Oxygen versus Reactive Oxygen in the Regulation of HIF-1α: The Balance Tips

Hagen, Thilo

doi:10.1155/2012/436981

Cited by 100Cancer, Hypoxia, and MetabolismRedox biology and oxidative stressErythropoietin and Anemia Treatment

Oxygen versus Reactive Oxygen in the Regulation of HIF-1α: The Balance Tips

Open access

Hagen, Thilo·2012·Biochemistry Research International

DOI 10.1155/2012/436981PMC PMC3474226

Open this paper in CoChat — free account Open PDF

Abstract

Hypoxia inducible factor (HIF) is known as the master regulator of the cellular response to hypoxia and is of pivotal importance during development as well as in human disease, particularly in cancer. It is composed of a constitutively expressed β subunit (HIF-1 β) and an oxygen-regulated α subunit (HIF-1 α and HIF-2 α), whose stability is tightly controlled by a family of oxygen- and iron-dependent prolyl hydroxylase enzymes. Whether or not mitochondria-derived reactive oxygen species (ROS) are involved in the regulation of Hypoxia Inducible Factor-1 α has been a matter of contention for the last 10 years, with equally compelling evidence in favor and against their contribution. A number of recent papers appear to tip the balance against a role for ROS. Thus, it has been demonstrated that HIF prolyl hydroxylases are unlikely to be physiological targets of ROS and that the increase in ROS that is associated with downregulation of Thioredoxin Reductase in hypoxia does not affect HIF-1 α stabilization. Finally, the protein CHCHD4, which modulates cellular HIF-1 α concentrations by promoting mitochondrial electron transport chain activity, has been proposed to exert its regulatory effect by affecting cellular oxygen availability. These reports are consistent with the hypothesis that mitochondria play a critical role in the regulation of HIF-1 α by controlling intracellular oxygen concentrations.

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

Crossref · 10.1155/2012/436981

Cites

36 of 36 references verified0 citation errors · 0 not checkable

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?

