The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy
Open accessAbstract
Autophagy, the process by which proteins and organelles are sequestered in double-membrane structures called autophagosomes and delivered to lysosomes for degradation, is critical in diseases such as cancer and neurodegeneration. Much of our understanding of this process has emerged from analysis of bulk cytoplasmic autophagy, but our understanding of how specific cargo, including organelles, proteins or intracellular pathogens, are targeted for selective autophagy is limited. Here we use quantitative proteomics to identify a cohort of novel and known autophagosome-enriched proteins in human cells, including cargo receptors. Like known cargo receptors, nuclear receptor coactivator 4 (NCOA4) was highly enriched in autophagosomes, and associated with ATG8 proteins that recruit cargo-receptor complexes into autophagosomes. Unbiased identification of NCOA4-associated proteins revealed ferritin heavy and light chains, components of an iron-filled cage structure that protects cells from reactive iron species but is degraded via autophagy to release iron through an unknown mechanism. We found that delivery of ferritin to lysosomes required NCOA4, and an inability of NCOA4-deficient cells to degrade ferritin led to decreased bioavailable intracellular iron. This work identifies NCOA4 as a selective cargo receptor for autophagic turnover of ferritin (ferritinophagy), which is critical for iron homeostasis, and provides a resource for further dissection of autophagosomal cargo-receptor connectivity.
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
“Cuprizone-mediated reduction in oligodendrocytes between days 1–4 coincides with reduction of the iron storage protein ferritin and an increase of the ferroptosis marker nuclear receptor coactivator 4 (NCOA4).”
From Oligodendrocyte death and myelin loss in the cuprizone model: an updated overview of the intrinsic and extrinsic causes of cuprizone demyelination (2022) · cites this paper as [287]
Experimental — accuracy not yet measuredIn the citing paper
“clinical trials have shown that hydroxychloroquine, which inhibits autophagic flux by preventing lysosomal acidification, enhances PDAC patient response to chemotherapy212,213”
From Pancreatic cancer: Advances and challenges (2023) · cites this paper as [213]
In the citing paper
“Recently, nuclear receptor coactivator 4 (NCOA4) was identified as the cargo receptor for autophagocytotic turnover of ferritin”
From Iron in immune cell function and host defense (2021) · cites this paper as [9]
In the citing paper
“This process is specifically mediated via NCOA4 to traffic ferritin to the autophagosome for degradation”
From Iron in immune cell function and host defense (2021) · cites this paper as [9]
In the citing paper
“Ferritin degradation was then stimulated with the iron chelator deferoxamine (Dfo) (50 µM) as previously described [51], [53], [56] and occurred substantially within 6 h of treatment (Fig. 5A(i)).”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [53]
In the citing paper
“Ferritinophagy, the process of ferritin being sequestered into autophagosomes and delivered to lysosomes for degradation, is important for liberating iron from ferritin and thus for maintaining cellular iron homeostasis [51], [53], [54], [55].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [53]
In the citing paper
“Ferritin is selectively targeted for autophagic/lysosomal degradation by the cargo receptor NCOA4 [53], a process required for liberating iron making it bioavailable to the cell [51], [53], [65].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [53]
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
NIH Image to ImageJ: 25 years of image analysis
Schneider, C. A., Rasband, W. S., & Eliceiri, K. W. (2012) · Nature Methods · doi:10.1038/nmeth.2089 · Cited by 64,638
