The DOI matches its Crossref record; 180 of the 180 references it cites were found in a registry or an index.
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.
Overview
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
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“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]
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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
Cited by
Sorted by citations
Items 901–1,000 of 1,003
Autophagy Intertwines with Different Diseases—Recent Strategies for Therapeutic Approaches
Ramesh, J., Ronsard, L., Gao, A., & Venugopal, B. (2019) · Diseases · doi:10.3390/diseases7010015 · Cited by 26
Autophagy-associated signal pathways of functional foods for chronic diseases
Xie, J., Liang, J., & Chen, N. (2019) · Food Science and Human Wellness · doi:10.1016/j.fshw.2019.03.002 · Cited by 26
Autophagy-dependent toxicity of amino-functionalized nanoparticles in ovarian cancer cells
Seca, C., Ferraresi, A., Phadngam, S., Vidoni, C., & Isidoro, C. (2019) · Journal of Materials Chemistry B · doi:10.1039/c9tb00935c · Cited by 25
Roles of Specialized Pro-Resolving Lipid Mediators in Autophagy and Inflammation
Recchiuti, A., Isopi, E., Romano, M., & Mattoscio, D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186637 · Cited by 26
Protein Homeostasis Networks and the Use of Yeast to Guide Interventions in Alzheimer’s Disease
Dhakal, S., & Macreadie, I. G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218014 · Cited by 26
Targeting regulated cell death pathways in cancers for effective treatment: a comprehensive review
Saxena, R., Welsh, C. M., & He, Y.-W. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1462339 · Cited by 29
Metabolic, autophagic, and mitophagic activities in cancer initiation and progression
Hjelmeland, A. B., & Zhang, J. (2016) · Biomedical Journal · doi:10.1016/j.bj.2015.10.002 · Cited by 24
Lapierre, J., Rodriguez, M., Ojha, C. R., & El‐Hage, N. (2018) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-018-9788-3 · Cited by 23
Study of mitophagy and ATP-related metabolomics based on β-amyloid levels in Alzheimer's disease
Xiong, X., Li, S., Han, T.-L., Zhou, F., Zhang, X., Tian, M., Tang, L. P., & Li, Y. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112266 · Cited by 24
Targeting Mitophagy in Alzheimer’s Disease
Jayatunga, D. P. W., Hone, E., Bharadwaj, P., Garg, M. L., Verdile, G., Guillemin, G. J., & Martins, R. N. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-191258 · Cited by 25
Kojima, W., Yamano, K., Kosako, H., Imai, K., Kikuchi, R., Tanaka, K., & Matsuda, N. (2021) · Autophagy · doi:10.1080/15548627.2021.1874133 · Cited by 24
Boonhok, R., Sangkanu, S., Chuprom, J., Srisuphanunt, M., Norouzi, R., Siyadatpanah, A., Mirzaei, F., Mitsuwan, W., Wisessombat, S., Pereira, M. D. L., et al. (2021) · Pathogens · doi:10.3390/pathogens10070842 · Cited by 24
Autophagy and antiviral defense
Ke, P. (2021) · IUBMB Life · doi:10.1002/iub.2582 · Cited by 23
Research progress on the relationship between autophagy and chronic complications of diabetes
Ge, X., Wang, L., Fei, A., Ye, S., & Zhang, Q. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.956344 · Cited by 25
Autophagy in the Lifetime of Plants: From Seed to Seed
Wang, S., Hu, W., & Liu, F. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911410 · Cited by 23
Iyaswamy, A., Lu, K., Guan, X.-J., Kan, Y., Su, C.-F., Liu, J., Jaganathan, R., Vasudevan, K., Paul, J., Thakur, A., et al. (2023) · Biomedicines · doi:10.3390/biomedicines11072056 · Cited by 25
Turnover of Lipidated LC3 and Autophagic Cargoes in Mammalian Cells
Rodríguez‐Arribas, M., Yakhine-Diop, S. M. S., González‐Polo, R. A., Niso‐Santano, M., & Fuentes, J. M. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.09.053 · Cited by 24
Autophagy and ER stress in LPS/GalN-induced acute liver injury
Shi, T., Song, W., & Xu, R. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7409 · Cited by 24
