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mTORC1 Phosphorylates the ULK1-mAtg13-FIP200 Autophagy Regulatory Complex
Abstract
High nutrient availability stimulates the mammalian target of rapamycin complex 1 (mTORC1) to coordinately activate anabolic processes, such as protein synthesis, while inhibiting the cellular catabolism of autophagy. Positive regulation of protein synthesis through the mTORC1 substrates p70 ribosomal S6 kinase (p70S6K) and eukaryotic initiation factor 4E binding protein 1 (4E-BP1) has been well characterized. The complementary inhibitory mechanism in which mTORC1 phosphorylates the autophagy regulatory complex containing unc-51-like kinase 1 (ULK1), the mammalian Atg13 protein, and focal adhesion kinase interacting protein of 200 kD (FIP200) has also been elucidated.
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In the citing paper
“However, mTORC1 signaling coordinately activates anabolic processes, such as protein synthesis, while inhibiting the cellular catabolism of autophagy (Chan, 2009).”
From Downregulation of MicroRNA-193b-3p Promotes Autophagy and Cell Survival by Targeting TSC1/mTOR Signaling in NSC-34 Cells (2017) · cites this paper as Chan, 2009
In the citing paper
“However, mTORC1 signaling coordinately activates anabolic processes, such as protein synthesis, while inhibiting the cellular catabolism of autophagy (Chan, 2009).”
From Downregulation of MicroRNA-193b-3p Promotes Autophagy and Cell Survival by Targeting TSC1/mTOR Signaling in NSC-34 Cells (2017) · cites this paper as Chan, 2009
In the citing paper
“mTORC1 negatively regulates autophagy through phosphorylating the mediators, unc-51-like kinase 1/2 (ULK-1 and ULK-2), in inhibitory sites”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Chan, 2009
Citations
Cites
Autophagy in the Pathogenesis of Disease
Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069
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
TOR signaling in growth and metabolism
Wullschleger, S., Loewith, R., & Hall, M. N. (2006) · Cell · doi:10.1016/j.cell.2006.01.016 · Cited by 5,787
Nutrient-dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy
Hosokawa, N., Hara, T., Kaizuka, T., Kishi, C., Takamura, A., Miura, Y., Iemura, S.-I., Natsume, T., Takehana, K., Yamada, N., et al. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1248 · Cited by 2,076
ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery
Jung, C. H., Jun, C. B., Ro, S.-H., Kim, Y.-M., Otto, N. M., Cao, J., Kundu, M., & Kim, D.-H. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1249 · Cited by 2,025
Isolation and characterization of autophagy‐defective mutants of Saccharomyces cerevisiae
Tsukada, M., & Ohsumi, Y. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80398-e · Cited by 1,837
ULK1·ATG13·FIP200 Complex Mediates mTOR Signaling and Is Essential for Autophagy
Ganley, I. G., Lam, D. H., Wang, J., Ding, X., Chen, S., & Jiang, X. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900573200 · Cited by 1,447
Tor-Mediated Induction of Autophagy via an Apg1 Protein Kinase Complex
Kamada, Y., Funakoshi, T., Shintani, T., Nagano, K., Ohsumi, M., & Ohsumi, Y. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.6.1507 · Cited by 1,145
Autophagy mediates the mitotic senescence transition
Young, A. R. J., Narita, M., Ferreira, M., Kirschner, K., Sadaie, M., Darot, J. F. J., Tavaré, S., Arakawa, S., Shimizu, S., Watt, F. M., et al. (2009) · Genes & Development · doi:10.1101/gad.519709 · Cited by 1,078
FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells
Hara, T., Takamura, A., Kishi, C., Iemura, S.-I., Natsume, T., Guan, J.-L., & Mizushima, N. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200712064 · Cited by 904
