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Disrupted Autophagy Leads to Dopaminergic Axon and Dendrite Degeneration and Promotes Presynaptic Accumulation of α-Synuclein and LRRK2 in the Brain
Open accessAbstract
Parkinson's disease (PD) is characterized pathologically by the formation of ubiquitin and α-synuclein (α-syn)-containing inclusions (Lewy bodies), dystrophic dopamine (DA) terminals, and degeneration of midbrain DA neurons. The precise molecular mechanisms underlying these pathological features remain elusive. Accumulating evidence has implicated dysfunctional autophagy, the cell self-digestion and neuroprotective pathway, as one of the pathogenic systems contributing to the development of idiopathic PD. Here we characterize autophagy-deficient mouse models and provide in vivo evidence for the potential role that impaired autophagy plays in pathogenesis associated with PD. Cell-specific deletion of essential autophagy gene Atg7 in midbrain DA neurons causes delayed neurodegeneration, accompanied by late-onset locomotor deficits. In contrast,Atg7-deficient DA neurons in the midbrain exhibit early dendritic and axonal dystrophy, reduced striatal dopamine content, and the formation of somatic and dendritic ubiquitinated inclusions in DA neurons. Furthermore, whole-brain-specific loss of Atg7 leads to presynaptic accumulation of α-syn and LRRK2 proteins, which are encoded by two autosomal dominantly inherited PD-related genes. Our results suggest that disrupted autophagy may be associated with enhanced levels of endogenous α-syn and LRRK2 proteins in vivo. Our findings implicate dysfunctional autophagy as one of the failing cellular mechanisms involved in the pathogenesis of idiopathic PD.
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“Friedman et al.9 demonstrated that DA neuron-specific autophagy deficiency leads to the restrictive presynaptic accumulation of synuclein in the dorsal striatum, suggesting that impaired autophagy plays a role in PD pathogenesis.”
From Loss of autophagy in dopaminergic neurons causes Lewy pathology and motor dysfunction in aged mice (2018) · cites this paper as [9]
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“Until now, we did not clarify the reason, but one of the explanation may be presynaptic dysfunction in Atg7-deficient mice9.”
From Loss of autophagy in dopaminergic neurons causes Lewy pathology and motor dysfunction in aged mice (2018) · cites this paper as [9]
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Cites
A new mathematical model for relative quantification in real-time RT-PCR
Pfaffl, M. W. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.9.e45 · Cited by 34,610
Autophagy fights disease through cellular self-digestion
Mizushima, N., Levine, B., Cuervo, A. M., & Klionsky, D. J. (2008) · Nature · doi:10.1038/nature06639 · Cited by 6,452
Dauer, W., & Przedborski, S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00568-3 · Cited by 5,469
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
Self-citationHomeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice.
Komatsu, M., Waguri, S., Koike, M., Sou, Y.-S., Ueno, T., Hara, T., Mizushima, N., Iwata, J.-I., Ezaki, J., Murata, S., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.035 · Cited by 2,124
Self-citationImpaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024 · cited 1×
“Moreover, chaperone-mediated autophagy (CMA), another lysosomal pathway, was shown to degrade human wild-type, but not mutant forms, of -syn (Cuervo et al., 2004).”