In-gel digestion for mass spectrometric characterization of proteins and proteomes
Shevchenko, A., Tomas, H., Havli, J., Olsen, J. V., & Mann, M. (2006) · Nature Protocols · doi:10.1038/nprot.2006.468 · Cited by 4,947
Autophagy and the Integrated Stress Response
Kroemer, G., Mariño, G., & Levine, B. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.023 · Cited by 3,506
Eaten alive: a history of macroautophagy
Yang, Z., & Klionsky, D. J. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-814 · Cited by 2,155
A tissue-specific atlas of mouse protein phosphorylation and expression
Huttlin, E. L., Jedrychowski, M. P., Elias, J. E., Goswami, T., Rad, R., Beausoleil, S. A., Villén, J., Haas, W., Sowa, M. E., & Gygi, S. P. (2010) · Cell · doi:10.1016/j.cell.2010.12.001 · Cited by 1,778
Self-citationDeconvoluting the context-dependent role for autophagy in cancer
White, E. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3262 · Cited by 1,758
Network organization of the human autophagy system
Behrends, C., Sowa, M. E., Gygi, S. P., & Harper, J. W. (2010) · Nature · doi:10.1038/nature09204 · Cited by 1,554
Self-citationDefining the Human Deubiquitinating Enzyme Interaction Landscape
Sowa, M. E., Bennett, E. J., Gygi, S. P., & Harper, J. W. (2009) · Cell · doi:10.1016/j.cell.2009.04.042 · Cited by 1,523
Self-citationPancreatic cancers require autophagy for tumor growth
Yang, S., Wang, X., Contino, G., Liesa, M., Sahin, E., Ying, H., Bause, A., Li, Y., Stommel, J. M., Dell'Antonio, G., et al. (2011) · Genes & Development · doi:10.1101/gad.2016111 · Cited by 1,498
Self-citationA Role for Ubiquitin in Selective Autophagy
Kirkin, V., McEwan, D. G., Novak, I., & Đikić, I. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.026 · Cited by 1,268
Cited by
Sorted by citations
Items 101–200 of 1,000
NUFIP1 is a ribosome receptor for starvation-induced ribophagy
Wyant, G. A., Abu-Remaileh, M., Frenkel, E. M., Laqtom, N. N., Dharamdasani, V., Lewis, C. A., Chan, S. H., Heinze, I., Ori, A., & Sabatini, D. M. (2018) · Science · doi:10.1126/science.aar2663 · Cited by 363
Non-canonical Glutamate-Cysteine Ligase Activity Protects against Ferroptosis
Kang, Y. P., Mockabee‐Macias, A., Jiang, C., Falzone, A., Prieto-Farigua, N., Stone, E. M., Harris, I. S., & DeNicola, G. M. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.12.007 · Cited by 358
Targeting iron metabolism in drug discovery and delivery
Crielaard, B. J., Lammers, T., & Rivella, S. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.248 · Cited by 352
Ferroptosis in health and disease
Berndt, C., Alborzinia, H., Skafar, V., Ayton, S., Barayeu, U., Bartelt, A., Bayır, H., Bebber, C. M., Birsoy, K., Böttcher, J. P., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103211 · Cited by 372
An essential role for functional lysosomes in ferroptosis of cancer cells
Torii, S., Shintoku, R., Kubota, C., Yaegashi, M., Torii, R., Sasaki, M., Suzuki, T., Mori, M., Yoshimoto, Y., Takeuchi, T., et al. (2016) · Biochemical Journal · doi:10.1042/bj20150658 · Cited by 349
The epigenetic regulators and metabolic changes in ferroptosis-associated cancer progression
Wu, Y., Zhang, S.-W., Gong, X., Tam, S., Xiao, D., Liu, S., & Tao, Y. (2020) · Molecular Cancer · doi:10.1186/s12943-020-01157-x · Cited by 343
Bayır, H., Dixon, S. J., Tyurina, Y. Y., Kellum, J. A., & Kagan, V. E. (2023) · Nature Reviews Nephrology · doi:10.1038/s41581-023-00689-x · Cited by 355
Ferritinophagy and ferroptosis in the management of metabolic diseases
Ajoolabady, A., Aslkhodapasandhokmabad, H., Libby, P., Tuomilehto, J. O., Lip, G. Y. H., Penninger, J. M., Richardson, D. R., Tang, D., Zhou, H., Wang, S., et al. (2021) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2021.04.010 · Cited by 341
Cell death in pancreatic cancer: from pathogenesis to therapy
Chen, X., Zeh, H. J., Kang, R., Kroemer, G., & Tang, D. (2021) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-021-00486-6 · Cited by 344
