Hypoxia and Selective Autophagy in Cancer Development and Therapy
Open accessAbstract
Low oxygen availability, a condition known as hypoxia, is a common feature of various pathologies including stroke, ischemic heart disease, and cancer. Hypoxia adaptation requires coordination of intricate pathways and mechanisms such as hypoxia-inducible factors (HIFs), the unfolded protein response (UPR), mTOR, and autophagy. Recently, great effort has been invested toward elucidating the interplay between hypoxia-induced autophagy and cancer cell metabolism. Although novel types of selective autophagy have been identified, including mitophagy, pexophagy, lipophagy, ERphagy and nucleophagy among others, their potential interface with hypoxia response mechanisms remains poorly understood. Autophagy activation facilitates the removal of damaged cellular compartments and recycles components, thus promoting cell survival. Importantly, tumor cells rely on autophagy to support self-proliferation and metastasis; characteristics related to poor disease prognosis. Therefore, a deeper understanding of the molecular crosstalk between hypoxia response mechanisms and autophagy could provide important insights with relevance to cancer and hypoxia-related pathologies. Here, we survey recent findings implicating selective autophagy in hypoxic responses, and discuss emerging links between these pathways and cancer pathophysiology.
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
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?
Autophagy can be induced by certain treatments or microenvironmental effects in relation to metabolic adaptation and resistance.
“Autophagy can be induced by certain treatments or microevironmental effects in relation to metabolic adaptation and resistance [45].”
From Hypoxia Signaling in Cancer: From Basics to Clinical Practice (2021) · 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.
Cites
3 retracted
Mitochondrial Autophagy Is an HIF-1-dependent Adaptive Metabolic Response to Hypoxia
Zhang, H., Bosch-Marce, M., Shimoda, L. A., Tan, Y. S., Baek, J. H., Wesley, J. B., Gonzalez, F. J., & Semenza, G. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800102200 · Cited by 1,601 · see citing works
RetractedRETRACTED: MiR‐137 functions as a tumor suppressor in pancreatic cancer by targeting MRGBP
Ding, F. H., Zhang, S., Gao, S., Shang, J., Li, Y., Cui, N., & Zhao, Q. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26676 · Cited by 31 · see citing works
RetractedRen, C., Liao, J.-Y., Huang, J., Chen, W., Ma, X., & Luo, X. (2017) · Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics · doi:10.3727/096504017x14954923820137 · Cited by 14 · see citing works
RetractedRepertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351 · see citing works
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 · see citing works
Targeting Hypoxia-Inducible Factors for the Treatment of Anemia in Chronic Kidney Disease Patients
Locatelli, F., Fishbane, S. N., Block, G. A., & Macdougall, I. C. (2017) · American Journal of Nephrology · doi:10.1159/000455166 · Cited by 4,834 · see citing works
Mechanism and medical implications of mammalian autophagy
Dikic, I., & Elazar, Z. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0003-4 · Cited by 2,771 · see citing works
Levy, J. M. M., Towers, C. G., & Thorburn, A. (2017) · Nature Reviews Cancer · doi:10.1038/nrc.2017.53 · Cited by 2,526 · see citing works
Hypoxia-inducible factors and the response to hypoxic stress
Majmundar, A. J., Wong, W. J., & Simon, M. C. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.022 · Cited by 2,380 · see citing works
HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
Papandreou, I., Cairns, R. A., Fontana, L., Lim, A. L., & Denko, N. C. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.01.012 · Cited by 2,267 · see citing works
Jung, C. H., Ro, S.-H., Cao, J., Otto, N. M., & Kim, D.-H. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.017 · Cited by 2,090 · see citing works
Oxygen sensing by HIF hydroxylases
Schofield, C. J., & Ratcliffe, P. J. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1366 · Cited by 2,068 · see citing works
HIF-1α pathway: role, regulation and intervention for cancer therapy
Masoud, G. N., & Li, W. (2015) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2015.05.007 · Cited by 1,871 · cited 1× · see citing works
“Despite the complexity of HIF-1 regulation, the role of HIF-1 in tumor progression through autophagy has long been appreciated (Masoud and Li, 2015).”
BackgroundHypoxia, HIF1 and glucose metabolism in the solid tumour
Denko, N. C. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2468 · Cited by 1,707 · see citing works
Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells
Liu, L., Feng, D., Chen, G., Chen, M., Zheng, Q., Song, P., Ma, Q., Zhu, C., Wang, R., Qi, W., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2422 · Cited by 1,689 · see citing works
Bellot, G., Garcia-Medina, R., Gounon, P., Chiche, J., Roux, D., Pouysségur, J., & Mazure, N. M. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00166-09 · Cited by 1,501 · see citing works
Brugarolas, J., Lei, K., Hurley, R. L., Manning, B. D., Reiling, J. H., Hafen, E., Witters, L. A., Ellisen, L. W., & Kaelin, W. G. (2004) · Genes & Development · doi:10.1101/gad.1256804 · Cited by 1,384 · see citing works
Nix is a selective autophagy receptor for mitochondrial clearance
Novak, I., Kirkin, V., McEwan, D. G., Zhang, J., Wild, P., Rozenknop, A., Rogov, V., Löhr, F., Popovic, D., Occhipinti, A., et al. (2010) · The EMBO Reports · doi:10.1038/embor.2009.256 · Cited by 1,309 · see citing works
Hypoxia-Induced Angiogenesis: Good and Evil
Krock, B. L., Skuli, N., & Simon, M. C. (2011) · Genes & Cancer · doi:10.1177/1947601911423654 · Cited by 1,179 · see citing works
UPR, autophagy, and mitochondria crosstalk underlies the ER stress response
Senft, D., & Ronai, Z. A. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.01.002 · Cited by 1,121 · see citing works
Role of BNIP3 and NIX in cell death, autophagy, and mitophagy
Zhang, J., & Ney, P. A. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2009.16 · Cited by 1,021 · see citing works
Autophagy at the crossroads of catabolism and anabolism
Kaur, J., & Debnath, J. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4024 · Cited by 993 · see citing works
Hypoxia-Inducible Factors: Master Regulators of Cancer Progression
Schito, L., & Semenza, G. L. (2016) · Trends in Cancer · doi:10.1016/j.trecan.2016.10.016 · Cited by 962 · see citing works
Regulation of endoplasmic reticulum turnover by selective autophagy
Khaminets, A., Heinrich, T., Mari, M., Grumati, P., Huebner, A. K., Akutsu, M., Liebmann, L., Stolz, A., Nietzsche, S., Koch, N., et al. (2015) · Nature · doi:10.1038/nature14498 · Cited by 956 · see citing works
Hypoxia signalling through mTOR and the unfolded protein response in cancer
Wouters, B. G., & Koritzinsky, M. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2501 · Cited by 894 · see citing works
Rozpędek‐Kamińska, W., Pytel, D., Mucha, B., Leszczynska, H., Diehl, J. A., & Majsterek, I. (2016) · Current Molecular Medicine · doi:10.2174/1566524016666160523143937 · Cited by 871 · see citing works
Rouschop, K. M. A., van den Beucken, T., Dubois, L., Niessen, H., Bussink, J., Savelkouls, K., Keulers, T., Mujcic, H., Landuyt, W., Voncken, J. W., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40027 · Cited by 829 · see citing works
XBP1 promotes triple-negative breast cancer by controlling the HIF1α pathway
Chen, X., Iliopoulos, D., Zhang, Q. H., Tang, Q., Greenblatt, M. B., Hatziapostolou, M., Lim, E., Tam, W. L., Ni, M., Chen, Y., et al. (2014) · Nature · doi:10.1038/nature13119 · Cited by 817 · see citing works
ER stress: Autophagy induction, inhibition and selection
Rashid, H.-O., Yadav, R. K., Kim, H., & Chae, H. (2015) · Autophagy · doi:10.1080/15548627.2015.1091141 · Cited by 796 · see citing works
The Interplay Between Mitochondrial Dynamics and Mitophagy
Twig, G., & Shirihai, O. S. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3779 · Cited by 778 · see citing works
Coordination of mitophagy and mitochondrial biogenesis during ageing in C. elegans
Palikaras, K., Lionaki, E., & Tavernarakis, N. (2015) · Nature · doi:10.1038/nature14300 · Cited by 770 · see citing works
Hanna, R. A., Quinsay, M. N., Orogo, A. M., Giang, K., Rikka, S., & Gustafsson, Å. B. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.322933 · Cited by 762 · see citing works
ER stress‐regulated translation increases tolerance to extreme hypoxia and promotes tumor growth
Bi, M., Naczki, C., Koritzinsky, M., Fels, D. R., Blais, J. D., Hu, N., Harding, H. P., Novoa, I., Varia, M. A., Raleigh, J. A., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600777 · Cited by 732 · see citing works
Hypoxia and Metabolic Adaptation of Cancer Cells
Eales, K. L., Hollinshead, K. E. R., & Tennant, D. A. (2016) · Oncogenesis · doi:10.1038/oncsis.2015.50 · Cited by 724 · cited 7× · see citing works
“These data raise the possibility that a feedback loop that coordinates HIF1, Pink1/Parkin levels and mitophagy exists.”
BackgroundInfluentialSowter, H., Ratcliffe, P. J., Watson, P. H., Greenberg, A. H., & Harris, A. L. (2001) · PubMed · Cited by 711 · see citing works
Src kinases as therapeutic targets for cancer
Kim, L. C., Song, L., & Haura, E. B. (2009) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2009.129 · Cited by 700 · see citing works
ATM and ATR as therapeutic targets in cancer
Weber, A. M., & Ryan, A. J. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.12.001 · Cited by 644 · see citing works
Hypoxia-induced autophagy: cell death or cell survival?
