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 measuredThe cited source says what the claim attributes to it.
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
“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
“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 201–300 of 1,000
Iron homeostasis: An anthropocentric perspective
Coffey, R., & Ganz, T. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.781823 · Cited by 194
Hu, Q., Wei, W., Wu, D., Huang, F., Li, M., Li, W., Yin, J., Peng, Y., Lu, Y., Zhao, Q., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.810327 · Cited by 194
Autophagy-Independent Lysosomal Targeting Regulated by ULK1/2-FIP200 and ATG9
Goodwin, J. M., Dowdle, W. E., DeJesus, R., Wang, Z., Bergman, P., Kobylarz, M. J., Lindeman, A., Xavier, R. J., McAllister, G., Nyfeler, B., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.034 · Cited by 189
Autophagy and Ferroptosis—What Is the Connection?
Kang, R., & Tang, D. (2017) · Current Pathobiology Reports · doi:10.1007/s40139-017-0139-5 · Cited by 186
Secretory autophagy maintains proteostasis upon lysosome inhibition
Solvik, T. A., Nguyen, T. A., Lin, Y.-H. T., Marsh, T., Huang, E. J., Wiita, A. P., Debnath, J., & Leidal, A. M. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202110151 · Cited by 195
Iron Overload, Oxidative Stress, and Ferroptosis in the Failing Heart and Liver
Mancardi, D., Mezzanotte, M., Arrigo, E., Barinotti, A., & Roetto, A. (2021) · Antioxidants · doi:10.3390/antiox10121864 · Cited by 188
iLIR database: A web resource for LIR motif-containing proteins in eukaryotes
Jacomin, A., Samavedam, S., Promponas, V. J., & Nezis, I. P. (2016) · Autophagy · doi:10.1080/15548627.2016.1207016 · Cited by 186
Iron Chaperone Poly rC Binding Protein 1 Protects Mouse Liver From Lipid Peroxidation and Steatosis
Protchenko, O. V., Baratz, E., Jadhav, S., Li, F., Shakoury‐Elizeh, M., Gavrilova, O., Ghosh, M. C., Cox, J. E., Maschek, J. A., Tyurin, V. A., et al. (2020) · Hepatology · doi:10.1002/hep.31328 · Cited by 182
Ferroptosis and ferritinophagy in diabetes complications
He, J., Li, Z., Xia, P., Shi, A., FuChen, X., Zhang, J., & Yu, P. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101470 · Cited by 187
Regulation of Autophagy By Signaling Through the Atg1/ULK1 Complex
Papinski, D., & Kraft, C. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.03.030 · Cited by 186
Zhang, X., Yu, K., Ma, L., Qian, Z., Tian, X., Miao, Y., Niu, Y., Xu, X., Guo, S., Yang, Y., et al. (2021) · Theranostics · doi:10.7150/thno.55482 · Cited by 176
Programmed Necrosis and Disease:We interrupt your regular programming to bring you necroinflammation
Kim, E. H., Wong, S., & Martinez, J. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0179-3 · Cited by 181
Zhao, T., Guo, X., & Sun, Y. (2021) · Aging and Disease · doi:10.14336/ad.2020.0912 · Cited by 180
Santana-Codina, N., del Rey, M. Q., Kapner, K. S., Zhang, H., Gikandi, A., Malcolm, C., Poupault, C. L., Kuljanin, M., John, K. M., Biancur, D. E., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-22-0043 · Cited by 182
Self-citationYang, N., Tan, S.-H., Ng, S., Shi, Y. P., Zhou, J., Tan, K. S. W., Wong, W. S. F., & Shen, H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.564567 · Cited by 175
Structural and functional analysis of the GABARAP interaction motif (GIM)
Rogov, V. V., Stolz, A., Ravichandran, A., Law, A., SUZUKI, H., Kniss, A., Rios-Szwed, D. O., Löhr, F., Wakatsuki, S., Dötsch, V., et al. (2017) · EMBO Reports · doi:10.15252/embr.201643587 · Cited by 177
NCOA4-mediated ferritinophagy promotes ferroptosis induced by erastin, but not by RSL3 in HeLa cells
Gryzik, M., Asperti, M., Denardo, A., Arosio, P., & Poli, M. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118913 · Cited by 177
Iron Dyshomeostasis and Ferroptosis: A New Alzheimer’s Disease Hypothesis?