HIF regulation by ROS is graded and redox-window-dependent, explaining how HIF signaling can be engaged under mild hypoxia or near-normoxic conditions in metabolically active or oncogenically transformed cells, rather than exhibiting a binary oxygen response.
“Importantly, this regulation is graded and redox-window–dependent, explaining how HIF signaling can be engaged under mild hypoxia or even near-normoxic conditions in metabolically active or oncogenically transformed cells, rather than exhibiting a binary oxygen response [[201], [202], [203], [204]].”
From HIF inhibition: Current strategies and clinical challenges (2026) · cites this paper as [201]
Split into 2 atoms — 0 confirmed, 1 partially supported, 1 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measured
These ROS inhibit prolyl hydroxylase (PHD) activity, leading to HIF-α stabilization at oxygen levels well above anoxia.
“and that these ROS inhibit prolyl hydroxylase (PHD) activity, leading to HIF-α stabilization at oxygen levels well above anoxia.”
From HIF inhibition: Current strategies and clinical challenges (2026) · cites this paper as [201]
The Introduction describes ROS inhibition of PHD as a proposed hypothesis, then says the evidence puts that mechanism in doubt: peroxide had only minor effects on HIF-1α prolyl hydroxylation, and mitochondrial superoxide production did not correlate with HIF-1α stability. The paper therefore does not present ROS-driven PHD inhibition as the explanation for stabilization above anoxia. No page number is available in our copy. (LLM, conf=0.90)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measured
Moderate reductions in oxygen tension increase mitochondrial superoxide and hydrogen peroxide generation, particularly at respiratory complexes I and III.
“Subsequent studies revealed that moderate reductions in oxygen tension increase mitochondrial superoxide and hydrogen peroxide generation, particularly at respiratory complexes I and III”
From HIF inhibition: Current strategies and clinical challenges (2026) · cites this paper as [201]
The Introduction (page not available in our copy) describes a hypothesis that hypoxia increases superoxide production at complex III, with possible conversion to hydrogen peroxide. It also says there is no consensus on whether hypoxia increases mitochondrial ROS overall and reports decreased superoxide flashes in mild hypoxia. It does not support the claim’s categorical increase or its specific inclusion of complex I. (LLM, conf=0.87)
Experimental — accuracy not yet measured
Mitochondrial ROS production is needed for HIF-1α stabilization even without fully functional oxidative phosphorylation.
“other studies indicate that mitochondrial reactive ROS production is needed for HIF-1α stabilization, even in the absence of fully functional oxidative phosphorylation [201,376].”
From HIF inhibition: Current strategies and clinical challenges (2026) · cites this paper as [201]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O <sub>2</sub> -Regulated Prolyl Hydroxylation
Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535 · 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
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O <sub>2</sub> Sensing
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735 · see citing works
C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation
Epstein, A. C. R., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00507-4 · Cited by 3,333 · see citing works
A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation
Semenza, G. L., & Wang, G. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5447 · Cited by 2,617 · see citing works
A conserved family of prolyl-4-hydroxylases that modify HIF
Bruick, R. K., & McKnight, S. L. (2001) · Science · doi:10.1126/science.1066373 · Cited by 2,549 · see citing works
Reactive oxygen species generated at mitochondrial complex III stabilize hypoxia-inducible factor-1α during hypoxia
Chandel, N. S., McClintock, D. S., Feliciano, C. E., Wood, T. M., Melendez, J. A., Rodriguez, A. M., & Schumacker, P. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001914200 · Cited by 2,000 · see citing works
Mitochondrial reactive oxygen species trigger hypoxia-induced transcription
Chandel, N. S., Maltepe, E., Goldwasser, E., Mathieu, C. E., Simon, M. C., & Schumacker, P. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11715 · Cited by 1,926 · see citing works
Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing
Guzy, R. D., Hoyos, B., Robin, E., Chen, H., Liu, L., Mansfield, K. D., Simon, M. C., Hammerling, U., & Schumacker, P. T. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.001 · Cited by 1,545 · see citing works
The sites and topology of mitochondrial superoxide production
Brand, M. D. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.003 · Cited by 1,217 · see citing works
Selective Targeting of a Redox-active Ubiquinone to Mitochondria within Cells
Kelso, G. F., Porteous, C. M., Coulter, C. V., Hughes, G., Porteous, W. K., Ledgerwood, E. C., Smith, R. A. J., & Murphy, M. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009093200 · Cited by 1,091 · see citing works
Oxygen sensing requires mitochondrial ROS but not oxidative phosphorylation
Brunelle, J. K., Bell, E. L., Quesada, N. M., Vercauteren, K., Tiranti, V., Zeviani, M., Scarpulla, R. C., & Chandel, N. S. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.002 · Cited by 763 · see citing works
Superoxide flashes in single mitochondria
Wang, W., Fang, H., Groom, L., Cheng, A., Zhang, W., Liu, J., Wang, X., Li, K., Han, P., Zheng, M., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.017 · Cited by 715 · see citing works
Redistribution of Intracellular Oxygen in Hypoxia by Nitric Oxide: Effect on HIF1α
Hagen, T., Taylor, C. T., Lam, F., & Moncada, S. (2003) · Science · doi:10.1126/science.1088805 · Cited by 704 · see citing works
Self-citation
Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-α activation
Mansfield, K. D., Guzy, R. D., Pan, Y., Young, R. M., Cash, T. P., Schumacker, P. T., & Simon, M. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.003 · Cited by 606 · see citing works
The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production
Bell, E. L., Klimova, T. A., Eisenbart, J., Moraes, C. T., Murphy, M. P., Budinger, G. R. S., & Chandel, N. S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609074 · Cited by 568 · see citing works
Hypoxia Triggers Subcellular Compartmental Redox Signaling in Vascular Smooth Muscle Cells
Waypa, G. B., Marks, J. D., Guzy, R. D., Mungai, P. T., Schriewer, J. M., Đokić, D., & Schumacker, P. T. (2009) · Circulation Research · doi:10.1161/circresaha.109.206334 · Cited by 358 · see citing works
Multiple Factors Affecting Cellular Redox Status and Energy Metabolism Modulate Hypoxia-Inducible Factor Prolyl Hydroxylase Activity In Vivo and In Vitro
Pan, Y., Mansfield, K. D., Bertozzi, C. C., Rudenko, V., Chan, D. A., Giaccia, A. J., & Simon, M. C. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01223-06 · Cited by 332 · see citing works
Mitochondrial reactive oxygen species regulate hypoxic signaling
Hamanaka, R. B., & Chandel, N. S. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.08.005 · Cited by 332 · see citing works
Mitochondrial reactive oxygen species trigger hypoxia-inducible factor-dependent extension of the replicative life span during hypoxia
Bell, E. L., Klimova, T. A., Eisenbart, J., Schumacker, P. T., & Chandel, N. S. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02265-06 · Cited by 237 · see citing works
Stabilization of Hypoxia-inducible Factor-1α Protein in Hypoxia Occurs Independently of Mitochondrial Reactive Oxygen Species Production
Chua, Y. L., Dufour, E., Dassa, E. P., Rustin, P., Jacobs, H. T., Taylor, C. T., & Hagen, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.158485 · Cited by 189 · see citing works
Self-citation
Oxygen Sensitivity of Mitochondrial Reactive Oxygen Species Generation Depends on Metabolic Conditions
Hoffman, D. L., & Brookes, P. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809512200 · Cited by 182 · see citing works
Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: implications for hypoxic cell signaling
Hoffman, D. L., Salter, J. D., & Brookes, P. S. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00699.2006 · Cited by 167 · see citing works
The FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity
Masson, N., Singleton, R. S., Sekirnik, R., Trudgian, D. C., Ambrose, L. J. A., Miranda, M. X., Tian, Y., Kessler, B. M., Schofield, C. J., & Ratcliffe, P. J. (2012) · EMBO Reports · doi:10.1038/embor.2012.9 · Cited by 144 · see citing works
Inhibition of mitochondrial respiration elevates oxygen concentration but leaves regulation of hypoxia-inducible factor (HIF) intact
Doege, K., Heine, S., Jensen, I., Jelkmann, W., & Metzen, E. (2005) · Blood · doi:10.1182/blood-2005-03-1138 · Cited by 128 · see citing works
Human CHCHD4 mitochondrial proteins regulate cellular oxygen consumption rate and metabolism and provide a critical role in hypoxia signaling and tumor progression
Yang, J., Staples, O. D., Thomas, L. W., Briston, T., Robson, M. P., Poon, E., Simões, M. L., El‐Emir, E., Buffa, F. M., Ahmed, A., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci58780 · Cited by 95 · see citing works
Monitoring of cell oxygenation and responses to metabolic stimulation by intracellular oxygen sensing technique
Zhdanov, A. V., Ogurtsov, V. I., Taylor, C. T., & Papkovsky, D. B. (2010) · Integrative Biology · doi:10.1039/c0ib00021c · Cited by 62 · see citing works
A Disulfide Relay System in Mitochondria
Tokatlidis, K. (2005) · Cell · doi:10.1016/j.cell.2005.06.019 · Cited by 58 · see citing works
Oligomycin inhibits HIF-1α expression in hypoxic tumor cells
Gong, Y., & Agani, F. H. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00443.2004 · Cited by 54 · see citing works
3,3′-Diindolylmethane reduces levels of HIF-1α and HIF-1 activity in hypoxic cultured human cancer cells
Riby, J. E., Firestone, G. L., & Bjeldanes, L. F. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.01.017 · Cited by 52 · see citing works
Reduced mitochondrial manganese-superoxide dismutase activity exacerbates glutamate toxicity in cultured mouse cortical neurons
Li, Y., Copin, J., Reola, L., Calagui, B., Gobbel, G. T., Chen, S. F., Sato, S., Epstein, C. J., & Chan, P. H. (1998) · Brain Research · doi:10.1016/s0006-8993(98)01082-8 · Cited by 52 · see citing works
Induction of HIF-2α is dependent on mitochondrial O2 consumption in an O2-sensitive adrenomedullary chromaffin cell line
Brown, S. T., & Nurse, C. A. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00007.2008 · Cited by 49 · see citing works
Spatial Patterning of Metabolism by Mitochondria, Oxygen, and Energy Sinks in a Model Cytoplasm
Niethammer, P., Kueh, H. Y., & Mitchison, T. J. (2008) · Current Biology · doi:10.1016/j.cub.2008.03.038 · Cited by 37 · see citing works
Mitochondria: Oxygen sinks rather than sensors?
Wenger, R. H. (2005) · Medical Hypotheses · doi:10.1016/j.mehy.2005.08.047 · Cited by 36 · see citing works
HIF-Independent Regulation of Thioredoxin Reductase 1 Contributes to the High Levels of Reactive Oxygen Species Induced by Hypoxia
Naranjo‐Suarez, S., Carlson, B. A., Tsuji, P. A., Yoo, M., Gladyshev, V. N., & Hatfield, D. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030470 · Cited by 33 · see citing works
Prolonged hypoxia during cell development protects mature manganese superoxide dismutase‐deficient astrocytes from damage by oxidative stress
Copin, J., Gasche, Y. G., Li, Y., & Chan, P. H. (2001) · The FASEB Journal · doi:10.1096/fj.00-0330com · Cited by 17 · see citing works