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Items 101–200 of 214
Perumpail, R. B. (2015) · World Journal of Hepatology · doi:10.4254/wjh.v7.i22.2384 · Cited by 45
Liu, X., Hu, X., Kuang, Y., Yan, P., Li, L., Li, C., Tao, Q., & Cai, X. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.02.030 · Cited by 45
The protective effect of natural compounds against rotenone‐induced neurotoxicity
Yarmohammadi, F., Hayes, A. W., Najafi, N., & Karimi, G. (2020) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.22605 · Cited by 43
Liu, P., Guo, J., Gan, W., & Wei, W. (2014) · Protein & Cell · doi:10.1007/s13238-014-0021-8 · Cited by 45
Autophagy Regulators as Potential Cancer Therapeutic agents: A Review
Li, S., Wang, L., Hu, Y., & Sheng, R. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150302105343 · Cited by 40
The Roles of ceRNAs-Mediated Autophagy in Cancer Chemoresistance and Metastasis
Zhang, H., & Lü, B. (2020) · Cancers · doi:10.3390/cancers12102926 · Cited by 41
Liao, M.-H., Lin, W., Wen, H.-C., & Pu, H. (2010) · Fitoterapia · doi:10.1016/j.fitote.2010.11.002 · Cited by 40
Kim, Y. H., Baek, S. H., Kim, E. K., Ha, J. M., Jin, S. Y., Lee, H. S., Ha, H. K., Song, S. H., Kim, S. J., Shin, H. K., et al. (2016) · FEBS Letters · doi:10.1002/1873-3468.12172 · Cited by 40
Targeting Mitochondrial Network Architecture in Down Syndrome and Aging
Mollo, N., Cicatiello, R., Aurilia, M., Scognamiglio, R., Genesio, R., Charalambous, M., Paladino, S., Conti, A. M. F., Nitsch, L., & Izzo, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093134 · Cited by 41
Deubiquitinase inhibition by WP1130 leads to ULK1 aggregation and blockade of autophagy
Drießen, S., Berleth, N., Friesen, O., Löffler, A. S., Böhler, P., Hieke, N., Stuhldreier, F., Peter, C., Schink, K. O., Schultz, S. W., et al. (2015) · Autophagy · doi:10.1080/15548627.2015.1067359 · Cited by 39
Hill, C. N., Hernández‐Cáceres, M. P., Asencio, C., Torres, B. M., Solis, B., & Owen, G. I. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.605314 · Cited by 38
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 39
The Interplay of HIV and Autophagy in Early Infection
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
The role of lysosomal membrane proteins in autophagy and related diseases
Xu, J., Gu, J., Pei, W., Zhang, Y., Wang, L., & Gao, J. (2023) · FEBS Journal · doi:10.1111/febs.16820 · Cited by 38
Chen, Y., Wei, H., Liu, F., & Guan, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.526335 · Cited by 37
Function and regulation of ULK1: From physiology to pathology
Rong, Z., Zheng, K., Chen, J., & Jin, X. (2022) · Gene · doi:10.1016/j.gene.2022.146772 · Cited by 38
De, P. K., Miskimins, K. W., Dey, N., & Leyland-Jones, B. R. (2013) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2012.12.002 · Cited by 34
Aging, metabolism and stem cells: Spotlight on muscle stem cells
García-Prat, L., & Muñoz-Cánoves, P. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.08.021 · Cited by 34
Cytoskeletal vimentin regulates cell size and autophagy through mTORC1 signaling
Mohanasundaram, P., Coelho‐Rato, L. S., Modi, M. K., Urbanska, M., Lautenschläger, F., Cheng, F., & Eriksson, J. (2022) · PLoS Biology · doi:10.1371/journal.pbio.3001737 · Cited by 34
AMPK in the central nervous system: physiological roles and pathological implications
Segatto, M., Rosso, P., Fioramonti, M., Fracassi, A., Marangoni, M., Taglietti, V., & Siteni, S. (2016) · Research and Reports in Biology · doi:10.2147/rrb.s90858 · Cited by 35
Xue, H., Ji, Y., Wei, S., Yu, Y., Yan, X., Liu, S., Zhang, M., Fan, Y., Lan, X., & Chen, L. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.04.004 · Cited by 33
Lei, Y., Huang, Y. J., Wen, X., Yin, Z., Zhang, Z., & Klionsky, D. J. (2022) · Antioxidants · doi:10.3390/antiox11020304 · Cited by 36