Wang, F., Wang, J., Shen, Y., Li, H., Rausch, W., & Huang, X. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.830569 · Cited by 180
Oxygen metabolism and barrier regulation in the intestinal mucosa
Glover, L. E., Lee, J. S., & Colgan, S. P. (2016) · Journal of Clinical Investigation · doi:10.1172/jci84429 · Cited by 173
Torti, S. V., & Torti, F. M. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-2017 · Cited by 183
Li, W., Yin, S., Shen, Y., Li, H., Yuan, L., & Zhang, X. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c13222 · Cited by 170
PCBP1 and NCOA4 regulate erythroid iron storage and heme biosynthesis
Ryu, M., Zhang, D., Protchenko, O. V., Shakoury‐Elizeh, M., & Philpott, C. C. (2017) · Journal of Clinical Investigation · doi:10.1172/jci90519 · Cited by 173
The emerging roles of MAPK-AMPK in ferroptosis regulatory network
Wang, X., Tan, X., Zhang, J., Wu, J., & Shi, H. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01170-9 · Cited by 178
Self-citationBiology of ferritin in mammals: an update on iron storage, oxidative damage and neurodegeneration
Finazzi, D., & Arosio, P. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1329-0 · Cited by 166
Exploiting ferroptosis vulnerabilities in cancer
Nakamura, T., & Conrad, M. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01425-8 · Cited by 172
Autophagy, Pyroptosis, and Ferroptosis: New Regulatory Mechanisms for Atherosclerosis
Lin, L., Zhang, M.-X., Zhang, L., Zhang, D., Li, C., & Li, Y. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.809955 · Cited by 166
Lin, Z., Liu, Y., Xue, N., Zheng, R., Yan, Y., Wang, Z., Li, Y., Ying, C.-Z., Song, Z., Tian, J., et al. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/7769355 · Cited by 173
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
Crossing the Iron Gate: Why and How Transferrin Receptors Mediate Viral Entry
Wessling‐Resnick, M. (2018) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-082117-051749 · Cited by 164
Ferritin: An Inflammatory Player Keeping Iron at the Core of Pathogen-Host Interactions
Moreira, A. C., Mesquita, G., & Gomes, M. S. (2020) · Microorganisms · doi:10.3390/microorganisms8040589 · Cited by 172
Ashraf, A., Clark, M., & So, P. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00065 · Cited by 163
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
To eat or not to eat — the metabolic flavor of ferroptosis
Gao, M., & Jiang, X. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.11.001 · Cited by 160
Ng, S., Norwitz, S. G., & Norwitz, E. R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133283 · Cited by 162
Morris, G., Berk, M., Carvalho, A. F., Maes, M. H. J., Walker, A. J., & Puri, B. K. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.12.036 · Cited by 155
Ferroptosis and the bidirectional regulatory factor p53
Xu, R., Wang, W., & Zhang, W. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01517-8 · Cited by 163
Role of Ferroptosis in Lung Diseases
Xu, W., Deng, H., Hu, S., Zhang, Y., Li, Z., Liu, M., Chen, Y., Wei, J., Yang, H., & Lv, X. (2021) · Journal of Inflammation Research · doi:10.2147/jir.s307081 · Cited by 155
Zhou, Y., Shen, Y., Chen, C., Sui, X., Yang, J., Wang, L., & Zhou, J. (2019) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2019.0158 · Cited by 157
Quirós-Roldán, E., Biasiotto, G., Magro, P., & Zanella, I. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104904 · Cited by 153
Nuciferine protects against folic acid‐induced acute kidney injury by inhibiting ferroptosis
Li, D., Liu, B., Fan, Y., Liu, M. R., Han, B., Meng, Y., Xu, X. L., Song, Z., Liu, X., Hao, Q., et al. (2021) · British Journal of Pharmacology · doi:10.1111/bph.15364 · Cited by 153
CALCOCO1 acts with VAMP‐associated proteins to mediate ER‐phagy