Mazure, N. M., & Pouysségur, J. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.11.015 · Cited by 620 · see citing works
Endoplasmic Reticulum Stress and the Hallmarks of Cancer
Urra, H., Dufey, E., Avril, T., Chevet, É., & Hetz, C. A. (2016) · Trends in cancer · doi:10.1016/j.trecan.2016.03.007 · Cited by 607 · see citing works
Chen, G., Han, Z., Feng, D., Chen, Y., Chen, L., Wu, H., Huang, L., Zhou, C., Cai, X., Fu, C., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.034 · Cited by 600 · see citing works
Mitophagy receptor FUNDC1 regulates mitochondrial dynamics and mitophagy
Chen, M., Chen, Z., Wang, Y., Tan, Z. L., Zhu, C., Li, Y., Han, Z., Chen, L., Gao, R., Liu, L., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1151580 · Cited by 600 · see citing works
ULK1 translocates to mitochondria and phosphorylates FUNDC1 to regulate mitophagy
Wu, W., Tian, W., Hu, Z., Chen, G., Huang, L. H., Li, W., Zhang, X., Xue, P., Zhou, C., Liu, L., et al. (2014) · EMBO Reports · doi:10.1002/embr.201438501 · Cited by 586 · see citing works
Dual role of autophagy in hallmarks of cancer
Singh, S. S., Vats, S., Chia, A. Y.-Q., Tan, T. Z., Deng, S., Ong, M. S., Arfuso, F., Yap, C. T., Goh, B. C., Sethi, G., et al. (2018) · Oncogene · doi:10.1038/s41388-017-0046-6 · Cited by 542 · see citing works
Hetz, C., Thielen, P., Matus, S., Nassif, M., Court, F., Kiffin, R., Martinez, G., Cuervo, A. M., Brown, R. H., & Glimcher, L. H. (2009) · Genes & Development · doi:10.1101/gad.1830709 · Cited by 530 · see citing works
Li, X., Jiang, Y., Meisenhelder, J., Yang, W., Hawke, D. H., Zheng, Y., Xia, Y., Aldape, K., He, J., Hunter, T. R., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.009 · Cited by 504 · see citing works
Zhu, Y., Maßen, S., Terenzio, M., Lang, V., Chen-Lindner, S., Eils, R., Novak, I., Đikić, I., Hamacher‐Brady, A., & Brady, N. R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.399345 · Cited by 491 · see citing works
Mitochondrial biogenesis and clearance: a balancing act
Ploumi, C., Daskalaki, I., & Tavernarakis, N. (2016) · FEBS Journal · doi:10.1111/febs.13820 · Cited by 465 · see citing works
Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery
Fumagalli, F., Noack, J., Bergmann, T. J., Cebollero, E., Pisoni, G. B., Fasana, E., Fregno, I., Galli, C., Loi, M., Soldà, T., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3423 · Cited by 461 · see citing works
mTORC1 and mTORC2 in cancer and the tumor microenvironment
Kim, L. C., Cook, R. S., & Chen, J. (2016) · Oncogene · doi:10.1038/onc.2016.363 · Cited by 443 · see citing works
Smith, M. D., Harley, M. E., Kemp, A. J., Wills, J. C., Lee, M. W., Arends, M. J., von Kriegsheim, A., Behrends, C., & Wilkinson, S. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.11.024 · Cited by 443 · see citing works
Full length RTN3 regulates turnover of tubular endoplasmic reticulum via selective autophagy
Grumati, P., Morozzi, G., Hölper, S., Mari, M. C., Harwardt, M.-L. I. E., Yan, R., Müller, S. P., Reggiori, F., Heilemann, M., & Đikić, I. (2017) · eLife · doi:10.7554/elife.25555 · Cited by 435 · see citing works
ATM functions at the peroxisome to induce pexophagy in response to ROS
Zhang, J., Tripathi, D. N., Ji, J., Alexander, A., Kim, J., Powell, R. T., Dere, R., Tait-Mulder, J., Lee, J., Paull, T. T., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3230 · Cited by 426 · see citing works
Lee, Y., Lee, H.-Y., Hanna, R. A., & Gustafsson, Å. B. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00368.2011 · Cited by 398 · see citing works
Mechanistic insights into selective autophagy pathways: lessons from yeast
Farré, J., & Subramani, S. E. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.74 · Cited by 397 · see citing works
<i>BNIP3</i> Is an RB/E2F Target Gene Required for Hypoxia-Induced Autophagy
Tracy, K., Dibling, B. C., Spike, B. T., Knabb, J. R., Schumacker, P., & Macleod, K. F. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02246-06 · Cited by 369 · see citing works
Wu, W., Lin, C., Wu, K., Jiang, L., Wang, X., Li, W., Zhuang, H., Zhang, X., Chen, H. H., Li, S., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593102 · Cited by 362 · see citing works
NBR1 acts as an autophagy receptor for peroxisomes
Deosaran, E., Larsen, K. B., Hua, R., Sargent, G., Wang, Y., Kim, S., Lamark, T., Jauregui, M., Law, K. B., Lippincott‐Schwartz, J., et al. (2012) · Journal of Cell Science · doi:10.1242/jcs.114819 · Cited by 359 · see citing works
Protein Kinase CK2 in Health and Disease
Trembley, J. H., Wang, G., Unger, G. M., Slaton, J. W., & Ahmed, K. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-9154-y · Cited by 354 · see citing works
Hypoxia induces the expression of the pro-apoptotic gene BNIP3
Guo, K., Searfoss, G. H., Krolikowski, D., Pagnoni, M., Franks, C. F., Clark, K. L., Yu, K. T., Jaye, M., & Ivashchenko, Y. (2001) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400810 · Cited by 353 · see citing works
Koh, M. Y., Lemos, R., Liu, X., & Powis, G. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-4142 · Cited by 350 · see citing works
Ray, R., Chen, G., Velde, C. V., Cizeau, J., Park, J. H., Reed, J. C., Gietz, R. D., & Greenberg, A. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.1439 · Cited by 349 · see citing works
Yang, Z., Fujii, H., Mohan, S. V., Goronzy, J. J., & Weyand, C. M. (2013) · Journal of Experimental Medicine · doi:10.1084/jem.20130252 · Cited by 334 · see citing works
PpAtg30 Tags Peroxisomes for Turnover by Selective Autophagy
Farré, J.-C., Manjithaya, R., Mathewson, R. D., & Subramani, S. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.12.011 · Cited by 331 · see citing works
Hexokinase-II Positively Regulates Glucose Starvation-Induced Autophagy through TORC1 Inhibition
Roberts, D. J., Tan‐Sah, V. P., Ding, E., Smith, J. M., & Miyamoto, S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.019 · Cited by 330 · see citing works
Targeting Src family kinases in anti-cancer therapies: turning promise into triumph
Zhang, S., & Yu, D. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.11.002 · Cited by 323 · see citing works
Fang, H.-Y., Hughes, R., Murdoch, C., Coffelt, S. B., Biswas, S. K., Harris, A. L., Johnson, R. S., Imityaz, H. Z., Simon, M. C., Fredlund, E., et al. (2009) · Blood · doi:10.1182/blood-2008-12-195941 · Cited by 319 · see citing works
Parkin-Independent Mitophagy Controls Chemotherapeutic Response in Cancer Cells
Villa, E., Proïcs, E., Rubio‐Patiño, C., Obba, S., Zunino, B., Bossowski, J. P., Rozier, R., Chiche, J., Mondragón, L., Riley, J. S., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.087 · Cited by 315 · see citing works
Cosín‐Roger, J., Simmen, S., Melhem, H., Atrott, K., Frey-Wagner, I. M., Hausmann, M., de Vallière, C., Spalinger, M. R., Spielmann, P., Wenger, R. H., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00213-3 · Cited by 309 · see citing works
Masson, N., & Ratcliffe, P. J. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-3 · Cited by 296 · see citing works
mTOR Pathways in Cancer and Autophagy
Paquette, M., El–Houjeiri, L., & Pause, A. (2018) · Cancers · doi:10.3390/cancers10010018 · Cited by 296 · see citing works
Mitochondrial E3 ligase MARCH5 regulates FUNDC1 to fine‐tune hypoxic mitophagy
Chen, Z., Liu, L., Cheng, Q., Li, Y., Wu, H., Zhang, W., Wang, Y., Sehgal, S. A., Siraj, S., Wang, X., et al. (2017) · EMBO Reports · doi:10.15252/embr.201643309 · Cited by 295 · see citing works
Shi, L., Pan, H., Liu, Z., Xie, J., & Han, W. (2017) · Signal Transduction and Targeted Therapy · doi:10.1038/sigtrans.2017.44 · Cited by 287 · see citing works
BNIP3 Protein Suppresses PINK1 Kinase Proteolytic Cleavage to Promote Mitophagy
Zhang, T., Xue, L., Li, L., Tang, C., Wan, Z., Wang, R., Tan, J., Tan, Y., Han, H., Tian, R., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.733410 · Cited by 285 · see citing works
Margariti, A., Li, H., Chen, T., Martin, D., Vizcay‐Barrena, G., Alam, S., Karamariti, E., Xiao, Q., Zampetaki, A., Zhang, Z., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.412783 · Cited by 284 · see citing works
Phosphoglycerate Kinase 1 Phosphorylates Beclin1 to Induce Autophagy
Qian, X., Li, X., Cai, Q., Zhang, C., Yu, Q., Jiang, Y., Lee, J.-H., Hawke, D. H., Wang, Y., Xia, Y., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.01.027 · Cited by 281 · see citing works
BNIP3L/NIX-mediated mitophagy protects against ischemic brain injury independent of PARK2
Yuan, Y., Zheng, Y., Zhang, X., Chen, Y., Wu, X., Wu, J., Shen, Z., Jiang, L., Wang, L., Yang, W. Y., et al. (2017) · Autophagy · doi:10.1080/15548627.2017.1357792 · Cited by 278 · see citing works
Bnip3 impairs mitochondrial bioenergetics and stimulates mitochondrial turnover
Rikka, S., Quinsay, M. N., Thomas, R. L., Kubli, D. A., Zhang, X., Murphy, A. N., & Gustafsson, Å. B. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.146 · Cited by 277 · see citing works
Schuck, S., Gallagher, C. M., & Walter, P. (2014) · Journal of Cell Science · doi:10.1242/jcs.154716 · Cited by 272 · see citing works
Li, Y., Wang, Y., Kim, E., Beemiller, P., Wang, C. Y., Swanson, J. A., You, M., & Guan, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705231200 · Cited by 269 · see citing works
Reciprocal influence of the p53 and the hypoxic pathways
Sermeus, A., & Michiels, C. (2011) · Cell Death and Disease · doi:10.1038/cddis.2011.48 · Cited by 267 · see citing works
Pex3‐anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae
Motley, A. M., Nuttall, J. M., & Hettema, E. H. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.151 · Cited by 267 · see citing works
Wei, H., Liu, L., & Chen, Q. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.03.013 · Cited by 256 · see citing works
HIF-1 in cancer therapy: two decade long story of a transcription factor
Soni, S., & Padwad, Y. S. (2017) · Acta Oncologica · doi:10.1080/0284186x.2017.1301680 · Cited by 251 · cited 2× · see citing works
“For example, BNIP3 and NIX are highly expressed in breast, macrophage, endothelial and epithelial cancer cells compared to healthy cells from the same patient upon hypoxia induction (Sowter et al., 2001).”
