The DOI matches its Crossref record; 49 of the 50 references it cites were found in a registry or an index.
Hypoxia-inducible Factor-1 Mediates Transcriptional Activation of the Heme Oxygenase-1 Gene in Response to Hypoxia
Open accessAbstract
Exposure of rats to hypoxia (7% O2) markedly increased the level of heme oxygenase-1 (HO-1) mRNA in several tissues. Accumulation of HO-1 transcripts was also observed after exposure of rat aortic vascular smooth muscle (VSM) cells to 1% O2, and this induction was dependent on gene transcription. Activation of the mouse HO-1 gene by all agents thus far tested is mediated by two 5'-enhancer sequences, SX2 and AB1, but neither fragment was responsive to hypoxia in VSM cells. Hypoxia-dependent induction of the chloramphenicol acetyltransferase (CAT) reporter gene was mediated by a 163-bp fragment located approximately 9.5 kilobases upstream of the transcription start site. This fragment contains two potential binding sites for hypoxia-inducible factor 1 (HIF-1). A role for HIF-1 in HO-1 gene regulation was established by the following observations: 1) HIF-1 specifically bound to an oligonucleotide spanning these sequences, 2) mutation of these sequences abolished HIF-1 binding and hypoxia-dependent gene activation in VSM cells, 3) hypoxia increased HIF-1alpha and HIF-1beta protein levels in VSM cells, and 4) hypoxia-dependent HO-1 mRNA accumulation was not observed in mutant hepatoma cells lacking HIF-1 DNA-binding activity. Taken together, these data demonstrate that hypoxia induces HO-1 expression in animal tissues and cell cultures and implicate HIF-1 in this response.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Other bona fide HIF-regulated genes involved in iron metabolism include transferrin, which transports serum iron in its ferric form (Fe3+), its high affinity receptor TFR1, 183–185 ceruloplasmin, which oxidizes Fe2+ to Fe3+ and is important for iron transport, 186 and heme-oxygenase-1, which is critical for the recycling of iron from phagocytosed erythrocytes.”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [186]
In the citing paper
“Other bona fide HIF-regulated genes involved in iron metabolism include transferrin, which transports serum iron in its ferric form (Fe3+), its high affinity receptor TFR1, 183–185 ceruloplasmin, which oxidizes Fe2+ to Fe3+ and is important for iron transport, 186 and heme-oxygenase-1, which is critical for the recycling of iron from phagocytosed erythrocytes.”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [187]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction
Chomczynski, P., & Sacchi, N. (1987) · Analytical Biochemistry · doi:10.1006/abio.1987.9999 · Cited by 65,515
Wang, G. L., Jiang, B. H., Rue, E. A., & Semenza, G. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5510 · Cited by 6,212
Self-citationVascular endothelial growth factor induced by hypoxia may mediate hypoxia-initiated angiogenesis
Shweiki, D., Itin, A., Soffer, D., & Keshet, E. (1992) · Nature · doi:10.1038/359843a0 · Cited by 4,617
Semenza, G. L., & Wang, G. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5447 · Cited by 2,617
Self-citationPurification and Characterization of Hypoxia-inducible Factor 1
Wang, G. L., & Semenza, G. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.3.1230 · Cited by 2,094
Self-citationTranscriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1.
Semenza, G., Roth, P. H., Fang, H. M., & Wang, G. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31580-6 · Cited by 1,892
Self-citationCell and environment interactions in tumor microregions: the multicell spheroid model.
Sutherland, R. M. (1988) · Science · doi:10.1126/science.2451290 · Cited by 1,803
General involvement of hypoxia-inducible factor 1 in transcriptional response to hypoxia.
