Development and Characterization of a New Parkinson's Disease Model Resulting from Impaired Autophagy
Open accessAbstract
Parkinson's disease (PD) is a progressive neurodegenerative disease caused by the interaction of genetic and environmental factors. However, the etiology of PD remains largely unknown. Macroautophagy is known to play an essential role in the degradation of abnormal proteins and organelles. Furthermore, the loss of autophagy-related (Atg) genes results in neurodegeneration and abnormal protein accumulation. Since these are also pathologic features of Parkinson's disease, the conditional impairment of autophagy may lead to improved animal models for the study of PD. Using transgenic mice expressing Cre recombinase under the control of either the dopamine transporter or the engrailed-1 promoters, we generated mice with the conditional deletion of Atg7 in the dopamine neurons of the substantia nigra pars compacta, other regions of the midbrain, and also the hindbrain. This conditional impairment of autophagy results in the age-related loss of dopaminergic neurons and corresponding loss of striatal dopamine, the accumulation of low-molecular-weight α-synuclein, and the presence of ubiquitinated protein aggregates, recapitulating many of the pathologic features of PD. These conditional knock-out animals provide insight into the process of autophagy in Parkinson's disease pathology.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Several lines of evidence indicate a role for autophagy in the regulation of synuclein homeostasis, suggesting that dysfunctional autophagic clearance may contribute to the development of synuclein inclusions.
“Several lines of evidence indicate a role for autophagy in the regulation of synuclein homeostasis5,6,15, suggesting that dysfunctional autophagic clearance may contribute to the development of synuclein inclusions.”
From Loss of autophagy in dopaminergic neurons causes Lewy pathology and motor dysfunction in aged mice (2018) · cites this paper as [15]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240 · see citing works
Autophagy in the Pathogenesis of Disease
Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069 · see citing works
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578 · see citing works
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026 · see citing works
AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
Krüger, R., Kuhn, W., Müller, T., Woitalla, D., Graeber, M., Kösel, S., Przuntek, H., Epplen, J. T., Schols, L., & Riess, O. (1998) · Nature Genetics · doi:10.1038/ng0298-106 · Cited by 3,836 · see citing works
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 · see citing works
Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276 · see citing works
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835 · see citing works
Homeostatic 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 · see citing works
Impaired 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 2× · see citing works
“Interestingly, aberrant A53T -synuclein is thought to be associated specifically with CMA (Cuervo et al., 2004; Winslow et al., 2010).”
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 · see citing works
Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease.
Anglade, P., Vyas, S., Javoy-Agid, F., Herrero, M. T., Michel, P. P., Marquez, J., Prigent, A., Ruberg, M., Hirsch, É. C., & Agid, Y. (1997) · PubMed · Cited by 1,045 · see citing works
α-Synuclein impairs macroautophagy: implications for Parkinson’s disease
Winslow, A. R., Chen, C.-W., Corrochano, S., Acevedo-Arozena, A., Gordon, D. E., Peden, A. A., Lichtenberg, M., Menzies, F. M., Ravikumar, B., Imarisio, S., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201003122 · Cited by 825 · see citing works
Vogiatzi, T., Xilouri, M., Vekrellis, K., & Stefanis, L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801992200 · Cited by 683 · see citing works
Diagnosis and treatment of Parkinson disease: molecules to medicine
Savitt, J. M. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29178 · Cited by 649 · see citing works
Self-citationUbiquitin Chain Editing Revealed by Polyubiquitin Linkage-Specific Antibodies
Newton, K., Matsumoto, M. L., Wertz, I. E., Kirkpatrick, D. S., Lill, J. R., Tan, J., Dugger, D. L., Gordon, N. C., Sidhu, S. S., Fellouse, F. A., et al. (2008) · Cell · doi:10.1016/j.cell.2008.07.039 · Cited by 553 · see citing works