BackgroundSquatrito, M., Brennan, C., Helmy, K. Y., Huse, J. T., Petrini, J. H. J., & Holland, E. C. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.10.034 · Cited by 238 · see citing works
Silencing of the Hypoxia-Inducible Cell Death Protein BNIP3 in Pancreatic Cancer
Okami, J., Simeone, D. M., & Logsdon, C. D. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0089 · Cited by 238 · see citing works
Acid Suspends the Circadian Clock in Hypoxia through Inhibition of mTOR
Walton, Z. E., Patel, C. H., Brooks, R. C., Yu, Y., Ibrahim‐Hashim, A., Riddle, M., Porcu, A., Jiang, T., Ecker, B. L., Tameire, F., et al. (2018) · Cell · doi:10.1016/j.cell.2018.05.009 · Cited by 226 · see citing works
Nagelkerke, A., Bussink, J., Mujčić, H., Wouters, B. G., Lehmann, S., Sweep, F. C. G. J., & Span, P. N. (2013) · Breast Cancer Research · doi:10.1186/bcr3373 · Cited by 223 · see citing works
Elsner, M., Gehrmann, W., & Lenzen, S. (2011) · Diabetes · doi:10.2337/db09-1401 · Cited by 221 · see citing works
Rouschop, K. M. A., Dubois, L. J., Keulers, T. G., van den Beucken, T., Lambin, P., Bussink, J., van der Kogel, A. J., Koritzinsky, M., & Wouters, B. G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1210633110 · Cited by 217 · see citing works
Mitochondrial Akt Regulation of Hypoxic Tumor Reprogramming
Chae, Y. C., Vaira, V., Caino, M. C., Tang, H., Seo, J. H., Kossenkov, A. V., Ottobrini, L., Martelli, C., Lucignani, G., Bertolini, I., et al. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.07.004 · Cited by 209 · see citing works
Wu, W., Li, W., Chen, H. H., Jiang, L., Zhu, R., & Feng, D. (2016) · Autophagy · doi:10.1080/15548627.2016.1193656 · Cited by 200 · see citing works
Peroxisomes in brain development and function
Berger, J., Dorninger, F., Forss-Petter, S., & Kunze, M. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.12.005 · Cited by 194 · cited 1× · see citing works
“Their key functions are oxygen-dependent and related to lipid synthesis, ROS metabolism and the degradation of both polyunsaturated fatty acids (PUFAs) and very long fatty acids (VLCFAs), among others (Berger et al., 2016).”
BackgroundEmergence of protein kinase CK2 as a key target in cancer therapy
Trembley, J. H., Chen, Z., Unger, G. M., Slaton, J. W., Kren, B. T., Waes, C. V., & Ahmed, K. (2010) · BioFactors · doi:10.1002/biof.96 · Cited by 194 · see citing works
Pereira, E. R., Frudd, K., Awad, W., & Hendershot, L. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.507194 · Cited by 190 · see citing works
The BCL2L1 and PGAM5 axis defines hypoxia-induced receptor-mediated mitophagy
Wu, H., Xue, D., Chen, G., Han, Z., Huang, L., Zhu, C., Wang, X., Jin, H., Wang, J., Zhu, Y., et al. (2014) · Autophagy · doi:10.4161/auto.29568 · Cited by 183 · see citing works
PEX2 is the E3 ubiquitin ligase required for pexophagy during starvation
Sargent, G., van Zutphen, T., Shatseva, T., Zhang, L., Giovanni, V. D., Bandsma, R., & Kim, P. K. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201511034 · Cited by 177 · see citing works
Palikaras, K., Daskalaki, I., Markaki, M., & Tavernarakis, N. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.04.005 · Cited by 175 · see citing works
Hif-2α Promotes Degradation of Mammalian Peroxisomes by Selective Autophagy
Walter, K., Schönenberger, M. J., Trötzmüller, M., Horn, M., Elsässer, H., Moser, A. B., Lucas, M. S., Schwarz, T., Gerber, P. A., Faust, P. L., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.09.017 · Cited by 163 · see citing works
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 · see citing works
Pereira, F. F., Bernardes, V. C. D., Eisemberg, C. C., Fantin, C., & Vogt, R. C. (2016) · Genetics and Molecular Research · doi:10.4238/gmr.15017335 · Cited by 161 · see citing works
Structural insights into the recognition of phosphorylated FUNDC1 by LC3B in mitophagy
Lv, M., Wang, C., Li, F., Peng, J., Wen, B., Gong, Q., Shi, Y., & Tang, Y. (2016) · Protein & Cell · doi:10.1007/s13238-016-0328-8 · Cited by 158 · see citing works
Structural basis for the phosphorylation of FUNDC1 LIR as a molecular switch of mitophagy
Kuang, Y., Ma, K., Zhou, C., Ding, P., Zhu, Y., Chen, Q., & Xia, B. (2016) · Autophagy · doi:10.1080/15548627.2016.1238552 · Cited by 153 · see citing works
Capello, M., Borgogno, S. F., Riganti, C., Chattaragada, M. S., Principe, M., Roux, C., Zhou, W., Petricoin, E. F., Cappello, P., & Novelli, F. (2015) · Oncotarget · doi:10.18632/oncotarget.6798 · Cited by 152 · see citing works
Roy, S., Leidal, A. M., Ye, J., Ronen, S. M., & Debnath, J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.020 · Cited by 151 · see citing works
Li, W., Zhang, X., Zhuang, H., Chen, H.-G., Chen, Y., Tian, W., Wu, W., Li, Y., Wang, S., Zhang, L., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.537050 · Cited by 145 · see citing works
Mujčić, H., Nagelkerke, A., Rouschop, K. M. A., Chung, S., Chaudary, N., Span, P. N., Clarke, B. A., Milosevic, M., Sykes, J. R., Hill, R. P., et al. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-0526 · Cited by 127 · see citing works
Di Conza, G., Trusso Cafarello, S., Loroch, S., Mennerich, D., Deschoemaeker, S., Di Matteo, M., Ehling, M., Gevaert, K., Prenen, H., Zahedi, R. P., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.01.051 · Cited by 119 · see citing works
Interplay between unfolded protein response and autophagy promotes tumor drug resistance
YAN, M.-M., Ni, J., Song, D., Ding, M., & Huang, J. X. (2015) · Oncology Letters · doi:10.3892/ol.2015.3508 · Cited by 116 · see citing works
Protein kinase activity of the glycolytic enzyme PGK1 regulates autophagy to promote tumorigenesis
Qian, X., Li, X., & Lu, Z. (2017) · Autophagy · doi:10.1080/15548627.2017.1313945 · Cited by 114 · see citing works
Regulation of hypoxia-induced autophagy in glioblastoma involves ATG9A
Rahim, S. A. A., Dirkse, A., Oudin, A., Schuster, A. M., Bohler, J., Barthelemy, V., Muller, A., Vallar, L., Janji, B., Golebiewska, A., et al. (2017) · British Journal of Cancer · doi:10.1038/bjc.2017.263 · Cited by 114 · see citing works
p53 directly suppresses BNIP3 expression to protect against hypoxia‐induced cell death
Feng, X., Liu, X., Zhang, W., & Xiao, W. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.248 · Cited by 111 · see citing works
Regulation and function of mitophagy in development and cancer
Lu, H., Li, G., Liu, L., Feng, L., Wang, X., & Jin, H. (2013) · Autophagy · doi:10.4161/auto.26550 · Cited by 105 · see citing works
Signaling pathways and mechanisms of hypoxia‐induced autophagy in the animal cells
Fang, Y., Tan, J., & Zhang, Q. (2015) · Cell Biology International · doi:10.1002/cbin.10463 · Cited by 102 · see citing works
Antagonism of E2F-1 regulated Bnip3 transcription by NF-κB is essential for basal cell survival
Shaw, J., Yurkova, N., Zhang, T., Gang, H., Aguilar, F., Weidman, D. R., Scramstad, C., Weisman, H., & Kirshenbaum, L. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807735105 · Cited by 102 · see citing works
Inhibition of 6-phosphofructo-2-kinase (PFKFB3) induces autophagy as a survival mechanism
Klarer, A. C., O’Neal, J., Imbert-Fernandez, Y., Clem, A. L., Ellis, S. R., Clark, J. A., Clem, B. F., Chesney, J. A., & Telang, S. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-2 · Cited by 102 · see citing works
Autophagy inhibition in cancer therapy: metabolic considerations for antitumor immunity
Townsend, K. N., Hughson, L. R. K., Schlie, K., Poon, V. I., Westerback, A., & Lum, J. J. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01141.x · Cited by 101 · see citing works
Role for casein kinase 2 in the regulation of HIF‐1 activity
Mottet, D., Ruys, S. P. D., Demazy, C., Raes, M. J., & Michiels, C. (2005) · International Journal of Cancer · doi:10.1002/ijc.21268 · Cited by 99 · see citing works
Mujčić, H., Rzymski, T., Rouschop, K. M. A., Koritzinsky, M., Milani, M., Harris, A. L., & Wouters, B. G. (2009) · Radiotherapy and Oncology · doi:10.1016/j.radonc.2009.08.017 · Cited by 97 · see citing works
Physiologic hypoxia promotes maintenance of CML stem cells despite effective BCR-ABL1 inhibition
Ng, K. P., Manjeri, A., Lee, K. L., Huang, W., Tan, S., Chuah, C. T. H., Poellinger, L., & Ong, S. T. (2014) · Blood · doi:10.1182/blood-2013-07-511907 · Cited by 96 · see citing works
Huang, Z., Wu, S., Kong, F., Cai, X., Ye, B., Shan, P., & Huang, W. (2016) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12990 · Cited by 95 · see citing works
Burton, T. R., Henson, E. S., Baijal, P. K., Eisenstat, D. D., & Gibson, S. B. (2005) · International Journal of Cancer · doi:10.1002/ijc.21547 · Cited by 92 · see citing works
The Cell Cycle Factor E2F-1 Activates Bnip3 and the Intrinsic Death Pathway in Ventricular Myocytes
Yurkova, N., Shaw, J., Blackie, K., Weidman, D. R., Jayas, R., Flynn, B., & Kirshenbaum, L. A. (2007) · Circulation Research · doi:10.1161/circresaha.107.164731 · Cited by 88 · see citing works
Weng, L., Du, J., Zhou, Q.-H., Cheng, B., Li, J., Zhang, D., & Ling, C. (2012) · Molecular Cancer · doi:10.1186/1476-4598-11-39 · Cited by 86 · see citing works
Carloni, S., Albertini, M. C., Galluzzi, L., Buonocore, G., Proietti, F., & Balduini, W. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.03.002 · Cited by 85 · see citing works
