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Essential role for autophagy protein Atg7 in the maintenance of axonal homeostasis and the prevention of axonal degeneration
Open accessAbstract
Autophagy is a regulated lysosomal degradation process that involves autophagosome formation and transport. Although recent evidence indicates that basal levels of autophagy protect against neurodegeneration, the exact mechanism whereby this occurs is not known. By using conditional knockout mutant mice, we report that neuronal autophagy is particularly important for the maintenance of local homeostasis of axon terminals and protection against axonal degeneration. We show that specific ablation of an essential autophagy gene, Atg7 , in Purkinje cells initially causes cell-autonomous, progressive dystrophy (manifested by axonal swellings) and degeneration of the axon terminals. Consistent with suppression of autophagy, no autophagosomes are observed in these dystrophic swellings, which is in contrast to accumulation of autophagosomes in the axonal dystrophic swellings under pathological conditions. Axonal dystrophy of mutant Purkinje cells proceeds with little sign of dendritic or spine atrophy, indicating that axon terminals are much more vulnerable to autophagy impairment than dendrites. This early pathological event in the axons is followed by cell-autonomous Purkinje cell death and mouse behavioral deficits. Furthermore, ultrastructural analyses of mutant Purkinje cells reveal an accumulation of aberrant membrane structures in the axonal dystrophic swellings. Finally, we observe double-membrane vacuole-like structures in wild-type Purkinje cell axons, whereas these structures are abolished in mutant Purkinje cell axons. Thus, we conclude that the autophagy protein Atg7 is required for membrane trafficking and turnover in the axons. Our study implicates impairment of axonal autophagy as a possible mechanism for axonopathy associated with neurodegeneration.
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“Interestingly, Purkinje cells lacking the essential autophagy genes Atg5 or Atg7 die over time2021.”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [20]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“axons in the deep cerebellar nuclei of mice lacking Atg5 and Atg7 in Purkinje cells displayed increased membranous and vacuole-like structures”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [20]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“For example, the conditional deletion of the autophagy genes Atg5 or Atg7 in Purkinje cells leads to degeneration of these cells2021.”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [20]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
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“Mice with mutations in the autophagy genes Atg5, Atg7, FIP200 and Epg5 show the importance of autophagy in neurons and their stem cell precursors20212223.”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [20]
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“In several in vivo models, neurons, and in particular Purkinje cells, demonstrate a striking requirement for functional autophagy in order to survive.”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [20]
In the citing paper
“Purkinje-specific deletion of Atg7 (encoding an essential E1-like enzyme required for activating ATG12, ATG8, and LC3-I) results in Purkinje cell-autonomous axonal dystrophy and degeneration in mice [376].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [376]
In the citing paper
“These encompass Purkinje cells in the cerebellum (leading to progressive dystrophy) (Komatsu et al, 2007)”
From Autophagy in major human diseases (2021) · cites this paper as Komatsu et al, 2007
In the citing paper
“In fact, these autophagosome-like structures were previously reported in Atg7-deficient brains14.”
From Loss of autophagy in dopaminergic neurons causes Lewy pathology and motor dysfunction in aged mice (2018) · cites this paper as [14]
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LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605
Self-citationCui, C., Cui, J., Jin, F., Cui, Y., Li, R., Jiang, X., Tian, Y., Wang, R. C., Jiang, P., & Gao, J. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479571 · Cited by 5,214
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
Levine, B., & Klionsky, D. J. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00099-1 · Cited by 3,728
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-citationBjørkøy, 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
Impairment of starvation-induced and constitutive autophagy in Atg7 -deficient mice
Komatsu, M., Waguri, S., Ueno, T., Iwata, J., Murata, S., Tanida, I., Ezaki, J., Mizushima, N., Ohsumi, Y., Uchiyama, Y., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412022 · Cited by 2,331
Self-citationMizushima, N., Yamamoto, A., Matsui, M., Yoshimori, T., & Ohsumi, Y. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-09-0704 · Cited by 2,105
Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study
Nixon, R. A., Wegiel, J., Kumar, A., Yu, W. H., Peterhoff, C., Cataldo, A., & Cuervo, A. M. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.113 · Cited by 1,588
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
Research works printed but not linked: 2
- P Anglade, S Vyas, F Javoy-Agid, MT Herrero, PP Michel, J Marquez, A Mouatt-Prigent, M Ruberg, EC Hirsch, Y Agid Histol Histopathol 12, 25–31 (1997).
- L Roizin, S Stellar, N Willson, J Whittier, JC Liu Trans Am Neurol Assoc 99, 240–243 (1974).