Dedicated SNAREs and specialized TRIM cargo receptors mediate secretory autophagy
Kimura, T., Jia, J., Kumar, S. G., Choi, S. W., Gu, Y., Mudd, M. H., Dupont, N., Jiang, S., Peters, R. S., Farzam, F., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201695081 · Cited by 340
Microbial Metabolite Signaling Is Required for Systemic Iron Homeostasis
Das, N. K., Schwartz, A. J., Barthel, G., Inohara, N., Liu, Q., Sankar, A., Hill, D. R., Ma, X., Lamberg, O., Schnizlein, M. K., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2019.10.005 · Cited by 331
Unraveling the Potential Role of Glutathione in Multiple Forms of Cell Death in Cancer Therapy
Lv, H., Zhen, C., Liu, J., Yang, P., Hu, L., & Shang, P. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3150145 · Cited by 320
Wang, Y., Yan, S. W., Liu, X., Deng, F., Wang, P., Yang, L., Hu, L., Huang, K., & He, J. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-00990-5 · Cited by 319
Achieving Life through Death: Redox Biology of Lipid Peroxidation in Ferroptosis
Bayır, H., Anthonymuthu, T. S., Tyurina, Y. Y., Patel, S. J., Amoscato, A. A., Lamade, A. M., Yang, Q., Vladimirov, G. K., Philpott, C. C., & Kagan, V. E. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.03.014 · Cited by 324
Khandia, R., Dadar, M., Munjal, A. K., Dhama, K., Karthik, K., Tiwari, R., Yatoo, M. I., Iqbal, H. M. N., Singh, K. P., Joshi, S. K., et al. (2019) · Cells · doi:10.3390/cells8070674 · Cited by 337
Emerging mechanisms and targeted therapy of ferroptosis in cancer
Wang, H., Cheng, Y., Mao, C., Liu, S., Xiao, D., Huang, J. X., & Tao, Y. (2021) · Molecular Therapy · doi:10.1016/j.ymthe.2021.03.022 · Cited by 326
Posttranslational modification of autophagy-related proteins in macroautophagy
Xie, Y., Kang, R., Sun, X., Zhong, M., Huang, J., Klionsky, D. J., & Tang, D. (2015) · Autophagy · doi:10.4161/15548627.2014.984267 · Cited by 302
Potential function for the Huntingtin protein as a scaffold for selective autophagy
Ochaba, J., Lukacsovich, T., Csikos, G., Zheng, S., Margulis, J., Salazar, L., Mao, K., Lau, A. L., Yeung, S. Y., Humbert, S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1420103111 · Cited by 308
The Role of NCOA4-Mediated Ferritinophagy in Ferroptosis
Santana-Codina, N., Gikandi, A., & Mancias, J. D. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-62026-4_4 · Cited by 329
Self-citationLysosomal Biology and Function: Modern View of Cellular Debris Bin
Trivedi, P. C., Bartlett, J. J., & Pulinilkunnil, T. (2020) · Cells · doi:10.3390/cells9051131 · Cited by 309
An overview of molecular basis of iron metabolism regulation and the associated pathologies
Silva, B., & Faustino, P. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.03.011 · Cited by 300
Iron in Neurodegeneration – Cause or Consequence?
Ndayisaba, A., Kaindlstorfer, C., & Wenning, G. K. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00180 · Cited by 305
The Role of Iron Regulation in Immunometabolism and Immune-Related Disease
Cronin, S. J. F., Woolf, C. J., Weiss, G., & Penninger, J. M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00116 · Cited by 299
Full-coverage regulations of autophagy by ROS: from induction to maturation
Zhou, J., Li, X., Liu, Y. J., Ji, F., Wu, Y., Shen, H., & Lu, G. (2021) · Autophagy · doi:10.1080/15548627.2021.1984656 · Cited by 304
Lysosomes as coordinators of cellular catabolism, metabolic signalling and organ physiology
Settembre, C., & Perera, R. M. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00676-x · Cited by 303
Ferritinophagy/ferroptosis: Iron‐related newcomers in human diseases
Tang, M., Chen, Z., Wu, D., & Chen, L. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26954 · Cited by 292
Hombach‐Klonisch, S., Mehrpour, M., Shojaei, S., Harlos, C. H., Pitz, M. W., Hamaï, A., Siemianowicz, K., Likus, W., Wiecheć, E., Toyota, B. D., et al. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.10.017 · Cited by 298
Limitations of Serum Ferritin in Diagnosing Iron Deficiency in Inflammatory Conditions
Dignass, A. U., Farrag, K., & Stein, J. M. (2018) · International Journal of Chronic Diseases · doi:10.1155/2018/9394060 · Cited by 309
Cell Death Mechanisms in Cerebral Ischemia–Reperfusion Injury
Zhang, Q., Jia, M., Wang, Y., Wang, Q., & Wu, J. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03697-8 · Cited by 332
Watch What You (Self-) Eat: Autophagic Mechanisms that Modulate Metabolism
Lahiri, V., Hawkins, W. D., & Klionsky, D. J. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.03.003 · Cited by 287
Iron and Alzheimer’s Disease: An Update on Emerging Mechanisms
Lane, D. J. R., Ayton, S., & Bush, A. I. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179944 · Cited by 287
Starvation induces rapid degradation of selective autophagy receptors by endosomal microautophagy
Mejlvang, J., Olsvik, H. L., Svenning, S., Bruun, J., Abudu, Y. P., Larsen, K. B., Brech, A., Hansen, T. E., Brenne, H. B., Hansen, T., et al. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201711002 · Cited by 292
New insights into iron deficiency and iron deficiency anemia
Camaschella, C. (2017) · Blood Reviews · doi:10.1016/j.blre.2017.02.004 · Cited by 290
Dynamic O-GlcNAcylation coordinates ferritinophagy and mitophagy to activate ferroptosis
Yu, F. D., Zhang, Q., Liu, H., Liu, J., Yang, S., Luo, X., Liu, W., Zheng, H., Liu, Q., Cui, Y., et al. (2022) · Cell Discovery · doi:10.1038/s41421-022-00390-6 · Cited by 289
Wurzer, B., Zaffagnini, G., Fracchiolla, D., Turco, E., Abert, C., Romanov, J., & Martens, S. (2015) · eLife · doi:10.7554/elife.08941 · Cited by 290
GPX4-independent ferroptosis—a new strategy in disease’s therapy
Ma, T., Du, J., Zhang, Y., Wang, Y., Wang, B., & Zhang, T. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-01212-0 · Cited by 291
Mechanism of Ferroptosis and Its Role in Type 2 Diabetes Mellitus
Sha, W., Hu, F., Yang, X., Chu, Y., & Bu, S. (2021) · Journal of Diabetes Research · doi:10.1155/2021/9999612 · Cited by 276
The function and mechanism of ferroptosis in cancer
Wang, Y., Wei, Z., Pan, K., Li, J., & Chen, Q. (2020) · APOPTOSIS · doi:10.1007/s10495-020-01638-w · Cited by 262
Kim, E. H., Shin, D., Lee, J., Jung, A. R., & Roh, J. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.06.018 · Cited by 265
Cellular and metabolic functions for autophagy in cancer cells
Kenific, C. M., & Debnath, J. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.09.001 · Cited by 270
Li, C., Zhang, Y., Cheng, X., Yuan, H., Zhu, S., Liu, J., Wen, Q., Xie, Y., Liu, J., Kroemer, G., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.07.012 · Cited by 266
ATM orchestrates ferritinophagy and ferroptosis by phosphorylating NCOA4
Wu, H., Liu, Q., Shan, X., Gao, W., & Chen, Q. (2023) · Autophagy · doi:10.1080/15548627.2023.2170960 · Cited by 267
Homeostasis and metabolism of iron and other metal ions in neurodegenerative diseases
Chen, L., Shen, Q., Liu, Y., Zhang, Y., Sun, L., Ma, X., Song, N., & Xie, J. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02071-0 · Cited by 279
GOT1 inhibition promotes pancreatic cancer cell death by ferroptosis
Kremer, D. M., Nelson, B. S., Lin, L., Yarosz, E. L., Halbrook, C. J., Kerk, S. A., Sajjakulnukit, P., Myers, A. L., Thurston, G., Hou, S. W., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24859-2 · Cited by 268
Li, C., Sun, G., Chen, B., Xu, L., Ye, Y., He, J., Bao, Z., Zhao, P., Miao, Z., Zhao, L., et al. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105933 · Cited by 264
Iron Metabolism, Ferroptosis, and the Links With Alzheimer’s Disease
Yan, N., & Zhang, J. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01443 · Cited by 256
Targeting iron metabolism in cancer therapy
Morales, M., & Xue, X. (2021) · Theranostics · doi:10.7150/thno.59092 · Cited by 262
Ferroptosis and its emerging roles in cardiovascular diseases
Li, N., Jiang, W., Wang, W., Xiong, R., Wu, X., & Geng, Q. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105466 · Cited by 256
NCOA4 deficiency impairs systemic iron homeostasis
Bellelli, R., Federico, G., Matte’, A., Colecchia, D., Iolascon, A., Chiariello, M., Santoro, M., De Franceschi, L., & Carlomagno, F. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.065 · Cited by 248
The lysosome as a master regulator of iron metabolism
Rizzollo, F., More, S., Vangheluwe, P., & Agostinis, P. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.07.003 · Cited by 243
Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation
Marshall, R. S., & Vierstra, R. D. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00040 · Cited by 243
Impaired lysosomal acidification triggers iron deficiency and inflammation in vivo
Yambire, K. F., Rostosky, C. M., Watanabe, T., Pacheu‐Grau, D., Torres-Odio, S., Sanchez-Guerrero, A., Senderovich, O., Meyron‐Holtz, E. G., Milošević, I., Frahm, J., et al. (2019) · eLife · doi:10.7554/elife.51031 · Cited by 232
Zhou, H., Zhou, Y., Mao, J.-A., Tang, L., Xu, J., Wang, Z., He, Y., & Li, M. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102413 · Cited by 239
Zirngibl, M., Assinck, P., Sizov, A., Caprariello, A. V., & Plemel, J. R. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00538-8 · Cited by 233
Chemistry and biology of ferritin
Plays, M., Müller, S., & Rodriguez, R. (2021) · Metallomics · doi:10.1093/mtomcs/mfab021 · Cited by 232
Lactate Dehydrogenase B Controls Lysosome Activity and Autophagy in Cancer
Brisson, L., Bański, P., Sboarina, M., Dethier, C., Danhier, P., Fontenille, M., Hée, V. F. V., Vazeille, T., Tardy, M., Falces, J., et al. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.08.005 · Cited by 229
Shen, M., Li, Y., Wang, Y., Shao, J., Zhang, F., Yin, G., Chen, A., Zhang, Z., & Zheng, S. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102151 · Cited by 230
Autophagy signal transduction by ATG proteins: from hierarchies to networks
Wesselborg, S., & Stork, B. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2034-8 · Cited by 241
Reggiori, F., & Molinari, M. (2022) · Physiological Reviews · doi:10.1152/physrev.00038.2021 · Cited by 232
Ironing out the role of ferroptosis in immunity
Bell, H. N., Stockwell, B. R., & Zou, W. (2024) · Immunity · doi:10.1016/j.immuni.2024.03.019 · Cited by 238
NCOA4-Mediated Ferritinophagy: A Potential Link to Neurodegeneration
Quiles del Rey, M., & Mancias, J. D. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00238 · Cited by 227
Self-citationIron Metabolism in Obesity and Metabolic Syndrome
González-Domínguez, Á., Visiedo-García, F. M., Domínguez-Riscart, J., González-Domínguez, R., Mateos, R. M., & Lechuga-Sancho, A. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155529 · Cited by 227
Ultrastructural analysis of autophagosome organization using mammalian autophagy-deficient cells
Kishi‐Itakura, C., Koyama‐Honda, I., Itakura, E., & Mizushima, N. (2014) · Journal of Cell Science · doi:10.1242/jcs.156034 · Cited by 235
Yang, R., Xu, W., Zheng, H., Zheng, X., Li, B., Jiang, L., & Jiang, S. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.30039 · Cited by 228
Metabolic Dependencies in RAS -Driven Cancers
Kimmelman, A. C. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2425 · Cited by 230
Self-citationFerritin is secreted via 2 distinct nonclassical vesicular pathways
Truman-Rosentsvit, M., Berenbaum, D., Spektor, L., Cohen, L. A., Belizowsky-Moshe, S., Lifshitz, L., Ma, J., Li, W., Kesselman, E., Abutbul-Ionita, I., et al. (2018) · Blood · doi:10.1182/blood-2017-02-768580 · Cited by 223
Sui, S., Zhang, J., Xu, S., Wang, Q., Wang, P., & Pang, D. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1564-7 · Cited by 223
Deng, F., Sharma, I., Dai, Y., Yang, M., & Kanwar, Y. S. (2019) · Journal of Clinical Investigation · doi:10.1172/jci129903 · Cited by 221
The mechanism of ferroptosis and its related diseases
Feng, S., Tang, D., Wang, Y., Li, X., Bao, H., Tang, C., Dong, X., Li, X., Yang, Q., Yan, Y., et al. (2023) · Molecular Biomedicine · doi:10.1186/s43556-023-00142-2 · Cited by 241
Mechanisms of selective autophagy and mitophagy: Implications for neurodegenerative diseases
Chu, C. T. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.015 · Cited by 218
New Insights into the Role of Ferritin in Iron Homeostasis and Neurodegenerative Diseases
Zhang, N., Yu, X., Xie, J., & Xu, H. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02277-7 · Cited by 223
Pancreatic Cancer Metabolism: Breaking It Down to Build It Back Up
Perera, R. M., & Bardeesy, N. M. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-0671 · Cited by 218
A guide to the regulation of selective autophagy receptors
Gubaš, A., & Đikić, I. (2021) · FEBS Journal · doi:10.1111/febs.15824 · Cited by 229
Chen, X., Tsvetkov, A. S., Shen, H., Isidoro, C., Ktistakis, N. T., Linkermann, A., Koopman, W. J. H., Simon, H., Galluzzi, L., Luo, S., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2319901 · Cited by 240
Ferroptosis Mediates Cuprizone-Induced Loss of Oligodendrocytes and Demyelination
Jhelum, P., Santos-Nogueira, E., Teo, W., Haumont, A., Lenoël, I., Stys, P. K., & David, S. (2020) · The Journal of Neuroscience · doi:10.1523/jneurosci.1749-20.2020 · Cited by 214
Contributions to magnetic susceptibility of brain tissue
Duyn, J. H., & Schenck, J. F. (2016) · NMR in Biomedicine · doi:10.1002/nbm.3546 · Cited by 223
Wang, Y., Hu, J., Wu, S., Fleishman, J. S., Li, Y., Xu, Y.-S., Zou, W., Wang, J., Feng, Y., Chen, J., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01720-0 · Cited by 225
Iron and copper: critical executioners of ferroptosis, cuproptosis and other forms of cell death
Li, Y., Du, Y., Zhou, Y., Chen, Q., Luo, Z., Ren, Y., Chen, X., & Chen, G. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01267-1 · Cited by 225
Origin and Consequences of Necroinflammation
Sarhan, M., Land, W. G., Tonnus, W., Hugo, C., & Linkermann, A. (2018) · Physiological Reviews · doi:10.1152/physrev.00041.2016 · Cited by 217
The Role of Autophagy in Cancer
Santana-Codina, N., Mancias, J. D., & Kimmelman, A. C. (2017) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-041816-122338 · Cited by 214
Self-citationIron imbalance in neurodegeneration
Levi, S., Ripamonti, M., Moro, A., & Cozzi, A. (2024) · Molecular Psychiatry · doi:10.1038/s41380-023-02399-z · Cited by 189
Ma, S., Dielschneider, R. F., Henson, E. S., Xiao, W., Choquette, T., Blankstein, A. R., Chen, Y., & Gibson, S. B. (2017) · PLoS ONE · doi:10.1371/journal.pone.0182921 · Cited by 204
YAP1 alleviates sepsis-induced acute lung injury via inhibiting ferritinophagy-mediated ferroptosis
Zhang, J., Zheng, Y., Wang, Y., Wang, J., Sang, A., Song, X., & Li, X. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.884362 · Cited by 206
Schwartz, A. J., Das, N. K., Ramakrishnan, S. K., Jain, C., Jurkovic, M. T., Wu, J., Nemeth, E., Lakhal-Littleton, S., Colacino, J. A., & Shah, Y. M. (2018) · Journal of Clinical Investigation · doi:10.1172/jci122359 · Cited by 203
Pannexin 1 mediates ferroptosis that contributes to renal ischemia/reperfusion injury
Su, L., Jiang, X., Yang, C., Zhang, J., Chen, B., Li, Y., Yao, S., Xie, Q., Gomez, H., Murugan, R., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010949 · Cited by 202
The multifaceted regulation of mitophagy by endogenous metabolites
Zhang, T., Liu, Q., Gao, W., Sehgal, S. A., & Wu, H. (2021) · Autophagy · doi:10.1080/15548627.2021.1975914 · Cited by 209
Fighting age-related orthopedic diseases: focusing on ferroptosis
Ru, Q., Li, Y., Xie, W., Ding, Y., Chen, L., Xu, G., Wu, Y., & Wang, F. (2023) · Bone Research · doi:10.1038/s41413-023-00247-y · Cited by 211
Iron deficiency: new insights into diagnosis and treatment
Camaschella, C. (2015) · Hematology · doi:10.1182/asheducation-2015.1.8 · Cited by 201
Yao, F., Peng, J.-J., Zhang, E., Ji, D., Gao, Z., Tang, Y., Yao, X., & Xia, X. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01046-4 · Cited by 206
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
Mitochondrial Iron in Human Health and Disease
Ward, D. M., & Cloonan, S. M. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114742 · Cited by 208
The ubiquitin-proteasome system and autophagy: Coordinated and independent activities
Cohen‐Kaplan, V., Livneh, I., Avni, N., Cohen-Rosenzweig, C., & Ciechanover, A. J. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.07.019 · Cited by 205
Mechanisms of Selective Autophagy in Normal Physiology and Cancer
Mancias, J. D., & Kimmelman, A. C. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.02.027 · Cited by 196
Self-citationAntimicrobial Mechanisms of Macrophages and the Immune Evasion Strategies of Staphylococcus aureus
Flannagan, R. S., Heit, B., & Heinrichs, D. E. (2015) · Pathogens · doi:10.3390/pathogens4040826 · Cited by 211
Iron, Ferritin, Hereditary Ferritinopathy, and Neurodegeneration
Muhoberac, B. B., & Vidal, R. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01195 · Cited by 198
Wu, J., Liu, Q., Zhang, X., Tan, M., Li, X., Liu, P., Wu, L., Jiao, F., Lin, Z., Wu, X., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05115-x · Cited by 211
Self-citationLoss of COPZ1 induces NCOA4 mediated autophagy and ferroptosis in glioblastoma cell lines
Zhang, Y., Kong, Y., Ma, Y., Ni, S., Wikerholmen, T., Xi, K., Zhao, F., Zhao, Z., Wang, J., Huang, B., et al. (2021) · Oncogene · doi:10.1038/s41388-020-01622-3 · Cited by 193
Hypoxia inhibits RANKL-induced ferritinophagy and protects osteoclasts from ferroptosis
Ni, S., Yuan, Y., Qian, Z., Zhong, Z., Lv, T., Kuang, Y., & Yu, B. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.04.027 · Cited by 192
Influence of Iron on Bone Homeostasis
Balogh, E., Paragh, G., & Jeney, V. (2018) · Pharmaceuticals · doi:10.3390/ph11040107 · Cited by 196
Iron in immune cell function and host defense
Haschka, D., Hoffmann, A., & Weiss, G. (2021) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2020.12.005 · Cited by 188
Metadata
- Authors
- Mancias, J. D., Wang, X., Gygi, S. P., Harper, J. W., & Kimmelman, A. C.
- Affiliations
- Beth Israel Deaconess Medical Center (US)
- Dana-Farber Cancer Institute (US)
- Harvard University (US)
- Corresponding author
- Harper, J. Wade
- Kimmelman, Alec C.
- Venue
- Nature
- Published
- 2014-03-30
- Volume
- 509
- Issue
- 7498
- Pages
- 105-109
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC4180099
- OpenAlex
- W1996152690
- Cited by
- 2,084
- References
- 30
- Citations by year
- 2026: 289 · 2025: 335 · 2024: 311 · 2023: 292 · 2022: 212 · 2021: 192 · 2020: 110 · 2019: 96 · 2018: 64 · 2017: 69 · 2016: 57 · 2015: 36 · 2014: 19
- FWCI
- 45.59
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Cancer Institute (P50CA127003, R01CA157490)
- National Institute of General Medical Sciences (R01GM095567, R01GM070565, GM095567, GM070565)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- NCOA4, ferritinophagy, selective autophagy, cargo receptors, autophagosomes, iron homeostasis, iron starvation, ferritin degradation, ATG8, lysosomal degradation, iron metabolism, quantitative proteomics, lysosomal biogenesis
- MeSH terms
- Autophagy-Related Protein 8 Family, Autophagy, Biological Availability, Ferritins, Homeostasis, Humans, Iron, Lysosomes, Microfilament Proteins, Phagosomes, Protein Binding, Substrate Specificity, Protein Transport, Proteomics, Adaptor Proteins, Signal Transducing, Nuclear Receptor Coactivators
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