Endoplasmic Reticulum Stress and Related Pathological Processes
Mei, Y. (2013) · Journal of Diagnostic Techniques and Biomedical Analysis · doi:10.4172/2327-4638.1000105 · Cited by 85 · see citing works
Cerrada, I., Ruiz‐Saurí, A., Carrero, R., Trigueros, C., Dorronsoro, A., Sánchez-Puelles, J.-M., Díez‐Juan, A., Montero, J., & Sepúlveda, P. (2012) · Stem Cells and Development · doi:10.1089/scd.2012.0340 · Cited by 83 · see citing works
Li, B., Feng, W., Luo, O., Xu, T., Cao, Y., Wu, H., Yu, D., & Ding, Y. (2017) · Scientific Reports · doi:10.1038/s41598-017-04811-5 · Cited by 82 · see citing works
Wolff, N. C., Vega-Rubín-de-Celis, S., Xie, X., Castrillón, D. H., Kabbani, W., & Brugarolas, J. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01393-10 · Cited by 81 · see citing works
Lee, H. J., Jung, Y. H., Choi, G. E., Ko, S. H., Lee, S. J., Lee, S. H., & Han, H. J. (2017) · Redox Biology · doi:10.1016/j.redox.2017.07.004 · Cited by 81 · see citing works
Ishaq, M., Khan, M. A., Sharma, K. K., Sharma, G., Dutta, R. K., & Majumdar, S. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.08.019 · Cited by 80 · see citing works
Hou, H., Er, P., Cheng, J., Chen, X., Ding, X., Wang, Y., Chen, X., Yuan, Z., Pang, Q., Wang, P., et al. (2017) · Cancer Medicine · doi:10.1002/cam4.1112 · Cited by 80 · see citing works
Src kinase activation: A switched electrostatic network
Özkırımlı, E., & Post, C. B. (2006) · Protein Science · doi:10.1110/ps.051999206 · Cited by 77 · see citing works
Targeting PDK1 with dichloroacetophenone to inhibit acute myeloid leukemia (AML) cell growth
Qin, L., Tian, Y., Yu, Z., Shi, D., Wang, J., Zhang, C., Peng, R., Chen, X., Liu, C., Chen, Y., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.6366 · Cited by 77 · see citing works
Impairment of peroxisomal biogenesis in human colon carcinoma
Lauer, C. (1999) · Carcinogenesis · doi:10.1093/carcin/20.6.985 · Cited by 75 · see citing works
miR-137 Modulates a Tumor Suppressor Network-Inducing Senescence in Pancreatic Cancer Cells
Neault, M., Mallette, F. A., & Richard, S. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.01.068 · Cited by 75 · see citing works
MARCH5-FUNDC1 axis fine-tunes hypoxia-induced mitophagy
Chen, Z., Siraj, S., Liu, L., & Chen, Q. (2017) · Autophagy · doi:10.1080/15548627.2017.1310789 · Cited by 75 · see citing works
Catalase inhibition induces pexophagy through ROS accumulation
Lee, J. N., Dutta, R. K., Maharjan, Y., Liu, Z., Lim, J.-Y., Kim, S.-J., Cho, D., So, H., Choe, S., & Park, R. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.05.050 · Cited by 74 · see citing works
Ryan, D., Carberry, S., Murphy, Á. C., Lindner, A. U., Fay, J., Hector, S., McCawley, N., Bacon, O., Concannon, C. G., Kay, E. W., et al. (2016) · Journal of Translational Medicine · doi:10.1186/s12967-016-0948-z · Cited by 73 · see citing works
Lipophagy Contributes to Testosterone Biosynthesis in Male Rat Leydig Cells
Ma, Y., Zhou, Y., Zhu, Y., Wang, S., Ping, P., & Chen, X. (2018) · Endocrinology · doi:10.1210/en.2017-03020 · Cited by 73 · see citing works
Sec62 Bridges the Gap from 3q Amplification to Molecular Cell Biology in Non–Small Cell Lung Cancer
Linxweiler, M., Linxweiler, J., Barth, M., Benedix, J., Jung, V., Kim, Y.-J., Bohle, R. M., Zimmermann, R., & Greiner, M. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.10.039 · Cited by 72 · see citing works
Cai, M., Sun, X., Wang, W., Lian, Z., Wu, P., Han, S., Chen, H., & Zhang, P. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.02.021 · Cited by 72 · see citing works
Regulation of Mitochondrial Integrity, Autophagy and Cell Survival by BNIP3
Tracy, K., & Macleod, K. F. (2007) · Autophagy · doi:10.4161/auto.4892 · Cited by 69 · see citing works
Chen, Q., Zhou, Y., Richards, M., & Wang, P. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.04.090 · Cited by 68 · see citing works
A Mechanistic Review of Mitophagy and Its Role in Protection against Alcoholic Liver Disease
Williams, J. A. R., & Ding, W. (2015) · Biomolecules · doi:10.3390/biom5042619 · Cited by 67 · see citing works
He, J., Pei, L., Jiang, H., Yang, W., Chen, J., & Liang, H. (2017) · Journal of Cancer · doi:10.7150/jca.18171 · Cited by 67 · see citing works
Neuronal hypoxia disrupts mitochondrial fusion
Sanderson, T. H., Raghunayakula, S., & Kumar, R. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.05.078 · Cited by 64 · see citing works
Islam, F., Gopalan, V., Vider, J., Wahab, R., Ebrahimi, F., Lu, C., Kasem, K., & Lam, A. K.-Y. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.05.021 · Cited by 64 · see citing works
Autophagy in non-small cell lung carcinogenesis
Rao, S., Yang, H., Penninger, J. M., & Kroemer, G. (2014) · Autophagy · doi:10.4161/auto.27643 · Cited by 63 · see citing works
Silencing of the SEC62 gene inhibits migratory and invasive potential of various tumor cells
Greiner, M., Kreutzer, B., Jung, V., Grobholz, R., Hasenfus, A., Stöhr, R., Tornillo, L., Dudek, J., Stöckle, M., Unteregger, G., et al. (2010) · International Journal of Cancer · doi:10.1002/ijc.25580 · Cited by 63 · see citing works
ATM kinase sustains HER2 tumorigenicity in breast cancer
Stagni, V., Manni, I., Oropallo, V., Mottolese, M., Benedetto, A. D., Piaggio, G., Falcioni, R., Giaccari, D., Carlo, S. E. D., Sperati, F., et al. (2015) · Nature Communications · doi:10.1038/ncomms7886 · Cited by 63 · see citing works
Hubert, A., Paris, S., Piret, J., Ninane, N., Raes, M. J., & Michiels, C. (2006) · Journal of Cell Science · doi:10.1242/jcs.03069 · Cited by 62 · see citing works
Koop, E. A., van Laar, T., van Wichen, D. F., de Weger, R. A., van der Wall, E., & van Diest, P. J. (2009) · BMC Cancer · doi:10.1186/1471-2407-9-175 · Cited by 61 · see citing works
Downregulation of microRNA-498 in colorectal cancers and its cellular effects
Gopalan, V., Smith, R. A., & Lam, A. K.-Y. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.08.006 · Cited by 60 · see citing works
Jung, V., Kindich, R., Kamradt, J., Jung, M., Müller, M., Schulz, W. A., Engers, R., Unteregger, G., Stöckle, M., Zimmermann, R., et al. (2006) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-05-0165 · Cited by 60 · see citing works
Hypoxia induces autophagy in cardiomyocytes via a hypoxia-inducible factor 1-dependent mechanism
GUI, L., LIU, B., & Lv, G. (2016) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2016.3190 · Cited by 58 · see citing works
Liu, K. E., & Frazier, W. A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0129667 · Cited by 56 · see citing works
Evaluation of protein biomarkers of prostate cancer aggressiveness
Rizzardi, A. E., Rosener, N. K., Koopmeiners, J. S., Vogel, R. I., Metzger, G. J., Forster, C. L., Marston, L. O., Tiffany, J. R., McCarthy, J. B., Turley, E. A., et al. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-244 · Cited by 55 · see citing works
MiR-498 regulated FOXO3 expression and inhibited the proliferation of human ovarian cancer cells
Liu, R., Liu, F., Li, L., Sun, M., & Kuisheng, C. (2015) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2015.04.005 · Cited by 54 · see citing works
Zhou, J., Li, C., Wang, Y., Alsiddig, M., Huo, L., Liu, H., & Miao, Y. (2018) · Biology of Reproduction · doi:10.1093/biolre/ioy061 · Cited by 54 · see citing works
Calnexin is a novel sero-diagnostic marker for lung cancer
Kobayashi, M., Nagashio, R., Jiang, S., Saito, K., Tsuchiya, B., Ryuge, S., Katono, K., Nakashima, H., Fukuda, E., Goshima, N., et al. (2015) · Lung Cancer · doi:10.1016/j.lungcan.2015.08.015 · Cited by 52 · see citing works
Peroxisomes protect lymphoma cells from HDAC inhibitor-mediated apoptosis
Dahabieh, M. S., Ha, Z., Pietro, E. D., Nichol, J. N., Bolt, A. M., Gonçalves, C., Dupéré-Richer, D., Pettersson, F., Mann, K. K., Braverman, N., et al. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.115 · Cited by 52 · see citing works
Wang, L., Fan, Z., Zhang, J., Changyi, Y., Huang, C., Gu, Y., Xu, Z., Tang, Z., Lu, W., Wei, X., et al. (2014) · International Journal of Cancer · doi:10.1002/ijc.29153 · Cited by 51 · see citing works
Activation of Ras Up-regulates Pro-apoptotic BNIP3 in Nitric Oxide-induced Cell Death
An, H., Maeng, O., Kang, K.-H., Lee, J., Kim, Y.-S., Paik, S., & Lee, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605819200 · Cited by 51 · see citing works
ATM kinase sustains breast cancer stem-like cells by promoting ATG4C expression and autophagy
Antonelli, M., Strappazzon, F., Arisi, I., Brandi, R., D’Onofrio, M., Sambucci, M., Manic, G., Vitale, I., Barilà, D., & Stagni, V. (2017) · Oncotarget · doi:10.18632/oncotarget.15537 · Cited by 50 · see citing works
Vadysirisack, D. D., & Ellisen, L. W. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-430-8_4 · Cited by 47 · see citing works
Functions and characteristics of PINK1 and Parkin in cancer
Matsuda, S. (2015) · Frontiers in bioscience · doi:10.2741/4321 · Cited by 47 · see citing works
Regulation of Peroxisomal Lipid Metabolism by Catalytic Activity of Tumor Suppressor H-rev107
Uyama, T., Ichi, I., Kono, N., Inoue, A., Tsuboi, K., Jin, X.-H., Araki, N., Aoki, J., Arai, H., & Ueda, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.267575 · Cited by 46 · see citing works
Long-Term Artificial Selection Reveals a Role of TCTP in Autophagy in Mammalian Cells