Flagged first, then by citations

Sorted by citations

Anoikis molecular pathways and its role in cancer progression
Paoli, P., Giannoni, E., & Chiarugi, P. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.026 · Cited by 1,160 · see citing works
HIF1α and metabolic reprogramming in inflammation
Corcoran, S. E., & O'Neill, L. A. J. (2016) · Journal of Clinical Investigation · doi:10.1172/jci84431 · Cited by 789 · see citing works
Metabolic zonation of the liver: The oxygen gradient revisited
Kietzmann, T. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.012 · Cited by 499 · see citing works
Regulation of Hypoxia-Inducible Factor-1a by Reactive Oxygen Species : New Developments in an Old Debate
Movafagh, S., Crook, S., & Vo, K. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25074 · Cited by 469 · see citing works
Krebs cycle Reborn in macrophage immunometabolism
Ryan, D. G., & O'Neill, L. A. J. (2020) · Annual Review of Immunology · doi:10.1146/annurev-immunol-081619-104850 · Cited by 444 · see citing works
The ever-expanding role of HIF in tumour and stromal biology
LaGory, E. L., & Giaccia, A. J. (2016) · Nature Cell Biology · doi:10.1038/ncb3330 · Cited by 432 · see citing works
Coupling Krebs cycle metabolites to signalling in immunity and cancer
Ryan, D. G., Murphy, M. P., Frezza, C., Prag, H. A., Chouchani, E. T., O’Neill, L. A., & Mills, E. L. (2018) · Nature Metabolism · doi:10.1038/s42255-018-0014-7 · Cited by 398 · see citing works
Oxygen battle in the gut: Hypoxia and hypoxia-inducible factors in metabolic and inflammatory responses in the intestine
Singhal, R., & Shah, Y. M. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.011188 · Cited by 379 · see citing works
Reactive oxygen species, nutrition, hypoxia and diseases: Problems solved?
Görlach, A., Dimova, E. Y., Petry, A., Martı́nez-Ruiz, A., Hernansanz‐Agustín, P., Rolo, A. P., Palmeira, C. M., & Kietzmann, T. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.016 · Cited by 351 · see citing works
Hypoxia signaling pathways in cancer metabolism: the importance of co-selecting interconnected physiological pathways
Masson, N., & Ratcliffe, P. J. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-3 · Cited by 296 · see citing works
Reactive Oxygen Species Formation in the Brain at Different Oxygen Levels: The Role of Hypoxia Inducible Factors
Chen, R., Lai, U. H., Zhu, L., Singh, A., AlKataan, M. A. A., & Forsyth, N. R. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00132 · Cited by 272 · see citing works
Ultrasmall Barium Titanate Nanoparticles for Highly Efficient Hypoxic Tumor Therapy via Ultrasound Triggered Piezocatalysis and Water Splitting
Wang, P., Tang, Q., Zhang, L., Xu, M., Sun, L., Sun, S., Zhang, J., Wang, S., & Liang, X. (2021) · ACS Nano · doi:10.1021/acsnano.1c00616 · Cited by 212 · see citing works
Gd-metallofullerenol nanomaterial as non-toxic breast cancer stem cell-specific inhibitor
Liu, Y., Chen, C., Qian, P., Lu, X., Sun, B., Zhang, X., Wang, L., Gao, X., Han, L., Chen, Z., et al. (2015) · Nature Communications · doi:10.1038/ncomms6988 · Cited by 204 · see citing works
Oxidative Dimerization of PHD2 is Responsible for its Inactivation and Contributes to Metabolic Reprogramming via HIF-1α Activation
Lee, G., Won, H., Lee, Y.-M., Choi, J.-W., Oh, T.-I., Jang, J.-H., Choi, D., Lim, B. O., Kim, Y. J., Park, J., et al. (2016) · Scientific Reports · doi:10.1038/srep18928 · Cited by 158 · see citing works
Acute hypoxia produces a superoxide burst in cells
Hernansanz‐Agustín, P., Izquierdo-Álvarez, A., Sánchez-Gómez, F. J., Ramos, E. M., Villa-Piña, T., Lamas, S., Bogdanova, A. Y., & Martı́nez-Ruiz, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.011 · Cited by 137 · see citing works
Nrf2 is the key to chemotherapy resistance in MCF7 breast cancer cells under hypoxia
Syu, J.-P., Chi, J., & Kung, H. (2016) · Oncotarget · doi:10.18632/oncotarget.7406 · Cited by 133 · see citing works
Targeting Hypoxia-Inducible Factor-1 (HIF-1) in Cancer: Emerging Therapeutic Strategies and Pathway Regulation
Qannita, R. A., Alalami, A., Harb, A. A., Aleidi, S. M., Taneera, J., Abu‐Gharbieh, E., El‐Huneidi, W., Saleh, M. A., Alzoubi, K. H., Semreen, M. H., et al. (2024) · Pharmaceuticals · doi:10.3390/ph17020195 · Cited by 122 · see citing works
Cyclic Hypoxia: An Update on Its Characteristics, Methods to Measure It and Biological Implications in Cancer
Bader, S. B., Dewhirst, M. W., & Hammond, E. M. (2020) · Cancers · doi:10.3390/cancers13010023 · Cited by 120 · see citing works
Targeting the ROS-HIF-1-endothelin axis as a therapeutic approach for the treatment of obstructive sleep apnea-related cardiovascular complications
Belaïdi, E., Morand, J., Gras, E., Pépin, J., & Godin‐Ribuot, D. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.07.010 · Cited by 107 · see citing works
Hypoxia Inducible Factor-1α: The Curator of Gut Homeostasis
Kumar, T., Pandey, R., & Chauhan, N. S. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.00227 · Cited by 106 · see citing works
2-Oxoglutarate-dependent dioxygenases are sensors of energy metabolism, oxygen availability, and iron homeostasis: potential role in the regulation of aging process
Salminen, A., Kauppinen, A., & Kaarniranta, K. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1978-z · Cited by 99 · see citing works
Living on the Edge: ROS Homeostasis in Cancer Cells and Its Potential as a Therapeutic Target
Brandl, N., Seitz, R., Sendtner, N., Müller, M., & Gülow, K. (2025) · Antioxidants · doi:10.3390/antiox14081002 · Cited by 104 · see citing works
LPA Induces Metabolic Reprogramming in Ovarian Cancer via a Pseudohypoxic Response
Ha, J. H., Radhakrishnan, R., Jayaraman, M., Yan, M., Ward, J. D., Fung, K., Moxley, K. M., Sood, A. K., Isidoro, C., Mukherjee, P., et al. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-1624 · Cited by 94 · see citing works
MicroRNAs in Tumor Cell Metabolism: Roles and Therapeutic Opportunities
Pedroza‐Torres, A., Romero-Cordoba, S. L., Justo-Garrido, M., Salido-Guadarrama, I., Rodríguez‐Bautista, R., Montaño, S., Muñiz-Mendoza, R., Arriaga-Canon, C., Fragoso‐Ontiveros, V., Álvarez-Gómez, R. M., et al. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01404 · Cited by 89 · see citing works
Hypoxia-Inducible Histone Lysine Demethylases: Impact on the Aging Process and Age-Related Diseases
Salminen, A., Kai, K., & Kauppinen, A. (2016) · Aging and Disease · doi:10.14336/ad.2015.0929 · Cited by 90 · see citing works
Molecular mechanisms of hypoxia‐inducible factor‐induced pulmonary arterial smooth muscle cell alterations in pulmonary hypertension