Nthiga, T. M., Shrestha, B. K., Sjøttem, E., Bruun, J., Larsen, K. B., Bhujabal, Z., Lamark, T., & Johansen, T. (2020) · The EMBO Journal · doi:10.15252/embj.2019103649 · Cited by 152
Zhang, J., Song, L., Xu, L., Fan, Y., Wang, T., Tian, W., Ju, J., & Xu, H. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.686726 · Cited by 153
Iron in the Tumor Microenvironment-Connecting the Dots
Pfeifhofer-Obermair, C., Tymoszuk, P., Petzer, V., Weiss, G., & Nairz, M. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00549 · Cited by 151
Mi, Y., Wei, C., Sun, L., Liu, H., Zhang, J., Luo, J., Yu, X., Ge, H., Ge, H., & Liu, P. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.114048 · Cited by 151
The Role of Iron in Cancer Progression
Guo, Q., Li, L., Hou, S., Yuan, Z., Li, C., Zhang, W., Zheng, L., & Li, X. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.778492 · Cited by 150
Ferritins: furnishing proteins with iron
Bradley, J. M., Brun, N. E. L., & Moore, G. R. (2016) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-016-1336-0 · Cited by 150
Autophagosomal Content Profiling Reveals an LC3C-Dependent Piecemeal Mitophagy Pathway
Guerroué, F. L., Eck, F., Jung, J., Starzetz, T., Mittelbronn, M. G. A., Kaulich, M., & Behrends, C. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.10.029 · Cited by 149
Parkinson's disease: Alterations in iron and redox biology as a key to unlock therapeutic strategies
Ma, L., Azad, M. G., Dharmasivam, M., Richardson, V., Quinn, R. J., Feng, Y., Pountney, D. L., Tonissen, K. F., Mellick, G. D., Yanatori, I., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101896 · Cited by 151
Yanatori, I., Richardson, D. R., Dhekne, H. S., Toyokuni, S., & Kishi, F. (2021) · Blood · doi:10.1182/blood.2021010995 · Cited by 148
Ferritinophagy and ferroptosis in cardiovascular disease: Mechanisms and potential applications
Qin, Y., Qiao, Y., Wang, D., Tang, C., & Yan, G. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111872 · Cited by 150
Role and mechanism of ferroptosis in neurological diseases
Ou, M., Jiang, Y., Ji, Y., Zhou, Q., Du, Z., Zhu, H., & Zhou, Z. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101502 · Cited by 150
Li, W., Li, W., Wang, Y., Leng, Y., & Xia, Z. (2021) · Cell Death Discovery · doi:10.1038/s41420-021-00656-0 · Cited by 145
Yue, D., Zhang, Q., Zhang, J., Liu, W., Chen, L., Wang, M., Li, R., Qin, S., Song, X., & Ji, Y. (2022) · Environment International · doi:10.1016/j.envint.2022.107706 · Cited by 147
Xu, Y., Li, K., Zhao, Y., Zhou, L., Liu, Y., & Zhao, J. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01196-6 · Cited by 151
Ferreira, A. C. E., Neves, P., & Gozzelino, R. (2019) · Pharmaceuticals · doi:10.3390/ph12030126 · Cited by 148
History of the Selective Autophagy Research: How Did It Begin and Where Does It Stand Today?
Kirkin, V. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.05.010 · Cited by 143
Ito, J., Omiya, S., Rusu, M.-C., Ueda, H., Murakawa, T., Tanada, Y., Abe, H., Nakahara, K., Asahi, M., Taneike, M., et al. (2021) · eLife · doi:10.7554/elife.62174 · Cited by 143
Myoferlin targeting triggers mitophagy and primes ferroptosis in pancreatic cancer cells
Rademaker, G., Boumahd, Y., Peiffer, R., Anania, S., Wissocq, T., Liegeois, M. A., Luis, G., Sounni, N. E., Agirman, F., Maloujahmoum, N., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102324 · Cited by 143
NCOA4 drives ferritin phase separation to facilitate macroferritinophagy and microferritinophagy
Ohshima, T., Yamamoto, H., Sakamaki, Y., Saito, C., & Mizushima, N. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202203102 · Cited by 148
Regulation of lysosomal ion homeostasis by channels and transporters
Xiong, J., & Zhu, M. X. (2016) · Science China Life Sciences · doi:10.1007/s11427-016-5090-x · Cited by 141
Ironing out mechanisms of iron homeostasis and disorders of iron deficiency
Koleini, N., Shapiro, J. S., Geier, J., & Ardehali, H. (2021) · Journal of Clinical Investigation · doi:10.1172/jci148671 · Cited by 161
TRIM7 modulates NCOA4-mediated ferritinophagy and ferroptosis in glioblastoma cells
Li, K., Chen, B., Xu, A., Shen, J.-L., Li, K., Hao, K., Hao, R., Yang, W. J., Jiang, W., Zheng, Y., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102451 · Cited by 141
Zhang, X., Tang, B., Luo, J., Yang, Y., Weng, Q., Fang, S., Zhao, Z., Tu, J., Chen, M., & Ji, J. (2024) · Molecular Cancer · doi:10.1186/s12943-024-02130-8 · Cited by 148
Vaites, L. P., Paulo, J. A., Huttlin, E. L., & Harper, J. W. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00392-17 · Cited by 120
Self-citationSTING promotes ferroptosis through NCOA4-dependent ferritinophagy in acute kidney injury
Jin, L., Yu, B., Wang, H., Shi, L., Yang, J., Wu, L., Gao, C., Pan, H., Han, F., Lin, W., et al. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.08.025 · Cited by 140
Saimoto, Y., Kusakabe, D., Morimoto, K., Matsuoka, Y., Kozakura, E., Kato, N., Tsunematsu, K., Umeno, T., Kiyotani, T., Matsumoto, S., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58909-w · Cited by 160
Insights on the crosstalk among different cell death mechanisms
Eskander, G., AbdelHamid, S. G., Wahdan, S. A., & Radwan, S. M. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02328-9 · Cited by 150
Sun, K., Hou, L., Guo, Z., Wang, G., Guo, J., Xu, J., Zhang, X., & Guo, F. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.03.008 · Cited by 136
The biological underpinnings of therapeutic resistance in pancreatic cancerPreprint
Beatty, G. L., Werba, G., Lyssiotis, C. A., & Simeone, D. M. (2021) · Genes & Development · doi:10.1101/gad.348523.121 · Cited by 139
Ferroptosis: A Novel Therapeutic Target for Ischemia-Reperfusion Injury
Chen, Y., Fan, H., Wang, S., Tang, G., Zhai, C., & Shen, L. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.688605 · Cited by 139
Ferroptosis Signaling and Regulators in Atherosclerosis
Wang, Y., Zhao, Y., Ye, T., Yang, L. M., Shen, Y., & Li, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.809457 · Cited by 136
Zhu, M., Peng, L., Huo, S., Peng, D., Gou, J., Shi, W., Tao, J., Jiang, T., Jiang, Y., Wang, Q., et al. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.03.003 · Cited by 137
Regulated cell death pathways in cardiomyopathy
Sheng, S., Li, J., Hu, X., & Wang, Y. (2023) · Acta Pharmacologica Sinica · doi:10.1038/s41401-023-01068-9 · Cited by 135
Lin, H., Buerki‐Thurnherr, T., Kaur, J., Wick, P., Pelin, M., Tubaro, A., Carniel, F. C., Tretiach, M., Emmanuel Flahaut, B., Iglesias, D., et al. (2024) · ACS Nano · doi:10.1021/acsnano.3c09699 · Cited by 136
Targeting quiescent leukemic stem cells using second generation autophagy inhibitors
Baquero, P., Dawson, A., Mukhopadhyay, A., Kuntz, E. M., Mitchell, R., Olivares, O., Ianniciello, A., Scott, M. T., Dunn, K. M., Nicastri, M. C., et al. (2018) · Leukemia · doi:10.1038/s41375-018-0252-4 · Cited by 132
Emerging and established modes of cell death during acetaminophen-induced liver injury
Jaeschke, H., Ramachandran, A., Chao, X., & Ding, W. (2019) · Archives of Toxicology · doi:10.1007/s00204-019-02597-1 · Cited by 135
David, S., Jhelum, P., Ryan, F., Jeong, S. Y., & Kroner, A. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0218 · Cited by 134
Decoding ferroptosis for cancer therapy
Wahida, A., & Conrad, M. (2025) · Nature reviews. Cancer · doi:10.1038/s41568-025-00864-1 · Cited by 168
Kalinowski, D. S., Stefani, C., Toyokuni, S., Ganz, T., Anderson, G. J., Subramaniam, V. N., Trinder, D., Olynyk, J. K., Chua, A. C. G., Jansson, P. J., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.01.026 · Cited by 131
Unraveling Cell Death Pathways during Malaria Infection: What Do We Know So Far?
Sena-dos-Santos, C., Braga-da-Silva, C., Marques, D., Pinheiro, J. A. D. S., Ribeiro‐dos‐Santos, Â., & Cavalcante, G. C. (2021) · Cells · doi:10.3390/cells10020479 · Cited by 132
Saponin Formosanin C-Induced Ferritinophagy and Ferroptosis in Human Hepatocellular Carcinoma Cells
Lin, P.-L., Tang, H. F., Wu, S., Shaw, N.-S., & Su, C. (2020) · Antioxidants · doi:10.3390/antiox9080682 · Cited by 129
Selective autophagy: Xenophagy
Bauckman, K., Owusu‐Boaitey, N., & Mysorekar, I. U. (2014) · Methods · doi:10.1016/j.ymeth.2014.12.005 · Cited by 127
Targeting Ferroptosis as a Promising Therapeutic Strategy for Ischemia-Reperfusion Injury
Pan, Y., Wang, X., Liu, X., Shen, L., Chen, Q., & Shu, Q. (2022) · Antioxidants · doi:10.3390/antiox11112196 · Cited by 129
Self-citationThe role of ferroptosis and its mechanism in ischemic stroke
Hu, X., Bao, Y., Li, M., Zhang, W., & Chen, C. (2023) · Experimental Neurology · doi:10.1016/j.expneurol.2023.114630 · Cited by 140
Ferritinophagy: research advance and clinical significance in cancers
Wang, J., Wu, N., Peng, M., Oyang, L., Jiang, X., Peng, Q., Zhou, Y., He, Z., & Liao, Q. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01753-y · Cited by 128
Lv, H., & Shang, P. (2018) · Metallomics · doi:10.1039/c8mt00048d · Cited by 127
Mechanisms and regulations of ferroptosis
Zhang, X.-D., Liu, Z., Wang, M.-S., Guo, Y.-X., Wang, X., Luo, K., Huang, S., & Li, R. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1269451 · Cited by 138
Self-citationRecent progress on targeting ferroptosis for cancer therapy
Xu, G., Wang, H., Li, X., Huang, R., & Luo, L. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114584 · Cited by 121
The Role of Ferritin in Health and Disease: Recent Advances and Understandings
Kotla, N. K., Dutta, P., Parimi, S., & Das, N. K. (2022) · Metabolites · doi:10.3390/metabo12070609 · Cited by 132
Wang, X., Li, H., Peng, P., Gong, Z., Huang, J. X., & Peng, H. (2022) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2022.110148 · Cited by 129
Self-citationLysosomes as Oxidative Targets for Cancer Therapy
Dielschneider, R. F., Henson, E. S., & Gibson, S. B. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/3749157 · Cited by 123
Tsai, Y., Xia, C., & Sun, Z. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.598555 · Cited by 124
Regulated cell death: discovery, features and implications for neurodegenerative diseases
Cui, J., Zhao, S., Li, Y., Zhang, D., Wang, B., Xie, J., & Wang, J. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00799-8 · Cited by 130
Therapeutic inhibition of ferroptosis in neurodegenerative disease
Ryan, S. K., Ugalde, C. L., Rolland, A., Skidmore, J., Devos, D., & Hammond, T. R. (2023) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2023.07.007 · Cited by 127
Systemic iron homeostasis and erythropoiesis
Papanikolaou, G. V., & Pantopoulos, K. (2017) · IUBMB Life · doi:10.1002/iub.1629 · Cited by 128
Cytosolic iron chaperones: Proteins delivering iron cofactors in the cytosol of mammalian cells
Philpott, C. C., Ryu, M., Frey, A. G., & Patel, S. J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.791962 · Cited by 128
Zhao, Y., Li, J., Guo, W., Li, H., & Lei, L. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-00356-1 · Cited by 122
Yao, L., Hou, J., Wu, X., Lu, Y., Jin, Z., Yu, Z., Yu, B., Li, J., Yang, Z., Li, C., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102923 · Cited by 137
Zellner, S., Schifferer, M., & Behrends, C. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.01.009 · Cited by 119
Zhao, J., Dar, H. H., Deng, Y., Croix, C. M. S., Li, Z., Minami, Y., Shrivastava, I. H., Tyurina, Y. Y., Etling, E. B., Rosenbaum, J. C., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1921618117 · Cited by 121
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