Chen, K., Huang, C., Yuan, J., Cheng, H., & Zhou, R. (2014) · Molecular Biology and Evolution · doi:10.1093/molbev/msu181 · Cited by 43 · see citing works
Feng, X., Li, H., Dean, M. L., Wilson, H., Kornaga, E. N., Enwere, E. K., Tang, P. A., Paterson, A. H. G., Lees‐Miller, S. P., Magliocco, A. M., et al. (2015) · Breast Cancer Research · doi:10.1186/s13058-015-0575-2 · Cited by 41 · see citing works
Identification of Novel FAM134B (JK1) Mutations in Oesophageal Squamous Cell Carcinoma
Haque, M. H., Gopalan, V., Chan, K.-W., Shiddiky, M. J. A., Smith, R. A., & Lam, A. K.-Y. (2016) · Scientific Reports · doi:10.1038/srep29173 · Cited by 40 · see citing works
Azad, M. B., & Gibson, S. B. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05778.x · Cited by 39 · see citing works
Initial evidence for Sec62 as a prognostic marker in advanced head and neck squamous cell carcinoma
Wemmert, S., LINDNER, Y., Linxweiler, J., Wagenpfeil, S., Bohle, R. M., Niewald, M., & Schick, B. (2016) · Oncology Letters · doi:10.3892/ol.2016.4135 · Cited by 39 · see citing works
Transcriptional response to hypoxic stress in melanoma and prognostic potential of GBE1 and BNIP3
Buart, S., Terry, S., Noman, M. Z., Lanoy, É., Boutros, C., Fogel, P., Dessen, P., Meurice, G., Gaston‐Mathé, Y., Vielh, P. R., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.22150 · Cited by 39 · see citing works
Calnexin Controls the STAT3-Mediated Transcriptional Response to EGF
Lakkaraju, A. K., & van der Goot, F. G. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.07.009 · Cited by 38 · see citing works
c-Kit Is Suppressed in Human Colon Cancer Tissue and Contributes to L1-Mediated Metastasis
Gavert, N. S., Shvab, A., Sheffer, M., Ben‐Shmuel, A., Haase, G., Bakos, E., Domany, E., & Ben‐Ze'ev, A. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-0576 · Cited by 36 · see citing works
Bochen, F., Adisurya, H., Wemmert, S., Lerner, C., Greiner, M., Zimmermann, R., Hasenfus, A., Wagner, M., Smola, S., Pfuhl, T., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.13986 · Cited by 36 · see citing works
Maugeri, G., D’Amico, A. G., Reitano, R., Saccone, S., Federico, C., Cavallaro, S., & D’Agata, V. (2016) · Cell and Tissue Research · doi:10.1007/s00441-015-2340-3 · Cited by 35 · see citing works
Yang, L., Wei, N., Wang, L., Wang, X., & Liu, Q. (2017) · Child s Nervous System · doi:10.1007/s00381-017-3622-8 · Cited by 35 · see citing works
Ruan, H., Li, X., Yang, H.-M., Song, Z., Tong, J., Cao, Q., Wang, K., Xiao, W., Xiao, H., Chen, X.-Y., et al. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.07.004 · Cited by 34 · see citing works
Linxweiler, M., Bochen, F., Schick, B., Wemmert, S., Kadah, B. A., Greiner, M., Hasenfus, A., Bohle, R.-M., Juhasz‐Böss, I., Solomayer, E., et al. (2016) · BMC Cancer · doi:10.1186/s12885-016-2739-6 · Cited by 33 · see citing works
Kasem, K., Gopalan, V., Salajegheh, A., Lu, C., Smith, R. A., & Lam, A. K.-Y. (2014) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2014.05.001 · Cited by 32 · see citing works
MicroRNA-498 is downregulated in non-small cell lung cancer and correlates with tumor progression
Wang, M., Zhang, Q., Wang, J., & Zhai, Y. (2015) · Journal of Cancer Research and Therapeutics · doi:10.4103/0973-1482.163859 · Cited by 28 · see citing works
Lee, J. T., Lee, T.-J., Kim, C., Kim, N.-S., & Kwon, T. K. (2009) · Cancer Letters · doi:10.1016/j.canlet.2009.01.035 · Cited by 28 · see citing works
Jin, T., Lin, H., Lin, H., Guo, L., Ge, N., Cai, X.-Y., Sun, R., Chen, W.-K., Li, Q., & Hu, W. (2012) · Journal of Translational Medicine · doi:10.1186/1479-5876-10-64 · Cited by 28 · see citing works
Profiling of a panel of radioresistant prostate cancer cells identifies deregulation of key miRNAs
McDermott, N., Meunier, A., Wong, S. C. K., Buchete, N., & Marignol, L. H. (2017) · Clinical and Translational Radiation Oncology · doi:10.1016/j.ctro.2017.01.005 · Cited by 28 · see citing works
Ding, M., van der Kwast, T., Vellanki, R. N., Foltz, W. D., McKee, T. D., Sonenberg, N., Pandolfi, P. P., Koritzinsky, M., & Wouters, B. G. (2018) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-17-0696 · Cited by 28 · see citing works
Li, Y., Zhang, X., Yang, J., Zhang, Y., Zhu, D., Zhang, L., Zhu, Y., Li, D., & Zhou, J. (2017) · Oncotarget · doi:10.18632/oncotarget.18736 · Cited by 27 · see citing works
Chen, T., Cai, S., Li, J., Qi, Z., Li, X.-Q., Ye, L., Xie, X., Hou, Y., Yao, L.-Q., Xu, M., et al. (2017) · Scientific Reports · doi:10.1038/srep44543 · Cited by 27 · see citing works
Islam, F., Gopalan, V., Pillai, S., Lu, C., Kasem, K., & Lam, A. K.-Y. (2018) · Genes Chromosomes and Cancer · doi:10.1002/gcc.22525 · Cited by 27 · see citing works
CK2 phosphorylation of human Sec63 regulates its interaction with Sec62
Ampofo, E., Welker, S., Jung, M., Müller, L., Greiner, M., Zimmermann, R., & Montenarh, M. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.12.020 · Cited by 25 · see citing works
EPAS1/HIF-2α is a driver of mammalian pexophagy
Schönenberger, M. J., Krek, W., & Kovacs, W. J. (2015) · Autophagy · doi:10.1080/15548627.2015.1045180 · Cited by 24 · see citing works
Jo, D. S., Bae, D., Park, S. J., Seo, H. M., Kim, H. B., Oh, J. S., Chang, J. W., Kim, S., Shin, J.-W., & Cho, D. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.09.153 · Cited by 22 · see citing works
Liu, R., Tang, J., Ding, C., Liang, W., Zhang, L., Chen, T., Xiong, Y., Dai, X., Li, W., Xu, Y., et al. (2017) · Cancer Letters · doi:10.1016/j.canlet.2016.12.040 · Cited by 21 · see citing works
Abdel-Mohsen, M. A., Malak, C. A. A., Yossef, M. A. A., & El‐Shafey, E. S. (2017) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/1871520617666170327144122 · Cited by 21 · see citing works
Expression and Functional Characterization of the BNIP3 Protein in Renal Cell Carcinomas
Macher‐Goeppinger, S., Keith, M., Hatiboglu, G., Hohenfellner, M., Schirmacher, P., Roth, W., & Tagscherer, K. E. (2017) · Translational Oncology · doi:10.1016/j.tranon.2017.08.008 · Cited by 20 · see citing works
Treatment of SEC62 over-expressing tumors by Thapsigargin and Trifluoperazine
Körbel, C., Linxweiler, M., Bochen, F., Wemmert, S., Schick, B., Meyer, M. R., Maurer, H. H., Menger, M. D., Zimmermann, R., & Greiner, M. (2018) · BioMolecular Concepts · doi:10.1515/bmc-2018-0006 · Cited by 20 · see citing works
H-ras up-regulates expression of BNIP3.
Kałas, W., Swiderek, E., Rapak, A., Kopij, M., Rak, J. W., & Strządała, L. (2011) · PubMed · Cited by 19 · see citing works
Expression of BRCA1, NBR1 and NBR2 Genes in Human Breast Cancer Cells
Dimitrov, S. D., Matoušková, E., & Forejt, J. (2001) · Folia Biologica · doi:10.14712/fb2001047040120 · Cited by 18 · see citing works
Autophagy degrades hypoxia inducible factors
DePavia, A., Jonasch, E. W., & Liu, X.-D. (2016) · Molecular & Cellular Oncology · doi:10.1080/23723556.2015.1104428 · Cited by 16 · see citing works
Zhang, M., & Luo, S. (2016) · Genetics and Molecular Research · doi:10.4238/gmr.15017496 · Cited by 16 · see citing works
Flagged first, then by citations
3 of the 216 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
The Roles of Autophagy in Cancer
Yun, C. W., & Lee, S. H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113466 · Cited by 965 · see citing works
Nedeljković, M., & Damjanović, A. (2019) · Cells · doi:10.3390/cells8090957 · Cited by 882 · see citing works
“These include: increased expression of ABC transporters (including ABCG2 and ABCC1) [105,106]; decreased proliferation [102]; complex modulation of cellular senescence and apoptosis [102]; induction of autophagy that aids in tumor survival [107]; enhanced genetic instability and subsequent clonal selection of aggressi…”
BackgroundGlioblastoma multiforme (GBM): An overview of current therapies and mechanisms of resistance
Wu, W. E., Klockow, J., Zhang, M., Lafortune, F., Chang, E., Jin, L., Wu, Y., & Daldrup-Link, H. E. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105780 · Cited by 833 · see citing works
Hypoxia signaling in human health and diseases: implications and prospects for therapeutics
Luo, Z., Tian, M., Yang, G., Tan, Q., Chen, Y., Li, G., Zhang, Q., Li, Y., Wan, P., & Wu, J. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01080-1 · Cited by 499 · see citing works
“Hypoxiainduced autophagy performs a certain function in tumor progression.(86) Several hypoxia-responsive genes’ transcription is regulated by HIF-1 activation under hypoxia stress.”
BackgroundYao, R.-Q., Ren, C., Xia, Z.-F., & Yao, Y.-M. (2021) · Autophagy · doi:10.1080/15548627.2020.1725377 · Cited by 441 · see citing works
“etiology of various severe conditions, initiates ER stress and functional changes in mitochondria concurrently, accompanied by activation of a variety of organelle-specific autophagies [10].”
BackgroundKhandia, 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 323 · see citing works
The Double-Edge Sword of Autophagy in Cancer: From Tumor Suppression to Pro-tumor Activity
Chavez-Dominguez, R., Perez-Medina, M., López-González, J. S., Galicia-Velasco, M., & Aguilar‐Cázares, D. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.578418 · Cited by 309 · see citing works
“Quin et al. reported in acute myeloid leukemia cells that PDK-1 associates with ULK-1 promoting its activation and leading to induction of autophagy (148).”