Veith, C., SCHERMULY, R. T., Brandes, R. P., & Weißmann, N. (2015) · The Journal of Physiology · doi:10.1113/jp270689 · Cited by 75 · see citing works
Early redox activities modulate Xenopus tail regeneration
Ferreira, F., Raghunathan, V. K., Luxardi, G., Zhu, K., & Zhao, M. (2018) · Nature Communications · doi:10.1038/s41467-018-06614-2 · Cited by 78 · see citing works
Turning the gun on cancer: Utilizing lysosomal P-glycoprotein as a new strategy to overcome multi-drug resistance
Seebacher, N. A., Lane, D. J. R., Richardson, D. R., & Jansson, P. J. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.201 · Cited by 76 · see citing works
ROS-associated immune response and metabolism: a mechanistic approach with implication of various diseases
Banerjee, S., Ghosh, S., Mandal, A., Ghosh, N., & Sil, P. C. (2020) · Archives of Toxicology · doi:10.1007/s00204-020-02801-7 · Cited by 73 · see citing works
Glucose modulation induces reactive oxygen species and increases P ‐glycoprotein‐mediated multidrug resistance to chemotherapeutics
Seebacher, N. A., Richardson, D. R., & Jansson, P. J. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13079 · Cited by 65 · see citing works
The role of the tumor microenvironment in colorectal cancer and the potential therapeutic approaches
Zafari, N., Khosravi, F., Rezaee, Z., Esfandyari, S., Bahiraei, M., Bahramy, A., Ferns, G. A., & Avan, A. (2022) · Journal of Clinical Laboratory Analysis · doi:10.1002/jcla.24585 · Cited by 61 · see citing works
Genetic and cellular modifiers of oxidative stress: What can we learn from fatty acid oxidation defects?
Olsen, R. K. J., Cornelius, N., & Gregersen, N. (2013) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2013.10.007 · Cited by 58 · see citing works
Mechanism for HIF-1 activation by cholesterol under normoxia: A redox signaling pathway for liver damage
Anavi, S., Hahn-Obercyger, M., Madar, Z., & Tirosh, O. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.007 · Cited by 58 · see citing works
Adipose HIF-1α causes obesity by suppressing brown adipose tissue thermogenesis
Jun, J. C., Devera, R., Unnikrishnan, D. C., Shin, M., Bevans‐Fonti, S., Yao, Q., Rathore, A., Younas, H., Halberg, N., Scherer, P. E., et al. (2016) · Journal of Molecular Medicine · doi:10.1007/s00109-016-1480-6 · Cited by 57 · see citing works
Role of Mitochondrial Reactive Oxygen Species in the Activation of Cellular Signals, Molecules, and Function
Indo, H. P., Hawkins, C. L., Nakanishi, I., Matsumoto, K., Matsui, H., Suenaga, S., Davies, M. J., Clair, D. K. S., Ozawa, T., & Majima, H. J. (2016) · Handbook of experimental pharmacology · doi:10.1007/164_2016_117 · Cited by 57 · see citing works
Metabolic reprogramming: A novel therapeutic target in diabetic kidney disease
Wang, M., Pang, Y., Guo, Y., Tian, L., Liu, Y., Shen, C., Liu, M., Meng, Y., Cai, Z., Wang, Y., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.970601 · Cited by 46 · see citing works
The Mitochondria-Targeted Antioxidants and Remote Kidney Preconditioning Ameliorate Brain Damage through Kidney-to-Brain Cross-Talk
Silachev, D. N., Исаев, Н. К., Pevzner, I. B., Zorova, L. D., Stelmashook, E. V., Novikova, S. V., Plotnikov, E. Y., Skulachev, V. P., & Zorov, D. B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051553 · Cited by 46 · see citing works
Molecular Mechanisms of Action and Therapeutic Uses of Pharmacological Inhibitors of HIF–Prolyl 4-Hydroxylases for Treatment of Ischemic Diseases
Selvaraju, V., Parinandi, N. L., Adluri, R. S., Goldman, J. W., Hussain, N., Sánchez, J. A., & Maulik, N. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5186 · Cited by 44 · see citing works
HIF-1 signaling: an emerging mechanism for mitochondrial dynamics
Xin, Y., Zhao, L., & Peng, R. (2023) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-023-00966-0 · Cited by 43 · see citing works
Oxidative folding in the mitochondrial intermembrane space: A regulated process important for cell physiology and disease
Chatzi, A., Manganas, P., & Tokatlidis, K. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.03.023 · Cited by 42 · see citing works
Perillyl alcohol, a pleiotropic natural compound suitable for brain tumor therapy, targets free radicals
Gomes, A. C. C. A., Mello, A. L. D. N., Ribeiro, M. G. L., Garcia, D. G., da Fonseca, C. O., Salazar, M. D., Schönthal, A. H., & Quírico‐Santos, T. (2017) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-017-0459-5 · Cited by 39 · see citing works
Berberine-mediated REDD1 down-regulation ameliorates senescence of retinal pigment epithelium by interrupting the ROS-DDR positive feedback loop
Chen, Q., Xin, G., Li, S., Dong, Y., Yu, X., Wan, C., Wei, Z., Zhu, Y., Zhang, K., Wang, Y., et al. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154181 · Cited by 37 · see citing works
Prolyl hydroxylase domain enzymes and their role in cell signaling and cancer metabolism
Nguyen, T.-L., & Durán, R. V. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.09.026 · Cited by 37 · see citing works
Kv3.1 and Kv3.4, Are Involved in Cancer Cell Migration and Invasion
Song, M. S., Park, S., Park, J., Byun, J., Jin, H. K., Seo, S., Ryu, P. D., & Lee, S. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19041061 · Cited by 36 · see citing works
Dysfunction in the mitochondrial Fe-S assembly machinery leads to formation of the chemoresistant truncated VDAC1 isoform without HIF-1α activation
Ferecatu, I., Canal, F., Fabbri, L., Mazure, N. M., Bouton, C., & Golinelli‐Cohen, M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0194782 · Cited by 34 · see citing works
Need (more than) two to Tango: Multiple tools to adapt to changes in oxygen availability
Fratantonio, D., Cimino, F., Speciale, A., & Virgili, F. (2018) · BioFactors · doi:10.1002/biof.1419 · Cited by 34 · see citing works
SEURAT-1 liver gold reference compounds: a mechanism-based review
Jennings, P., Schwarz, M., Landesmann, B., Maggioni, S., Γούμενου, Μ., Bower, D., Leonard, M. O., & Wiseman, J. S. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1410-8 · Cited by 32 · see citing works
Mitochondrial metabolism regulation and epigenetics in hypoxia
Laird, M., Ku, J. C., Raiten, J., Sriram, S., Moore, M., & Li, Y. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1393232 · Cited by 26 · see citing works
Looking for the Holy Grail—Drug Candidates for Glioblastoma Multiforme Chemotherapy
Pająk, B. (2022) · Biomedicines · doi:10.3390/biomedicines10051001 · Cited by 24 · see citing works
Non-electron transfer chain mitochondrial defects differently regulate HIF-1α degradation and transcription
Shvetsova, A., Mennerich, D., Kerätär, J. M., Hiltunen, J. K., & Kietzmann, T. (2017) · Redox Biology · doi:10.1016/j.redox.2017.05.003 · Cited by 24 · see citing works