Wang, G. L., & Semenza, G. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.9.4304 · Cited by 1,468
Self-citationChoi, A. M., & Alam, J. (1996) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.15.1.8679227 · Cited by 1,126
Self-citationTranscriptional Regulation of the Rat Vascular Endothelial Growth Factor Gene by Hypoxia
Levy, A. P., Levy, N. S., Wegner, S. A., & Goldberg, M. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13333 · Cited by 1,073
Research works printed but not linked: 4
- Yao, 1994, Mol. Cell. Biol., 14, 5997
- Semenza, 1992, Mol. Cell. Biol., 12, 5447
- Chomczynski, 1987, Anal. Biochem., 162, 156, 10.1016/0003-2697(87)90021-2 · DOI
- Ausserer, 1994, Mol. Cell. Biol., 14, 5032
Cited by
Sorted by citations
Items 101–200 of 772
Deramaudt, B. M. J. ‐., Braunstein, S. E., Rémy, P., & Abraham, N. G. (1998) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19980101)68:1 · Cited by 215
Roles of the human hypoxia-inducible factor (HIF)-3α variants in the hypoxia response
Heikkilä, M., Pasanen, A., Kivirikko, K. I., & Myllyharju, J. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0679-5 · Cited by 213
Komatsu, D. E., & Hadjiargyrou, M. (2004) · Bone · doi:10.1016/j.bone.2003.12.024 · Cited by 212
Deindl, E., Buschmann, I. R., Hoefer, I. E., Podzuweit, T., Boengler, K., Vogel, S., van Royen, N., Fernández, B., & Schaper, W. K. A. (2001) · Circulation Research · doi:10.1161/hh2101.098613 · Cited by 211
Hypoxic Regulation of Angiopoietin-2 Expression in Endothelial Cells
Pichiule, P., Chavez, J. C., & LaManna, J. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m305146200 · Cited by 217
Heme Oxygenase and Atherosclerosis
Morita, T. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000178169.95781.49 · Cited by 206
Hypoxia-inducible factor 1 and the molecular physiology of oxygen homeostasis
Semenza, G. L. (1998) · Journal of Laboratory and Clinical Medicine · doi:10.1016/s0022-2143(98)90091-9 · Cited by 207
Self-citationBiological Chemistry of Carbon Monoxide
Piantadosi, C. A. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602753666316 · Cited by 201
Warnecke, C., Griethe, W., Weidemann, A., Jürgensen, J. S., Willam, C., Bachmann, S., Ivashchenko, Y., Wagner, I., Frei, U. A., Wiesener, M., et al. (2003) · The FASEB Journal · doi:10.1096/fj.02-1062fje · Cited by 201
Caveolae compartmentalization of heme oxygenase‐1 in endothelial cells
Kim, H. P., Wang, X., Galbiati, F., Ryter, S. W., & Choi, A. M. K. (2004) · The FASEB Journal · doi:10.1096/fj.03-1391com · Cited by 198
Self-citationMolecular Basis of Heme Oxygenase-1 Induction: Implications for Chemoprevention and Chemoprotection
Prawan, A., Kundu, J. K., & Surh, Y. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1688 · Cited by 198
HIF-1: the knowns and unknowns of hypoxia sensing.
Zagórska, A., & Dulak, J. (2004) · Acta Biochimica Polonica · doi:10.18388/abp.2004_3545 · Cited by 194
Chilov, D., Camenisch, G., Kvietikova, I., Ziegler, U., Gassmann, M., & Wenger, R. H. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.8.1203 · Cited by 194
Goyal, P., Weißmann, N., Grimminger, F., Hegel, C., Bader, L., Rose, F., Fink, L., Ghofrani, H. A., SCHERMULY, R. T., Schmidt, H. H. H. W., et al. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.02.071 · Cited by 192
Palmer, L. A., Gaston, B. M., & Johns, R. A. (2000) · Molecular Pharmacology · doi:10.1124/mol.58.6.1197 · Cited by 191
Targeting dysregulation of brain iron homeostasis in Parkinson's disease by iron chelators
Weinreb, O., Mandel, S. A., Youdim, M. B. H., & Amit, T. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.01.017 · Cited by 199
Gao, N., Ding, M., Zheng, J. Z., Zhang, Z., Leonard, S. S., Liu, K. J., Shi, X., & Jiang, B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200082200 · Cited by 191
Self-citationHIF-1-mediated activation of transferrin receptor gene transcription by iron chelation
Bianchi, L., Tacchini, L., & Cairo, G. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.21.4223 · Cited by 189