Backgroundα-Synuclein Is Degraded by Both Autophagy and the Proteasome
Webb, J. L., Ravikumar, B., Atkins, J., Skepper, J. N., & Rubinsztein, D. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300227200 · Cited by 1,429
Dissection of Autophagosome Formation Using Apg5-Deficient Mouse Embryonic Stem Cells
Mizushima, N., Yamamoto, A., Hatano, M., Kobayashi, Y., Kabeya, Y., Suzuki, K., Tokuhisa, T., Ohsumi, Y., & Yoshimori, T. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.4.657 · Cited by 1,361
Kirisako, T., Ichimura, Y., Okada, H., Kabeya, Y., Mizushima, N., Yoshimori, T., Ohsumi, M., Takao, T., Noda, T., & Ohsumi, Y. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.2.263 · Cited by 1,024
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Items 201–300 of 303
Vargová, I., Urdzíková, L. M., Kárová, K., Šmejkalová, B., Sursal, T., Cimermanova, V., Turnovcová, K., Gandhi, C. D., Jhanwar‐Uniyal, M., & Jendelová, P. (2021) · Biomedicines · doi:10.3390/biomedicines9060593 · Cited by 17
TFE3-Mediated Autophagy is Involved in Dopaminergic Neurodegeneration in Parkinson’s Disease
He, X., Xie, Y., Zheng, Q., Zhang, Z., Ma, S., Li, J., Li, M., & Huang, Q. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.761773 · Cited by 16
Canonical and noncanonical autophagy: involvement in Parkinson’s disease
Sakurai, M., & Kuwahara, T. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1518991 · Cited by 16
Mitochondrial Regulation by PINK1-Parkin Signaling
Imai, Y. (2012) · ISRN Cell Biology · doi:10.5402/2012/926160 · Cited by 15
Targeting leucine-rich repeat kinase 2 in Parkinson's disease
Chan, S. L., Angeles, D. C., & Tan, E. (2013) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.842978 · Cited by 15
Choi, J., Polcher, A. A., & Joas, A. (2016) · EFSA Supporting Publications · doi:10.2903/sp.efsa.2016.en-955 · Cited by 18
Valderhaug, V. D., Heiney, K., Ramstad, O. H., Bråthen, G., Kuan, W., Nichele, S., Sandvig, A., & Sandvig, I. (2021) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00413.2020 · Cited by 13
Azam, S., Haque, M. E., Cho, D.-Y., Kim, J.-S., Jakaria, M., Kim, I., & Choi, D. (2022) · Molecules · doi:10.3390/molecules27092827 · Cited by 15
Zhao, B., & Zhao, B. (2025) · Journal of Nutrition · doi:10.1016/j.tjnut.2025.02.010 · Cited by 15
Non-canonical autophagy in aging and age-related diseases
Kumar, A. V., & Mills, J. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1137870 · Cited by 15
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
Dopaminergic Neuron-Specific Autophagy-Deficient Mice
Sato, S., & Hattori, N. (2018) · Methods in molecular biology · doi:10.1007/7651_2018_156 · Cited by 14
Szelągowski, A., & Kozakiewicz, M. (2023) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2023/7759053 · Cited by 14
Nitrate Metabolism: A Curse or Blessing to Humanity?
Nnate, D., & Achi, N. K. (2016) · Journal of Scientific Research and Reports · doi:10.9734/jsrr/2016/26773 · Cited by 14
Clearance Pathways for α‐Synuclein in Parkinson's Disease
Ho, M. S.-C. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70124 · Cited by 16
Plotegher, N., & Civiero, L. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.3588-12.2012 · Cited by 12
Kuijpers, M., Kochlamazashvili, G., Stumpf, A., Puchkov, D., Swaminathan, A., Lucht, M. T., Krause, E., Maritzen, T., Schmitz, D., & Haucke, V. (2020) · bioRxiv · doi:10.1101/2020.07.06.189522 · Cited by 167
Pech, U., Janssens, J., Schoovaerts, N., Kuenen, S., Calatayud, C., Gallego, S. F., Makhzami, S., Hulselmans, G. J., Poovathingal, S. K., Davie, K., et al. (2024) · eLife · doi:10.1101/2023.03.11.532176 · Cited by 18
Goldsmith, J., Ordureau, A., Boecker, C. A., Arany, M., Harper, J. W., & Holzbaur, E. L. F. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.03.510717 · Cited by 10
Zhang, J., Fu, Z., Wen, F., Lyu, P., Huang, S., Cai, X., Zhang, Z., Zhang, Y., Fan, C. C., Man, W., et al. (2025) · Journal of Neurophysiology · doi:10.1152/jn.00497.2024 · Cited by 9
Autophagy at the synapse, an early site of dysfunction in neurodegeneration
Jasutkar, H. G., & Yamamoto, A. (2023) · Current Opinion in Physiology · doi:10.1016/j.cophys.2023.100631 · Cited by 9
Is Disrupted Mitophagy a Central Player to Parkinson’s Disease Pathology?