Reactive Oxygen Species Mechanisms that Regulate Protein–Protein Interactions in Cancer
Iliadis, S., & Papanikolaou, N. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25179255 · Cited by 26 · see citing works
The role of myoglobin in epithelial cancers: Insights from transcriptomics
Bicker, A., Nauth, T., Gerst, D., Aboouf, M. A., Fandrey, J., Kristiansen, G., Gorr, T. A., & Hankeln, T. (2019) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2019.4433 · Cited by 22 · see citing works
Iodine Affects Differentiation and Migration Process in Trophoblastic Cells
Olivo‐Vidal, Z. E., Rodríguez, R. C., & Arroyo-Helguera, O. E. (2015) · Biological Trace Element Research · doi:10.1007/s12011-015-0433-1 · Cited by 22 · see citing works
Molecular Fingerprint of High Fat Diet Induced Urinary Bladder Metabolic Dysfunction in a Rat Model
Oberbach, A., Jehmlich, N., Schlichting, N. S., Heinrich, M., Lehmann, S., Loeffler‐Wirth, H., Till, H., Stolzenburg, J., Völker, U., Adams, V., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066636 · Cited by 21 · see citing works
The Mechanisms of Action of Hyperbaric Oxygen in Restoring Host Homeostasis during Sepsis
Vinkel, J., Arenkiel, B., & Hyldegaard, O. (2023) · Biomolecules · doi:10.3390/biom13081228 · Cited by 20 · see citing works
TCDD Induces the Hypoxia-Inducible Factor (HIF)-1α Regulatory Pathway in Human Trophoblastic JAR Cells
Liao, T.-L., Chen, S., Tzeng, C.-R., & Kao, S. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151017733 · Cited by 20 · see citing works
Polydatin Ameliorates High Fructose-Induced Podocyte Oxidative Stress via Suppressing HIF-1α/NOX4 Pathway
Ding, H., Tang, C., Wang, W., Pan, Y., Jiao, R., & Kong, L. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14102202 · Cited by 19 · see citing works
The cytosolic 5′-nucleotidase cN-II lowers the adaptability to glucose deprivation in human breast cancer cells
Bricard, G., Cadassou, O., Cassagnes, L., Cros‐Perrial, E., Payen, L. F., Puy, J.-Y., Lefèbvre, I., Tozzi, M. G., Dumontet, C., & Jordheim, L. P. (2017) · Oncotarget · doi:10.18632/oncotarget.18653 · Cited by 19 · see citing works
The impact of high salt exposure on cardiovascular development in the early chick embryo
Wang, G., Zhang, N., Wei, Y.-F., Jin, Y.-M., Zhang, S., Cheng, X., Ma, Z., Zhao, S.-Z., Chen, Y.-P., Chuai, M., et al. (2015) · Journal of Experimental Biology · doi:10.1242/jeb.129486 · Cited by 18 · see citing works
Instability of Succinate Dehydrogenase in SDHD Polymorphism Connects Reactive Oxygen Species Production to Nuclear and Mitochondrial Genomic Mutations in Yeast
Chang, Y.-L., Hsieh, M., Chang, W., Wang, H., Lin, M., Wang, C., Lou, P., & Teng, S. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5966 · Cited by 17 · see citing works
Dimethyloxalylglycine (DMOG), a Hypoxia Mimetic Agent, Does Not Replicate a Rat Pheochromocytoma (PC12) Cell Biological Response to Reduced Oxygen Culture
Chen, R., AlKataan, M. A. A., & Forsyth, N. R. (2022) · Biomolecules · doi:10.3390/biom12040541 · Cited by 18 · see citing works
Characterization of H2O2-Induced Alterations in Global Transcription of mRNA and lncRNA
Liu, S., Qiu, Y., Xiang, R., & Huang, P. (2022) · Antioxidants · doi:10.3390/antiox11030495 · Cited by 15 · see citing works
Protein trafficking in the mitochondrial intermembrane space: mechanisms and links to human disease
MacPherson, L., & Tokatlidis, K. (2017) · Biochemical Journal · doi:10.1042/bcj20160627 · Cited by 15 · see citing works
Hematopoietic Stem/Progenitor Cells Express Myoglobin and Neuroglobin: Adaptation to Hypoxia or Prevention from Oxidative Stress?
D’Aprile, A., Scrima, R., Quarato, G., Tataranni, T., Falzetti, F., Ianni, M. D., Gemei, M., Vecchio, L. D., Piccoli, C., & Capitanio, N. (2014) · Stem Cells · doi:10.1002/stem.1646 · Cited by 14 · see citing works
Development of LC–MS method for analysis of paclitaxel-inhibited growth and enhanced therapeutic response in human glioblastoma cells
Lin, C., Lin, X., Lin, L., Wang, J.-M., Lin, Z.-X., & Lin, J.-M. (2015) · Chinese Chemical Letters · doi:10.1016/j.cclet.2015.03.007 · Cited by 13 · see citing works
Imidazole‐based alkaloid derivative LCB 54‐0009 suppresses ocular angiogenesis and lymphangiogenesis in models of experimental retinopathy and corneal neovascularization
Kim, B., Lee, J., Choi, J., Park, D. Y., Song, H. Y., Park, T. K., Cho, C., Ye, S., Joo, C., Koh, G. Y., et al. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13177 · Cited by 13 · see citing works
Mechanisms of sensing and adaptive responses to low oxygen conditions in mammals and yeasts
Trendeleva, T. A., Aliverdieva, D. A., & Zvyagilskaya, R. A. (2014) · Biochemistry (Moscow) · doi:10.1134/s0006297914080033 · Cited by 13 · see citing works
Role of ROS/Kv/HIF Axis in the Development of Hypoxia-Induced Pulmonary Hypertension
Wen, W., Li, Y., & Dunquan, X. (2017) · Chinese Medical Sciences Journal · doi:10.24920/j1001-9294.2017.037 · Cited by 12 · see citing works
A redox-sensitive signaling pathway mediates pro-angiogenic effect of chlordecone via estrogen receptor activation
Alibrahim, E. A., Andriantsitohaina, R., Hardonnière, K., Soleti, R., Faure, S., & Simard, G. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2018.02.008 · Cited by 12 · see citing works
Hypoxia potentiates the cytotoxic effect of piperlongumine in pheochromocytoma models
Bullova, P., Cougnoux, A., Abunimer, L., Kopáček, J., Pastoreková, S., & Pacák, K. (2016) · Oncotarget · doi:10.18632/oncotarget.9643 · Cited by 12 · see citing works
Prenatal hypoxia increases susceptibility to kidney injury
Cargill, K. R., Chiba, T., Murali, A., Mukherjee, E., Crinzi, E. A., & Sims‐Lucas, S. (2020) · PLoS ONE · doi:10.1371/journal.pone.0229618 · Cited by 10 · see citing works
Traditional Chinese medicine Youguiyin decoction ameliorate glucocorticoid-induced osteonecrosis in rat by modulating ROS/PHD2/HIF-1α oxidative stress signaling pathway in bone marrow mesenchymal stem cells
Xi, H., Chen, H., Fu, J., He, S., Liu, X., Sun, G.-Q., & Du, B. (2025) · Chinese Medicine · doi:10.1186/s13020-025-01113-1 · Cited by 8 · see citing works
Neutrophil-Derived Myeloperoxidase and Hypochlorous Acid Critically Contribute to 20-Hydroxyeicosatetraenoic Acid Increases that Drive Postischemic Angiogenesis
Azcona, J. A., Tang, S., Berry, E., Zhang, F. F., Garvey, R., Falck, J. R., Schwartzman, M. L., Yi, T., Jeitner, T. M., & Guo, A. M. (2022) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.121.001036 · Cited by 8 · see citing works
Aerobic Exercise Improves Radiation Therapy Efficacy in Non-Small Cell Lung Cancer: Preclinical Study Using a Xenograft Mouse Model