Heme Oxygenase-1: Molecular Mechanisms of Gene Expression in Oxygen-Related Stress
Ryter, S. W., & Choi, A. M. K. (2002) · Antioxidants and Redox Signaling · doi:10.1089/15230860260220120 · Cited by 189
Self-citationWood, S. M., Wiesener, M. S., Yeates, K. M., Okada, N., Pugh, C. W., Maxwell, P. H., & Ratcliffe, P. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.14.8360 · Cited by 189
Transcriptional Activation of the Human Leptin Gene in Response to Hypoxia
Ambrosini, G., Nath, A. K., Sierra-Honigmann, M. R., & Flores-Riveros, J. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205172200 · Cited by 188
Renoprotective Properties of Angiotensin Receptor Blockers beyond Blood Pressure Lowering
Izuhara, Y., Nangaku, M., Inagi, R., Tominaga, N., Aizawa, T., Kurokawa, K., de Strihou, C. V. Y., & Miyata, T. (2005) · Journal of the American Society of Nephrology · doi:10.1681/asn.2005050522 · Cited by 188
Carbon monoxide and hydrogen sulfide: gaseous messengers in cerebrovascular circulation
Leffler, C. W., Parfenova, H., Jaggar, J. H., & Wang, R. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00793.2005 · Cited by 186
HIFs and tumors—causes and consequences
Höpfl, G., Ogunshola, O. O., & Gassmann, M. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00538.2003 · Cited by 186
Heme oxygenase-1, a critical arbitrator of cell death pathways in lung injury and disease
Morse, D., Lin, L., Choi, A. M. K., & Ryter, S. W. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.04.007 · Cited by 185
Self-citationKietzmann, T., Samoylenko, A., & Immenschuh, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m203929200 · Cited by 182
Pagé, E. L., Chan, D. A., Giaccia, A. J., Levine, M., & Richard, D. E. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-06-0612 · Cited by 181
Tacchini, L. (2001) · Carcinogenesis · doi:10.1093/carcin/22.9.1363 · Cited by 178
Torti, S. V., & Torti, F. M. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-2017 · Cited by 183
Regulation of heme oxygenase-1 gene expression in vascular smooth muscle cells by nitric oxide
Hartsfield, C. L., Alam, J., Cook, J. L., & Choi, A. M. K. (1997) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1997.273.5.l980 · Cited by 176
Self-citationBlatzer, M., Barker, B. M., Willger, S. D., Beckmann, N., Blosser, S. J., Cornish, E. J., Mazurie, A., Grahl, N., Haas, H., & Cramer, R. A. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002374 · Cited by 175
New Insights into Intracellular Locations and Functions of Heme Oxygenase-1
Dunn, L., Midwinter, R. G., Ni, J., Hamid, H. A., Parish, C. R., & Stocker, R. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5675 · Cited by 181
HIF hydroxylation and cellular oxygen sensing
Metzen, E., & Ratcliffe, P. J. (2004) · Biological Chemistry · doi:10.1515/bc.2004.016 · Cited by 175
Nitric Oxide-Mediated Regulation of Chemosensitivity in Cancer Cells
Matthews, N. E., Adams, M. A., Maxwell, L., Gofton, T. E., & Graham, C. H. (2001) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/93.24.1879 · Cited by 167
The Nrf2-HO-1 system and inflammaging
O’Rourke, S. A., Shanley, L. C., & Dunne, A. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1457010 · Cited by 177
Role of Bach1 and Nrf2 in up‐regulation of the heme oxygenase‐1 gene by cobalt protoporphyrin
Shan, Y., Lambrecht, R. W., Donohue, S. E., & Bonkovsky, H. L. (2006) · The FASEB Journal · doi:10.1096/fj.06-6346fje · Cited by 169
Emerging ROS-Modulating Technologies for Augmentation of the Wound Healing Process
Polaka, S., Katare, P., Pawar, B., Vasdev, N., Gupta, T., Rajpoot, K., Sengupta, P., & Tekade, R. K. (2022) · ACS Omega · doi:10.1021/acsomega.2c02675 · Cited by 169
Lanser, L., Fuchs, D., Kurz, K., & Weiß, G. (2021) · Nutrients · doi:10.3390/nu13113732 · Cited by 179
Hypoxia-induced Angiogenesis during Carcinogenesis
Choe, G.-S., Bae, M.-G., Jeong, J.-W., Mun, H.-E., & Kim, G.-W. (2003) · BMB Reports · doi:10.5483/bmbrep.2003.36.1.120 · Cited by 166