Role of autophagy in G2019S‐LRRK2‐associated neurite shortening in differentiated SH‐SY5Y cells
Plowey, E., Cherra, S. J., Liu, Y.-J., & Chu, C. T. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05217.x · Cited by 523 · see citing works
Kuusisto, E., Salminen, A., & Alafuzoff, I. I. (2001) · Neuroreport · doi:10.1097/00001756-200107200-00009 · Cited by 347 · see citing works
Two lineage boundaries coordinate vertebrate apical ectodermal ridge formationPreprint
Kimmel, R. A., Turnbull, D. H., Blanquet, V., Wurst, W., Loomis, C. A., & Joyner, A. L. (2000) · Genes & Development · doi:10.1101/gad.14.11.1377 · Cited by 341 · see citing works
Targeted gene expression in dopamine and serotonin neurons of the mouse brain
Zhuang, X., Masson, J., Gingrich, J. A., Rayport, S., & Hen, R. (2004) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2004.09.020 · Cited by 316 · see citing works
All-you-can-eat: autophagy in neurodegeneration and neuroprotection
Jaeger, P. A., & Wyss‐Coray, T. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-16 · Cited by 175 · see citing works
Bcl-x Is Required for Proper Development of the Mouse Substantia Nigra
Savitt, J. M., Jang, S. S., Mu, W., Dawson, V. L., & Dawson, T. M. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0760-05.2005 · Cited by 173 · see citing works
Self-citationThe emerging role of autophagy in Parkinson's disease
Cheung, Z. H., & Ip, N. Y. (2009) · Molecular Brain · doi:10.1186/1756-6606-2-29 · Cited by 88 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Understanding Dopaminergic Cell Death Pathways in Parkinson Disease
Michel, P. P., Hirsch, É. C., & Hunot, S. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.038 · Cited by 594 · see citing works
Synaptopathies: synaptic dysfunction in neurological disorders – A review from students to students
Lepeta, K., Lourenco, M. V., Schweitzer, B. C., Martino Adami, P. V., Banerjee, P., Catuara‐Solarz, S., de La Fuente Revenga, M., Guillem, A. M., Haidar, M., Ijomone, O. M., et al. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13713 · Cited by 386 · see citing works
Autophagy in Parkinson's Disease
Hou, X., Watzlawik, J. O., Fiesel, F. C., & Springer, W. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.037 · Cited by 355 · see citing works
Lysosomal impairment in Parkinson's disease
Dehay, B., Martinez‐Vicente, M., Caldwell, G. A., Caldwell, K. A., Yue, Z., Cookson, M. R., Klein, C., Vila, M., & Bezard, E. (2013) · Movement Disorders · doi:10.1002/mds.25462 · Cited by 340 · see citing works
Hale, A. N., Ledbetter, D., Gawriluk, T. R., & Rucker, E. B. (2013) · Autophagy · doi:10.4161/auto.24273 · Cited by 336 · see citing works
Stavoe, A. K. H., & Holzbaur, E. L. F. (2019) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100818-125242 · Cited by 328 · see citing works
Lysosomal Biology and Function: Modern View of Cellular Debris Bin
Trivedi, P., Bartlett, J., & Pulinilkunnil, T. (2020) · Cells · doi:10.3390/cells9051131 · Cited by 240 · see citing works
Autophagy and A lpha‐ S ynuclein: R elevance to P arkinson's D isease and R elated S ynucleopathies
Xilouri, M., Brekk, O. R., & Stefanis, L. (2016) · Movement Disorders · doi:10.1002/mds.26477 · Cited by 266 · see citing works
Role of metabolism in neurodegenerative disorders
Procaccini, C., Santopaolo, M., Faicchia, D., Colamatteo, A., Formisano, L., de Candia, P., Galgani, M., De Rosa, V., & Matarese, G. (2016) · Metabolism · doi:10.1016/j.metabol.2016.05.018 · Cited by 258 · see citing works
The role of the LRRK2 gene in Parkinsonism
Li, J.-Q., Tan, L., & Yu, J.-T. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-47 · Cited by 249 · see citing works
Singh, N., Haldar, S., Tripathi, A. K., Horback, K., Wong, J., Sharma, D., Beserra, A., Suda, S., Anbalagan, C., Dev, S., et al. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4931 · Cited by 205 · see citing works
The Autophagy Lysosomal Pathway and Neurodegeneration
Finkbeiner, S. (2020) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033993 · Cited by 196 · see citing works
Ghosh, A., Tyson, T., George, S., Hildebrandt, E. N., Steiner, J. A., Madaj, Z., Schulz, E., Machiela, E., McDonald, W. G., Galvis, M. L. E., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aag2210 · Cited by 187 · see citing works
How is alpha‐synuclein cleared from the cell?