Jo, S., Jeon, J., Park, G., Do, H.-K., Kang, J., Ahn, K. J., Ma, S. Y., Choi, Y. M., Kim, D. H., Youn, B., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052757 · Cited by 7 · see citing works
Metabolic interaction of hydrogen peroxide and hypoxia in zebrafish fibroblasts
Dikova, V., Vorhauser, J., Geng, A., Pelster, B., & Sandbichler, A. M. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.11.015 · Cited by 7 · see citing works
ROS and Oxidative Stress in Cancer: Recent Advances
Varol, M. (2020) · Springer eBooks · doi:10.1007/978-981-15-7586-0_6 · Cited by 6 · see citing works
Synthesis of a near infrared-actuated phthalocyanine-lipid vesicle system for augmented photodynamic therapy
Nwahara, N., Managa, M., Stoffels, M., Britton, J. E., Prinsloo, E., & Nyokong, T. (2021) · Synthetic Metals · doi:10.1016/j.synthmet.2021.116811 · Cited by 6 · see citing works
Hypoxia-Mediated Upregulation of Xanthine Oxidoreductase Causes DNA Damage of Colonic Epithelial Cells in Colitis
Li, H., Li, X., Wang, Y., Han, W., Li, H., & Zhang, Q. (2024) · Inflammation · doi:10.1007/s10753-024-01966-y · Cited by 6 · see citing works
The Efficacy of Radiation is Enhanced by Metformin and Hyperthermia Alone or Combined Against FSaII Fibrosarcoma in C3H Mice
Kim, H.-K., Kim, D., Kim, W., Kim, E., Jang, W. I., & Kim, M. (2022) · Radiation Research · doi:10.1667/rade-21-00231.1 · Cited by 5 · see citing works
The DUX4–HIF1α Axis in Murine and Human Muscle Cells: A Link More Complex Than Expected
Nguyen, T.-H., Limpens, M., Bouhmidi, S., Paprzycki, L., Legrand, A., Declèves, A., Heher, P., Belayew, A., Banerji, C. R. S., Zammit, P. S., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25063327 · Cited by 5 · see citing works
Stress Response Pathways
Leonard, M. O., Limonciel, A., & Jennings, P. (2014) · Methods in pharmacology and toxicology · doi:10.1007/978-1-4939-0521-8_19 · Cited by 4 · see citing works
Regulatory effect of immunosuppressive agents in mice with renal ischemia reperfusion injury
Zhang, W. Y., Zhao, J., Cao, F., & Li, S. (2018) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2018.6642 · Cited by 4 · see citing works
Oxygen and Aging
Pitt, J. N., Leiser, S. F., & Kaeberlein, M. R. (2014) · Annual Review of Gerontology and Geriatrics · doi:10.1891/0198-8794.34.59 · Cited by 4 · see citing works
To decipher the hypoxic pulmonary hypertension: Vascular heterogeneity and the hypothesis of hypoxic responsive threshold
Ma, H., Xu, D.-Q., Wu, Y., Ma, Y., & Li, Z. (2015) · Journal of Medical Hypotheses and Ideas · doi:10.1016/j.jmhi.2015.01.002 · Cited by 3 · see citing works
Chemo-sensitizing agents from natural origin for colorectal cancer: Pharmacodynamic and cellular pharmacokinetics approaches
Allam, R. M., Halawany, A. M. E., & Al-Abd, A. M. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819937-4.00006-6 · Cited by 3 · see citing works
HIF inhibition: Current strategies and clinical challenges
Więch-Walów, A., Bartoszewska, S., Barton, A., Czechowicz, P., Dudzik, J., Wielockx, B., Collawn, J. F., & Bartoszewski, R. (2026) · Redox biology · doi:10.1016/j.redox.2026.104220 · Cited by 3 · see citing works
“Importantly, this regulation is graded and redox-window – dependent, explaining how HIF signaling can be engaged under mild hypoxia or even near-normoxic conditions in metabolically active or oncogenically transformed cells, rather than exhibiting a binary oxygen response [201 – 204].”
A paradigm shift from penetration: Material-based solutions for multidimensional spatiotemporal, hypoxic, and optical challenges in cutaneous photodynamic therapy
Feng, X., Fan, H., Zhou, L., Zhao, Z., Mu, Y., Sun, X., & Chen, Y. (2026) · Materials Today Bio · doi:10.1016/j.mtbio.2026.102872 · Cited by 2 · see citing works
Reactive Oxygen Species and Metabolic Re-Wiring in Acute Leukemias
Robinson, A. J., Darley, R. L., & Tonks, A. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.94829 · Cited by 2 · see citing works
Hypoxia-inducible factor HIF-1α modulates drugs resistance in colon cancer cells
Pinzón‐Daza, M. L., Cuellar, Y., Ondo-Méndez, A., Matheus, L. M., Prendes, L. D. R., Castillo, F., & Garzón, R. (2018) · Revista de la Facultad de Medicina · doi:10.15446/revfacmed.v66n4.55149 · Cited by 2 · see citing works
Hypoxia and the Hypoxia-Inducible Factors in Lymphocyte Differentiation and Function
Boothby, M. R., & Cho, S. H. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-62731-6_6 · Cited by 1 · see citing works
ROS-Fueled Allies: STAT3, PKM2, and HIF-1α Influencing Energy Metabolism in Hormone-Independent Cancers
Fiorini, S., Maras, B., Mignogna, G., Perugini, M., Retali, F., Meschiari, G., Macone, A., Botta, S., Fabio Altieri, F., Eufemi, M., et al. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27052357 · Cited by 1 · see citing works
The Hypoxic Response and Aging
Leiser, S. F., Miller, H. A., & Kaeberlein, M. R. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-411596-5.00004-6
Hypoxia-inducible factor-1: A new neuroprotective agent for the treatment of hyperglycemia after stroke
Hernández, M. I., Zugaza, J. L., & Martín, A. (2026) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00794
Genomic alterations and their correlation with metabolic-related genes in lung cancer
Gaur, G., Jha, N. K., Gambhir, L., Acharya, S. V., & Kumar, D. (2026) · Clinical & Translational Oncology · doi:10.1007/s12094-026-04229-4
Role of VDAC1 hypoxic form, VDAC1-∆C, in the expression of primary cilia and tumor progression
Fabbri, L. (2019) · theses.fr (ABES) · doi:10.70675/7a53239dzc652z4ea4z8b95z4a71961c83b4
Impact of oxygen and glucose differential availability on human neutrophil viability, metabolism and activation
Injarabian, L. (2020) · theses.fr (ABES) · doi:10.70675/d505f876z0405z4419zbe01z07bf7a8dc156
Etude de la physiopathologie des formes héritables d'hypertension artérielle pulmonaire
Manaud, G. (2020) · doi:10.70675/5da7bf4azaee0z4784z81a0z9548d94727d0
Non-canonical activation of VEGFA through TIMM44-dependent mitochondrial remodelling
Chaudhary, T., Bhat, S. M., Pradhan, P., Joshi, M. B., & Sinha, D. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104381
MAVS undergoes aggregation under hypoxia to enhance the hypoxia signaling pathway by promoting the generation of mitochondrial ROS
Sun, X., Zhu, C., Liu, W., Wang, Z., Deng, H., Jia, S., Shi, S., Xiang, Y., Luo, Y., Gui, J., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2612849123
Exercise, DNA methylation, and Alzheimer’s disease: Mechanistic links and future directions in intergenerational research
Said, G., da Silva, A. S. R., & Rodrigues, G. D. S. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103415