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Cabrera-Rodríguez, R., Pérez-Yanes, S., Estévez‐Herrera, J., Márquez-Arce, D., Cabrera, C., Espert, L., Blanco, J., & Valenzuela-Fernández, A. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.661446 · Cited by 37
Autophagy dysregulation and the fate of retinal ganglion cells in glaucomatous optic neuropathy
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Shin, J. H., Lee, Y. A., Lee, J. K., Lee, Y. B., Cho, W., Im, D. S., Lee, J. H., Yun, B. S., Springer, J. E., & Gwag, B. J. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07771.x · Cited by 36
Loss of proteostasis induced by amyloid beta peptide in brain endothelial cells
Fonseca, A. C. R. G., Oliveira, C. R., Pereira, C., & Cardoso, S. M. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.02.016 · Cited by 39
Alternative autophagy: mechanisms and roles in different diseases
Feng, H., Wang, N., Zhang, N., & Liao, H.-H. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00851-1 · Cited by 39
Sin, O., & Nollen, E. A. A. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1985-0 · Cited by 43
Cell Specific Changes of Autophagy in a Mouse Model of Contusive Spinal Cord Injury
Muñoz‐Galdeano, T., Reigada, D., del Águila, Á., Velez, I., Caballero-López, M. J., Maza, R. M., & Nieto‐Díaz, M. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00164 · Cited by 37
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Decet, M., & Verstreken, P. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.790721 · Cited by 34
Protein clearing pathways in ALS.
Ferrucci, M., Fulceri, F., Toti, L., Soldani, P., Siciliano, G., Paparelli, A., & Fornai, F. (2011) · PubMed · doi:10.4449/aib.v149i1.1258 · Cited by 35
Recent insights on principles of synaptic protein degradation
Cohen, L. D., & Ziv, N. E. (2017) · F1000Research · doi:10.12688/f1000research.10599.1 · Cited by 35
Valek, L., Heidler, J., Scheving, R., Wittig, I., & Tegeder, I. (2018) · Redox Biology · doi:10.1016/j.redox.2018.10.002 · Cited by 35
Limanaqi, F., Busceti, C. L., Celli, R., Biagioni, F., & Fornai, F. (2021) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2021.102112 · Cited by 40
Au, A. K., Chen, Y., Du, L., Smith, C. M., Manole, M. D., Baltagi, S. A., Chu, C. T., Aneja, R. K., Bayır, H., Kochanek, P. M., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.06.007 · Cited by 35
Morello, G., Guarnaccia, M., Spampinato, A. G., Cognata, V. L., D’Agata, V., & Cavallaro, S. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0393-x · Cited by 36
14-3-3 proteins: an important regulator of autophagy in diseases.
Jia, H., Liang, Z., Zhang, X., Wang, J., Xu, W., & Qian, H. (2017) · Europe PMC (PubMed Central) · Cited by 33
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Cao, Y. H., Zhang, S., Yuan, N., Wang, J., Li, X., Xu, F., Lin, W., Song, L., Fang, Y., Wang, Z., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.650028 · Cited by 33
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Tegeder, I. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.10.019 · Cited by 33
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Fellner, L., Gabassi, E., Haybaeck, J., & Edenhofer, F. (2021) · Cells · doi:10.3390/cells10113143 · Cited by 36
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Yu, X., Muñoz‐Alarcón, A., Ajayi, A., Webling, K., Steinhof, A., Langel, Ü., & Ström, A. (2013) · Journal of Molecular Neuroscience · doi:10.1007/s12031-013-0012-x · Cited by 33
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Pan, P., Zhu, Y., Shen, Y., & Yue, Z. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.04.020 · Cited by 33
Self-citationWang, P., Chen, X., Wang, Y., Jia, C., Liu, X., Wang, Y., Wu, H., Cai, H., Shen, H., & Le, W. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03412-5 · Cited by 31
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Shehata, M. H., & Inokuchi, K. (2014) · Reviews in the Neurosciences · doi:10.1515/revneuro-2014-0002 · Cited by 33
Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival
Redmann, V., Lamb, C. A., Hwang, S., Orchard, R. C., Kim, S., Razi, M., Milam, A., Park, S., Yokoyama, C. C., Kambal, A., et al. (2016) · Scientific Reports · doi:10.1038/srep23326 · Cited by 31
Wei, X., Manandhar, L., Kim, H., Chhetri, A., Hwang, J., Jang, G., Park, C., & Park, R. (2025) · Antioxidants · doi:10.3390/antiox14020126 · Cited by 39
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Wang, J., Fang, Y., Yan, L., Yuan, N., Zhang, S., Li, X., Nie, M., Zhang, X., & Wang, J. (2016) · Scientific Reports · doi:10.1038/srep24641 · Cited by 30
Costantini, A., Skarp, S., Kämpe, A. J., Mäkitie, R. E., Pettersson, M., Männikkö, M., Jiao, H., Taylan, F., Lindstrand, A., & Mäkitie, O. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00380 · Cited by 31
Vernizzi, L., Paiardi, C., Licata, G., Vitali, T., Santarelli, S., Raneli, M., Manelli, V., Rizzetto, M., Gioria, M., Pasini, M. E., et al. (2020) · Cells · doi:10.3390/cells9010196 · Cited by 31
Mirzaei, M., Gupta, V., Chitranshi, N., Deng, L., Pushpitha, K., Abbasi, M., Chick, J. M., Rajput, R., Wu, Y., McKay, M. J., et al. (2020) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29822 · Cited by 30
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Liu, M., Liu, S., Lin, Z.-H., Chen, X., Jiao, Q., Du, X., & Jiang, H. F. (2025) · Biomolecules · doi:10.3390/biom15010149 · Cited by 32
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Walkley, S. U., Sikora, J., Micsenyi, M. C., Davidson, C. D., & Dobrenis, K. (2010) · Biochemical Society Transactions · doi:10.1042/bst0381436 · Cited by 30
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Vargas, J. A. G., Castro-Álvarez, J. F., Berruecos, J. F. Z., Abdul‐Rahim, K., & Arteaga‐Noriega, A. (2022) · Biomedical Reports · doi:10.3892/br.2022.1510 · Cited by 31
Saffari, A., Brechmann, B., Böger, C., Saber, W. A., Jumo, H., Whye, D., Wood, D., Wahlster, L., Alecu, J. E., Ziegler, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-023-44264-1 · Cited by 32
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Yoon, J. S., Lee, H. J., Chae, M. K., & Lee, E. J. (2015) · Thyroid · doi:10.1089/thy.2014.0300 · Cited by 29
Coleman, M. P. (2011) · Advances in genetics · doi:10.1016/b978-0-12-380860-8.00005-7 · Cited by 31
Sano, T., Kohyama‐Koganeya, A., Kinoshita, M. O., Tatsukawa, T., Shimizu, C., Oshima, E., Yamada, K., Le, T. D., Akagi, T., Tohyama, K., et al. (2018) · Neuroscience Research · doi:10.1016/j.neures.2018.02.006 · Cited by 29
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Tan, S., & Wong, E. S. P. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.09.084 · Cited by 29
Bedford, L., Paine, S., Rezvani, N., Mee, M., Lowe, J. S., & Mayer, R. J. (2009) · Autophagy · doi:10.4161/auto.5.2.7389 · Cited by 29
In search of new targets for retinal neuroprotection: is there a role for autophagy?
Russo, R., Berliocchi, L., Adornetto, A., Amantea, D., Nucci, C., Tassorelli, C., Morrone, L. A., Bagetta, G., & Corasaniti, M. T. (2012) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2012.09.004 · Cited by 27
Cicardi, M. E., Cristofani, R., Crippa, V., Ferrari, V., Tedesco, B., Casarotto, E., Chierichetti, M., Galbiati, M., Piccolella, M., Messi, E., et al. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00569 · Cited by 27
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Lee, S. H., Shim, K. S., Kim, C. Y., & Park, T. K. (2021) · Scientific Reports · doi:10.1038/s41598-021-85181-x · Cited by 27
Brain metabolism as a modulator of autophagy in neurodegeneration
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Balanced actions of protein synthesis and degradation in memory formationPreprint
Park, H., & Kaang, B. (2019) · Learning & Memory · doi:10.1101/lm.048785.118 · Cited by 26
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O’Keefe, L. V., & Denton, D. (2018) · BioMed Research International · doi:10.1155/2018/5195416 · Cited by 25
Liu, X., Wang, Y., Cao, Z., Dou, C., Bai, Y., Liu, C., Dong, S., & Fei, J. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.02.062 · Cited by 24
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Weber, J. J., Sena, P. P., Singer, E., & Nguyen, H. P. (2019) · BioMed Research International · doi:10.1155/2019/4741252 · Cited by 27
