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The machinery of macroautophagy
Open accessAbstract
Autophagy is a primarily degradative pathway that takes place in all eukaryotic cells. It is used for recycling cytoplasm to generate macromolecular building blocks and energy under stress conditions, to remove superfluous and damaged organelles to adapt to changing nutrient conditions and to maintain cellular homeostasis. In addition, autophagy plays a critical role in cytoprotection by preventing the accumulation of toxic proteins and through its action in various aspects of immunity including the elimination of invasive microbes and its participation in antigen presentation. The most prevalent form of autophagy is macroautophagy, and during this process, the cell forms a double-membrane sequestering compartment termed the phagophore, which matures into an autophagosome. Following delivery to the vacuole or lysosome, the cargo is degraded and the resulting macromolecules are released back into the cytosol for reuse. The past two decades have resulted in a tremendous increase with regard to the molecular studies of autophagy being carried out in yeast and other eukaryotes. Part of the surge in interest in this topic is due to the connection of autophagy with a wide range of human pathophysiologies including cancer, myopathies, diabetes and neurodegenerative disease. However, there are still many aspects of autophagy that remain unclear, including the process of phagophore formation, the regulatory mechanisms that control its induction and the function of most of the autophagy-related proteins. In this review, we focus on macroautophagy, briefly describing the discovery of this process in mammalian cells, discussing the current views concerning the donor membrane that forms the phagophore, and characterizing the autophagy machinery including the available structural information.
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“ATG7 is strictly required for autophagosome formation; it is an E1-like activating enzyme present in ubiquitin-like conjugation systems that promotes both cleavage and lipidation of LC3 and GABARAP [43].”
From A gene toolbox for monitoring autophagy transcription (2021) · cites this paper as [43]
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“ULK1 is considered as the master regulator of autophagy induction, triggering a cascade of signals, through direct phosphorylation of ATG proteins, that culminate in autophagosome formation [3, 43].”
From A gene toolbox for monitoring autophagy transcription (2021) · cites this paper as [43]
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“Indeed, autophagy functions as a quality control mechanism, maintaining cellular homeostasis by destroying aggregate-prone proteins and damaged organelles [45].”
From Unlocking the Therapeutic Potential of Medicinal Plants for Alzheimer’s Disease: Preclinical to Clinical Trial Insights (2023) · cites this paper as [45]
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Cites
AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue
Duve, C. D., Pressman, B. C., Gianetto, R., Wattiaux, R., & Appelmans, F. (1955) · Biochemical Journal · doi:10.1042/bj0600604 · Cited by 4,176
Autophagy: process and functionPreprint
Mizushima, N. (2007) · Genes & Development · doi:10.1101/gad.1599207 · Cited by 4,104
Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1
Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481
Induction of autophagy and inhibition of tumorigenesis by beclin 1
Liang, X. H., Jackson, S., Seaman, M., Brown, K., Kempkes, B., Hibshoosh, H., & Levine, B. (1999) · Nature · doi:10.1038/45257 · Cited by 3,347
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273
de Duve, C., & Wattiaux, R. (1966) · Annual Review of Physiology · doi:10.1146/annurev.ph.28.030166.002251 · Cited by 3,033
