Hypoxia-inducible factors in physiology and medicine
Open accessAbstract
Oxygen homeostasis represents an organizing principle for understanding metazoan evolution, development, physiology, and pathobiology. The hypoxia-inducible factors (HIFs) are transcriptional activators that function as master regulators of oxygen homeostasis in all metazoan species. Rapid progress is being made in elucidating homeostatic roles of HIFs in many physiological systems, determining pathological consequences of HIF dysregulation in chronic diseases, and investigating potential targeting of HIFs for therapeutic purposes.
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Deoxygenation can activate the hypoxia-inducible factor (HIF) transcription system, which triggers the expression of most genes responsible for cellular adaptation to varying O2 levels.
“deoxygenation can also activate the hypoxia-inducible factor (HIF) transcription system, which triggers the expression of most genes responsible for cellular adaptation to varying O2 levels (Semenza et al., 1991; Wang et al., 1995; Semenza, 2012).”
From Toward Best Practices for Controlling Mammalian Cell Culture Environments (2022) · cites this paper as Semenza, 2012
The Hypoxia-Inducible Factors section (page not specified) reports that HIF-1 levels rise as oxygen falls and that hundreds of genes show HIF-1-dependent responses to hypoxia. The Introduction calls HIFs master regulators of oxygen homeostasis, but the copy does not establish that they trigger expression of most genes responsible for cellular adaptation. (LLM, conf=0.86)
Experimental — accuracy not yet measuredPathological HIF activation contributes to diverse conditions characterized by chronic hypoxia, oxidative stress, and inflammation.
“Beyond cancer and metabolic disease, pathological HIF activation contributes to diverse conditions characterized by chronic hypoxia, oxidative stress, and inflammation [256].”
From HIF inhibition: Current strategies and clinical challenges (2026) · cites this paper as [256]
Oxygen-dependent regulation of HIF-1α stabilization involves hypoxic inhibition of PHD activity, leading to impaired post-translational HIF1α hydroxylation at P402 and P564 in the ODD domain.
“The oxygen-dependent regulation of HIF-1 a (HIF1 a ) stabilization involves hypoxic inhibition of prolyl hydroxylase domain enzyme (PHD) activity, leading to impaired post-translational HIF1 a hydroxylation at proline 402 (P402) and proline 564 (P564) in the oxygen-dependent degradation (ODD) domain.”
From Ferritin-Mediated Iron Sequestration Stabilizes Hypoxia-Inducible Factor-1α upon LPS Activation in the Presence of Ample Oxygen (2015) · cites this paper as Semenza, 2012
Hypoxic inhibition of PHD diminishes VHL-dependent HIF1α ubiquitination and proteasomal degradation.
“This diminishes VHL (von Hippel-Lindau tumor suppressor)-dependent HIF1 a ubiquitination and proteasomal degradation (reviewed in Kaelin and Ratcliffe, 2008; Semenza, 2012).”
From Ferritin-Mediated Iron Sequestration Stabilizes Hypoxia-Inducible Factor-1α upon LPS Activation in the Presence of Ample Oxygen (2015) · cites this paper as Semenza, 2012
When O2 availability is low, HIF-1α protein is stabilized because of reduced PHD activity, resulting in increased HIF-1α-dependent transcription.
“When O2 availability is low, HIF-1α protein is stabilized because of reduced PHD activity, resulting in increased HIF-1α-dependent transcription (97).”
From Fueling Immunity: Insights into Metabolism and Lymphocyte Function (2013) · cites this paper as [97]
HIF-1 and HIF-2 coordinate the adaptive cellular response to low oxygen tensions by activating gene expression programs controlling glucose uptake, metabolism, angiogenesis, erythropoiesis, cell proliferation, differentiation, and apoptosis.