Ko, T. K., & Tan, D. J. Y. (2023) · Cureus · doi:10.7759/cureus.35458 · Cited by 9
The BEACH Domain Is Critical for Blue Cheese Function in a Spatial and Epistatic Autophagy Hierarchy
Sim, J. P. L., Osborne, K. A., García, I. A., Matysik, A. S., & Kraut, R. S. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00129 · Cited by 8
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
Self-citationSynuclein and Parkinson’s Disease: An Update
Jellinger, K. A. (2013) · Royal Society of Chemistry eBooks · doi:10.1039/9781849737357-00175 · Cited by 9
Autophagy as an Anti-senescent in Aging Neurocytes
Marzoog, B. A. (2023) · Current Molecular Medicine · doi:10.2174/1566524023666230120102718 · Cited by 9
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Heng, Y., Eggen, B. J. L., Boddeke, E., & Kooistra, S. M. (2017) · Drug Discovery Today Disease Models · doi:10.1016/j.ddmod.2018.10.002 · Cited by 8
Pathogenic insights to Parkin-linked model mice
Sato, S., Noda, S., & Hattori, N. (2020) · Neuroscience Research · doi:10.1016/j.neures.2020.03.014 · Cited by 8
Molecular aspects of optic nerve autophagy in glaucoma
Kitaoka, Y., & Sase, K. (2023) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2023.101217 · Cited by 8
Parkinson's Disease: Leucine-Rich Repeat Kinase 2 and Autophagy, Intimate Enemies
Pedro, J. M. B., Gómez‐Sánchez, R., Pizarro‐Estrella, E., Niso‐Santano, M., González‐Polo, R. A., & Fuentes, J. M. (2012) · Parkinson s Disease · doi:10.1155/2012/151039 · Cited by 8
Pech, U., Janssens, J., Schoovaerts, N., Kuenen, S., Makhzami, S., Hulselmans, G. J., Poovathingal, S. K., Bademosi, A. T., Swerts, J., Vilain, S., et al. (2024) · eLife · doi:10.7554/elife.98348.1 · Cited by 8
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
Advances in autophagy for Parkinson’s disease pathogenesis and treatment
Zhang, X., Zhang, H., Dong, J., Cai, H., & Le, W. (2025) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2024.33 · Cited by 10
Abubakar, M., Alom, S., Ali, F., Ali, S. R., Adhikary, K., Sarika, S., Gupta, P. K., Puppala, E. R., Murti, K., Nand, S., et al. (2026) · Current Neuropharmacology · doi:10.2174/011570159x446831260303200516 · Cited by 7
Recent Insight into the Role of Sphingosine-1-Phosphate Lyase in Neurodegeneration
Wieczorek, I., & Strosznajder, R. P. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076180 · Cited by 7
Vo, M., Choi, S. H., Lee, J.-H., Hong, C. H., Kim, J. S., Lee, U. H., Chung, H., Lee, B. J., Park, J. W., & Cho, W. J. (2017) · Oncotarget · doi:10.18632/oncotarget.16706 · Cited by 7
Inhibition of Autophagy In Vivo Extends Methamphetamine Toxicity to Mesencephalic Cell Bodies
Ferrucci, M., Biagioni, F., Busceti, C. L., Vidoni, C., Castino, R., Isidoro, C., Ryskalin, L., Frati, A., Puglisi‐Allegra, S., & Fornai, F. (2021) · Pharmaceuticals · doi:10.3390/ph14101003 · Cited by 7
CK and LRRK2 Involvement in Neurodegenerative Diseases
Bova, V., Mannino, D., Capra, A. P., Lanza, M., Palermo, N., Filippone, A., & Esposito, E. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111661 · Cited by 6
Secretory Clusterin Inhibits Dopamine Neuron Apoptosis in MPTP Mice by Preserving Autophagy Activity
Zhu, D., Zhang, S., Wang, X., Xiao, C., Cui, G., & Yang, X. (2024) · Neuroscience · doi:10.1016/j.neuroscience.2024.01.010 · Cited by 6
Shi, J., Xu, J., Li, Y., Li, B., Ming, H., Nice, E. C., Huang, C., Li, Q., & Wang, C. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.990665 · Cited by 6
Cheng, C., Yang, H., Tian, L., Ni, Y., Jia, C., Le, W., & Wang, Q. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1612389 · Cited by 5
Wan, S.-X., Pan, X., Qian, J., Shu, Y., Xu, P., Zhao, J., Gong, Q.-X., & Yin, J. (2020) · PubMed Central · Cited by 5