BackgroundInfluentialMechanism of interaction between autophagy and apoptosis in cancer
Das, S., Shukla, N., Singh, S. S., Kushwaha, S., & Shrivastava, R. (2021) · APOPTOSIS · doi:10.1007/s10495-021-01687-9 · Cited by 262 · see citing works
He, R., Wang, Z., Cui, M., Liu, S., Wu, W., Chen, M., Wu, Y., Qu, Y., Lin, H., Chen, S., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1872227 · Cited by 233 · see citing works
“BNIP3-BNIP3L-induced mitophagy upon hypoxia additionally requires the activity of essential autophagy components such as ATG7 and the interaction with LC3B [78,79].”
BackgroundSelective Autophagy Regulates Cell Cycle in Cancer Therapy
Zheng, K., He, Z., Kitazato, K., & Wang, Y. (2018) · Theranostics · doi:10.7150/thno.30308 · Cited by 226 · see citing works
Reggiori, F., & Molinari, M. (2022) · Physiological Reviews · doi:10.1152/physrev.00038.2021 · Cited by 222 · see citing works
Outstanding Questions in Mitophagy: What We Do and Do Not Know
Montava‐Garriga, L., & Ganley, I. G. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.06.032 · Cited by 209 · see citing works
“metabolic switch to upregulate glycolytic genes, attenuate mitochondria respiration and trigger mitophagy [88,90,91].”
BackgroundMolecular Mechanisms, Biomarkers and Emerging Therapies for Chemotherapy Resistant TNBC
Ferrari, P., Scatena, C., Ghilli, M., Bargagna, I., Lorenzini, G., & Nicolini, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031665 · Cited by 210 · see citing works
Role and regulation of autophagy in cancer
Rakesh, R., Dharshini, L. C. P., Sakthivel, K. M., & Rasmi, R. R. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2022.166400 · Cited by 196 · see citing works
Nonsense-mediated RNA decay: an emerging modulator of malignancy
Tan, K., Stupack, D. G., & Wilkinson, M. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00481-2 · Cited by 151 · see citing works
Hypoxia-Driven Effects in Cancer: Characterization, Mechanisms, and Therapeutic Implications
Shi, R., Liao, C., & Zhang, Q. H. (2021) · Cells · doi:10.3390/cells10030678 · Cited by 148 · see citing works
Inflammation and Metabolism in Cancer Cell—Mitochondria Key Player
Neagu, M. T., Constantin, C., Popescu, I., Zipeto, D., Tzanakakis, G. N., Nikitovic, D., Fenga, C., Stratakis, C. A., Spandidos, D. A., & Tsatsakis, A. M. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00348 · Cited by 147 · see citing works
AGE-RAGE synergy influences programmed cell death signaling to promote cancer
Waghela, B. N., Vaidya, F. U., Ranjan, K., Chhipa, A. S., Tiwari, B. S., & Pathak, C. (2020) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-020-03928-y · Cited by 134 · see citing works
“Hypoxia plays a key role in cancer metastasis and is also intricately related to autophagy machinery in cancer cells [95].”
BackgroundT cell exhaustion in malignant gliomas
Watowich, M., Gilbert, M. R., & Larion, M. (2023) · Trends in cancer · doi:10.1016/j.trecan.2022.12.008 · Cited by 130 · see citing works
Hypoxia-induced alternative splicing: the 11th Hallmark of Cancer
Farina, A. R., Cappabianca, L. A., Sebastiano, M., Zelli, V., Guadagni, S., & Mackay, A. R. (2020) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-020-01616-9 · Cited by 131 · see citing works
“This caspase-independent cell death mechanism is characterized by cellular vacuolation, cellular swelling and necrotic cell lysis is mediated by RIPK1, RIPK3 and MLKL, induced by the UPR, and also involves unconventional XPB1s splicing and hypoxiainduced autophagy, which regulate autophagosome/lysosome fusion [5, 175].”
BackgroundHepatic Tumor Microenvironments and Effects on NK Cell Phenotype and Function
Fernández, J. P., Luddy, K. A., Harmon, C., & O’Farrelly, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20174131 · Cited by 119 · see citing works
Niu, Y., Lin, Z., Wan, A., Sun, L., Yan, S., Liang, H., Zhan, S., Chen, D., Bu, X., Liu, P., et al. (2021) · Hepatology · doi:10.1002/hep.31846 · Cited by 115 · see citing works
“The homeostatic response to intratumoral hypoxic environment is mediated by hypoxia-inducible factor (HIF-1), consisting of HIF-1α and HIF-1β subunits (7), which triggers a variety of cellular responses such as angiogenesis (8), erythropoiesis (9), apoptosis (10), metastasis (11), drug-resistance (12), autophagy (13)…”
BackgroundTargeting Autophagy in Breast Cancer
Cocco, S., Leone, A., Piezzo, M., Caputo, R., Lauro, V. D., Rella, F. D., Fusco, G., Capozzi, M., Gioia, G. D., Budillon, A., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217836 · Cited by 116 · see citing works
Hypoxia Signaling in Cancer: From Basics to Clinical Practice
Sebestyén, A., Kopper, L., Dankó, T., & Tímár, J. (2021) · Pathology and Oncology Research · doi:10.3389/pore.2021.1609802 · Cited by 110 · see citing works
“reduces oxygen consumption and/or induces autophagy [45] leading slower metabolic activity and forces cellular survival mechanisms with balanced bioenergetics [46].”
BackgroundPlasticity of cancer invasion and energy metabolism
Parlani, M., Jorgez, C. J., & Friedl, P. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.09.009 · Cited by 106 · see citing works
Sirtuins' control of autophagy and mitophagy in cancer
Aventaggiato, M., Vernucci, E., Barreca, F., Russo, M. A., & Tafani, M. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107748 · Cited by 103 · see citing works
Li, J., Feng, Y., Li, Y., He, P., Zhou, Q.-Y., Tian, Y., Yao, R.-Q., & Yao, Y.-M. (2024) · Cell Proliferation · doi:10.1111/cpr.13621 · Cited by 102 · see citing works
“36,37 While increasing knowledge continues to reveal that NCOA4-mediated ferritin degradation is regarded as conservative catabolism.”
BackgroundThe Interplay Between Tumor Suppressor p53 and Hypoxia Signaling Pathways in Cancer
Zhang, C., Liu, J., Wang, J., Zhang, T., Xu, D., Hu, W., & Feng, Z. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.648808 · Cited by 97 · see citing works
“In addition to apoptosis, hypoxia induces autophagy via both HIF-1-dependent and -independent pathways, such as the mTOR pathway, unfolded protein response (UPR) pathway and PKCδ-JNK1 pathway (Fang et al., 2015; Daskalaki et al., 2018).”
BackgroundRaudenská, M., Balvan, J., & Masařík, M. (2021) · Molecular Cancer · doi:10.1186/s12943-021-01423-6 · Cited by 96 · see citing works
Autophagy as a novel therapeutic target in vascular calcification
Phadwal, K., Feng, D., Zhu, D., & MacRae, V. E. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.107430 · Cited by 90 · see citing works
Oxygen releasing materials: Towards addressing the hypoxia-related issues in tissue engineering
Agarwal, T., Kazemi, S., Costantini, M., Perfeito, F. G., Correia, C. R., Gaspar, V. M., Montazeri, L., Maria, C. D., Mano, J. F., Vosough, M., et al. (2021) · Materials Science and Engineering C · doi:10.1016/j.msec.2021.111896 · Cited by 90 · see citing works
Hypoxia-inducible factor-1: Regulatory mechanisms and drug development in stroke
Pan, Z., Ma, G., Kong, L., & Du, G. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105742 · Cited by 90 · see citing works
Mitofusins: Disease Gatekeepers and Hubs in Mitochondrial Quality Control by E3 Ligases
Escobar‐Henriques, M., & Joaquim, M. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00517 · Cited by 81 · see citing works
Qian, X., Pan, Y., Huang, Q.-Y., Shi, Y., Huang, Q.-Y., Hu, Z., & Xiong, L. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s191317 · Cited by 80 · see citing works
“ments and recycle components, thereby preventing cells from apoptosis and increasing survivability.(64)”
BackgroundThe Role of Ceramide Metabolism and Signaling in the Regulation of Mitophagy and Cancer Therapy
Sheridan, M., & Öğretmen, B. (2021) · Cancers · doi:10.3390/cancers13102475 · Cited by 79 · see citing works
Mitochondrial Perturbations Couple mTORC2 to Autophagy in C. elegans
Aspernig, H., Heimbucher, T., Qi, W., Gangurde, D., Curic, S., Yan, Y., von Gromoff, E. D., Baumeister, R., & Thien, A. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.09.072 · Cited by 75 · see citing works
The role of autophagy in cancer: from molecular mechanism to therapeutic window
Jalali, P., Shahmoradi, A., Samii, A., Mazloomnejad, R., Hatamnejad, M. R., Saeed, A., Namdar, A., & Salehi, Z. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1528230 · Cited by 81 · see citing works
“In the cancer microenvironment, autophagy provides cellular energy and inhibits cytotoxicity under stressful conditions (34, 35).”
Autophagy in cancer cell remodeling and quality control
Hernandez, G. A., & Perera, R. M. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.03.023 · Cited by 73 · see citing works
Autophagy: a double-edged sword in ischemia–reperfusion injury
Tang, L., Zhang, W., Yan, L., Wang, W., Deng, X., Wang, C., & Shi, W. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00713-x · Cited by 75 · see citing works
Castelli, S., Ciccarone, F., Tavian, D., & Ciriolo, M. R. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-01887-w · Cited by 69 · see citing works
Autophagy and Breast Cancer: Connected in Growth, Progression, and Therapy
Wu, Q., & Sharma, D. (2023) · Cells · doi:10.3390/cells12081156 · Cited by 69 · see citing works
Lin, C., Blessing, A. M., Pulliam, T. L., Shi, Y., Wilkenfeld, S. R., Han, J. J., Murray, M. M., Pham, A. H., Duong, K., Brun, S. N., et al. (2021) · Oncogene · doi:10.1038/s41388-021-01658-z · Cited by 63 · see citing works
“Conversely, in more advanced cancers, 106 autophagy can enable cells to evade apoptosis in hypoxic and nutrient-deficient 107 environments as well as promote drug resistance(21-24).”