Barbosa, M. G. D. M., Silva, B. J. D. A., Assis, T. Q., Prata, R. B. D. S., Ferreira, H., Andrade, P. R., de Oliveira, J. A. D. P., da Silva, G. M. S., Nery, J. A. D. C., Sarno, E. N., et al. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01223 · Cited by 24
Fischer, S., Rijal, R., Frommolt, P., Wagle, P., Konertz, R., Faix, J., Meßling, S., & Eichinger, L. (2019) · Cells · doi:10.3390/cells8010072 · Cited by 24
Wang, Y., Chen, Y., Chen, X., Liang, Y., Yang, D., Dong, J., Yang, N., & Liang, Z. (2019) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2019.7985 · Cited by 24
Beclin 2 negatively regulates innate immune signaling and tumor development
Zhu, M., Deng, G., Tan, P., Xing, C., Guan, C., Jiang, C., Zhang, Y., Ning, B., Li, C., Yin, B., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci133283 · Cited by 27
Gao, Y., Feng, C., Ma, J., & Yan, Q. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116048 · Cited by 26
Li, B., Rong-hu, L., Li, M., Jin, M., Li, G., Han, X., Yang, Y.-Y., Sun, B., Xu, L., & Feng, X. (2017) · Brain Research · doi:10.1016/j.brainres.2017.05.019 · Cited by 23
Roles of Autophagy in Ischemic Heart Diseases and the Modulatory Effects of Chinese Herbal Medicine
Wang, D., Weiqing, Y., Liu, Y., Zhong, G., Zhao, Z., Xia, Y., & Liu, Q. (2017) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x17500768 · Cited by 23
Autophagy at synapses in neurodegenerative diseases
Lee, W., & Kim, S. H. (2019) · Archives of Pharmacal Research · doi:10.1007/s12272-019-01148-7 · Cited by 23
Lin, Y., & Jones, M. L. (2020) · Plant Science · doi:10.1016/j.plantsci.2020.110713 · Cited by 23
microRNA-based autophagy inhibition as targeted therapy in pancreatic cancer
Liang, S., Li, X., Gao, C., & Zhang, L. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110799 · Cited by 25
Links between mitochondrial retrograde response and mitophagy in pathogenic cell signalling
Strobbe, D., Sharma, S., & Campanella, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03770-5 · Cited by 24
Autophagy in sexual plant reproduction: new insights
Zhou, X., Zhao, P., & Sun, M. (2021) · Journal of Experimental Botany · doi:10.1093/jxb/erab366 · Cited by 20
HDAC6 Inhibition Extinguishes Autophagy in Cancer: Recent Insights
Passaro, E., Papulino, C., Chianese, U., Toraldo, A., Congi, R., Gaudio, N. D., Nicoletti, M. M., Benedetti, R., & Altucci, L. (2021) · Cancers · doi:10.3390/cancers13246280 · Cited by 25
Feng, K., Zhang, H., Jiang, Z., Zhou, M., Min, Y., Dèng, F., Li, P., Wáng, H., & Ning, Y. (2022) · Journal of Medical Virology · doi:10.1002/jmv.28371 · Cited by 23
Autophagy-dependent ferroptosis in kidney disease
Yang, Y., Cheng, J., Lin, Q., & Ni, Z. (2023) · Frontiers in Medicine · doi:10.3389/fmed.2022.1071864 · Cited by 24
Liu, M., Liu, Z., Qin, G., Ren, J., & Qu, X. (2023) · Nano Letters · doi:10.1021/acs.nanolett.3c00798 · Cited by 25
Key autophagic targets and relevant small‐molecule compounds in cancer therapy
Tong, X. ‐., Chen, Y., Zhang, S. ‐., Xie, T., Tian, M., Guo, M., Kasimu, R., Ouyang, L., & Wang, J. ‐. (2014) · Cell Proliferation · doi:10.1111/cpr.12154 · Cited by 23
Photodynamic therapy: Promotion of efficacy by a sequential protocol
Kessel, D. H. (2016) · Journal of Porphyrins and Phthalocyanines · doi:10.1142/s1088424616500073 · Cited by 23
Methods to Assess Autophagy and Chronological Aging in Yeast
Kainz, K., Tadić, J., Zimmermann, A., Pendl, T., Carmona‐Gutiérrez, D., Ruckenstuhl, C., Eisenberg, T., & Madeo, F. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.09.086 · Cited by 24
Macrophage-Mediated Clofazimine Sequestration Is Accompanied by a Shift in Host Energy Metabolism
Trexel, J., Yoon, G. S., Keswani, R. K., McHugh, C. E., Yeomans, L., Vitvitsky, V., Banerjee, R. V., Sud, S., Sun, Y., Rosania, G. R., et al. (2016) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2016.12.009 · Cited by 23
Invalidation of mitophagy by FBP1-mediated repression promotes apoptosis in breast cancer