Role of LRRK2 in axonal transport and Parkinson’s disease
Twellsieck, B., & Boecker, C. A. (2025) · Biochemical Journal · doi:10.1042/bcj20253133 · Cited by 7
Morphology, clearing efficacy, and mTOR dependency of the organelle autophagoproteasome
Limanaqi, F., Biagioni, F., Salvetti, A., Puglisi‐Allegra, S., Lenzi, P., & Fornai, F. (2021) · European Journal of Histochemistry · doi:10.4081/ejh.2021.3220 · Cited by 4
Beier, E. E., & Richardson, J. R. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800228-5.00013-3 · Cited by 4
Shimizu, T., Isik, S., Kamath, N., & Yue, Z. (2026) · Translational Neurodegeneration · doi:10.1186/s40035-026-00555-3 · Cited by 3
Self-citationRen, Y.-H., Niu, X., Huang, H.-J., Hao, X., Wang, P.-X., Chi, Y.-L., Ding, Y., & Liao, M. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.11.037 · Cited by 3
New insights into lysosomal dysfunction in parkinson's disease: An emerging role for ATP13A2
Rochet, J. (2012) · Movement Disorders · doi:10.1002/mds.25118 · Cited by 3
A retrograde transit filter mediated by optineurin controls mitostasis in distal axonsPreprint
Marahori, N. A., Gailer, B., Schifferer, M., Kleele, T., Iatroudi, A., Hannan, S. B., Avramopoulos, P., Engelhardt, S. H., Lakadamyali, M., Brill, M. S., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.28.604753 · Cited by 4
Mukhtar, S., Kataria, S., Cimaglia, G., & Beccano-Kelly, D. A. (2025) · Current Research in Physiology · doi:10.1016/j.crphys.2025.100166 · Cited by 2
Mahmoud, S. H., Hamad, S. M., Seiwan, A. N., El-Waseef, D. A. E.-D. A., El-Kharashi, O. A., Elshaer, A. M., Sindi, E. R., Al-Hazani, T. M. I., Ezzat, S. F., Essmat, A., et al. (2025) · Microscopy and Microanalysis · doi:10.1093/mam/ozaf118 · Cited by 2
Profes, M. S., Gora, C., Lavoie‐Cardinal, F., Saghatelyan, A., & Lévesque, M. (2026) · Journal of Neuroscience · doi:10.1523/jneurosci.1224-25.2026 · Cited by 3
Cuevas, E., Guzmán, A., Burks, S. M., Ramirez-Lee, A., Ali, S. F., & Imam, S. Z. (2022) · Toxicology Reports · doi:10.1016/j.toxrep.2022.03.047 · Cited by 2
Altered autophagy on the path to Parkinson's disease
Sanchez-Mirasierra, I., Hernández-Díaz, S., Ghimire, S., Main, P., & Soukup, S. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822003-0.00006-1 · Cited by 2
LIR-dependent LMX1A/LMX1B autophagy crosstalk shapes human midbrain dopaminergic neuronal resiliencePreprint
Jiménez-Moreno, N., Stathakos, P., Antón, Z., Shoemark, D. K., Sessions, R. B., Witzgall, R., Caldwell, M. A., & Lane, J. D. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/636712 · Cited by 2
Zhou, X., Lee, Y.-K., Li, X., Kim, H., Sánchez-Priego, C., Han, X., Tan, H., Zhou, S., Fu, Y., Purtell, K., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.04.519029 · Cited by 2
Self-citationAbraham, K. J., & Dharmasaroja, P. (2025) · Advances in Pharmacological and Pharmaceutical Sciences · doi:10.1155/adpp/5567858 · Cited by 1
Choi, Y., Huh, E., Ju, I. G., Lee, H., Kim, J. H., Lee, S., Park, S., Choi, M., Jang, Y. P., Park, H.-J., et al. (2025) · Metabolic Brain Disease · doi:10.1007/s11011-025-01764-x · Cited by 1
Pandey, G., Garcia, R. C., Das, D., Mohan, A. R., Rodriguez, C., Pollock, D., Karthik, N., Nalluri, S., Nguyen, T., Polo, C., et al. (2026) · Journal of Neuroscience · doi:10.1523/jneurosci.1368-25.2026 · Cited by 1
Noda, S., & Hattori, N. (2026) · Frontiers in Neurology · doi:10.3389/fneur.2026.1924943 · Cited by 1
Roles of autophagy in brain homeostasis and disease
Kim, H., Wickstead, E. S., Zhou, X., Choi, I., & Yue, Z. (2026) · Nature Neuroscience · doi:10.1038/s41593-026-02426-6 · Cited by 1
Self-citationControl of Autophagy in Parkinson’s Disease
González‐Polo, R. A., Gómez‐Sánchez, R., Pizarro‐Estrella, E., Yakhine-Diop, S. M. S., Rodríguez‐Arribas, M., & Fuentes, J. M. (2015) · Current topics in neurotoxicity · doi:10.1007/978-3-319-13939-5_6 · Cited by 1
Methods for Measuring Autophagosome Flux—Impact and Relevance
du Toit, A., Hofmeyr, J. S., & Loos, B. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805420-8.00002-0 · Cited by 1
Lewis, P. A., Pérez‐Carrión, M. D., & Piccoli, G. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803783-6.00006-7 · Cited by 2
Fricke, M., Mechel, A., Evers, L., Twellsieck, B., Grein, J. M., Cima‐Omori, M., Al‐Azzani, M., Outeiro, T. F., Zweckstetter, M., Holzbaur, E. L. F., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117364 · Cited by 2
Aging and Parkinson’s Disease: Pathological Insight on Model Mice
Sato, S., & Hattori, N. (2022) · Springer eBooks · doi:10.1007/978-981-16-7977-3_23 · Cited by 1
Sim, J. P. L., Osborne, K. A., García, I. A., Matysik, A. S., & Kraut, R. S. (2016) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/084434 · Cited by 1
ULK1 and JNK are involved in mitophagy incurred by LRRK2 G2019S expression ESEARCH ARTICLE R
Zhu, Y., Wang, C., Yu, M. Y., Cui, J., Liu, L., & Xu, Z. (2013)
Valutazione delle lesioni dell’articolazione temporomandibolare: danni iatrogeni e traumatologici
Manfredini, D., & Guarda‐Nardini, L. (2008) · Revista Portuguesa do Dano Corporal · doi:10.14195/1647-8630_18_6
Necrosis, Apoptosis and Autophagy in Acute Brain Injury: The Utilities of Biomarkers
Sadasivan, S., Wang, K., & Zhang, Z. (2014) · CRC Press eBooks · doi:10.1201/b17644-6
The role of autophagy in neurotoxicity caused by extracellular ASYN
Djuranovic, A., Jeremić, M., Zogovic, N. S., Tovilović-Kovačević, G., & Dulović, M. (2016) · Medicinski podmladak · doi:10.5937/mp67-12608
Protein Oxidation, Quality-Control Mechanisms and Parkinson’s Disease
Hernández-Franco, P., Anandhan, A., & Franco, R. (2017) · Royal Society of Chemistry eBooks · doi:10.1039/9781782622888-00277
Investigating early functional alteration in a human iPSC-based model of Parkinson’s Disease
Carola, G. (2019) · Dipòsit Digital de la Universitat de Barcelona (Universitat de Barcelona)
Machine learning discriminates parkinsonian movement disorders in zebrafish
Hughes, G. L. (2019) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York)
Profes, M. S., Saghatelyan, A., & Lévesque, M. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.09.333435
Huo, Y., Sawant, A., Tan, Y., Mahdi, A., Li, T., Ma, H., Bhatt, V. D., Yan, R., Coleman, J., Dreyfus, C. F., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.07.447248
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Galvin, J. E., & Brás, J. (2017) · Oxford University Press eBooks · doi:10.1093/med/9780190681425.003.0055
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Zou, M., Wang, J., Lv, R., Nie, S., Zhu, L.-B., & Liu, X. (2022) · Neurology Asia · doi:10.54029/2022nkt
Self-citationZhang, M., Liu, X., Chang, J., Chen, D., Qian, S., & Kou, X. (2023) · Research Square · doi:10.21203/rs.3.rs-2449269/v1
Metaxakis, A., Pavlidis, M. A., & Tavernarakis, N. (2023) · Cells · doi:10.3390/cells12162024
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宋, 明. (2024) · Bioprocess · doi:10.12677/bp.2024.142013
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Churilova, A. V. (2024) · Успехи физиологических наук · doi:10.31857/s0301179824030056
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Sun, Y., Liu, W., Rao, X., Yu, L., & Chen, X. (2024) · International Conference on Bioinformatics and Biomedical Technology (ICBBT) · doi:10.1145/3674658.3674669
Pech, U., Janssens, J., Schoovaerts, N., Kuenen, S., Calatayud, C., Gallego, S. F., Makhzami, S., Hulselmans, G. J., Poovathingal, S. K., Davie, K., et al. (2025) · eLife · doi:10.7554/elife.98348.2