“The hypoxia-inducible transcription factors HIF-1 and HIF-2 coordinate the adaptive cellular response to low oxygen tensions by activating gene expression programs controlling glucose uptake, metabolism, angiogenesis, erythropoiesis, cell proliferation, differentiation, and apoptosis”
From Hypoxic control of metastasis (2016) · cites this paper as [1]
Cells respond to reduced O2 availability through changes in gene expression mediated by hypoxia-inducible factors composed of an O2-regulated HIF-α subunit and a constitutively expressed HIF-1β subunit.
“Cells respond to reduced O2 availability through changes in gene expression that are mediated by hypoxia-inducible factors, which are composed of an O2-regulated HIF-α subunit (HIF-1α, HIF-2α, or HIF-3α) and a constitutively expressed HIF-1β subunit [10, 11].”
From The hypoxic tumor microenvironment: A driving force for breast cancer progression (2016) · cites this paper as [11]
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“HIFs activate transcription of genes that play key roles in critical aspects of cancer biology, including stem cell maintenance (Wang et al., 2011), cell immortalization, epithelial-mesenchymal transition (Mak et al., 2010), genetic instability (Huang et al., 2007), vascularization (Liao and…”
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Self-citationProteasomal Regulation of the Hypoxic Response Modulates Aging in C. elegans
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Mutation of von Hippel–Lindau Tumour Suppressor and Human Cardiopulmonary Physiology
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Regulation of human metabolism by hypoxia-inducible factor
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Liu, L., Marti, G. P., Wei, X., Zhang, X., Zhang, H., Liu, Y. V., Nastai, M., Semenza, G. L., & Harmon, J. W. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21503 · Cited by 162 · see citing works
Self-citationLiu, Y. V., Hubbi, M. E., Pan, F., McDonald, K. R., Mansharamani, M., Cole, R. N., Liu, J. O., & Semenza, G. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705015200 · Cited by 146 · see citing works
Self-citationBernhardt, W. M., Göttmann, U., Doyon, F., Buchholz, B., Câmpean, V., Schödel, J., Reisenbuechler, A., Klaus, S. J., Arend, M., Flippin, L. A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903978106 · Cited by 145 · see citing works
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Hypoxia-induced genetic instability—a calculated mechanism underlying tumor progression
Huang, E. L., Bindra, R. S., Glazer, P. M., & Harris, A. L. (2006) · Journal of Molecular Medicine · doi:10.1007/s00109-006-0133-6 · Cited by 143 · see citing works
Adenoviral transfer of HIF-1α enhances vascular responses to critical limb ischemia in diabetic mice
Sarkar, K., Fox-Talbot, K., Steenbergen, C., Bosch‐Marcé, M., & Semenza, G. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910561106 · Cited by 140 · see citing works
Self-citationHIF-1 mediates pathogenic inflammatory responses to intestinal ischemia-reperfusion injury
Feinman, R., Deitch, E. A., Watkins, A. C., Abungu, B., Colorado, I., Kannan, K. B., Sheth, S. U., Caputo, F. J., Lu, Q., Ramanathan, M., et al. (2010) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00065.2010 · Cited by 136 · see citing works
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Self-citationRey, S., Lee, K., Wang, C. J., Gupta, K., Chen, S., McMillan, A., Bhise, N. S., Levchenko, A., & Semenza, G. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911921106 · Cited by 120 · see citing works
Self-citationDigoxin inhibits retinal ischemia‐induced HIF‐1α expression and ocular neovascularization
Yoshida, T., Zhang, H., Iwase, T., Shen, J., Semenza, G. L., & Campochiaro, P. A. (2010) · The FASEB Journal · doi:10.1096/fj.09-145664 · Cited by 113 · see citing works
Self-citationJiang, X., Khan, M. A., Tian, W., Beilke, J. N., Natarajan, R., Kosek, J. C., Yöder, M. C., Semenza, G. L., & Nicolls, M. R. (2011) · Journal of Clinical Investigation · doi:10.1172/jci46192 · Cited by 104 · see citing works
Self-citationHypoxia-dependent anti-inflammatory pathways in protection of cancerous tissues
Lukashev, D. E., Ohta, A., & Sitkovsky, M. V. (2007) · Cancer and Metastasis Reviews · doi:10.1007/s10555-007-9054-2 · Cited by 103 · see citing works