BackgroundRacanè, L., Ptiček, L., Fajdetić, G., Tralić‐Kulenović, V., Klobučar, M., Pavelić, S. K., Perić, M., Paljetak, H. Č., Verbanac, D., & Starčević, K. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.103537 · Cited by 65 · see citing works
Ikeda, S., Abe, F., Matsuda, Y., Kitadate, A., Takahashi, N., & Tagawa, H. (2020) · Cancer Science · doi:10.1111/cas.14614 · Cited by 62 · see citing works
Cancer cells adapt FAM134B/BiP mediated ER-phagy to survive hypoxic stress
Chipurupalli, S., Ganesan, R., Martini, G., Mele, L. L., Reggio, A., Esposito, M., Kannan, E., Namasivayam, V., Grumati, P., Desiderio, V., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04813-w · Cited by 62 · see citing works
“It is also speculated that its upregulation is HIF-1α dependent [57].”
BackgroundYang, T., Qu, X., Wang, X., Xu, D., Sheng, M., Lin, Y., Ke, M., Song, C., Xia, Q., Jiang, L., et al. (2023) · Hepatology · doi:10.1097/hep.0000000000000638 · Cited by 59 · see citing works
“As HIF-1 α stabilization and nuclear translocation are involved in autophagy induction, [36] we proposed that there might be a crosstalk between PD1 and HIF-1 α in response to fatty acid stimulation.”
Hypoxia and Extracellular Acidification as Drivers of Melanoma Progression and Drug Resistance
Dratkiewicz, E., Simiczyjew, A., Mazurkiewicz, J., Ziętek, M., Matkowski, R., & Nowak, D. (2021) · Cells · doi:10.3390/cells10040862 · Cited by 61 · see citing works
Shafabakhsh, R., Arianfar, F., Vosough, M., Mirzaei, H. R., Mahjoubin‐Tehran, M., Khanbabaei, H., Kowsari, H., Shojaie, L., Azar, M. E. F., Hamblin, M. R., et al. (2021) · Cancer Gene Therapy · doi:10.1038/s41417-020-00272-7 · Cited by 57 · see citing works
HIF-1a regulates hypoxia-induced autophagy via translocation of ANKRD37 in colon cancer
Deng, M., Zhang, W., Yuan, L., Tan, J., & Chen, Z. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112175 · Cited by 54 · see citing works
Rani, S., Roy, S., Singh, M., & Kaithwas, G. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2407223 · Cited by 56 · see citing works
“Interestingly, data revealed that the expression of BNIP3 is elevated in parallel with the transcriptional activities of HIF-1 α , whereas nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κ B) are responsible for its downregulation [90, 91].”
Signs of ROS-Associated Autophagy in Testis and Sperm in a Rat Model of Varicocele
Sadeghi, N., Erfani-Majd, N., Tavalaee, M., Tabandeh, M. R., Drevet, J. R., & Nasr‐Esfahani, M. H. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/5140383 · Cited by 52 · see citing works
“This catabolic process can be activated under various stress conditions such as oxidative stress [4], thermal stress [5, endoplasmic reticulum stress [6], hypoxia [7], and unbalanced diet [8].”
BackgroundRole of Mitofusins and Mitophagy in Life or Death Decisions
Joaquim, M., & Escobar‐Henriques, M. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.572182 · Cited by 49 · see citing works
“…and SIAH-1 (Liu et al., 2012; Fu et al., 2013; Cilenti et al., 2014; Yun et al., 2014; Tang et al., 2015; Mukherjee and Chakrabarti, 2016a,b; Szargel et al., 2016; Chen et al., 2017; Daskalaki et al., 2018; Di Rita et al., 2018; Ferrucci et al., 2018; Lampert et al., 2019; Shefa et al., 2019).”
Mitochondrial quality surveillance: mitophagy in cardiovascular health and disease
Diao, R. Y., & Gustafsson, Å. B. (2021) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00360.2021 · Cited by 49 · see citing works
Molecular Mechanism of Autophagy and Its Regulation by Cannabinoids in Cancer
Lee, X. C., Werner, E., & Falasca, M. (2021) · Cancers · doi:10.3390/cancers13061211 · Cited by 45 · see citing works
Targeting Cytoprotective Autophagy to Enhance Anticancer Therapies
Xiao, M., Benoit, A., Hasmim, M., Duhem, C., Vogin, G., Berchem, G., Noman, M. Z., & Janji, B. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.626309 · Cited by 44 · see citing works
“Other factors interacting with the autophagy process could also be considered as potential targets to inhibit autophagy and overcome therapy resistance, such as AMPK and HIF-1a, which are reported as key inducers of autophagy through negative regulation of the mTOR pathways and inducing hypoxic conditions, respectivel…”
BackgroundPhysicochemical aspects of the tumour microenvironment as drivers of vasculogenic mimicry
Andreucci, E., Peppicelli, S., Ruzzolini, J., Bianchini, F., & Calorini, L. (2022) · Cancer and Metastasis Reviews · doi:10.1007/s10555-022-10067-x · Cited by 43 · see citing works
Autophagy and cancer: Basic mechanisms and inhibitor development
Hama, Y., Ogasawara, Y., & Noda, N. N. (2023) · Cancer Science · doi:10.1111/cas.15803 · Cited by 44 · see citing works
Subhan, M. A. (2022) · RSC Advances · doi:10.1039/d2ra02005j · Cited by 42 · see citing works
Shim, S. M., Choi, H. R., Kwon, S. C., Kim, H. Y., Sung, K. W., Jung, E. J., Mun, S. R., Bae, T. H., Kim, D. H., Son, Y. S., et al. (2022) · Autophagy · doi:10.1080/15548627.2022.2126617 · Cited by 39 · see citing works
Lyu, P., Wen, J., Zhang, W., Liu, N., Stolzer, I., Gießl, A., Jia, Y., Mauro, D., Zhang, F., Ciccia, F., et al. (2024) · Annals of the Rheumatic Diseases · doi:10.1136/ard-2023-224491 · Cited by 36 · see citing works
“33 34 .”
Multitarget Pharmacology of Sulfur–Nitrogen Heterocycles: Anticancer and Antioxidant Perspectives
Drakontaeidi, A., Papanotas, I., & Pontiki, E. A. (2024) · Antioxidants · doi:10.3390/antiox13080898 · Cited by 35 · see citing works
Tao, G., Wang, X., Wang, J., Ye, Y., Zhang, M., Yan, L., & Ding, S. (2024) · British Journal of Pharmacology · doi:10.1111/bph.17373 · Cited by 35 · see citing works
“Bnip3-Bnip3L-induced mitophagy upon hypoxia additionally requires the activity of essential autophagy components such as ATG7 and the interaction with LC3B (Daskalaki et al., 2018; Park et al., 2013).”
Greville, G., Llop, E., Huang, C., Creagh-Flynn, J., Pfister, S., O’Flaherty, R., Madden, S. F., Peracaula, R., Rudd, P. M., McCann, A. H., et al. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01218 · Cited by 34 · see citing works
“Tumor cells use autophagy to support self-proliferation and metastasis; leading to poor disease prognosis (52), which indicates that hypoxia aids to these tumor features.”
BackgroundAutophagy and senescence in cancer therapy
Patel, N. H., Bloukh, S., Alwohosh, E., Alhesa, A., Saleh, T., & Gewirtz, D. A. (2021) · Advances in cancer research · doi:10.1016/bs.acr.2021.01.002 · Cited by 33 · see citing works
Autophagy and Apoptosis: Current Challenges of Treatment and Drug Resistance in Multiple Myeloma
Al‐Odat, O. S., Guirguis, D. A., Schmalbach, N. K., Yao, G., Budak-Alpdoǧan, T., Jonnalagadda, S. C., & Pandey, M. K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010644 · Cited by 33 · see citing works
Yang, H., Hu, T., Hu, P., Qi, C., & Lin, Q. (2021) · Molecular Medicine Reports · doi:10.3892/mmr.2021.11995 · Cited by 32 · see citing works
“Autophagy is a highly conserved cellular process, which is activated by various factors, such as hypoxia (38).”
The Peroxisome-Autophagy Redox Connection: A Double-Edged Sword?
Li, H., Lismont, C., Revenco, I., Hussein, M. A. F., Costa, C. F., & Fransen, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.814047 · Cited by 33 · see citing works
“However, under hypoxic conditions, these proteins are stabilized and translocated to the nucleus to initiate the transcription of genes involved in cellular adaptation and survival, including a set of genes essential for autophagy (e.g., ATG5, ATG7, ATG9A, BECN1, BNIP3, and BNI3L) (Daskalaki et al., 2018).”
BackgroundInfluentialPan, Y., Liu, Y., Wei, W., Yang, X., Wang, Z., & Xin, W. (2023) · Small · doi:10.1002/smll.202205739 · Cited by 32 · see citing works
The HIF target ATG9A is essential for epithelial barrier function and tight junction biogenesis
Dowdell, A. S., Cartwright, I. M., Goldberg, M. S., Kostelecky, R. E., Ross, T., Welch, N. M., Glover, L. E., & Colgan, S. P. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e20-05-0291 · Cited by 30 · see citing works
“…autophagy can be induced through at least three separate pathways, namely, the unfolded protein response (e.g., protein misfolding in the ER), AMPK activation as a result of energetic stress, and stabilization of HIF-α isoforms and subsequent induction of autophagy genes (Daskalaki et al., 2018).”
BackgroundInfluentialZhu, F., Wang, X., Zeng, H., Yin, Z., & Ye, Z. (2019) · Oncology Letters · doi:10.3892/ol.2019.10881 · Cited by 29 · see citing works
“Among the five previously identified ARGs associated with MM, HIF1A is the most widely studied (59,60).”
BackgroundNucleic Acid Delivery with Red-Blood-Cell-Based Carriers
Pelle, G. D., & Kostevšek, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105264 · Cited by 30 · see citing works
Autophagic-Related Proteins in Brain Gliomas: Role, Mechanisms, and Targeting Agents
Pizzimenti, C., Fiorentino, V., Franchina, M., Martini, M., Giuffrè, G., Lentini, M., Silvestris, N., Pietro, M. D., Fadda, G., Tuccari, G., et al. (2023) · Cancers · doi:10.3390/cancers15092622 · Cited by 31 · see citing works
The Autophagy Machinery Contributes to E-cadherin Turnover in Breast Cancer
Damiano, V., Spessotto, P., Vanin, G., Perin, T., Maestro, R., & Santarosa, M. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00545 · Cited by 28 · see citing works
“Mounting evidence suggests that autophagy endows tumor cells with the capability to survive anoikis, hypoxia and chemotherapy treatments (Levine and Kroemer, 2008; Levy et al., 2014; Daskalaki et al., 2018).”