Liu, Y., Jiang, Y., Wang, N., Jin, Q., Ji, F., Zhong, C., Zhang, Z., Yang, J., Ye, X., & Chen, T. (2017) · Tumor Biology · doi:10.1177/1010428317708779 · Cited by 24
Conserved and unique features of the fission yeast core Atg1 complex
Nanji, T., Liu, X., Chew, L. H., Li, F. K. K., Biswas, M., Yu, Z.-Q., Lu, S., Dong, M., Du, L., Klionsky, D. J., et al. (2017) · Autophagy · doi:10.1080/15548627.2017.1382782 · Cited by 23
GRASP55 facilitates autophagosome maturation under glucose deprivation
Zhang, X., & Wang, Y. (2018) · Molecular & Cellular Oncology · doi:10.1080/23723556.2018.1494948 · Cited by 23
Lysosomal enzyme activities as possible CSF biomarkers of synucleinopathies
Paciotti, S., Gatticchi, L., Beccari, T., & Parnetti, L. (2019) · Clinica Chimica Acta · doi:10.1016/j.cca.2019.03.1627 · Cited by 23
Abdel‐Maksoud, F. M., Hussein, M. T., & Attaai, A. (2019) · Microscopy and Microanalysis · doi:10.1017/s1431927619014557 · Cited by 23
Jeffrey, J. D., Jeffries, K. M., & Suski, C. D. (2019) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2019.100614 · Cited by 23
Maestro, I., Boya, P., & Martínez, A. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1730328 · Cited by 22
Li, Y., Zhu, Y., Fang, J., Li, W., Li, S., Liu, X., Liu, Z., Song, G., Shang, C., Cong, J., et al. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01026 · Cited by 23
TRIM21 enhances bortezomib sensitivity in multiple myeloma by halting prosurvival autophagy
Chen, J., Cao, W., Huang, X., Chen, Q., Ye, S., Qu, J., Liu, Y., Guo, X., Yao, S., Zhang, E., et al. (2023) · Blood Advances · doi:10.1182/bloodadvances.2022008241 · Cited by 22
Zhang, Y., Ma, P., Wang, S., Chen, S., & Deng, H. (2025) · Nature Communications · doi:10.1038/s41467-025-60196-4 · Cited by 25
Programmed cell death in triple-negative breast cancer
Liu, Y., He, J., Chen, J., Chen, T., Li, W., Yang, Z., & Zeng, F. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00789-5 · Cited by 27
Mechanisms of Cell Death Induced by Optical Hyperthermia
Pérez-Hernández, M. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813928-8.00008-9 · Cited by 22
Deciphering the Role Played by Autophagy in Leishmania Infection
Veras, P. S. T., de Menezes, J. P. B., & Dias, B. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02523 · Cited by 23
TGFβ-like DAF-7 acts as a systemic signal for autophagy regulation in C. elegans
Zhang, Y., Qi, L., & Zhang, H. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201907196 · Cited by 22
Nam, S.-E., Cheung, Y. W. S., Nguyen, T. N., Gong, M., Chan, S., Lazarou, M., & Yip, C. K. (2021) · Communications Biology · doi:10.1038/s42003-021-01830-x · Cited by 22
Lee, J., Kim, J., Shin, J., Kang, Y., Choi, J., & Cheong, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179182 · Cited by 23
Autophagy-related signaling pathways in non-small cell lung cancer
Wang, J., Gong, M., Fan, X., Huang, D., Zhang, J., & Huang, C. (2021) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-021-04280-5 · Cited by 24
The Genetics of Autophagy in Multicellular Organisms
Zhang, H. (2022) · Annual Review of Genetics · doi:10.1146/annurev-genet-022422-095608 · Cited by 23
Tong, X., Yu, G., Fu, X., Song, R., Gu, J., & Liu, Z. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179846 · Cited by 23
Wong, T. Y., Yan, N., Kwan, K. K., Pan, Y., Liu, J., Xiao, Y., Wu, L., & Lam, H. (2022) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2022.130599 · Cited by 22
Arlia‐Ciommo, A., Svistkova, V., Mohtashami, S., & Titorenko, V. I. (2015) · Oncotarget · doi:10.18632/oncotarget.6440 · Cited by 22
To beat or not to beat: degradation of Cx43 imposes the heart rhythm
Martins‐Marques, T., Catarino, S., Marques, C., Pereira, P., & Girão, H. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150046 · Cited by 21
Torossian, A., Broin, N., Frentzel, J., Daugrois, C., Gandarillas, S., Saati, T. A., Lamant, L., Brousset, P., Giuriato, S., & Espinos, E. (2019) · Haematologica · doi:10.3324/haematol.2017.181966 · Cited by 22