Hirota, S. A., Fines, K., Ng, J., Traboulsi, D., Lee, J., Ihara, E., Li, Y., Willmore, W. G., Chung, D. C., Scully, M. M., et al. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.03.045 · Cited by 100 · see citing works
Opposing roles for HIF-1α and HIF-2α in the regulation of angiogenesis by mononuclear phagocytes
Eubank, T. D., Roda, J. M., Liu, H., O'Neil, T., & Marsh, C. B. (2010) · Blood · doi:10.1182/blood-2010-01-261792 · Cited by 94 · see citing works
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Inhibition of Prolyl Hydroxylase Domain Proteins Promotes Therapeutic Revascularization
Loinard, C., Ginouvès, A., Vilar, J., Cochain, C., Zouggari, Y., Récalde, A., Duriez, M., Levy, B. I., Pouysségur, J., Berra, E., et al. (2009) · Circulation · doi:10.1161/circulationaha.108.813303 · Cited by 82 · see citing works
Zhang, X., Liu, L., Wei, X., Tan, Y. S., Tong, L. X., Ryan Chang, B., Ghanamah, M., Reinblatt, M., Marti, G. P., Harmon, J. W., et al. (2010) · Wound Repair and Regeneration · doi:10.1111/j.1524-475x.2010.00570.x · Cited by 73 · see citing works
Self-citationRey, S., Luo, W., Shimoda, L. A., & Semenza, G. L. (2011) · Blood · doi:10.1182/blood-2010-11-321190 · Cited by 68 · see citing works
Self-citationHypoxia. 5. Hypoxia and hematopoiesis
Yoon, D., Ponka, P., & Prchal, J. T. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00044.2011 · Cited by 61 · see citing works
Aging impairs the mobilization and homing of bone marrow-derived angiogenic cells to burn wounds
Zhang, X., Sarkar, K., Rey, S., Sebastian, R., Andrikopoulou, E., Marti, G. P., Fox-Talbot, K., Semenza, G. L., & Harmon, J. W. (2011) · Journal of Molecular Medicine · doi:10.1007/s00109-011-0754-2 · Cited by 57 · see citing works
Self-citationThe synergism of age and db/db genotype impairs wound healing☆
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Self-citationChronic lung allograft rejection and airway microvasculature: Is HIF-1 the missing link?
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ROS function in redox signaling and oxidative stress
Schieber, M., & Chandel, N. S. (2014) · Current Biology · doi:10.1016/j.cub.2014.03.034 · Cited by 6,931 · see citing works
Fundamentals of Cancer Metabolism
DeBerardinis, R. J., & Chandel, N. S. (2016) · Science Advances · doi:10.1126/sciadv.1600200 · Cited by 3,013 · see citing works
Mitochondrial TCA cycle metabolites control physiology and disease
Martínez-Reyes, I., & Chandel, N. S. (2020) · Nature Communications · doi:10.1038/s41467-019-13668-3 · Cited by 2,813 · see citing works
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From Krebs to clinic: glutamine metabolism to cancer therapy
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Hypoxic microenvironment in cancer: molecular mechanisms and therapeutic interventions
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Fueling Immunity: Insights into Metabolism and Lymphocyte Function
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Cellular Adaptation to Hypoxia through Hypoxia Inducible Factors and beyond
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Metformin inhibits mitochondrial complex I of cancer cells to reduce tumorigenesis
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The role of HIF in immunity and inflammation
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Hypoxia and Metabolic Adaptation of Cancer Cells
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Regulation of Immunity and Inflammation by Hypoxia in Immunological Niches
Taylor, C. T., & Colgan, S. P. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2017.103 · Cited by 713 · see citing works
Conquering the Hypoxia Limitation for Photodynamic Therapy
Wan, Y., Fu, L., Li, C., Lin, J., & Huang, P. (2021) · Advanced Materials · doi:10.1002/adma.202103978 · Cited by 705 · see citing works
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“Moreover, under low oxygen condition, the transcription of glycolytic genes is upregu- lated by hypoxia-inducible factor (HIF), and increased glycolytic ATP produced by enhanced glyco- lytic flux can partially supply cellular energy demands (Iyer et al., 1998; Seagroves et al., 2001; Semenza, 2012).”