Regulated cell death: Discovery, features, and implications for neurodegenerative diseases
Pandey, S. K., Nanda, A., Singh, S., & Singh, R. K. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-32852-7.00001-2
Stem Cell Therapy for Neurological Disorders: From Bench to Bedside
Barbuti, P. A. (2014) · Springer eBooks · doi:10.1007/978-81-322-2110-4_4
Atg7-dependent autophagy is indispensable for mice spiral ganglion neurons
Sun, C., Gao, X., Zhang, Y., Li, Y., Cheng, C., Li, S., Gao, X., 钱晓云, & Zhou, H. (2026) · Hearing Research · doi:10.1016/j.heares.2026.109607
Mechanisms of programmed cell death in neurodegenerative diseases and their therapeutic potential
GENG, L., Pan, J., & Li, J. (2026) · Scientia Sinica Vitae · doi:10.1360/ssv-2025-0282
Sargent, D. (2018) · theses.fr (ABES) · doi:10.70675/2cd4ead6z0cd7z476dz8376z54bb3bd9a0ea
Gubinelli, F. (2019) · theses.fr (ABES) · doi:10.70675/b37261d3zcc7bz45bezb526z9e35982e09bb
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Sanchez-Mirasierra, I. (2023) · theses.fr (ABES) · doi:10.70675/7104d6d5z945ez494eza917zda9e6be1eea6
Gilloteaux, J., Suain, V., Charlier, C., & Nicaise, C. (2026) · Ultrastructural Pathology · doi:10.1080/01913123.2026.2668403
Sanchez-Mirasierra, I., Hernández-Díaz, S., Barry-Carroll, L., Marti, A. A., Ghimire, S., Delpech, J.-C., & Soukup, S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.26.727892
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Metadata
- Authors
- Friedman, L. G., Lachenmayer, M. L., Wang, J., He, L., Poulose, S. M., Komatsu, M., Holstein, G. R., & Yue, Z.
- Affiliations
- Icahn School of Medicine at Mount Sinai (US)
- Tokyo Metropolitan Institute of Medical Science (JP)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2012-05-30
- Volume
- 32
- Issue
- 22
- Pages
- 7585-7593
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC3382107
- OpenAlex
- W2126478464
- Cited by
- 303
- References
- 30
- Citations by year
- 2026: 14 · 2025: 20 · 2024: 18 · 2023: 21 · 2022: 18 · 2021: 23 · 2020: 29 · 2019: 19 · 2018: 22 · 2017: 19 · 2016: 24 · 2015: 20 · 2014: 13 · 2013: 30 · 2012: 12
- FWCI
- 15.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation (9724504, 1 S10 RR0 9145-01)
- Michael J. Fox Foundation for Parkinson's Research
- Bachmann-Strauss Dystonia and Parkinson Foundation
- Parkinson Alliance
- Deutsche Forschungsgemeinschaft
- National Institutes of Health (1S10 RR0 9145-01)
- U.S. Public Health Service (RNS055683A)
- Parkinsonfonden
- National Institute of Mental Health (T32MH096678)
- National Cancer Institute (R24CA095823)
- National Institute of Neurological Disorders and Stroke (R21NS055683, R01NS072359, R01NS060809, NS060809, R01NS060123)
- National Center for Research Resources (1 S10RR0 9145-01)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Keywords
- Parkinson's disease, autophagy, ATG7, dopaminergic neurons, axonal degeneration, dendritic degeneration, alpha-synuclein, LRRK2, Lewy bodies, midbrain, striatal dopamine, locomotor deficits, neurodegeneration
- MeSH terms
- Autophagy-Related Protein 5, Autophagy-Related Protein 7, Animals, Autophagy, Brain, Cells, Cultured, Inclusion Bodies, Chromatography, High Pressure Liquid, Dendrites, Disease Models, Animal, Dopamine, Embryo, Mammalian, Fibroblasts, Gene Expression Regulation, Intermediate Filament Proteins, Mice, Transgenic, Microtubule-Associated Proteins, Motor Activity, Movement Disorders, Nerve Degeneration, Nerve Tissue Proteins, Tyrosine 3-Monooxygenase, Presynaptic Terminals, Ubiquitin, Ephrin-B1, Mice, alpha-Synuclein, Dopaminergic Neurons, Nestin
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