Dai, X., Xu, W., Li, T., Lu, J., Yang, Y., Li, Q., Zeng, Z., & Ai, Y. (2019) · Chinese Medical Journal · doi:10.1097/cm9.0000000000000448 · Cited by 22
Low-dose nicotine promotes autophagy of cardiomyocytes by upregulating HO-1 expression
Xing, R., Cheng, X., Qi, Y., Tian, X., Yan, C., Liu, D., & Han, Y. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.11.086 · Cited by 22
Downregulation of autophagy by Met30-mediated Atg9 ubiquitination
Feng, Y., Ariosa, A., Yang, Y., Hu, Z., Dengjel, J., & Klionsky, D. J. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2005539118 · Cited by 23
Qiu, Y. F., Ma, Y., Jiang, M., Li, S., Zhang, J., Chen, H., Xu, M., Gao, S., Tian, L., Bo, T., et al. (2021) · Stem Cells International · doi:10.1155/2021/8120403 · Cited by 22
Mechanisms and implications of podocyte autophagy in chronic kidney disease
Njeim, R., Merscher, S., & Fornoni, A. (2024) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00415.2023 · Cited by 23
Atg5-Mediated Lipophagy Induces Ferroptosis in Corneal Epithelial Cells in Dry Eye Disease
Zuo, X., Zeng, H., Yang, X., He, D., Wang, B., & Yuan, J. (2024) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.65.14.12 · Cited by 21
ATG8 delipidation is not universally critical for autophagy in plants
Zou, Y., Ohlsson, J., Holla, S., Sabljić, I., Leong, J. X., Ballhaus, F., Krebs, M., Schumacher, K., Moschou, P. N., Stael, S., et al. (2025) · Nature Communications · doi:10.1038/s41467-024-55754-1 · Cited by 23
Autophagy in Pulmonary Innate Immunity
Rao, L., & Eissa, N. T. (2019) · Journal of Innate Immunity · doi:10.1159/000497414 · Cited by 21
Altered Proteostasis in Neurodegenerative Tauopathies
Papanikolopoulou, K., & Skoulakis, E. M. C. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38266-7_7 · Cited by 23
Meng, D., Jin, H., Zhang, X., Yan, W., Xia, Q., Shen, S., Xie, S., Cui, M., Ding, B., Gu, Y., et al. (2021) · Cancer Cell International · doi:10.1186/s12935-021-02073-w · Cited by 21
How Lipids Contribute to Autophagosome Biogenesis, a Critical Process in Plant Responses to Stresses
Gomez, R. E., Lupette, J., Chambaud, C., Castets, J., Ducloy, A., Cacas, J., Masclaux‐Daubresse, C., & Bernard, A. (2021) · Cells · doi:10.3390/cells10061272 · Cited by 23
At the Crossroads: Mechanisms of Apoptosis and Autophagy in Cell Life and Death
Shliapina, V. L., Yurtaeva, S. V., Rubtsova, M. P., & Dontsova, O. А. (2021) · Acta Naturae · doi:10.32607/actanaturae.11208 · Cited by 22
Neuroprotective properties of queen bee acid by autophagy induction
Martínez-Chacón, G., Paredes-Barquero, M., Yakhine-Diop, S. M. S., Uribe-Carretero, E., Bargiela, A., Sabater-Arcis, M., Morales-Garcia, J. A., Alarcón-Gil, J., Alegre-Cortés, E., Canales-Cortés, S., et al. (2021) · Cell Biology and Toxicology · doi:10.1007/s10565-021-09625-w · Cited by 22
The emerging roles of ATG1/ATG13 kinase complex in plants
Wang, Q., & Hou, S. (2022) · Journal of Plant Physiology · doi:10.1016/j.jplph.2022.153653 · Cited by 21
Autophagy and its consequences for platelet biology
Schwertz, H., & Middleton, E. A. (2022) · Thrombosis Research · doi:10.1016/j.thromres.2022.08.019 · Cited by 24
Liu, H., Shao, W., Liu, W., Shang, W., Liu, J., Wang, L., & Tong, C. (2023) · Autophagy · doi:10.1080/15548627.2023.2222556 · Cited by 21
A noncanonical function of SKP1 regulates the switch between autophagy and unconventional secretion
Li, J., Krause, G. J., Gui, Q., Kaushik, S., Róna, G., Zhang, Q., Liang, F., Dhabaria, A., Anerillas, C., Martindale, J. L., et al. (2023) · Science Advances · doi:10.1126/sciadv.adh1134 · Cited by 21
Friends and Foes: The Ambivalent Role of Autophagy in HIV-1 Infection
Klute, S., & Sparrer, K. M. J. (2024) · Viruses · doi:10.3390/v16040500 · Cited by 21
Yusri, K., Kumar, S., Fong, S., Gruber, J., & Sorrentino, V. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25126793 · Cited by 23
Biomolecular condensates as drivers of membrane trafficking and remodelling