BackgroundThe Two Faces of Reactive Oxygen Species in Cancer
Reczek, C. R., & Chandel, N. S. (2017) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-041916-065808 · Cited by 602 · see citing works
“However, during hypoxia, the HIF-α protein is allowed to dimerize with the HIF-β subunit and translocate to the nucleus to induce expression of proangiogenic genes, such as vascular endothelial growth factor and genes involved in cell survival, glycolysis, and metastasis (Semenza 2003, 2012).”
BackgroundWhat a difference a hydroxyl makes: mutant IDH, (<i>R</i>)-2-hydroxyglutarate, and cancer
Losman, J.-A., & Kaelin, W. G. (2013) · Genes & Development · doi:10.1101/gad.217406.113 · Cited by 570 · see citing works
An HIF-1α/VEGF-A Axis in Cytotoxic T Cells Regulates Tumor Progression
Palazon, A., Tyrakis, P. A., Macias, D., Veliça, P., Rundqvist, H., Fitzpatrick, S., Vojnovic, N., Phan, A. T., Loman, N., Hedenfalk, I., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.10.003 · Cited by 521 · see citing works
“…will activate the HIF pathway, which is thought to become highly active at levels corresponding to less than 5% oxygen in tissue culture systems (Semenza, 2012); we found by oxygen electrode measurements that murine spleens have a mean pO2 of approximately 22 mmHg, which would approximate a…”
BackgroundInfluentialThe hypoxic tumor microenvironment: A driving force for breast cancer progression
Semenza, G. L. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.05.036 · Cited by 535 · see citing works
Self-citationSimcox, J. A., & McClain, D. A. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.02.007 · Cited by 545 · see citing works
Mitohormesis: Promoting Health and Lifespan by Increased Levels of Reactive Oxygen Species (ROS)
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Pathogenesis of alcoholic liver disease: Role of oxidative metabolism
Ceni, E., Mello, T., & Galli, A. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i47.17756 · Cited by 521 · see citing works
The effect of HIF on metabolism and immunity
Taylor, C. T., & Scholz, C. C. (2022) · Nature Reviews Nephrology · doi:10.1038/s41581-022-00587-8 · Cited by 517 · 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
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Oligodendrocyte-Encoded HIF Function Couples Postnatal Myelination and White Matter Angiogenesis
Yuen, T. J., Silbereis, J. C., Griveau, A., Chang, S. M., Daneman, R., Fancy, S. P. J., Zahed, H., Maltepe, E., & Rowitch, D. H. (2014) · Cell · doi:10.1016/j.cell.2014.04.052 · Cited by 433 · see citing works
Phototherapy in cancer treatment: strategies and challenges
Cai, Y., Chai, T., Nguyen, W., Liu, J., Xiao, E., Ran, X., Ran, Y., Du, D., Chen, W., & Chen, X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02140-y · Cited by 453 · see citing works
Macrophages and Iron Metabolism
Soares, M. P., & Hamza, I. (2016) · Immunity · doi:10.1016/j.immuni.2016.02.016 · Cited by 401 · see citing works
Mitochondrial ROS regulation of proliferating cells
Diebold, L., & Chandel, N. S. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.198 · Cited by 391 · see citing works
Oldham, W. M., Clish, C. B., Yang, Y., & Loscalzo, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.06.021 · Cited by 364 · see citing works
“This programmed response is mediated primarily through stabilization of hypoxia-inducible factor 1a (HIF1a), a transcription factor that coordinates a shift in energy metabolism away from oxidative phosphorylation and toward glycolysis and lactate fermentation through the increased expression of glucose transporters (…”
Structural integration in hypoxia-inducible factors
Wu, D., Potluri, N., Lu, J., Kim, Y., & Rastinejad, F. (2015) · Nature · doi:10.1038/nature14883 · Cited by 346 · see citing works
Hypoxia-inducible factors and the regulation of lipid metabolism
Mylonis, I., Simos, G., & Paraskeva, E. (2019) · Cells · doi:10.3390/cells8030214 · Cited by 316 · see citing works
The Proto-oncometabolite Fumarate Binds Glutathione to Amplify ROS-Dependent Signaling
Sullivan, L. B., Martinez-Garcia, E., Nguyen, H., Mullen, A. R., Dufour, E., Sudarshan, S., Licht, J. D., Deberardinis, R. J., & Chandel, N. S. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.05.003 · Cited by 304 · see citing works
Mechanisms of hypoxia signalling: new implications for nephrology
Schödel, J., & Ratcliffe, P. J. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0182-z · Cited by 309 · see citing works
The role of osteoblasts in energy homeostasis
Dirckx, N., Moorer, M. C., Clemens, T. L., & Riddle, R. C. (2019) · Nature Reviews Endocrinology · doi:10.1038/s41574-019-0246-y · Cited by 292 · see citing works
Pharmacologic Targeting of Hypoxia-Inducible Factors
Semenza, G. L. (2019) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010818-021637 · Cited by 288 · see citing works
Self-citationThe EGLN-HIF O 2 -Sensing System: Multiple Inputs and Feedbacks
Ivan, M., & Kaelin, W. G. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.002 · Cited by 273 · see citing works
Bersten, D. C., Sullivan, A. E., Peet, D. J., & Whitelaw, M. L. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3621 · Cited by 267 · see citing works
Role of hypoxia-inducible factors in breast cancer metastasis
Gilkes, D. M., & Semenza, G. L. (2013) · Future Oncology · doi:10.2217/fon.13.92 · Cited by 274 · see citing works
Self-citationHypoxia-inducible factor 3 biology: complexities and emerging themes
Duan, C. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00315.2015 · Cited by 269 · see citing works
Direct regulation of GAS6/AXL signaling by HIF promotes renal metastasis through SRC and MET
Rankin, E. B., Fuh, K. C., Castellini, L., Viswanathan, K., Finger, E. C., Diep, A. N., LaGory, E. L., Kariolis, M. S., Chan, A., Lindgren, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1404848111 · Cited by 269 · see citing works
Hypoxia regulates Hippo signalling through the SIAH2 ubiquitin E3 ligase
Ma, B., Chen, Y., Chen, L., Cheng, H., Mu, C., Li, J., Gao, R., Zhou, C., Cao, L., Liu, J., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3073 · Cited by 266 · see citing works
Luo, W., Chang, R., Zhong, J., Pandey, A., & Semenza, G. L. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217394109 · Cited by 228 · see citing works
Self-citationHIF-2α activation potentiates oxidative cell death in colorectal cancers by increasing cellular iron
Singhal, R., Mitta, S. R., Das, N. K., Kerk, S. A., Sajjakulnukit, P., Solanki, S., Andren, A., Kumar, R., Olive, K. P., Banerjee, R., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci143691 · Cited by 215 · see citing works
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Kung-Chun Chiu, D., Pui-Wah Tse, A., Law, C.-T., Ming-Jing Xu, I., Lee, D., Chen, M., Kit-Ho Lai, R., Wai-Hin Yuen, V., Wing-Sum Cheu, J., Wai-Hung Ho, D., et al. (2019) · Cell Death & Disease · doi:10.1038/s41419-019-2155-3 · Cited by 192 · see citing works
Hypoxia-inducible factors: a central link between inflammation and cancer
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Tissue damage control in disease tolerance
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Crosstalk between Hypoxia and ER Stress Response: a Key Regulator of Macrophage Polarization
Díaz-Bulnes, P., Saiz, M. L., López-Larrea, C., & Rodríguez, R. M. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02951 · Cited by 175 · see citing works
Metabolic changes in cancer: beyond the Warburg effect
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HIF-1-Independent Mechanisms Regulating Metabolic Adaptation in Hypoxic Cancer Cells
Lee, S.-H., Golinska, M., & Griffiths, J. R. (2021) · Cells · doi:10.3390/cells10092371 · Cited by 169 · see citing works
Iron and the pathophysiology of diabetes
Harrison, A. V., Lorenzo, F. R., & McClain, D. A. (2023) · Annual Review of Physiology · doi:10.1146/annurev-physiol-022522-102832 · Cited by 161 · see citing works
The Pathogenesis of Adenomyosis vis-à-vis Endometriosis
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“Once hypoxic, evolutionarily conserved adaptive processes, such as hypoxia-inducible factors (HIFs), are activated [73].”