The Role of Atg Proteins in Autophagosome Formation
Mizushima, N., Yoshimori, T., & Ohsumi, Y. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154005 · Cited by 2,978
Autophagy in Health and Disease: A Double-Edged Sword
Shintani, T., & Klionsky, D. J. (2004) · Science · doi:10.1126/science.1099993 · Cited by 2,559
Flagged first, then by citations
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Items 101–200 of 1,003
Autophagy and mitophagy in diabetic cardiomyopathy
Kobayashi, S., & Liang, Q. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.05.020 · Cited by 206
Oxidation of Atg3 and Atg7 mediates inhibition of autophagy
Frudd, K., Burgoyne, T., & Burgoyne, J. R. (2018) · Nature Communications · doi:10.1038/s41467-017-02352-z · Cited by 209
Li, T., Yu, Y., Sun, Z., & Duan, J. (2022) · Particle and Fibre Toxicology · doi:10.1186/s12989-022-00507-5 · Cited by 210
Prey for the Proteasome: Targeted Protein Degradation—A Medicinal Chemist's Perspective
Luh, L. M., Scheib, U., Juenemann, K., Wortmann, L., Brands, M., & Cromm, P. M. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202004310 · Cited by 201
Autophagy in cellular metabolism and cancer
Jiang, X., Overholtzer, M., & Thompson, C. B. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73942 · Cited by 202
The Role and Mechanism of SIRT1 in Resveratrol-regulated Osteoblast Autophagy in Osteoporosis Rats
Yang, X., Jiang, T., Wang, Y., & Guo, L. (2019) · Scientific Reports · doi:10.1038/s41598-019-44766-3 · Cited by 201
The Role of the Multifunctional BAG3 Protein in Cellular Protein Quality Control and in Disease
Stürner, E., & Behl, C. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00177 · Cited by 202
Role and regulation of autophagy in cancer
Rakesh, R., Dharshini, L. C. P., Sakthivel, K. M., & Rasmi, R. R. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2022.166400 · Cited by 198
Regulation of nutrient recycling via autophagy
Masclaux‐Daubresse, C., Chen, Q., & Havé, M. (2017) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2017.05.001 · Cited by 191
Regulation of autophagy by amino acids and MTOR-dependent signal transduction
Meijer, A. J., Lorin, S., Blommaart, E. F. C., & Codogno, P. (2014) · Amino Acids · doi:10.1007/s00726-014-1765-4 · Cited by 203
Lipid droplet–mediated ER homeostasis regulates autophagy and cell survival during starvation
Velázquez, A. P., Tatsuta, T., Ghillebert, R., Drescher, I., & Graef, M. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201508102 · Cited by 188
Mitophagy and Oxidative Stress: The Role of Aging
Gaetano, A. D., Gibellini, L., Zanini, G., Nasi, M., Cossarizza, A., & Pinti, M. (2021) · Antioxidants · doi:10.3390/antiox10050794 · Cited by 196
LRRK2 at the interface of autophagosomes, endosomes and lysosomes
Roosen, D. A., & Cookson, M. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0140-1 · Cited by 186
Zhao, Y. G., Liu, N., Miao, G., Chen, Y., Zhao, H., & Zhang, H. (2018) · Current Biology · doi:10.1016/j.cub.2018.03.002 · Cited by 182
Mechanisms of Long Non-Coding RNAs in Cancers and Their Dynamic Regulations
Zhang, X., Liu, H., & Chen, S. (2020) · Cancers · doi:10.3390/cancers12051245 · Cited by 183
Neyra, J. A., Hu, M. C., & Moe, O. W. (2020) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.02840320 · Cited by 184
Rab5-dependent autophagosome closure by ESCRT
Zhou, F., Wu, Z., Zhao, M., Murtazina, R., Cai, J., Zhang, A., Li, R. Q., Sun, D., Li, W., Zhao, L. Q., et al. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201811173 · Cited by 179
Emerging role of mitophagy in cardiovascular physiology and pathology
Morales, P. E., Arias-Durán, C., Ávalos-Guajardo, Y., Aedo, G., Verdejo, H., Parra, V., & Lavandero, S. (2019) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.09.006 · Cited by 179