Stabilization of Hypoxia-inducible Factor-1α Protein in Hypoxia Occurs Independently of Mitochondrial Reactive Oxygen Species Production
Chua, Y. L., Dufour, E., Dassa, E. P., Rustin, P., Jacobs, H. T., Taylor, C. T., & Hagen, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.158485 · Cited by 189 · see citing works
Self-citation
Mitochondrial oxygen sensing: regulation of hypoxia-inducible factor by mitochondrial generated reactive oxygen species
Bell, E. L., & Chandel, N. S. (2007) · Essays in Biochemistry · doi:10.1042/bse0430017 · Cited by 90 · see citing works
A targeted antioxidant reveals the importance of mitochondrial reactive oxygen species in the hypoxic signaling of HIF‐1α
Sanjuán-Pla, A., Cervera, A. M., Apostolova, N., Garcia-Bou, R., Víctor, V. M., Murphy, M. P., & McCreath, K. J. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.088 · Cited by 134 · see citing works
Oxidants are dispensable for HIF1α stability in hypoxiaPreprint
Kumar, A., Vaish, M., Karuppagounder, S. S., Gazaryan, I. G., Cave, J. W., Starkov, A. A., Anderson, E. T., Zhang, S., Pinto, J. T., Rountree, A. M., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.05.079681
Regulation of hypoxia-inducible factor is preserved in the absence of a functioning mitochondrial respiratory chain
Vaux, E. C., Metzen, E., Yeates, K. M., & Ratcliffe, P. J. (2001) · Blood · doi:10.1182/blood.v98.2.296 · Cited by 198 · see citing works

