi:10.1016/j.bbr.2020.112786 · Cited by 2

Protein Interaction Studies for Understanding the Tremor Pathway in Parkinson’s Disease

Dogra, N., Mani, R. J., & Katare, D. P. (2020) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527319666200905115548 · Cited by 2

Neighbouring modifications interfere with the detection of phosphorylated alpha-synuclein at Serine 129: Revisiting the specificity of pS129 antibodiesPreprint

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