Ravindran, R., & Michnick, S. W. (2024) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2024.102393 · Cited by 20
Novel and functional ATG12 gene variants in sporadic Parkinson's disease
Li, Y., Huang, J. A., Pang, S., Wang, H., Zhang, A., Hawley, R. G., & Yan, B. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.02.028 · Cited by 22
Khan, M. A., Imam, H., & Siddiqui, A. (2018) · Liver Research · doi:10.1016/j.livres.2018.09.002 · Cited by 21
Nikseresht, M., Shahverdi, M., Dehghani, M., Abidi, H., Mahmoudi, R., Ghalamfarsa, G., Manzouri, L., & Ghavami, S. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.27467 · Cited by 21
Cyclic AMP induction of Dictyostelium prespore gene expression requires autophagy
Yamada, Y., & Schaap, P. (2019) · Developmental Biology · doi:10.1016/j.ydbio.2019.04.017 · Cited by 21
Rsp5 and Mdm30 reshape the mitochondrial network in response to age-induced vacuole stress
Goodrum, J. M., Lever, A. R., Coody, T. K., Gottschling, D. E., & Hughes, A. L. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-02-0094 · Cited by 23
The Function of Autophagy in Lace Plant Programmed Cell Death
Dauphinee, A. N., Denbigh, G. L., Rollini, A., Fraser, M. S., Lacroix, C. R., & Gunawardena, A. H. L. A. N. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.01198 · Cited by 21
The tripartite interaction of phosphate, autophagy, and αKlotho in health maintenance
Shi, M., Maique, J., Shaffer, J., Davidson, T. L., Sebti, S., Fernández, Á. F., Zou, Z., Yan, S. X., Levine, B., Moe, O. W., et al. (2020) · The FASEB Journal · doi:10.1096/fj.201902127r · Cited by 20
Mitochondrial Fusion Machinery Specifically Involved in Energy Deprivation-Induced Autophagy
Wu, C., Yao, W., Kai, W., Liu, W., Wang, W., Li, S., Chen, Y., Wu, X., Wang, L., Li, Y., et al. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00221 · Cited by 21
Santarelli, R., Granato, M., Faggioni, A., & Cirone, M. (2015) · Journal of Immunology Research · doi:10.1155/2015/546063 · Cited by 21
The Role of Organelle Stresses in Diabetes Mellitus and Obesity: Implication for Treatment
Chang, Y., Hee, S., Hsieh, M.-L., Jeng, Y., & Chuang, L. (2015) · Analytical Cellular Pathology · doi:10.1155/2015/972891 · Cited by 21
The importance of microlipophagy in liver
Goodman, J. M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2024058118 · Cited by 20
Rigault, M., Citerne, S., Masclaux‐Daubresse, C., & Dellagi, A. (2021) · Scientific Reports · doi:10.1038/s41598-021-83067-6 · Cited by 20
Kang, S. Y., Hwang, D., Shin, S., Park, J., Kim, M., Rahman, M. H., Rahman, M. A., Ko, S., & Kim, B. (2021) · Cancers · doi:10.3390/cancers13184502 · Cited by 20
Non-coding RNA-mediated autophagy in cancer: A protumor or antitumor factor?
Liang, J., Zhang, L., & Cheng, W. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188642 · Cited by 20
Increased ATG5 Expression Predicts Poor Prognosis and Promotes EMT in Cervical Carcinoma
Zhou, S., Wang, X., Ding, J., Yang, H., & Xie, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.757184 · Cited by 21
Nutraceuticals as Modulators of Autophagy: Relevance in Parkinson’s Disease
Rakowski, M., Lekki-Porębski, S. A., & Grzelak, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073625 · Cited by 20
Nutritional strategies for autophagy activation and health consequences of autophagy impairment
Kocot, A. M., & Wróblewska, B. (2022) · Nutrition · doi:10.1016/j.nut.2022.111686 · Cited by 22
Tan, J., Xu, T., Gou, Y., Wang, H., Liang, Z., Cao, Y., Wang, H., Yu, Y., Jiao, N., & Zhang, Z. (2022) · Stem Cell Research & Therapy · doi:10.1186/s13287-022-02981-2 · Cited by 22
Pathogenic Roles of Heparan Sulfate and Its Use as a Biomarker in Mucopolysaccharidoses
Minami, K., Morimoto, H., Morioka, H., Imakiire, A., Kinoshita, M., Yamamoto, R., Hirato, T., & Sonoda, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911724 · Cited by 19
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
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