Durgan, J., & Florey, O. (2022) · Science Advances · doi:10.1126/sciadv.abo1274 · Cited by 181
Role of apoptosis and autophagy in tuberculosis
Lam, A., Prabhu, R., Groß, C., Riesenberg, L. A., Singh, V., & Aggarwal, S. (2017) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00162.2017 · Cited by 182
Remodeling of ER‐exit sites initiates a membrane supply pathway for autophagosome biogenesis
Ge, L., Zhang, M., Kenny, S. J., Liu, D., Maeda, M., Saito, K., Mathur, A., Xu, K., & Schekman, R. W. (2017) · EMBO Reports · doi:10.15252/embr.201744559 · Cited by 174
Palikaras, K., Daskalaki, I., Markaki, M., & Tavernarakis, N. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.04.005 · Cited by 181
Xu, R., Ji, Z., Chen, X., & Zhu, J. (2018) · Medicine · doi:10.1097/md.0000000000012912 · Cited by 172
Autophagy-Regulating microRNAs and Cancer
Gözüaçık, D., Akkoç, Y., Öztürk, D. G., & Koçak, M. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00065 · Cited by 180
The PINK1, synphilin-1 and SIAH-1 complex constitutes a novel mitophagy pathway
Szargel, R., Shani, V., Elghani, F. A., Mekies, L. N., Liani, E., Rott, R., & Engelender, S. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw189 · Cited by 174
Autophagy induction by trehalose: Molecular mechanisms and therapeutic impacts
Moghaddam, K. H., Caraglia, M., & Sahebkar, A. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26583 · Cited by 173
Liquid–liquid phase separation in autophagy
Noda, N. N., Wang, Z., & Zhang, H. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202004062 · Cited by 175
Jacquin, É., Leclerc‐Mercier, S., Judon, C., Blanchard, E., Fraitag, S., & Florey, O. (2017) · Autophagy · doi:10.1080/15548627.2017.1287653 · Cited by 168
Endosomal Rab cycles regulate Parkin-mediated mitophagy
Yamano, K., Wang, C., Sarraf, S. A., Münch, C., Kikuchi, R., Noda, N. N., Hizukuri, Y., Kanemaki, M. T., Harper, J. W., Tanaka, K., et al. (2018) · eLife · doi:10.7554/elife.31326 · Cited by 174
Autophagy as a pro‐death pathway
Denton, D., Xu, T., & Kumar, S. (2014) · Immunology and Cell Biology · doi:10.1038/icb.2014.85 · Cited by 168
The N-Degron Pathway Mediates ER-phagy
Ji, C. H., Kim, H. Y., Heo, A. J., Lee, S. H., Lee, M. J., Kim, S., Srinivasrao, G., Mun, S. R., Cha‐Molstad, H., Ciechanover, A. J., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.028 · Cited by 166
NBR1 enables autophagy-dependent focal adhesion turnover
Kenific, C. M., Stehbens, S. J., Goldsmith, J., Leidal, A. M., Faure, N., Ye, J., Wittmann, T., & Debnath, J. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201503075 · Cited by 163
Autophagy: A new strategy for host-directed therapy of tuberculosis
Paik, S., Kim, J. K., Chung, C., & Jo, E.-K. (2018) · Virulence · doi:10.1080/21505594.2018.1536598 · Cited by 168
Unravelling the mechanisms regulating muscle mitochondrial biogenesis
Hood, D. A., Tryon, L. D., Carter, H. N., Kim, Y., & Chen, C. C. W. (2016) · Biochemical Journal · doi:10.1042/bcj20160009 · Cited by 159
Farfel-Becker, T., Roney, J. C., Cheng, X.-T., Li, S., Cuddy, S. R., & Sheng, Z.-H. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.06.013 · Cited by 152
GRASP55 Senses Glucose Deprivation through O-GlcNAcylation to Promote Autophagosome-Lysosome Fusion
Zhang, X., Wang, L., Lak, B., Li, J., Jokitalo, E., & Wang, Y. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.03.023 · Cited by 157
Congenital disorders of autophagy: an emerging novel class of inborn errors of neuro-metabolism
Ebrahimi‐Fakhari, D., Saffari, A., Wahlster, L., Lu, J., Byrne, S., Hoffmann, G. F., Jungbluth, H., & Şahin, M. (2015) · Brain · doi:10.1093/brain/awv371 · Cited by 165
Identification of transcription factors that regulate ATG8 expression and autophagy in Arabidopsis