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Castets, P., Ham, D. J., & Rüegg, M. A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00162 · Cited by 29
Elbialy, A. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30021 · Cited by 24
Santarelli, S., Londero, C., Soldano, A., Candelaresi, C., Todeschini, L., Vernizzi, L., & Bellosta, P. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1082047 · Cited by 25
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
Mir505–3p regulates axonal development via inhibiting the autophagy pathway by targeting Atg12
Yang, K., Yu, B., Cheng, C., Cheng, T., Yuan, B., Li, K., Xiao, J., Qiu, Z., & Zhou, Y. (2017) · Autophagy · doi:10.1080/15548627.2017.1353841 · Cited by 24
Asai, E., Yamamoto, M., Ueda, K., & Waguri, S. (2018) · FUKUSHIMA JOURNAL OF MEDICAL SCIENCE · doi:10.5387/fms.2016-13 · Cited by 23
Cheng, W.-T., Guo, Z.-X., Lin, C.-A., Lin, M.-Y., Tung, L.-C., & Fang, K. (2009) · BMC Cell Biology · doi:10.1186/1471-2121-10-91 · Cited by 10
Hai, B., Ma, Y., Pan, X., Yong, L., Chen, L., He, G., Yang, C., Zhu, B., & Liu, X. (2019) · Clinical Interventions in Aging · doi:10.2147/cia.s193765 · Cited by 22
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Ruiz, R., Pérez-Villegas, E. M., Bachiller, S., Rosa, J. L., & Armengol, J. A. (2016) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2016.00042 · Cited by 25
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Farshbaf, M. J., & Ghaedi, K. (2016) · BioMetals · doi:10.1007/s10534-016-9981-x · Cited by 22
Tong, Y., Park, S. H., Wu, D., Xu, W., Guillot, S. J., Jin, L., Li, X. J., Wang, Y., Lin, C., & Fu, Z. (2017) · FEBS Letters · doi:10.1002/1873-3468.12644 · Cited by 21
Nanduri, R., Kalra, R., Bhagyaraj, E., Chacko, A. P., Ahuja, N., Tiwari, D., Kumar, S. R., Jain, M., Parkesh, R., & Gupta, P. K. (2019) · Autophagy · doi:10.1080/15548627.2019.1571717 · Cited by 22
Dangi, A., Huang, C., Tandon, A., Stolz, D. B., Wu, T., & Gandhi, C. R. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.25055 · Cited by 21
High glucose promotes apoptosis and autophagy of MC3T3-E1 osteoblasts
Zhang, P., Liao, J., Wang, X., & Feng, Z. (2020) · Archives of Medical Science · doi:10.5114/aoms.2020.101307 · Cited by 20
Morawe, M. P., Liao, F., Amberg, W., van Bergeijk, J., Chang, R., Gulino, M., Hamilton, C., Hoft, C., Lumpkin, C. J., Mastis, B., et al. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.175301 · Cited by 20
Rhythms in barriers and fluids: Circadian clock regulation in the aging neurovascular unit
Skapetze, L., Owino, S., Lo, E. H., Arai, K., Merrow, M. W., & Harrington, M. E. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106120 · Cited by 20
Lentinan alleviates sciatic nerve injury by promoting autophagy to remove myelin fragments
Xiao, H., Wei, C., Liu, H., Li, Z., Zheng, C., & Luo, J. F. (2023) · Phytotherapy Research · doi:10.1002/ptr.7862 · Cited by 19
Song, F., Han, X., Zeng, T., Zhang, C., Zou, C., & Xie, K. (2012) · Toxicology Letters · doi:10.1016/j.toxlet.2012.02.011 · Cited by 20
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Heitz, S., Grant, N., Leschiera, R., Haeberlé, A., Demais, V., Bombarde, G., & Bailly, Y. (2010) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00245.x · Cited by 25
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Barbera, L. L., Vedele, F., Nobili, A., D’Amelio, M., & Krashia, P. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-1557-7 · Cited by 21
Singer, E., Walter, C., Fabbro, D., Rageot, D., Beaufils, F., Wymann, M. P., Rischert, N., Rieß, O., Hillmann, P., & Nguyen, H. P. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.107812 · Cited by 20
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Fornai, F., & Puglisi‐Allegra, S. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.01.015 · Cited by 20
Development of a specific live-cell assay for native autophagic flux
Safren, N., Tank, E. M. H., Malik, A. M., Chua, J. P., Santoro, N., & Barmada, S. J. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101003 · Cited by 18
Chen, L., Shao, Q., Zhang, W., Yang, M., Chang, Q., Chen, R., & Chen, J. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz230 · Cited by 20
Purkinje Cells Are More Vulnerable to the Specific Depletion of Cathepsin D Than to That of Atg7
Koike, M., Shibata, M., Sunabori, T., Yamaguchi, J., Sakimura, K., Komatsu, M., Tanaka, K., & Uchiyama, Y. (2017) · American Journal Of Pathology · doi:10.1016/j.ajpath.2017.02.020 · Cited by 20
Self-citationThe role of Atg7-mediated autophagy in ionizing radiation-induced neural stem cell damage
Shi, W., Liu, W., Ma, J., Lu, J., Yang, X., Wang, J., Cao, J., Tian, Y., Yang, H., & Zhang, L. (2020) · Gene · doi:10.1016/j.gene.2020.144485 · Cited by 19
Zhou, J.-L., He, H., Zhang, J.-J., Liu, X., Yao, W., Li, C., Xu, T., Yin, S.-Y., Wu, D., Dou, C.-L., et al. (2022) · Autophagy · doi:10.1080/15548627.2022.2055285 · Cited by 18
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Sidibe, D. K., Kulkarni, V. V., Dong, A., Herr, J. B., Vogel, M. C., Stempel, M. H., & Maday, S. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102673 · Cited by 23
Jasutkar, H. G., Wasserlein, E. M., Ishola, A. O., Litt, N. A., Staniszewski, A., Arancio, O., & Yamamoto, A. (2024) · Autophagy · doi:10.1080/15548627.2024.2368335 · Cited by 20
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Tutas, J., Tolve, M., Ozer, E., Ickert, L., Klein, I., Silverman, Q., Liebsch, F., Dethloff, F., Giavalisco, P., Endepols, H., et al. (2025) · Nature Metabolism · doi:10.1038/s42255-024-01196-4 · Cited by 20
Upregulation of neuronal astrocyte elevated gene-1 protects nigral dopaminergic neurons in vivo
Leem, E., Kim, H., Choi, M., Kim, S., Oh, Y., Lee, K. J., Choe, Y., Um, J., Shin, W.-H., Jeong, J. Y., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0491-3 · Cited by 19
Du, Z., Chai, X., Li, X., Ren, G., Yang, X. A., & Yang, Z. R. (2021) · Toxicology Mechanisms and Methods · doi:10.1080/15376516.2021.1964665 · Cited by 18
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Castagna, C., Merighi, A., & Lossi, L. (2016) · Annals of Anatomy - Anatomischer Anzeiger · doi:10.1016/j.aanat.2016.01.010 · Cited by 18
Metadata
- Authors
- Komatsu, M., Wang, Q. J., Holstein, G. R., Friedrich, V. L., Iwata, J.-I., Kominami, E., Chait, B. T., Tanaka, K., & Yue, Z.
- Affiliations
- Juntendo University (JP)
- Rockefeller University (US)
- Icahn School of Medicine at Mount Sinai (US)
- *Laboratory of Frontier Science, Tokyo Metropolitan Institute of Medical Science, Bunkyo-ku, Tokyo 113-8613, Japan;
- Tokyo Metropolitan Institute of Medical Science (JP)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2007-09-04
- Volume
- 104
- Issue
- 36
- Pages
- 14489-14494
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1964831
- OpenAlex
- W2120640283
- Cited by
- 614
- References
- 34
- Citations by year
- 2026: 12 · 2025: 24 · 2024: 25 · 2023: 24 · 2022: 25 · 2021: 42 · 2020: 40 · 2019: 49 · 2018: 39 · 2017: 44 · 2016: 39 · 2015: 32 · 2014: 39 · 2013: 32 · 2012: 43
- FWCI
- 16.81
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Public Health Service (RNS055683A)
- National Institute of Neurological Disorders and Stroke (R21NS055683)
- National Center for Research Resources (RR00862, P41RR000862, RR 022220, U54RR022220)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Hereditary Neurological Disorders
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Keywords
- autophagy, ATG7, axonal degeneration, Purkinje cells, axonal dystrophy, axonal swellings, autophagosomes, membrane trafficking, neurodegeneration, axonopathy, conditional knockout mice, Purkinje cell death
- MeSH terms
- Autophagy-Related Protein 7, Sequestosome-1 Protein, Animals, Autophagy, Axons, Cell Membrane, Heat-Shock Proteins, Homeostasis, Mice, Transgenic, Microtubule-Associated Proteins, Nerve Degeneration, Neuropeptides, Purkinje Cells, Spine, Genes, Reporter, Guanine Nucleotide Exchange Factors, Microscopy, Electron, Transmission, Cell Shape, Adaptor Proteins, Signal Transducing, Mice
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