Stefanis, L., Emmanouilidou, E., Pantazopoulou, M., Kirik, D., Vekrellis, K., & Tofaris, G. K. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14704 · Cited by 174 · see citing works
LRRK2 pathobiology in Parkinson's disease
Martin, I., Kim, J. W., Dawson, V. L., & Dawson, T. M. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12949 · Cited by 168 · see citing works
Self-citationGlucocerebrosidase gene therapy prevents α-synucleinopathy of midbrain dopamine neurons
Rocha, E. M., Smith, G. A., Park, E. Y. H., Cao, H., Brown, E., Hayes, M. A., Beagan, J. A., McLean, J. R., Izen, S. C., Perez-Torres, E., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.09.009 · Cited by 157 · see citing works
Tu, H., Yuan, B., Hou, X., Zhang, X., Pei, C., Ma, Y., Yang, Y., Fan, Y., Qin, Z., Liu, C., et al. (2021) · Aging Cell · doi:10.1111/acel.13522 · Cited by 152 · see citing works
Dysfunction of Cellular Proteostasis in Parkinson’s Disease
Lehtonen, Š., Sonninen, T.-M., Wojciechowski, S., Goldsteins, G., & Koıstınaho, J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00457 · Cited by 145 · see citing works
Rocha, E. M., Smith, G. A., Park, E. Y. H., Cao, H., Graham, A.-R., Brown, E., McLean, J. R., Hayes, M. A., Beagan, J. A., Izen, S. C., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6307 · Cited by 144 · see citing works
Autophagy in axonal and dendritic degeneration
Yang, Y., Coleman, M. P., Zhang, L., Zheng, X., & Yue, Z. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.04.001 · Cited by 144 · see citing works
Macroautophagy in CNS health and disease
Griffey, C. J., & Yamamoto, A. (2022) · Nature reviews. Neuroscience · doi:10.1038/s41583-022-00588-3 · Cited by 144 · see citing works
“LRRK2: Autophagy and Lysosomal Activity”
Madureira, M., Connor‐Robson, N., & Wade‐Martins, R. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00498 · Cited by 141 · see citing works
Lionaki, E., Markaki, M., Palikaras, K., & Tavernarakis, N. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.04.010 · Cited by 134 · see citing works
Impairment of chaperone-mediated autophagy induces dopaminergic neurodegeneration in rats
Xilouri, M., Brekk, O. R., Polissidis, A., Chrysanthou‐Piterou, M., Kloukina, I., & Stefanis, L. (2016) · Autophagy · doi:10.1080/15548627.2016.1214777 · Cited by 126 · see citing works
Loss of autophagy in dopaminergic neurons causes Lewy pathology and motor dysfunction in aged mice
Sato, S., Uchihara, T., Fukuda, T., Noda, S., Kondo, H., Saiki, S., Komatsu, M., Uchiyama, Y., Tanaka, K., & Hattori, N. (2018) · Scientific Reports · doi:10.1038/s41598-018-21325-w · Cited by 125 · see citing works
Zhang, M., Deng, Y., Zhang, J., Liu, J., Li, Y., Su, H., & Qu, Q. (2018) · Aging and Disease · doi:10.14336/ad.2017.0517 · Cited by 125 · see citing works
The Vicious Cycle Between α ‐Synuclein Aggregation and Autophagic‐Lysosomal Dysfunction
Bellomo, G., Paciotti, S., Gatticchi, L., & Parnetti, L. (2019) · Movement Disorders · doi:10.1002/mds.27895 · Cited by 114 · see citing works
Parkinson’s disease: experimental models and reality
Jiang, P., & Dickson, D. W. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1788-5 · Cited by 113 · see citing works
Wang, Z., Liu, J., Zhu, Z., Su, C.-F., Sreenivasmurthy, S. G., Iyaswamy, A., Lu, J., Chen, G., Song, J., & Li, M. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110968 · Cited by 108 · see citing works
Lotfi, P., Tse, D. Y., Di Ronza, A., Seymour, M. L., Martano, G., Cooper, J. D., Pereira, F. A., Passafaro, M., Wu, S. M., & Sardiello, M. (2018) · Autophagy · doi:10.1080/15548627.2018.1474313 · Cited by 106 · see citing works
Animal Models of Parkinson's Disease: A Gateway to Therapeutics?
Le, W., Sayana, P., & Jankovic, J. J. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0234-1 · Cited by 106 · see citing works
Autophagy in neuronal cells: general principles and physiological and pathological functions
Daμμe, M., Suntio, T., Säftig, P., & Eskelinen, E. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1361-4 · Cited by 102 · see citing works
Ren, H., Zhai, W., Lu, X., & Wang, G. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.691881 · Cited by 101 · see citing works
Kett, L. R., Stiller, B., Bernath, M. M., Tasset, I., Blesa, J., Jackson-Lewis, V. R., Chan, R., Zhou, B., Paolo, G. D., Przedborski, S., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.0632-14.2015 · Cited by 100 · see citing works
Alpha-Synuclein defects autophagy by impairing SNAP29-mediated autophagosome-lysosome fusion
Tang, Q., Gao, P., Arzberger, T., Höllerhage, M., Herms, J. W., Höglinger, G. U., & Koeglsperger, T. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04138-0 · Cited by 99 · see citing works
Morris, G., Anderson, G., Berk, M., & Maes, M. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8477-8 · Cited by 96 · see citing works
LncRNA HOTAIR targets miR-126-5p to promote the progression of Parkinson’s disease through RAB3IP
Lin, Q., Hou, S., Dai, Y., Jiang, N., & Lin, Y. (2019) · Biological Chemistry · doi:10.1515/hsz-2018-0431 · Cited by 94 · see citing works
The endosomal pathway in Parkinson's disease
Perrett, R. M., Alexopoulou, Z., & Tofaris, G. K. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.02.009 · Cited by 87 · see citing works
Kumaran, R., & Cookson, M. R. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv236 · Cited by 86 · see citing works
How Parkinson's disease meets nucleolar stress
Parlato, R., & Liss, B. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.12.014 · Cited by 86 · see citing works
Wang, J.-D., Cao, Y.-L., Li, Q., Yang, Y., Jin, M., Chen, D., Wang, F., Wang, G., Qin, Z., Hu, L., et al. (2015) · Autophagy · doi:10.1080/15548627.2015.1100930 · Cited by 82 · see citing works
Molecular Events Underlying Parkinson’s Disease – An Interwoven Tapestry
Lim, K., & Zhang, C. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00033 · Cited by 79 · see citing works
Candelise, N., Schmitz, M., Thüne, K., Cramm, M., Rábano, A., Zafar, S., Stoops, E., Vanderstichele, H., Villar‐Piqué, A., Llorens, F., et al. (2020) · Translational Neurodegeneration · doi:10.1186/s40035-019-0181-9 · Cited by 76 · see citing works
Dysregulation of the autophagic-lysosomal pathway in Gaucher and Parkinson's disease
Pitcairn, C., Wani, W. Y., & Mazzulli, J. R. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.03.008 · Cited by 75 · see citing works
Parkinson's disease: acid‐glucocerebrosidase activity and alpha‐synuclein clearance
Blanz, J., & Säftig, P. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13517 · Cited by 70 · see citing works
Wang, M., Cheng, X.-Y., Jin, M., Cao, Y.-L., Yang, Y., Wang, J.-D., Li, Q., Wang, F., Hu, L., & Liu, C. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.05.008 · Cited by 70 · see citing works
Manzoni, C., & Lewis, P. A. (2013) · The FASEB Journal · doi:10.1096/fj.12-223842 · Cited by 62 · see citing works
Role of Sirt1 During the Ageing Process: Relevance to Protection of Synapses in the Brain
Godoy, J. A., Zolezzi, J. M., Braidy, N., & Inestrosa, N. C. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8645-5 · Cited by 60 · see citing works
Pathological and Therapeutic Advances in Parkinson’s Disease: Mitochondria in the Interplay
Naren, P., Cholkar, A., Kamble, S., Khan, S. S., Srivastava, S., Madan, J., Mehra, N. K., Tiwari, V., Singh, S. B., & Khatri, D. K. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220682 · Cited by 57 · see citing works
Assous, M., Had‐Aissouni, L., Gubellini, P., Melon, C., Nafia, I., Salin, P., Goff, L. K., & Kachidian, P. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.01.011 · Cited by 55 · see citing works
Rekaik, H., de Thé, F.-X. B., Prochiantz, A., Fuchs, J., & Joshi, R. L. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.10.002 · Cited by 54 · see citing works
Lipophagy: a new player in CNS disorders
Haidar, M., Loix, M., Bogie, J. F. J., & Hendriks, J. J. A. (2021) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2021.08.010 · Cited by 51 · see citing works
Pradas, E., & Martínez‐Vicente, M. (2023) · Cells · doi:10.3390/cells12010191 · Cited by 50 · see citing works
Assessment of Autophagy in Neurons and Brain Tissue
Benito‐Cuesta, I., Díez, H., Ordóñez‐Gutiérrez, L., & Wandosell, F. G. (2017) · Cells · doi:10.3390/cells6030025 · Cited by 49 · see citing works
The unlikely partnership between LRRK 2 and α‐synuclein in Parkinson's disease
Cresto, N., Gardier, C., Gubinelli, F., Gaillard, M., Liot, G., West Andrew, B., & Brouillet, E. (2018) · European Journal of Neuroscience · doi:10.1111/ejn.14182 · Cited by 48 · see citing works
Loss of PINK1 Impairs Stress-Induced Autophagy and Cell Survival
Parganlija, D., Klinkenberg, M., Domínguez-Bautista, J. A., Hetzel, M., Gispert, S., Chimi, M. A., Dröse, S., Mai, S., Brandt, U., Auburger, G. W. J., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095288 · Cited by 46 · see citing works
Kim, H., Calatayud, C., Guha, S. K., Fernández‐Carasa, I., Berkowitz, L. A., Carballo‐Carbajal, I., Ezquerra, M., Fernández‐Santiago, R., Kapahi, P., Raya, Á., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0881-7 · Cited by 46 · see citing works
Fernandes, T., Domingues, M. R., Moreira, P. I., & Pereira, C. (2023) · Biology · doi:10.3390/biology12030414 · Cited by 44 · see citing works
Alpha-Synuclein and the Endolysosomal System in Parkinson’s Disease: Guilty by Association
Teixeira, M., Sheta, R., Idi, W., & Oueslati, A. (2021) · Biomolecules · doi:10.3390/biom11091333 · Cited by 43 · see citing works
Endolysosomal dysfunction in Parkinson's disease: Recent developments and future challenges
Kett, L. R., & Dauer, W. T. (2016) · Movement Disorders · doi:10.1002/mds.26797 · Cited by 42 · see citing works
Singh, N., Haldar, S., Tripathi, A. K., McElwee, M. K., Horback, K., & Beserra, A. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5874 · Cited by 41 · see citing works
Exploring the Role of Autophagy Dysfunction in Neurodegenerative Disorders
Rana, T., Behl, T., Sehgal, A., Mehta, V., Singh, S., Bhatia, S., Al‐Harrasi, A., & BUNGAU, S. G. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02472-0 · Cited by 41 · see citing works
Urate promotes SNCA/α-synuclein clearance via regulating mTOR-dependent macroautophagy
Sheng, Y., Chen, X., Hou, X., Yuan, X., Yuan, B., Yuan, Y., Zhang, Q., Cao, X., Liu, C., Luo, W., et al. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.08.007 · Cited by 40 · see citing works
Chen, M., & Wu, R. (2018) · Journal of Biomedical Science · doi:10.1186/s12929-018-0454-0 · Cited by 40 · see citing works
Hunn, B. H. M., Vingill, S., Threlfell, S., Alegre-Abarrategui, J., Magdelyns, M., Deltheil, T., Bengoa-Vergniory, N., Oliver, P. L., Cioroch, M., Doig, N. M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.09.029 · Cited by 38 · see citing works
Lian, X., Liu, Z., Gan, Z., Yan, Q., Tong, L., Qiu, L., Liu, Y., Chen, J., & Li, Z. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00764 · Cited by 38 · see citing works
Navarro-Yepes, J., Anandhan, A., Bradley, E., Bohovych, I., Yarabe, B., de Jong, A., Ovaa, H., Zhou, Y., Khalimonchuk, O., Quintanilla‐Vega, B., et al. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9414-9 · Cited by 38 · see citing works
Homeostatic p62 levels and inclusion body formation in CHCHD2 knockout mice
Sato, S., Noda, S., Torii, S., Amo, T., Ikeda, A., Funayama, M., Yamaguchi, J., Fukuda, T., Kondo, H., Tada, N., et al. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab057 · Cited by 38 · see citing works
Current Evidence for a Role of Neuropeptides in the Regulation of Autophagy
Catalani, E., Palma, C. D., Perrotta, C., & Cervia, D. (2017) · BioMed Research International · doi:10.1155/2017/5856071 · Cited by 37 · see citing works
Genetic Modifiers of Neurodegeneration in a Drosophila Model of Parkinson’s Disease
Lavoy, S., Chittoor-Vinod, V. G., Chow, C. Y., & Martin, I. (2018) · Genetics · doi:10.1534/genetics.118.301119 · Cited by 37 · see citing works
Autophagy Stimulation Decreases Dopaminergic Neuronal Death Mediated by Oxidative Stress
Ramirez-Moreno, M. J., Duarte-Jurado, A. P., Gopar‐Cuevas, Y., González-Alcocer, A., Loera‐Arias, M. D. J., Cárdenas, O. S., Montes‐de‐Oca‐Luna, R., Rodríguez‐Rocha, H., & García‐García, A. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-01654-1 · Cited by 37 · see citing works
Gottschalk, G., Peterson, D. L., Knox, K. K., Maynard, M., Whelan, R. J., & Roy, A. (2022) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2022.103731 · Cited by 36 · see citing works
Tang, H., Zheng, Z., Wang, H., Wang, L., Zhao, G., & Wang, P. (2022) · Nutrients · doi:10.3390/nu14071504 · Cited by 35 · see citing works
Role of Ceramides and Sphingolipids in Parkinson's Disease
Vos, M. H., Klein, C., & Hicks, A. A. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168000 · Cited by 35 · see citing works
LRRK2 interferes with aggresome formation for autophagic clearance
Bang, Y., Kim, K., Seol, W., & Choi, H. J. (2016) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2016.06.007 · Cited by 35 · see citing works
Novel Targets for Parkinson’s Disease: Addressing Different Therapeutic Paradigms and Conundrums
Rane, P., Sarmah, D., Bhute, S., Kaur, H., Goswami, A., Kalia, K., Borah, A., Dave, K. R., Sharma, N., & Bhattacharya, P. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00180 · Cited by 35 · see citing works
A Cleaning Crew: The Pursuit of Autophagy in Parkinson’s Disease
Parekh, P., Sharma, N., Gadepalli, A., Shahane, A., Sharma, M., & Khairnar, A. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00244 · Cited by 34 · see citing works
Protein recycling pathways in neurodegenerative diseases
Fecto, F., Esengul, Y. T., & Siddique, T. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt243 · Cited by 33 · see citing works
Rapamycin and bafilomycin A1 alter autophagy and megakaryopoiesis
Wang, Q., You, T., Fan, H., Wang, Y., Chu, T., Poncz, M., & Zhu, L. (2016) · Platelets · doi:10.1080/09537104.2016.1204436 · Cited by 33 · see citing works
Neuroprotective Transcription Factors in Animal Models of Parkinson Disease
de Thé, F.-X. B., Rekaik, H., Prochiantz, A., Fuchs, J., & Joshi, R. L. (2015) · Neural Plasticity · doi:10.1155/2016/6097107 · Cited by 33 · see citing works
Jiang, L., Yuan, F., Yin, X., & Dong, J. (2014) · Connective Tissue Research · doi:10.3109/03008207.2014.942419 · Cited by 33 · see citing works
Rivero-Ríos, P., Romo-Lozano, M., Fasiczka, R., Naaldijk, Y., & Hilfiker, S. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00556 · Cited by 32 · see citing works
Silva, F. D., Rode, M. P., Vietta, G. G., Iop, R. D. R., Creczynski‐Pasa, T. B., Martin, A., & da Silva, R. (2021) · Molecular Medicine Reports · doi:10.3892/mmr.2021.12257 · Cited by 32 · see citing works
Padilla-Godínez, F. J., Ramos-Acevedo, R., Martínez-Becerril, H. A., Bernal-Conde, L. D., Garrido-Figueroa, J. F., Hiriart, M., Hernández-López, A., Argüero‐Sánchez, R., Callea, F., & Guerra‐Crespo, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212467 · Cited by 32 · see citing works
Autophagy and lysosomal pathways in nervous system disorders
Bingol, B. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.04.009 · Cited by 31 · see citing works
Alpha-lipoic acid alleviated 6-OHDA-induced cell damage by inhibiting AMPK/mTOR mediated autophagy
Zhou, L., & Cheng, Y. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.04.009 · Cited by 31 · see citing works
Pitcairn, C., Murata, N., Zalon, A. J., Stojkovska, I., & Mazzulli, J. R. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.0610-22.2023 · Cited by 29 · see citing works
Convergent pathways in Parkinson’s disease
Cherubini, M., & Wade‐Martins, R. (2017) · Cell and Tissue Research · doi:10.1007/s00441-017-2700-2 · Cited by 28 · see citing works
Fibroblast growth factor 21 and autophagy: A complex interplay in Parkinson disease
Kakoty, V., Sarathlal, K. C., Tang, R.-D., Yang, C. H., Dubey, S. K., & Taliyan, R. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110145 · Cited by 27 · see citing works
Macroautophagy and Mitophagy in Neurodegenerative Disorders: Focus on Therapeutic Interventions
Magalhães, J. D., Fão, L., Vilaça, R., Cardoso, S. M., & Rego, A. C. (2021) · Biomedicines · doi:10.3390/biomedicines9111625 · Cited by 27 · see citing works
α-Synuclein disrupts microglial autophagy through STAT1-dependent suppression of Ulk1 transcription
Pei, C., Hou, X., Ma, Z., Tu, H., Qian, H.-C., Li, Y., Li, K., Liu, C., Ouyang, L., Liu, J., et al. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-024-03268-4 · Cited by 26 · see citing works
Hou, X., Tu, H., Qian, H.-C., Li, Q., Yang, Y., Xu, G., Wang, F., Liu, C., Wang, Y.-L., & Hu, L. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105187 · Cited by 25 · see citing works
The pallidopyramidal syndromes
Kara, E., Hardy, J., & Houlden, H. (2013) · Current Opinion in Neurology · doi:10.1097/wco.0b013e3283632e83 · Cited by 24 · see citing works
Deletion of autophagy-related gene 7 in dopaminergic neurons prevents their loss induced by MPTP
Niu, X., Huang, H.-J., Zhang, J., Zhang, C., Chen, W., Sun, C., Ding, Y., & Liao, M. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.09.037 · Cited by 24 · see citing works
Song, Y., Ding, W., Xiao, Y. C., & Lu, K.-J. (2015) · Neuroscience Journal · doi:10.1155/2015/543758 · Cited by 23 · see citing works
Inoue, K., Rispoli, J. M., Yang, L., MacLeod, D., Beal, M. F., Klann, E., & Abeliovich, A. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003845 · Cited by 22 · see citing works
Zhang, Z., Guo, P., Huang, S., Jia, Z., Chen, T., Liu, X. B., Feng, H., & Chen, Y. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/4177317 · Cited by 22 · see citing works
Yang, X., Li, Y., Chen, L., Xu, M., Wu, J., Zhang, P., Nel, D., & Sun, B. (2020) · Pharmaceutical Biology · doi:10.1080/13880209.2020.1784237 · Cited by 21 · see citing works
Proteomics as a new paradigm to tackle Parkinson’s disease research challenges
Licker, V., & Burkhard, P. R. (2014) · Translational Proteomics · doi:10.1016/j.trprot.2014.08.001 · Cited by 21 · see citing works
Zhang, S., Xue, Z., Huang, L., Fang, R., He, Y., Li, L., & Fang, Y. (2013) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-013-9964-1 · Cited by 20 · see citing works
- Authors
- Ahmed, I., Liang, Y., Schools, S., Dawson, V. L., Dawson, T. M., & Savitt, J. M.
- Affiliations
- Johns Hopkins University (US)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2012-11-14
- Volume
- 32
- Issue
- 46
- Pages
- 16503-16509
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC3508432
- OpenAlex
- W2026969412
- Cited by
- 144
- References
- 23
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 5 · 2023: 6 · 2022: 10 · 2021: 19 · 2020: 10 · 2019: 13 · 2018: 10 · 2017: 8 · 2016: 16 · 2015: 12 · 2014: 16 · 2013: 12
- FWCI
- 8.36
- 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)
- Europe PMC (PubMed Central) (acceptedVersion)
- Funders
- Parkinson's Disease Foundation
- Adrienne Helis Malvin Medical Research Foundation
- JPB Foundation
- Johns Hopkins University
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (P50NS38377, K08NS052624, P50NS038377)
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
- Keywords
- Parkinson's disease, autophagy, ATG7, conditional knockout mice, dopaminergic neurons, substantia nigra pars compacta, alpha-synuclein aggregation, ubiquitinated protein aggregates, striatal dopamine, neurodegeneration, transgenic mice
- MeSH terms
- Autophagy-Related Protein 7, Dynactin Complex, Animals, Autophagy, Cell Count, Chromatography, High Pressure Liquid, Disease Models, Animal, Dopamine, Electrochemistry, Immunohistochemistry, Microtubule-Associated Proteins, Parkinson Disease, Blotting, Western, Neostriatum, Gene Deletion, Mice, Knockout, Neurotransmitter Agents, Ubiquitin, Polyubiquitin, Mice, alpha-Synuclein, Dopaminergic Neurons
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