Neuropathology of multiple sclerosis—new concepts
Kornek, B., & Lassmann, H. (2003) · Brain Research Bulletin · doi:10.1016/s0361-9230(03)00095-9 · Cited by 164
Cross Talk Between Carbon Monoxide and Nitric Oxide
Hartsfield, C. L. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602753666352 · Cited by 163
Shan, Y., Zheng, J., Lambrecht, R. W., & Bonkovsky, H. L. (2007) · Gastroenterology · doi:10.1053/j.gastro.2007.08.002 · Cited by 162
Ischemia Activates the ATF6 Branch of the Endoplasmic Reticulum Stress Response
Doroudgar, S., Thuerauf, D. J., Marcinko, M. C., Belmont, P. J., & Glembotski, C. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.018036 · Cited by 162
HIF‐prolyl hydroxylases as therapeutic targets in erythropoiesis and iron metabolism
Haase, V. H. (2017) · Hemodialysis International · doi:10.1111/hdi.12567 · Cited by 165
Bento, C. F., & Pereira, P. (2011) · Diabetologia · doi:10.1007/s00125-011-2191-8 · Cited by 163
Rosenberger, C., Heyman, S. N., Rosen, S., Shina, A., Goldfarb, M., Griethe, W., Frei, U. A., Reinke, P., Bachmann, S., & Eckardt, K. (2005) · Kidney International · doi:10.1111/j.1523-1755.2005.67110.x · Cited by 159
Dhodda, V. K., Sailor, K. A., Bowen, K. K., & Vemuganti, R. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02316.x · Cited by 158
Hypoxia induces hexokinase II gene expression in human lung cell line A549
Riddle, S. R., Ahmad, A. M., Ahmad, S., Deeb, S. S., Malkki, M., Schneider, B. K., Allen, C. B., & White, C. W. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.278.2.l407 · Cited by 153
HIF-1α in Epidermis: Oxygen Sensing, Cutaneous Angiogenesis, Cancer, and Non-Cancer Disorders
Rezvani, H. R., Ali, N., Nissen, L. J., Harfouche, G., de Verneuil, H., Taïeb, A., & Mazurier, F. (2011) · Journal of Investigative Dermatology · doi:10.1038/jid.2011.141 · Cited by 161
The Diverse Roles of Heme Oxygenase-1 in Tumor Progression
Hoang, K. N. L., Anstee, J. E., & Arnold, J. N. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.658315 · Cited by 152
Regulation and role of heme oxygenase in oxidative injury
Dennery, P. A. (2001) · Current topics in cellular regulation · doi:10.1016/s0070-2137(01)80008-x · Cited by 151
Unfolded protein response (UPR) integrated signaling networks determine cell fate during hypoxia
Bartoszewska, S., & Collawn, J. F. (2020) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-020-00212-1 · Cited by 155
Vadlapatla, R. K., Vadlapudi, A. D., & Mitra, A. K. (2013) · Current Drug Targets · doi:10.2174/13894501113149990015 · Cited by 148
The subtle side to hypoxia inducible factor (HIFα) regulation
Bilton, R. L., & Booker, G. W. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03446.x · Cited by 150
Iron homeostasis and tumorigenesis: molecular mechanisms and therapeutic opportunities
Zhang, C., & Zhang, F. (2014) · Protein & Cell · doi:10.1007/s13238-014-0119-z · Cited by 149
Li, Q. F., Wang, X. R., Yang, Y. W., & Lin, H. (2006) · Cell Research · doi:10.1038/sj.cr.7310072 · Cited by 151
Jiang, N., Zhao, H., Han, Y., Li, L., Xiong, S., Zeng, L., Xiao, Y., Wei, L., Xiong, X., Gao, P., et al. (2020) · Cell Proliferation · doi:10.1111/cpr.12909 · Cited by 145
Andaloussi, A. E., & Lesniak, M. S. (2007) · Journal of Neuro-Oncology · doi:10.1007/s11060-006-9314-y · Cited by 142
Whitehead, A., Triant, D. A., Champlin, D. M., & Nacci, D. E. (2010) · Molecular Ecology · doi:10.1111/j.1365-294x.2010.04829.x · Cited by 140
Gong, P., Hu, B., Stewart, D., Ellerbe, M., Figueroa, Y. G., Blank, V., Beckman, B. S., & Alam, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103658200 · Cited by 140
Self-citationBartoszewska, S., Rochan, K., Piotrowski, A., Kamysz, W., Ochocka, J. R., Collawn, J. F., & Bartoszewski, R. (2014) · The FASEB Journal · doi:10.1096/fj.14-267054 · Cited by 139
Halle, C., Andersen, E. K. F., Lando, M., Aarnes, E., Hasvold, G., Holden, M., Syljuåsen, R. G., Sundfør, K., Kristensen, G. B., Holm, R., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-1085 · Cited by 138