Autophagosomal Protein Dynamics and Influenza Virus Infection
Dumit, V. I., & Dengjel, J. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00043 · Cited by 31
Inactivation/deficiency of DHODH induces cell cycle arrest and programed cell death in melanoma
Liu, L., Dong, Z., Lei, Q., Yang, J., Hu, H., Li, Q., Ji, Y., Guo, L., Zhang, Y., Liu, Y., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.19379 · Cited by 31
Autophagy in Cardiac Plasticity and Disease
Hill, J. A. (2011) · Pediatric Cardiology · doi:10.1007/s00246-010-9883-6 · Cited by 30
McCarty, M. F. (2011) · Medical Hypotheses · doi:10.1016/j.mehy.2011.07.004 · Cited by 27
Role of DAPK1 in neuronal cell death, survival and diseases in the nervous system
Alsaadi, M. S. (2019) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2019.02.003 · Cited by 28
Zhang, L., Zhu, Y., Zhang, J., Zhang, L., & Chen, L. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.966012 · Cited by 29
The crosstalk between sonodynamic therapy and autophagy in cancer
Zhang, Y., Zhao, Y., Zhang, Y., Liu, Q., Zhang, M., & Tu, K. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.961725 · Cited by 28
Targeting PRAS40 for multiple diseases
Chong, Z. Z. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.04.005 · Cited by 28
Halofuginone dually regulates autophagic flux through nutrient-sensing pathways in colorectal cancer
Chen, G., Gong, R., Yang, D., Zhang, G., Lü, A., Yan, S., Lin, S., & Bian, Z. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.203 · Cited by 28
Khan, S. H., & Kumar, R. (2011) · Molecular BioSystems · doi:10.1039/c1mb05265a · Cited by 27
The Role of Autophagy in Breast Cancer Metastasis
Kim, H. M., & Koo, J. S. (2023) · Biomedicines · doi:10.3390/biomedicines11020618 · Cited by 26
Takegaki, J., Ogasawara, R., Kotani, T., Tamura, Y., Takagi, R., Nakazato, K., & Ishii, N. (2019) · Physiological Reports · doi:10.14814/phy2.14155 · Cited by 25
The role of membrane proteins in mammalian autophagy.
Tooze, S. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.03.007 · Cited by 25
The TOR Pathway at the Neuromuscular Junction: More Than a Metabolic Player?
Castets, P., Ham, D. J., & Rüegg, M. A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00162 · Cited by 29
Autophagy Regulates Craniofacial Bone Acquisition
Thomas, N., Choi, H. K., Wei, X., Wang, L., Mishina, Y. M., Guan, J., & Liu, F. (2019) · Calcified Tissue International · doi:10.1007/s00223-019-00593-2 · Cited by 23
Nutraceutical and Dietary Strategies for Up-Regulating Macroautophagy
McCarty, M. F. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042054 · Cited by 21
Takegaki, J., Sase, K., Kono, Y., Nakano, D., Fujita, T., Konishi, S., & Fujita, S. (2021) · Scientific Reports · doi:10.1038/s41598-021-00627-6 · Cited by 19
Nutritional Status and Cardiac Autophagy
Ahn, J., & Kim, J. (2013) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2013.37.1.30 · Cited by 18
Mattam, U., Talari, N. K., Paripati, A. K., Krishnamoorthy, T., & Sepuri, N. B. V. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118852 · Cited by 19
Recent advances in amino acid sensing and new challenges for protein nutrition in aquaculture
Liu, C., Wang, X., Zhou, H., Mai, K., & He, G. (2019) · Marine Life Science & Technology · doi:10.1007/s42995-019-00022-1 · Cited by 18
Alam, R., Kabir, M. F., Kim, H., & Chae, H. (2022) · Cells · doi:10.3390/cells11233773 · Cited by 16
Alkaline stress‐induced autophagy is mediated by mTORC1 inactivation
Suk, J., Kwak, S. S., Lee, J. H., Choi, J. H., Lee, S., Lee, D. H., Byun, B., Lee, G., & Joe, C. O. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23181 · Cited by 17
Vitamin D/VDR in the pathogenesis of intervertebral disc degeneration: Does autophagy play a role?
Lan, T., Shen, Z., Hu, Z., & Yan, B. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112739 · Cited by 17
Qin, Y., Huang, J., & Zhao, X. (2022) · Cellular Signalling · doi:10.1016/j.cellsig.2022.110328 · Cited by 17
Rapamycin Promotes Mouse 4T1 Tumor Metastasis that Can Be Reversed by a Dendritic Cell-Based Vaccine
Lin, T.-J., Liang, W., Hsiao, P., S, P. M., Wei, W., Lin, H.-T., Yin, S., & Yang, N. (2015) · PLoS ONE · doi:10.1371/journal.pone.0138335 · Cited by 18
Perspective on alcohol-induced organ damage via autophagy-dependent cellular changes
Bakheet, A., Anbazhagan, M., Barve, S. S., Dasarathy, S., Dickinson, J. J., Ding, W., Donohue, T. M., Gopal, T., Gukovskaya, A. S., Kharbanda, K. K., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103879 · Cited by 17
Soto‐Moreno, E. J., Balboula, A. Z., Spinka, C., & Rivera, R. M. (2021) · PLoS ONE · doi:10.1371/journal.pone.0260123 · Cited by 15
Barbone, D., Follo, C., Echeverry, N., Gerbaudo, V. H., Klampatsa, A., Bueno, R., Felley‐Bosco, E., & Broaddus, V. C. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134825 · Cited by 16
Dynamics of autophagosome formation: a pulse and a sequence of waves
Ktistakis, N. T., Karanasios, E., & Manifava, M. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140183 · Cited by 14
Overcoming resistance to rapalogs in gliomas by combinatory therapies
Grzmil, M., & Hemmings, B. A. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.01.041 · Cited by 15
Karanasios, E., & Ktistakis, N. T. (2014) · Methods · doi:10.1016/j.ymeth.2014.12.007 · Cited by 15
The Core Molecular Machinery of Autophagosome Formation
Jin, M., & Klionsky, D. J. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6561-4_2 · Cited by 15
ULK1 ubiquitylation is regulated by phosphorylation on its carboxy terminus
Nazio, F., Carinci, M., & Cecconi, F. (2017) · Cell Cycle · doi:10.1080/15384101.2017.1361063 · Cited by 14
Deri, E., Ojha, S. K., Kartawy, M., Khaliulin, I., & Amal, H. (2025) · Scientific Reports · doi:10.1038/s41598-025-95860-8 · Cited by 15
Molecular mechanisms of interplay between autophagy and metabolism in cancer
Raj, S., Chandel, V., Kumar, A. J., Kesari, K. K., Asthana, S., Ruokolainen, J., Kamal, M. A., & Kumar, D. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118184 · Cited by 14
The Important Role of Protein Kinases in the p53 Sestrin Signaling Pathway
Gülow, K., Tümen, D., & Kunst, C. (2023) · Cancers · doi:10.3390/cancers15225390 · Cited by 13
Ikari, S., Lu, S.-L., Hao, F., Imai, K., Araki, Y., Yamamoto, Y., Tsai, C., Nishiyama, Y., Shitan, N., Yoshimori, T., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0230156 · Cited by 11
Cheng, Y., Zhao, E., Yang, X., Luo, C., Zi, G., Wang, R., Xu, Y., & Peng, B. (2024) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2024.125024 · Cited by 11
Kasak, L., Näks, M., Eek, P., Piirsoo, A., Bhadoria, R., Starkov, P., Saarma, M., Kasvandik, S., & Piirsoo, M. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00356 · Cited by 11
Xu, Z., Liu, Q., Li, J., Wang, J., Yang, Z., Wang, J., Gao, L., Cheng, J., He, J., Dong, Y., et al. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110832 · Cited by 10
RB1CC1 Protein Suppresses Type II Collagen Synthesis in Chondrocytes and Causes Dwarfism
Nishimura, I., Chano, T., Kita, H., Matsusue, Y., & Okabe, H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.264192 · Cited by 10
The coordinated management of ribosome and translation during injury and regeneration
Nguyen, T., Mills, J. C., & Cho, C. J. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1186638 · Cited by 9
Prognostic significance of RB1 ‐inducible coiled‐coil 1 in salivary gland cancers
Tameno, H., Chano, T., Ikebuchi, K., Ochi, Y., Arai, A., Kishimoto, M., Shimada, T., Hisa, Y., & Okabe, H. (2011) · Head & Neck · doi:10.1002/hed.21797 · Cited by 9
ACSS2-related autophagy has a dual impact on memory
Zhang, H., Xiong, Z., He, Q., & Fan, F. (2019) · Chinese Neurosurgical Journal · doi:10.1186/s41016-019-0162-y · Cited by 10
Regulation of Autophagy by Protein Phosphorylation
Stork, B., Alers, S., Antje, S., & Wesselborg, S. (2012) · InTech eBooks · doi:10.5772/48502 · Cited by 8
Autophagy: New Questions from Recent Answers
Reggiori, F. (2012) · ISRN Molecular Biology · doi:10.5402/2012/738718 · Cited by 8
Lin, H.-Y., Wang, W.-K., Lin, C.-H., Kuei, C., Lee, H., Lin, Y.-H. K., Chiu, H., & Lin, Y. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.06.049 · Cited by 8
Parkhitko, A. A., Favorova, O. O., & Henske, E. P. (2011) · Acta Naturae · doi:10.32607/20758251-2011-3-3-71-76 · Cited by 8
Contribution of mammalian target of rapamycin in the pathophysiology of cirrhotic cardiomyopathy
Saravi, S. S. S., Ghazi‐Khansari, M., Mehr, S. E., Nobakht, M., Mousavi, S. E., & Dehpour, A. R. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i19.4685 · Cited by 8
Xu, T., Deng, Y.-Y., Yu, X., Li, M., & Fu, Y. (2024) · Acta Pharmacologica Sinica · doi:10.1038/s41401-024-01356-y · Cited by 7
Chikungunya Virus-Induced Autophagy and Apoptosis
Judith, D., Couderc, T., & Lecuit, M. (2016) · Springer eBooks · doi:10.1007/978-3-319-42958-8_9 · Cited by 6
Heo, H., Cha, B., Jang, D., Park, C., Park, G., Kwak, B.-M., Bin, B., Park, J.-H., & Lee, M. (2022) · Scientific Reports · doi:10.1038/s41598-022-17896-4 · Cited by 6
Seale, B. C., Slotabec, L. A., Nguyen, J. D., Wang, H., Patterson, C., Filho, F., Rouhi, N., Adenawoola, M. I., & Li, J. (2024) · The FASEB Journal · doi:10.1096/fj.202401404r · Cited by 6
Sriratanasak, N., Wattanathana, W., & Pithi Chanvorachote, B. (2022) · Molecules · doi:10.3390/molecules27196230 · Cited by 5
Zhang, S., Zhang, T., Cao, Z., Yang, Y., & Lü, P. (2025) · Microbial Pathogenesis · doi:10.1016/j.micpath.2025.107609 · Cited by 4
FIP200 Methylation by SETD2 Prevents Trim21-Induced Degradation and Preserves Autophagy Initiation
Dai, Y., Luo, W., Li, W., Chen, Z., Wang, X., & Chang, J. (2022) · Cells · doi:10.3390/cells11213333 · Cited by 4
Chowdhury, I. J. K., Siregar, T. A. P., Haque, M. F., & Ponpuak, M. (2025) · Critical Reviews in Microbiology · doi:10.1080/1040841x.2025.2562930 · Cited by 4
ULK1 Can Suppress or Promote Tumor Growth Under Different Conditions
Mao, T., & Liang, O. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805420-8.00012-3 · Cited by 3
Liu, X., & Klionsky, D. J. (2014) · Wiley eBooks · doi:10.1002/9781118677551.ch1 · Cited by 3
[Autophagy and its relationship with tumor proliferation, invasion, and treatment].
Shanwei, S., & Li, Y. (2015) · PubMed Central · doi:10.7518/hxkq.2015.01.022 · Cited by 2
The PI3K-AKT-mTOR Signaling Network in AML
Beagle, B. R., & Fruman, D. A. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1393-0_17 · Cited by 2
Molecular Machinery and Genetics of the Autophagy Pathway
Herr, D. R., & Finley, K. D. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-385101-7.00002-4 · Cited by 2
Zheng, P., Yuan, W., Xiao, X., Xiong, K., Li, X., Holck, A. L., & Liu, R. (2020) · ES Food & Agroforestry · doi:10.30919/esfaf0012 · Cited by 2
Park, H. L., Zhang, W., Chien, Y., Park, C., & Yoon, G. M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.31.606019 · Cited by 2
Gao, S., Yuan, D., & van der Veen, S. (2025) · Infectious Microbes & Diseases · doi:10.1097/im9.0000000000000193 · Cited by 1
Autophagy in Cardiac Physiology and Disease
Hill, J. A., Lavandero, S., & Rothermel, B. A. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-381510-1.00030-2 · Cited by 1
Präneoplastische glykogenotische Läsionen der Leber und der Niere
Ribback, S. (2020) · Der Pathologe · doi:10.1007/s00292-020-00879-5 · Cited by 1
Introduction to Autophagy in Physiology and Pathophysiology
Tavassoly, I. (2015) · Springer theses · doi:10.1007/978-3-319-14962-2_1 · Cited by 1
Cardiac Plasticity in Health and Disease
Gondalia, R., Rothermel, B. A., Lavandero, S., Gillette, T. G., & Hill, J. A. (2012) · Humana Press eBooks · doi:10.1007/978-1-61779-891-7_7 · Cited by 1
Mechanisms of Cell Death in the Developing Brain
Thornton, C., & Hagberg, H. (2016) · Elsevier eBooks · doi:10.1016/b978-0-323-35214-7.00007-x · Cited by 1
Rapamycin: Current and Future Uses
Scheibye‐Knudsen, M. (2013) · Springer eBooks · doi:10.1007/978-94-007-6214-5_16
The Protective Role of Sestrins Against Chronic TOR Activation and Oxidative Stress
Lee, J. H., & Bier, E. (2011) · Wiley eBooks · doi:10.1002/9781118148143.ch24
The role of KRAS mutations signalling in autophagy control in Colorectal Carcinomas
Castro, P. J. T. D. (2012) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
Checkley, L. A. (2012) · Digital Commons-TMC (Texas Medical Center)
Autophagic Pathology and Calcium Deregulation in Neurodegeneration
Gómez‐Suaga, P., & Hilfiker, S. (2015) · Current topics in neurotoxicity · doi:10.1007/978-3-319-13939-5_13
REGULATION OF CARDIAC AUTOPHAGY IN RESPONSE TO LIPID OVERLOAD
Jaishy, B. P. (2013)
Occurrence of noncirrhotic HCC in NAFLD
Torres, D. M., & Harrison, S. A. (2016) · doi:10.1002/9781118924938.ch7
Metadata
- Authors
- Chan, E. Y.
- Affiliations
- University of Strathclyde (GB)
- Corresponding author
- Chan, Edmond Y.
- Venue
- Science Signaling
- Published
- 2009-08-18
- Volume
- 2
- Issue
- 84
- Pages
- pe51-pe51
- ISSN
- 1937-9145 (ISSN-L)
- 1945-0877
- OpenAlex
- W2165068125
- Cited by
- 214
- References
- 25
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 5 · 2023: 6 · 2022: 15 · 2021: 8 · 2020: 16 · 2019: 10 · 2018: 14 · 2017: 13 · 2016: 16 · 2015: 21 · 2014: 15 · 2013: 16 · 2012: 16
- FWCI
- 10.72
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science Signaling (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- mTORC1, ULK1, ATG13, FIP200, autophagy regulation, protein phosphorylation, nutrient signaling, p70S6K, 4E-BP1, anabolic-catabolic balance
- MeSH terms
- Autophagy-Related Proteins, Autophagy-Related Protein-1 Homolog, Mechanistic Target of Rapamycin Complex 1, Animals, Autophagy, Humans, Models, Biological, Phosphorylation, Protein-Tyrosine Kinases, Proteins, Transcription Factors, Signal Transduction, Protein Serine-Threonine Kinases, Multiprotein Complexes, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, TOR Serine-Threonine Kinases
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