Wang, P., Nolan, T. M., Yin, Y., & Bassham, D. C. (2019) · Autophagy · doi:10.1080/15548627.2019.1598753 · Cited by 152
Loss of TAX1BP1-Directed Autophagy Results in Protein Aggregate Accumulation in the Brain
Sarraf, S. A., Shah, H. V., Kanfer, G., Pickrell, A. M., Holtzclaw, L. A., Ward, M. E., & Youle, R. J. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.10.041 · Cited by 143
Granato, M., Santarelli, R., Farina, A., Gonnella, R., Lotti, L. V., Faggioni, A., & Cirone, M. (2014) · Journal of Virology · doi:10.1128/jvi.02199-14 · Cited by 153
Selective sorting and destruction of mitochondrial membrane proteins in aged yeast
Hughes, A. L., Hughes, C. E., Henderson, K. A., Yazvenko, N., & Gottschling, D. E. (2016) · eLife · doi:10.7554/elife.13943 · Cited by 155
Issa, A.-R., Sun, J., Petitgas, C., Mesquita, A., Dulac, A., Robin, M., Mollereau, B., Jenny, A., Chérif‐Zahar, B., & Birman, S. (2018) · Autophagy · doi:10.1080/15548627.2018.1491489 · Cited by 156
Cellular and Molecular Connections between Autophagy and Inflammation
Lapaquette, P., Guzzo, J., Brétillon, L., & Bringer, M.-A. (2015) · Mediators of Inflammation · doi:10.1155/2015/398483 · Cited by 155
Li, M., Gao, P., & Zhang, J. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17030332 · Cited by 156
Hydroxycinnamic acids and human health: recent advances
Coman, V., & Vodnar, D. C. (2019) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.10010 · Cited by 158
Autophagy in health and disease: focus on the cardiovascular system
Mialet‐Perez, J., & Vindis, C. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170022 · Cited by 151
Down-regulation of OGT promotes cisplatin resistance by inducing autophagy in ovarian cancer
Zhou, F., Yang, X., Zhao, H., Liu, Y., Yang, F., An, R. F., Lv, X., Li, J., & Chen, B. (2018) · Theranostics · doi:10.7150/thno.27806 · Cited by 148
Defective autophagy in atherosclerosis: to die or to senesce?
Grootaert, M. O. J., Roth, L., Schrijvers, D. M., De Meyer, G. R. Y., & Martinet, W. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/7687083 · Cited by 147
Lysosomal quality control of cell fate: a novel therapeutic target for human diseases
Zhu, S., Yao, R.-Q., Li, Y., Zhao, P., Ren, C., Du, X., & Yao, Y.-M. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03032-5 · Cited by 149
Huang, X., Zheng, C., Liu, F., Yang, C., Zheng, P., Lu, X., Tian, J., Chung, T., Otegui, M. S., Xiao, S., et al. (2019) · The Plant Cell · doi:10.1105/tpc.19.00066 · Cited by 139
Huang, Q., Liu, Y., Zhang, S., Yap, Y. T., Li, W., Zhang, D., Gardner, A., Zhang, L., Song, S., Hess, R. A., et al. (2020) · Autophagy · doi:10.1080/15548627.2020.1783822 · Cited by 149
Acetylation of STX17 (syntaxin 17) controls autophagosome maturation
Shen, Q., Shi, Y. P., Liu, J., Su, H., Huang, J., Zhang, Y., Peng, C., Zhou, T., Sun, Q., Wan, W., et al. (2020) · Autophagy · doi:10.1080/15548627.2020.1752471 · Cited by 142
Mareninova, O. A., Sendler, M., Malla, S. R., Yakubov, I., French, S. W., Tokhtaeva, E., Vagin, O., Oorschot, V. M. J., Lüllmann‐Rauch, R., Blanz, J., et al. (2015) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2015.07.006 · Cited by 143
Autophagy and ethanol neurotoxicity
Luo, J. (2014) · Autophagy · doi:10.4161/15548627.2014.981916 · Cited by 141
Autophagy Roles in the Modulation of DNA Repair Pathways
Gomes, L., Menck, C. F. M., & Leandro, G. D. S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18112351 · Cited by 147
AIM/CD5L: a key protein in the control of immune homeostasis and inflammatory disease
Sanjurjo, L., Aran, G., Roher, N., Valledor, A. F., & Sarrias, M. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.3ru0215-074r · Cited by 141
Aparicio, R., Rana, A., & Walker, D. W. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.06.070 · Cited by 129
Autophagy in lung disease pathogenesis and therapeutics
Ryter, S. W., & Choi, A. M. K. (2015) · Redox Biology · doi:10.1016/j.redox.2014.12.010 · Cited by 140
Differential regulation of autophagy and mitophagy in pulmonary diseases
Aggarwal, S., Mannam, P., & Zhang, J. (2016) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00128.2016 · Cited by 137
Zhang, J. (2015) · Redox Biology · doi:10.1016/j.redox.2015.01.003 · Cited by 141
AMPK/mTOR Signaling in Autophagy Regulation During Cisplatin-Induced Acute Kidney Injury
Wang, Y. X., Liu, Z., Shu, S., Cai, J., Tang, C., & Dong, Z. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.619730 · Cited by 137
A gene toolbox for monitoring autophagy transcription
Bordi, M., De Cegli, R., Testa, B., Nixon, R. A., Ballabio, A., & Cecconi, F. (2021) · Cell Death & Disease · doi:10.1038/s41419-021-04121-9 · Cited by 131
“Of note, RNA-seq analysis on starved human HAP1 cells revealed that, besides ATG14, NBR1, ULK1, and WDR45, also ATG16L1, ATG3, PINK1, BCL2, GABARAPL1, WIPI1, SQSTM1, OPTN, MAP1LC3B, UVRAG, GABARAP were significantly upregulated, while upon mTOR hyperactivation, almost all these targets did not show relevant modificati…”
BackgroundInfluentialVPS37A directs ESCRT recruitment for phagophore closure
Takahashi, Y., Liang, X., Hattori, T., Tang, Z., He, H., Chen, H., Liu, X., Abraham, T., Kawasawa, Y. I., Buchkovich, N. J., et al. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201902170 · Cited by 142
Pexophagy: A Model for Selective Autophagy
Germain, K., & Kim, P. K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020578 · Cited by 133
Microglial-to-neuronal CCR5 signaling regulates autophagy in neurodegeneration
Festa, B. P., Siddiqi, F. H., Jimenez-Sanchez, M., Won, H., Rob, M., Djajadikerta, A., Stamatakou, E., & Rubinsztein, D. C. (2023) · Neuron · doi:10.1016/j.neuron.2023.04.006 · Cited by 129
Mitophagy in Acute Kidney Injury and Kidney Repair
Wang, Y., Cai, J., Tang, C., & Dong, Z. (2020) · Cells · doi:10.3390/cells9020338 · Cited by 130
Schläfli, A. M., Adams, O., Galván, J. A., Gugger, M., Savic, S., Bubendorf, L., Schmid, R. A., Becker, K.-F., Tschan, M. P., Langer, R., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9647 · Cited by 123
Organelle biogenesis in the endoplasmic reticulum
Joshi, A., Zhang, H., & Prinz, W. A. (2017) · Nature Cell Biology · doi:10.1038/ncb3579 · Cited by 126
Annexin A2 in Inflammation and Host Defense
Dallacasagrande, V., & Hajjar, K. A. (2020) · Cells · doi:10.3390/cells9061499 · Cited by 128
Cui, L., Li, H., Xi, Y., Hu, Q., Liu, H., Fan, J., Xiang, Y., Zhang, X., Shui, W., & Lai, Y. (2022) · Molecular Biomedicine · doi:10.1186/s43556-022-00090-3 · Cited by 142
Defective autophagy is a key feature of cerebral cavernous malformations
Marchi, S., Corricelli, M., Trapani, E., Bravi, L., Pittaro, A., Monache, S. D., Ferroni, L., Patergnani, S., Missiroli, S., Goitre, L., et al. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201505316 · Cited by 129
Architecture of the ATG2B-WDR45 complex and an aromatic Y/HF motif crucial for complex formation
Zheng, J., Li, Y., Ding, Y., Liu, J., Zhang, M., Dong, M., Wang, H., & Yu, L. (2017) · Autophagy · doi:10.1080/15548627.2017.1359381 · Cited by 125
Exosomal miRNA in chemoresistance, immune evasion, metastasis and progression of cancer
Kulkarni, B., Kirave, P., Gondaliya, P., Jash, K., Jain, A. K., Tekade, R. K., & Kalia, K. (2019) · Drug Discovery Today · doi:10.1016/j.drudis.2019.06.010 · Cited by 128
Hallmarks and detection techniques of cellular senescence and cellular ageing in immune cells
Zhou, D., Borsa, M., & Simon, A. K. (2021) · Aging Cell · doi:10.1111/acel.13316 · Cited by 138
Autophagy in health and disease: From molecular mechanisms to therapeutic target
Lu, G. X., Wang, Y., Shi, Y. P., Zhang, Z., Huang, C., He, W., Wang, C., & Shen, H. (2022) · MedComm · doi:10.1002/mco2.150 · Cited by 135
Altered TFEB-mediated lysosomal biogenesis in Gaucher disease iPSC-derived neuronal cells
Awad, O., Sarkar, C., Panicker, L. M., Miller, D., Zeng, X., Sgambato, J. A., Lipinski, M. M., & Feldman, R. A. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv297 · Cited by 121
Zientara‐Rytter, K., & Subramani, S. E. (2019) · Cells · doi:10.3390/cells8010040 · Cited by 128
Acute promyelocytic leukemia (APL): a review of the literature
Jimenez, J. J., Chale, R. S., Abad, A. C., & Schally, A. V. (2020) · Oncotarget · doi:10.18632/oncotarget.27513 · Cited by 126
EMT Regulation by Autophagy: A New Perspective in Glioblastoma Biology
Colella, B., Faienza, F., & Bartolomeo, S. D. (2019) · Cancers · doi:10.3390/cancers11030312 · Cited by 128
Autophagy in Female Fertility: A Role in Oxidative Stress and Aging
Peters, A. E., Mihalas, B. P., Bromfield, E. G., Roman, S. D., Nixon, B., & Sutherland, J. M. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7986 · Cited by 125
The role of interaction between autophagy and apoptosis in tumorigenesis (Review)
Xi, H., Wang, S., Wang, B., Hong, X., Liu, X., Li, M., Shen, R., & Dong, Q. (2022) · Oncology Reports · doi:10.3892/or.2022.8423 · Cited by 136
Sestrin2 promotes Unc‐51‐like kinase 1 mediated phosphorylation of p62/sequestosome‐1
Ro, S., Semple, I. A., Park, H., Park, H., Park, H., Kim, M., Kim, J. S., & Lee, J. H. (2014) · FEBS Journal · doi:10.1111/febs.12905 · Cited by 127
Organelle autoregulation--stress responses in the ER, Golgi, mitochondria and lysosome
Sasaki, K. E., & Yoshida, H. (2015) · The Journal of Biochemistry · doi:10.1093/jb/mvv010 · Cited by 125
Kilchrist, K. V., Dimobi, S. C., Jackson, M. A., Evans, B. C., Werfel, T. A., Dailing, E. A., Bedingfield, S. K., Kelly, I. B., & Duvall, C. L. (2019) · ACS Nano · doi:10.1021/acsnano.8b05482 · Cited by 124
Birgisdottir, Å. B., Mouilleron, S., Bhujabal, Z., Wirth, M., Sjøttem, E., Evjen, G., Zhang, W., Lee, R., O’Reilly, N., Tooze, S. A., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1581009 · Cited by 123
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Ni, Y., & Liu, Y. (2021) · Aging and Disease · doi:10.14336/ad.2021.0603 · Cited by 127
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Self-citationLi, F., Xu, D., Wang, Y., Zhou, Z., Liu, J., Hu, S., Gong, Y., Yuan, J., & Pan, L. (2018) · Autophagy · doi:10.1080/15548627.2017.1391970 · Cited by 120
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Ryter, S. W., Bhatia, D., & Choi, M. E. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7518 · Cited by 117
Metadata
- Authors
- Feng, Y., He, D., Yao, Z., & Klionsky, D. J.
- Affiliations
- University of Michigan (US)
- Corresponding author
- Klionsky, Daniel J
- Venue
- Cell Research
- Published
- 2013-12-24
- Volume
- 24
- Issue
- 1
- Pages
- 24-41
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- PMC
- PMC3879710
- OpenAlex
- W2044621729
- Cited by
- 2,083
- References
- 180
- Citations by year
- 2026: 84 · 2025: 130 · 2024: 193 · 2023: 180 · 2022: 238 · 2021: 215 · 2020: 200 · 2019: 185 · 2018: 177 · 2017: 161 · 2016: 161 · 2015: 109 · 2014: 45 · 2013: 3
- FWCI
- 12.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cell Research (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM053396)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- macroautophagy, autophagy machinery, phagophore formation, autophagosomes, autophagy-related proteins, autophagy regulation, lysosomes, cellular homeostasis, cytoprotection, neurodegenerative diseases, cancer, yeast autophagy
- MeSH terms
- Animals, Autophagy, Homeostasis, Humans, Lysosomes, Phagosomes, Pichia, Saccharomyces cerevisiae, Vacuoles, Protein Serine-Threonine Kinases
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