Authors: Hagen, T.
Affiliations: National University of Singapore (SG)
Corresponding author: Hagen, Thilo
ORCID: Hagen, Thilo
Venue: Biochemistry Research International
Publisher: Wiley
Published: 2012
Volume: 2012
Pages: 1-5
ISSN: 2090-2247 (ISSN-L)
2090-2255
DOI: 10.1155/2012/436981
PMC: PMC3474226
OpenAlex: W1967013639
Cited by: 100
References: 36
Citations by year: 2026: 8 · 2025: 2 · 2024: 7 · 2023: 2 · 2022: 9 · 2021: 3 · 2020: 10 · 2019: 4 · 2018: 10 · 2017: 6 · 2016: 12 · 2015: 11 · 2014: 11 · 2013: 4 · 2012: 1
FWCI: 2.87
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/3.0/ (unspecified)
Locations: Biochemistry Research International (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
National University of Singapore (submittedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
Keywords: hypoxia-inducible factor-1α, reactive oxygen species, mitochondrial reactive oxygen species, prolyl hydroxylase, HIF-1α stabilization, hypoxia, thioredoxin reductase, CHCHD4, mitochondrial electron transport chain, HIF-2α

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

Oxygen versus Reactive Oxygen in the Regulation of HIF-1α: The Balance Tips

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks