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Hypoxia-inducible nuclear factors bind to an enhancer element located 3' to the human erythropoietin gene.
Open accessAbstract
Human erythropoietin gene expression in liver and kidney is inducible by anemia or hypoxia. DNase I-hypersensitive sites were identified 3' to the human erythropoietin gene in liver nuclei. A 256-base-pair region of 3' flanking sequence was shown by DNase I protection and electrophoretic mobility-shift assays to bind four or more different nuclear factors, at least two of which are induced by anemia in both liver and kidney, and the region functioned as a hypoxia-inducible enhancer in transient expression assays. These results provide insight into the molecular basis for the regulation of gene expression by a fundamental physiologic stimulus, hypoxia.
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“which coordinate transcriptional and post-transcriptional programs that promote metabolic adaptation, angiogenesis, erythropoiesis, and redox balance”
From HIF inhibition: Current strategies and clinical challenges (2026) · cites this paper as [30]
In the citing paper
“hypoxia-inducible factors (HIFs) form the central transcriptional axis governing cellular adaptation to oxygen deprivation”
From HIF inhibition: Current strategies and clinical challenges (2026) · cites this paper as [30]
In the citing paper
“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 et al., 1991
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Cites
Dignam, J. D., Lebovitz, R. M., & Roeder, R. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.5.1475 · Cited by 11,262
Kalantar‐Zadeh, K. (2017) · American Journal of Nephrology · doi:10.1159/000455387 · Cited by 1,149
Cloning and expression of the human erythropoietin gene.
Lin, F. K., Suggs, S. V., Lin, C.-W., Browne, J. K., Smalling, R., Egrie, J. C., Chen, K. K., Fox, G. M., Martin, F., & Stabinsky, Z. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.22.7580 · Cited by 1,131
Regulation of the Erythropoietin Gene: Evidence That the Oxygen Sensor Is a Heme Protein
Goldberg, M. A., Dunning, S. P., & Bunn, H. F. (1988) · Science · doi:10.1126/science.2849206 · Cited by 1,032
Jones, N., Rigby, P. W. J., & Ziff, E. B. (1988) · Genes & Development · doi:10.1101/gad.2.3.267 · Cited by 675
Homologous recognition of a promoter domain common to the MSV LTR and the HSV tk gene
Graves, B. J., Johnson, P. F., & McKnight, S. L. (1986) · Cell · doi:10.1016/0092-8674(86)90266-7 · Cited by 533
Localization of erythropoietin synthesizing cells in murine kidneys by in situ hybridization
Koury, S., Bondurant, M. C., & Koury, M. (1988) · Blood · doi:10.1182/blood.v71.2.524.524 · Cited by 469
Kourembanas, S., Hannan, R. L., & Faller, D. V. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114759 · Cited by 386
The regulated expression of erythropoietin by two human hepatoma cell lines.
Goldberg, M. A., Glass, G. A., Cunningham, J. M., & Bunn, H. F. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.22.7972 · Cited by 358
Koury, S. T., Koury, M., Bondurant, M. C., Caro, J., & Gräber, S. E. (1989) · Blood · doi:10.1182/blood.v74.2.645.645 · Cited by 252
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Gaseous monoxides: a new class of micro vascular regulator in the liver
Suematsu, M., Wakabayashi, Y., & Ishimura, Y. (1996) · Cardiovascular Research · doi:10.1016/0008-6363(96)00109-5 · Cited by 104
Xu, L., Pathak, P. S., & Fukumura, D. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-0953-03 · Cited by 106
Role of oxygen in the zonation of carbohydrate metabolism and gene expression in liver
Jungermann, K. A., & Kietzmann, T. (1997) · Kidney International · doi:10.1038/ki.1997.53 · Cited by 99
Zhang, H., Zhang, G., Gonzalez, F. J., Park, S.-M., & Cai, D. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001112 · Cited by 105
Wierońska, J. M., Cieślik, P., & Kalinowski, L. (2021) · Biomolecules · doi:10.3390/biom11081097 · Cited by 105
Erythropoietin and transferrin metabolism in nephrotic syndrome
Vaziri, N. D. (2001) · American Journal of Kidney Diseases · doi:10.1053/ajkd.2001.25174 · Cited by 100
Prolyl Hydroxylase Domain Inhibitors: A Route to HIF Activation and Neuroprotection
Harten, S. K., Ashcroft, M. A., & Maxwell, P. H. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2870 · Cited by 99
Hypoxia-Responsive CAR-T Cells Exhibit Reduced Exhaustion and Enhanced Efficacy in Solid Tumors
Zhu, X., Chen, J., Li, W., Xu, Y., Shan, J., Hong, J., Zhao, Y., Xu, H., Ma, J., Shen, J., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-23-1038 · Cited by 109
Paone, A., Galli, R., Gabellini, C., Lukashev, D. E., Starace, D., Görlach, A., Cesaris, P. D., Elio Ziparo, A., Bufalo, D. D., Sitkovsky, M. V., et al. (2010) · Neoplasia · doi:10.1593/neo.92106 · Cited by 97
Nanomedicine Strategies in Conquering and Utilizing the Cancer Hypoxia Environment
Pan, Y., Liu, L., Mou, X., & Cai, Y. (2023) · ACS Nano · doi:10.1021/acsnano.3c07763 · Cited by 98
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Lee, C.-T., Boss, M., & Dewhirst, M. W. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5759 · Cited by 98
Gaspar, J. M., & Velloso, L. A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00813 · Cited by 97
Kawanami, D., Mahabeleshwar, G. H., Lin, Z., Atkins, G. B., Hamik, A., Haldar, S. M., Maemura, K., LaManna, J. C., & Jain, M. K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.025346 · Cited by 97
The role of hypoxia-inducible factor 1 in atherosclerosis: Figure 1
Gao, L., Chen, Q., Zhou, X., & Li, F. (2012) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2012-200828 · Cited by 94
Hypoxia‐Inducible Factor and the Development of Stem Cells of the Cardiovascular System
Ramírez‐Bergeron, D. L., & Simon, M. C. (2001) · Stem Cells · doi:10.1634/stemcells.19-4-279 · Cited by 95
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Tarade, D., & Ohh, M. (2017) · Oncogene · doi:10.1038/onc.2017.338 · Cited by 93
Ariazi, J. L., Duffy, K. J., Adams, D. F., Fitch, D. M., Luo, L., Pappalardi, M. B., Biju, M. P., DiFilippo, E. H., Shaw, T., Wiggall, K., et al. (2017) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.117.242503 · Cited by 94
Hypoxia: the tumor's gateway to progression along the angiogenic pathway
Brahimi‐Horn, C., Berra, E., & Pouysségur, J. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)82185-1 · Cited by 93
A new HIF-1 alpha variant induced by zinc ion suppresses HIF-1-mediated hypoxic responses
Chun, Y., Choi, E., Yeo, E.-J., Lee, J.-H., Kim, M.-S., & Park, J. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.22.4051 · Cited by 93
Shibata, T., Akiyama, N., Noda, M., Sasai, K., & Hiraoka, M. (1998) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/s0360-3016(98)00298-3 · Cited by 93
The Molecular Adaptive Responses of Skeletal Muscle to High-Intensity Exercise/Training and Hypoxia
Li, J., Li, Y., ATAKAN, M. M., Kuang, J., Hu, Y., Bishop, D. J., & Yan, X. (2020) · Antioxidants · doi:10.3390/antiox9080656 · Cited by 99
HIF-1: structure, biology and natural modulators
Yang, C., Zhong, Z., Wang, S., Vong, C. T., Yu, B., & Wang, Y. (2021) · Chinese Journal of Natural Medicines · doi:10.1016/s1875-5364(21)60051-1 · Cited by 98
Erythropoietin, a Novel Versatile Player Regulating Energy Metabolism beyond the Erythroid System
Wang, L., Di, L., & Noguchi, C. T. (2014) · International Journal of Biological Sciences · doi:10.7150/ijbs.9518 · Cited by 91
Targeting Hypoxia Signaling for Perioperative Organ Injury
Yuan, X., Lee, J. W., Bowser, J. L., Neudecker, V., Sridhar, S., & Eltzschig, H. K. (2017) · Anesthesia & Analgesia · doi:10.1213/ane.0000000000002288 · Cited by 95
Ježek, P., Plecitá‐Hlavatá, L., Smolková, K., & Rossignol, R. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.11.008 · Cited by 96
Beall, C. M. (2013) · American Journal of Human Biology · doi:10.1002/ajhb.22355 · Cited by 92
Metabolic requirements of pulmonary fibrosis: role of fibroblast metabolism
Hamanaka, R. B., & Mutlu, G. M. (2021) · FEBS Journal · doi:10.1111/febs.15693 · Cited by 94
Makita, T., Hernández‐Hoyos, G., Chen, T. H.-P., Wu, H., Rothenberg, E. V., & Sucov, H. M. (2001) · Genes & Development · doi:10.1101/gad.871601 · Cited by 90
Mechanisms of induction of adenosine receptor genes and its functional significance
Hilaire, C. S., Carroll, S. H., Chen, H., & Ravid, K. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21579 · Cited by 89
Transcriptional regulation of erythropoiesis
Perry, C., & Soreq, H. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02999.x · Cited by 87
Goteri, G., Lucarini, G., Montik, N., Zizzi, A., Stramazzotti, D., Fabris, G., Tranquilli, A. L., & Ciavattini, A. (2009) · International Journal of Gynecological Pathology · doi:10.1097/pgp.0b013e318182c2be · Cited by 88
The Hypoxia-Inducible Factor and Tumor Progression Along the Angiogenic Pathway
Brahimi-Horn, M. C., & Pouysségur, J. (2004) · International review of cytology · doi:10.1016/s0074-7696(04)42004-x · Cited by 87
Hypoxia-induced adrenomedullin production in the kidney
Nagata, D., Hirata, Y., Suzuki, E., Kakoki, M., Hayakawa, H., Goto, A., Ishimitsu, T., Minamino, N., Ono, Y., Kangawa, K., et al. (1999) · Kidney International · doi:10.1046/j.1523-1755.1999.00361.x · Cited by 87
Age-dependent metabolic dysregulation in cancer and Alzheimer’s disease
Harris, R. A., Tindale, L. C., & Cumming, R. C. (2014) · Biogerontology · doi:10.1007/s10522-014-9534-z · Cited by 85
Yan, L. Y., Colandrea, V. J., & Hale, J. J. (2010) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2010.510836 · Cited by 87
An adenoviral vector regulated by hypoxia for the treatment of ischaemic disease and cancer
Binley, K. E., Iqball, S., Kingsman, A. J., Kingsman, S. M., & Naylor, S. (1999) · Gene Therapy · doi:10.1038/sj.gt.3301001 · Cited by 86
Welsh, D., PEACOCK, A. J., MacLean, M. R., & Harnett, M. M. (2001) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.164.2.2008054 · Cited by 85
Wen, W., Ding, J., Sun, W. C., Wu, K., Ning, B., Gong, W., He, G., Huang, S., Ding, X., Yin, P., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-08-4910 · Cited by 86
Lung Cell Hypoxia: Role of Mitochondrial Reactive Oxygen Species Signaling in Triggering Responses
Schumacker, P. T. (2011) · Proceedings of the American Thoracic Society · doi:10.1513/pats.201103-032mw · Cited by 87
Molecular mechanism of hypoxia‐mediated hepatic gluconeogenesis by transcriptional regulation
Choi, J., Park, M. J., Kim, K. W., Choi, Y. H., Park, S. H., An, W. G., Yang, U. S., & Cheong, J. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.097 · Cited by 84
Nanotechnology for treatment of glioblastoma multiforme
Michael, J. S., Lee, B., Zhang, M., & Yu, J. S. (2018) · Journal of Translational Internal Medicine · doi:10.2478/jtim-2018-0025 · Cited by 84
Davis, L., Recktenwald, M., Hutt, E., Fuller, S., Briggs, M., Goel, A., & Daringer, N. (2022) · Cancers · doi:10.3390/cancers14051259 · Cited by 83
Research progress on tumor hypoxia-associative nanomedicine
Xu, X., Chen, S., Yi, N.-B., Li, X., Chen, S., Lei, Z., Cheng, D., & Sun, T. (2022) · Journal of Controlled Release · doi:10.1016/j.jconrel.2022.09.003 · Cited by 86
An extra-erythrocyte role of haemoglobin body in chondrocyte hypoxia adaption
Zhang, F., Zhang, B., Wang, Y., Jiang, R., Liu, J., Wei, Y., Gao, X., Zhu, Y., Wang, X., Sun, M., et al. (2023) · Nature · doi:10.1038/s41586-023-06611-6 · Cited by 85
Hypoxia promotes oxidative base modifications in the pulmonary artery endothelial cell VEGF gene
Grishko, V. I., Solomon, M., Breit, J. F., Killilea, D. W., LeDoux, S. P., Wilson, G. L., & Gillespie, M. N. (2001) · The FASEB Journal · doi:10.1096/fj.00-0755fje · Cited by 80
Yin, H., & Blanchard, K. L. (2000) · Blood · doi:10.1182/blood.v95.1.111 · Cited by 81
Molecular biology of erythropoietin
Ratcliffe, P. J. (1993) · Kidney International · doi:10.1038/ki.1993.327 · Cited by 83
Von Hippel–Lindau protein signalling in clear cell renal cell carcinoma
Liao, C., Hu, L., & Zhang, Q. H. (2024) · Nature Reviews Urology · doi:10.1038/s41585-024-00876-w · Cited by 84
Bras, A. L., Lionneton, F., Mattot, V., Lelièvre, E., Caëtano, B., Spruyt, N., & Soncin, F. (2007) · Oncogene · doi:10.1038/sj.onc.1210566 · Cited by 83
c- erb B-2 Related Aggressiveness in Breast Cancer Is Hypoxia Inducible Factor-1α Dependent
Giatromanolaki, A. N., Koukourakis, M. I., Simopoulos, C., Polychronidis, A., Gatter, K. C., Harris, A. L., & Sivridis, E. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-1068 · Cited by 81
Hypoxia Regulation of Gene Transcription
Caro, J. (2001) · High Altitude Medicine & Biology · doi:10.1089/152702901750265251 · Cited by 80
Comparative Response of Brain to Chronic Hypoxia and Hyperoxia
Terraneo, L., & Samaja, M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091914 · Cited by 82
Regulation of Cellular Gas Exchange, Oxygen Sensing, and Metabolic Control
Clanton, T. L., Hogan, M. C., & Gladden, L. B. (2013) · Comprehensive physiology · doi:10.1002/cphy.c120030 · Cited by 91
Heat acclimation and cross tolerance to hypoxia
Ely, B. R., Lovering, A. T., Horowitz, M., & Minson, C. T. (2014) · Temperature · doi:10.4161/temp.29800 · Cited by 78
Erythropoietin: the story of hypoxia and a finely regulated hematopoietic hormone
Koury, M. J. (2005) · Experimental Hematology · doi:10.1016/j.exphem.2005.06.031 · Cited by 78
RNA‐binding protein Csx1 mediates global control of gene expression in response to oxidative stress
Rodríguez‐Gabriel, M. A., Burns, G., McDonald, W. H., Martín, V., Yates, J. R., Bähler, J., & Russell, P. R. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg597 · Cited by 78
Azarnoush, K., Ribes, A. M., Sebbah, L., Carrion, C., Bissery, A., Mandet, C., Pouly, J., Bruneval, P., Hagège, A. A., & Menasché, P. (2005) · Journal of Thoracic and Cardiovascular Surgery · doi:10.1016/j.jtcvs.2004.11.044 · Cited by 78
Gene Expression in Low Oxygen Tension
Helfman, T., & Falanga, V. (1993) · The American Journal of the Medical Sciences · doi:10.1097/00000441-199307000-00010 · Cited by 78
Veith, C., SCHERMULY, R. T., Brandes, R. P., & Weißmann, N. (2015) · The Journal of Physiology · doi:10.1113/jp270689 · Cited by 75
Kang, S., Gil, Y., Min, D., & Jang, H. (2020) · ACS Nano · doi:10.1021/acsnano.9b09974 · Cited by 76
Regulatory mechanism of HIF-1α and its role in liver diseases: a narrative review
Chu, Q., Gu, X., Zheng, Q., & Zhu, H. (2021) · Annals of Translational Medicine · doi:10.21037/atm-21-4222 · Cited by 84
Woo, S. K., Kwon, M. S., Geng, Z., Chen, Z., Ivanov, A. V., Bhatta, S., Gerzanich, V., & Simard, J. M. (2011) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2011.159 · Cited by 77
Fujita, T., Miyamoto, S., Onoyama, I., Sonoda, K., Mekada, E., & Nakano, H. (2003) · Cancer Letters · doi:10.1016/s0304-3835(02)00713-9 · Cited by 77
Expression of Erythropoietin and Erythropoietin Receptor in Non–Small Cell Lung Carcinomas
Dagnon, K., Pacary, E., Commo, F., Antoine, M., Bernaudin, M., Bernaudin, J., & Callard, P. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.993.11.3 · Cited by 77
Hypoxia-inducible factor in cancer angiogenesis: Structure, regulation and clinical perspectives
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Valsecchi, V., Pignataro, G., Prete, A. D., Sirabella, R., Matrone, C., Boscia, F., Scorziello, A., Sisalli, M. J., Esposito, E., Zambrano, N., et al. (2011) · Stroke · doi:10.1161/strokeaha.110.597583 · Cited by 75
Portron, S., Merceron, C., Gauthier, O., Lesoeur, J., Sourice, S., Masson, M., Fellah, B. H., Geffroy, O., Lallemand, E. A., Weiss, P., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062368 · Cited by 74
A dominant-negative isoform lacking exons 11 and 12 of the human hypoxia-inducible factor-1α gene
Chun, Y., Choi, E., Kim, T., Kim, M.-S., & Park, J. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3620071 · Cited by 74
Martini, M., Teofili, L., Cenci, T., Giona, F., Torti, L., Rea, M., Foa, R., Leone, G., & Larocca, L. M. (2008) · Haematologica · doi:10.3324/haematol.13210 · Cited by 73
Hypoxia signalling manipulation for bone regeneration
Drager, J., Harvey, E. J., & Barralet, J. E. (2015) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2015.4 · Cited by 73
Complex role of protein phosphorylation in gene activation by hypoxia
Salceda, S., Beck, I., Srinivas, V., & Caro, J. (1997) · Kidney International · doi:10.1038/ki.1997.78 · Cited by 73
Control of Erythropoietin Gene Expression and its Use in Medicine
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Deng, A., Arndt, M. A., Satriano, J. A., Singh, P., Rieg, T., Thomson, S. C., Tang, T., & Blantz, R. C. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00153.2010 · Cited by 71
Gene expression profiling of hypoxia signaling in human hepatocellular carcinoma cells
Vengellur, A., Phillips, J. M., Hogenesch, J. B., & LaPres, J. J. (2005) · Physiological Genomics · doi:10.1152/physiolgenomics.00045.2004 · Cited by 72
Hypoxia‐induced pathways in breast cancer
Goonewardene, T. I., Sowter, H., & Harris, A. L. (2002) · Microscopy Research and Technique · doi:10.1002/jemt.10175 · Cited by 71
Hypoxia-Inducible Regulation of a Prodrug-Activating Enzyme for Tumor-Specific Gene Therapy
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Soñanez‐Organis, J. G., Racotta, I. S., & Yepiz-Plascencia, G. M. (2010) · Journal of Experimental Marine Biology and Ecology · doi:10.1016/j.jembe.2010.06.031 · Cited by 71
Roles of Brahma and Brahma/SWI2-Related Gene 1 in Hypoxic Induction of the Erythropoietin Gene
Wang, F., Zhang, R., Beischlag, T. V., Muchardt, C., Yaniv, M., & Hankinson, O. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409002200 · Cited by 71
Huang, E. L., Ho, V. T., Arany, Z. P., Krainc, D., Galson, D. L., Tendler, D. S., Livingston, D. M., & Bunn, H. F. (1997) · Kidney International · doi:10.1038/ki.1997.76 · Cited by 71
Activation of γ-globin expression by hypoxia-inducible factor 1α
Feng, R., Mayuranathan, T., Huang, P., Doerfler, P. A., Li, Y., Yao, Y., Zhang, J., Palmer, L. E., Mayberry, K. D., Christakopoulos, G. E., et al. (2022) · Nature · doi:10.1038/s41586-022-05312-w · Cited by 69
Mwaikambo, B. R., Yang, C., Chemtob, S., & Hardy, P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.033480 · Cited by 74
Mobilization of hematopoietic stem cells from the bone marrow niche to the blood compartment
Hoggatt, J., & Pelus, L. M. (2011) · Stem Cell Research & Therapy · doi:10.1186/scrt54 · Cited by 76
Extracellular matrix genes as hypoxia-inducible targets
Myllyharju, J., & Schipani, E. (2009) · Cell and Tissue Research · doi:10.1007/s00441-009-0841-7 · Cited by 72
Hypoxia-inducible Factor 1α (HIF-1α) Is a Non-heme Iron Protein
Srinivas, V., Zhu, X., Salceda, S., Nakamura, R., & Caro, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.29.18019 · Cited by 69
RetractedHIF-1α Metabolic Pathways in Human Cancer
Elzakra, N., & Kim, Y. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-51652-9_17 · Cited by 72
How oxygenation shapes immune responses: emerging roles for physioxia and pathological hypoxia
Mirchandani, A. S., Sánchez-García, M. A., & Walmsley, S. R. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-024-01087-5 · Cited by 77
Erythropoietin in the control of red cell production
JELKMANN, W. E. B., & Metzen, E. (1996) · Annals of Anatomy - Anatomischer Anzeiger · doi:10.1016/s0940-9602(96)80124-5 · Cited by 65
Hypoxia-inducible factor in cancer: from pathway regulation to therapeutic opportunity
Ortmann, B. M. (2024) · BMJ Oncology · doi:10.1136/bmjonc-2023-000154 · Cited by 67
Hypoxia and cancer related pathology
Xiong, Q., Liu, B., Ding, M., Zhou, J., Yang, C., & Chen, Y. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.05.002 · Cited by 71
Hypoxia induces immunosuppression, metastasis and drug resistance in pancreatic cancers
Zhang, H., Cao, K., Xiang, J., Zhang, M., Zhu, M., & Xi, Q. (2023) · Cancer Letters · doi:10.1016/j.canlet.2023.216345 · Cited by 68
Hypoxia-inducible gene expression
Fandrey, J. (1995) · Respiration Physiology · doi:10.1016/0034-5687(95)00013-4 · Cited by 67
Characterization of Physiologically Regulated Vectors for the Treatment of Ischemic Disease
Boast, K., Binley, K., Iqball, S., Price, T., Spearman, H., Kingsman, S. M., Kingsman, A. J., & Naylor, S. (1999) · Human Gene Therapy · doi:10.1089/10430349950017185 · Cited by 67
Cellular oxygen sensing in health and disease
Mole, D. R., & Ratcliffe, P. J. (2007) · Pediatric Nephrology · doi:10.1007/s00467-007-0632-x · Cited by 67
The genetic basis of high-altitude pulmonary oedema
Mortimer, H., Patel, S., & Peacock, A. J. (2004) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2003.11.003 · Cited by 66
Regulation of hypoxia-inducible gene expression after HIF activation
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Metadata
- Authors
- Semenza, G. L., Nejfelt, M. K., Chi, S. M., & Antonarakis, S. E.
- Affiliations
- Johns Hopkins University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1991-07
- Volume
- 88
- Issue
- 13
- Pages
- 5680-5684
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC51941
- OpenAlex
- W2090627731
- Cited by
- 990
- References
- 25
- Citations by year
- 2026: 24 · 2025: 35 · 2024: 46 · 2023: 58 · 2022: 43 · 2021: 53 · 2020: 62 · 2019: 34 · 2018: 26 · 2017: 30 · 2016: 38 · 2015: 30 · 2014: 22 · 2013: 41 · 2012: 25
- FWCI
- 8.88
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Keywords
- erythropoietin gene, hypoxia-inducible factor, enhancers, 3' flanking region, DNase I hypersensitive sites, anemia, hypoxia, gene expression regulation, liver, kidney, transcription factor binding
- MeSH terms
- Animals, Hypoxia, Base Sequence, Cell Nucleus, Chromosome Mapping, Deoxyribonuclease I, DNA-Binding Proteins, Enhancer Elements, Genetic, Erythropoietin, Gene Expression Regulation, Genes, Humans, Mice, Transgenic, Molecular Sequence Data, Nuclear Proteins, Regulatory Sequences, Nucleic Acid, Restriction Mapping, Mice
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