BackgroundTET1 regulates hypoxia-induced epithelial-mesenchymal transition by acting as a co-activator
Tsai, Y.-P., Chen, H.-F., Chen, S.-Y., Cheng, W.-C., Wang, H.-W., Shen, Z.-J., Song, C., Teng, S.-C., He, C., & Wu, K.-J. (2014) · Genome biology · doi:10.1186/s13059-014-0513-0 · Cited by 152 · see citing works
The role of tumor suppressor p53 in the antioxidant defense and metabolism
Budanov, A. V. (2014) · Subcellular Biochemistry · doi:10.1007/978-94-017-9211-0_18 · Cited by 157 · see citing works
Zhao, T., Ren, H., Jia, L., Chen, J., Xin, W., Yan, F., Li, J., Wang, X., Gao, S., Qian, D., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.2948 · Cited by 142 · see citing works
“Initially identified as a critical transcription factor mediating cell adaption to hypoxia [9], it was recently found that HIF-1α is overexpressed in pancreatic cancer even under normoxia condition and levels of HIF-1α are positively correlated with tumor progression, angiogenesis, cell migration…”
BackgroundCollagen Remodeling in the Hypoxic Tumor-Mesothelial Niche Promotes Ovarian Cancer Metastasis
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“HIF2α can also bind to HIF-1β, and it plays a role in vascularization, pulmonary development, and erythropoiesis [118].”
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HIF inhibition: Current strategies and clinical challenges
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“Beyond cancer and metabolic disease, pathological HIF activation contributes to diverse conditions characterized by chronic hypoxia, oxidative stress, and inflammation [256].”
- Authors
- Semenza, G. L.
- Affiliations
- Johns Hopkins University (US)
- Corresponding author
- Semenza, Gregg L.
- ORCID
- Semenza, Gregg L.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2012-02
- Volume
- 148
- Issue
- 3
- Pages
- 399-408
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3437543
- OpenAlex
- W2087377825
- Cited by
- 3,645
- References
- 107
- Citations by year
- 2026: 474 · 2025: 326 · 2024: 287 · 2023: 251 · 2022: 281 · 2021: 302 · 2020: 257 · 2019: 227 · 2018: 187 · 2017: 190 · 2016: 181 · 2015: 202 · 2014: 216 · 2013: 179 · 2012: 83
- FWCI
- 16.28
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 532 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Public Health Service (HHS-N268201000032C)
- National Heart, Lung, and Blood Institute (P01-HL65608, HHS-N268201000032C, P01HL065608)
- National Cancer Institute (U54CA143868)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Kruppel-like factors research
- Keywords
- hypoxia-inducible factor, oxygen homeostasis, transcriptional regulation, chronic disease, HIF-targeted therapy, animal evolution, development (biology), physiology, pathobiology
- MeSH terms
- Animals, Hypoxia, Chronic Disease, Biological Evolution, Humans, Oxygen, Embryonic Development, Basic Helix-Loop-Helix Proteins
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