BackgroundGuo, Y., Zhai, Y., Wu, L., Wang, Y., Wu, P., & Xiong, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23062927 · Cited by 28 · see citing works
Autophagy and oxidative stress in solid tumors: Mechanisms and therapeutic opportunities
Carretero-Fernández, M., Cabrera-Serrano, A. J., Sánchez‐Maldonado, J. M., Ruiz-Durán, L., Jiménez-Romera, F., García‐Verdejo, F. J., González‐Olmedo, C., Cardús, A., Díaz-Beltrán, L., Gutiérrez‐Bautista, J. F., et al. (2025) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2025.104820 · Cited by 34 · see citing works
“On the other hand, HIF-1 α , which is stabilized under oxidative stress, has been shown to activate autophagy pathways, including the AMPK/mTOR signaling axis, highlighting the crucial role of ROS in modulating autophagic activity (Daskalaki et al., 2018; J. Li et al., 2022; Zhou et al., 2018).”
Roperto, S., Falco, F. D., Perillo, A., Cătoi, C., & Roperto, F. P. (2019) · Veterinary Microbiology · doi:10.1016/j.vetmic.2019.108396 · Cited by 27 · see citing works
Zhang, S., Gong, F., Liu, J., Liu, T., Yang, J., & Hu, J. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113004 · Cited by 27 · see citing works
Host cell egress of Brucella abortus requires BNIP3L‐mediated mitophagy
Verbeke, J., Fayt, Y., Martin, L. S., Yilmaz, O., Sędzicki, J., Reboul, A., Jadot, M., Renard, P., Dehio, C., Renard, H., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2022112817 · Cited by 26 · see citing works
Zhu, X., Yang, C., Yu, Q., & Han, L. (2024) · Meat Science · doi:10.1016/j.meatsci.2024.109692 · Cited by 26 · see citing works
Beyond Self-Recycling: Cell-Specific Role of Autophagy in Atherosclerosis
Henderson, J. M., Weber, C., & Santovito, D. (2021) · Cells · doi:10.3390/cells10030625 · Cited by 27 · see citing works
HIF1α is required for NK cell metabolic adaptation during virus infection
Victorino, F., Bigley, T. M., Park, E., Yao, C.-H., Benoit, J. B., Yang, L., Piersma, S. J., Lauron, E. J., Davidson, R. M., Patti, G. J., et al. (2021) · eLife · doi:10.7554/elife.68484 · Cited by 24 · see citing works
“The 1 α KO NK cells had an increase in apoptosis as a result of decreased expression of glycolytic genes and abnormal glucose metabolism that have been previously associated with apoptosis ( Dengler et al., 2014 ; El Mjiyad et al., 2011 ; Greer et al., 2012 ; MacFarlane et al., 2012 ).”
InfluentialAutophagy and its role in regeneration and remodeling within invertebrate
Song, Q., Liu, H., Zhen, H., & Zhao, B. (2020) · Cell & Bioscience · doi:10.1186/s13578-020-00467-3 · Cited by 24 · see citing works
Chen, J., Wen, B., Wang, Y., Wu, S., Zhang, X., Gu, Y., Wang, Z., Wang, J., Zhang, W., & Yong, J. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110898 · Cited by 24 · see citing works
Jiao, B., Liu, S., Zhao, H., Zhuang, Y., Ma, S., Lin, C., Hu, J., & Liu, X. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05114-y · Cited by 24 · see citing works
“Additionally, HIF-1α and HIF-2α can transcribe independent but overlapping sets of target genes when hypoxia develops [3, 4] (Fig.”
BackgroundMechanistic Insights into Autophagy-Dependent Cell Death (ADCD): A Novel Avenue for Cancer Therapy
Rahman, M. A., Jalouli, M., Al-Zharani, M. M., Apu, E. H., & Harrath, A. H. (2025) · Cells · doi:10.3390/cells14141072 · Cited by 23 · see citing works
“In hypoxic situations, hypoxia-inducible factor 1-alpha (HIF-1 α ) stimulates autophagy to supply an alternate energy source [88].”
Friend or Foe: Paradoxical Roles of Autophagy in Gliomagenesis
Batara, D. C., Choi, M., Shin, H.-U., Kim, H., & Kim, S.-H. (2021) · Cells · doi:10.3390/cells10061411 · Cited by 24 · see citing works
“Phosphoglycerate kinase 1 (PGK1), glucose transporters 1/3 (GLUT1/3), lactate dehydrogenase (LDHA), enolase 1 (ENO1), hexokinases (HK1/2), pyruvate dehydrogenase kinase 1 (PDK1), and 6-Phosphofructokinase-2 (PFK-2) or fructose bisphosphatase-2 (FBPase-2) are all influenced by HIF-1 [86].”
BackgroundTargeting Autophagy in Thyroid Cancer: EMT, Apoptosis, and Cancer Stem Cells
Holm, T. M., Yeo, S. K., Turner, K. M., & Guan, J. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.821855 · Cited by 23 · see citing works
“…to men, the underlying molecular biology driving this mutation has not yet been elucidated and recent epidemiologic studies suggest that the observed disparity between men and women is due to overdiagnosis (Song et al., 2013; Meng et al., 2014; Daskalaki et al., 2018; Gugnoni et al., 2021).”
BackgroundThe Multifaceted Effects of Autophagy on the Tumor Microenvironment
Kang, R., Zeh, H. J., Lotze, M. T., & Tang, D. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-35727-6_7 · Cited by 22 · see citing works
Focus on the Multimodal Role of Autophagy in Rheumatoid Arthritis
Chadha, S., Behl, T., BUNGAU, S. G., Kumar, A., Kaur, R., Venkatachalam, T., Gupta, A. B., Kandhwal, M., & Chandel, D. (2020) · Inflammation · doi:10.1007/s10753-020-01324-8 · Cited by 21 · see citing works
“From various studies, the role of autophagy is observed in rheumatoid arthritis as well as systemic lupus erythematosus [33, 34].”
BackgroundLiu, R., Tang, J., Ding, C., Liang, W., Zhang, L., Chen, T., Xiong, Y., Dai, X., Li, W., Xu, Y., et al. (2017) · Cancer Letters · doi:10.1016/j.canlet.2016.12.040 · Cited by 21 · see citing works
Pizzimenti, C., Fiorentino, V., Ruggeri, C., Franchina, M., Ercoli, A., Tuccari, G., & Ieni, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212118 · Cited by 20 · see citing works
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 20 · see citing works
“Novel increasing evidence showed that the process of EMT could be promoted or inhibited by autophagy (Catalano et al., 2015; Dash et al., 2018; Daskalaki et al., 2018; Wang et al., 2019; Wu et al., 2019; Liu et al., 2020).”
BackgroundWang, N., Muhetaer, G., Zhang, X., Yang, B., Wang, C., Zhang, Y., Wang, X., Zhang, J., Wang, S., Zheng, Y., et al. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.591400 · Cited by 20 · see citing works
“With regard to hypoxic stress, Hif-1α has been extensively explored in several studies regarding hypoxia-induced autophagy during cancer metastasis (Daskalaki et al., 2018).”
BackgroundJena, B. C., Rout, L., Dey, A., & Mandal, M. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30419 · Cited by 20 · see citing works
“Moreover, TGF‐β and hypoxia reprogram the tumor cells towards self‐renewal of CSC and angiogenesis, resulting in EMT and tumor metastasis (Daskalaki et al., 2018; Hardy et al., 2017; Jiang et al., 2016).”
BackgroundFasting promotes acute hypoxic adaptation by suppressing mTOR-mediated pathways
Zhao, R., Zhao, X., Wang, X., Liu, Y., Yang, J., Jiang, S., Zhou, X., Jiao, B., Zhang, L., Liu, Y., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04351-x · Cited by 20 · see citing works
“BNIP3 is a transmembrane protein in the outer mitochondrial membrane that contains an LIR motif region on the cytoplasmic side, which can be recognized by LC3 to form autophagosomes, engulfing mitochondria [27].”
BackgroundLee, J., Lee, S.-A., Son, S., Choi, J., Nguyen, T. D., Kim, J., Son, D., & Song, C. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-01107-2 · Cited by 20 · see citing works
“In hypoxia, BNIP3 is the target gene of hypoxia-inducible factor-1-alpha (HIF1α) [28, 29]; however, it is not clear whether BNIP3 is regulated by HIF1α during Mtb infection in the absence of hypoxia.”
BackgroundResultInfluentialAutophagy Modulation by Viral Infections Influences Tumor Development
Leonardi, L., Sibéril, S., Alifano, M., Cremer, I., & Joubert, P.-E. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.743780 · Cited by 16 · see citing works
Mechanisms of HIF-driven immunosuppression in tumour microenvironment
Bandopadhyay, S., & Patranabis, S. (2023) · Journal of the Egyptian National Cancer Institute · doi:10.1186/s43046-023-00186-z · Cited by 19 · see citing works
“This autophagic degradation of cellular components is attributed to hypoxic stress response [82].”
BackgroundInfluentialSATB2 knockdown decreases hypoxia‑induced autophagy and stemness in oral squamous cell carcinoma
Dong, W., Chen, Y., Qian, N., Sima, G., Zhang, J., Guo, Z., & Wang, C. (2020) · Oncology Letters · doi:10.3892/ol.2020.11589 · Cited by 16 · see citing works
“malignancy of cancer cells during hypoxic stress that ultimately leads to poor clinical outcomes (10,11).”
BackgroundFUNDC1-mediated mitophagy in bovine papillomavirus-infected urothelial cells
Roperto, S., Russo, V., Falco, F. D., Rosati, A., Cătoi, C., & Roperto, F. P. (2019) · Veterinary Microbiology · doi:10.1016/j.vetmic.2019.05.017 · Cited by 15 · see citing works
- Authors
- Daskalaki, I., Gkikas, I., & Tavernarakis, N.
- Affiliations
- University of Crete (GR)
- Corresponding author
- Tavernarakis, Nektarios
- Venue
- Frontiers in Cell and Developmental Biology
- Publisher
- Frontiers Media SA
- Published
- 2018-09-10
- Volume
- 6
- Pages
- 104-104
- ISSN
- 2296-634X (ISSN-L)
- PMC
- PMC6139351
- OpenAlex
- W2890767393
- Cited by
- 188
- References
- 216
- Citations by year
- 2026: 17 · 2025: 20 · 2024: 21 · 2023: 19 · 2022: 31 · 2021: 39 · 2020: 22 · 2019: 15 · 2018: 3 · 2017: 1
- FWCI
- 2.82
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Frontiers in Cell and Developmental Biology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- European Commission
- H2020 European Research Council (695190, 737599)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- hypoxia, selective autophagy, cancer, hypoxia-inducible factor, unfolded protein response, mTOR, cancer metabolism, mitophagy, pexophagy, lipophagy, nucleophagy, metastasis, tumor cell survival
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