The role of hypoxia-inducible factors in cancer
Maynard, M. A., & Ohh, M. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7082-2 · Cited by 139
Molecular targets in radiation-induced blood-brain barrier disruption
Nordal, R., & Wong, C. S. (2005) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2005.01.039 · Cited by 138
Oxygen‐dependent regulation of hypoxia‐inducible factors by prolyl and asparaginyl hydroxylation
Lando, D., Gorman, J. J., Whitelaw, M. L., & Peet, D. J. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03445.x · Cited by 138
Yeligar, S. M., Machida, K., & Kalra, V. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.138636 · Cited by 140
Heme oxygenase-1 and carbon monoxide in pulmonary medicine
Slebos, D., Ryter, S. W., & Choi, A. M. K. (2003) · Respiratory Research · doi:10.1186/1465-9921-4-7 · Cited by 138
Self-citationFilippo, C. D., Marfella, R., Cuzzocrea, S., Piegari, E., Petronella, P., Giugliano, D., Rossi, F., & D’Amico, M. (2005) · Diabetes · doi:10.2337/diabetes.54.3.803 · Cited by 132
Camhi, S. L., Alam, J., Wiegand, G. W., Chin, B. Y., & Choi, A. M. K. (1998) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.18.2.2910 · Cited by 130
Self-citationLactate as a marker of energy failure in critically ill patients: hypothesis.
Valenza, F., Aletti, G., Fossali, T., Chevallard, G., Sacconi, F., Irace, M., & Gattinoni, L. (2005) · Critical Care · doi:10.1186/cc3818 · Cited by 130
Semenza, G. L., Agani, F. H., Iyer, N. V., Jiang, B., Leung, S., Wiener, C., & Yu, A. Y. (1998) · CHEST Journal · doi:10.1378/chest.114.1_supplement.40s · Cited by 127
Self-citationGao, N., Shen, L., Zhang, Z., Leonard, S. S., He, H., Zhang, X., Shi, X., & Jiang, B. (2003) · Molecular and Cellular Biochemistry · doi:10.1023/b:mcbi.0000007259.65742.16 · Cited by 128
Self-citationHaem oxygenase-1: a novel player in cutaneous wound repair and psoriasis?
Hanselmann, C., Mauch, C., & Werner, S. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530459 · Cited by 126
Laderoute, K. R., Mendonca, H. L., Calaoagan, J. M., Knapp, A. M., Giaccia, A. J., & Stork, P. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.18.12890 · Cited by 127
Retrovirus-mediated HO gene transfer into endothelial cells protects against oxidant-induced injury
Yang, L. M., Quan, S., & Abraham, N. G. (1999) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1999.277.1.l127 · Cited by 126
Hypoxia‐inducible factor 1: a new hope to counteract neurodegeneration?
Correia, S. C., & Moreira, P. I. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06443.x · Cited by 125
Oncogenes in Tumor Metabolism, Tumorigenesis, and Apoptosis
Dang, C. V., Lewis, B. C., Dolde, C. E., Dang, G., & Shim, H. (1997) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1022446730452 · Cited by 125
Godschalk, R., van Schooten, F., & Bartsch, H. (2003) · BMB Reports · doi:10.5483/bmbrep.2003.36.1.001 · Cited by 131
Gene-Targeting of Phd2 Improves Tumor Response to Chemotherapy and Prevents Side-Toxicity
de Oliveira, R. L., Deschoemaeker, S., Henze, A., Debackere, K., Finisguerra, V., Takeda, Y., Roncal, C., Dettori, D., Tack, E., Jönsson, Y., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.06.028 · Cited by 125
Adaptation of iron requirement to hypoxic conditions at high altitude
Gassmann, M., & Muckenthaler, M. U. (2015) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00248.2015 · Cited by 128
Review: Ischemia Reperfusion Injury—A Translational Perspective in Organ Transplantation
Renaldo, A., Sánchez-Tarjuelo, R., Cravedi, P., Ochando, J., & López‐Hoyos, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228549 · Cited by 126
Differential activation of vascular genes by hypoxia in primary endothelial cells
Nilsson, I., Shibuya, M., & Wennström, S. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.06.005 · Cited by 125
Iron Regulatory Proteins: From Molecular Mechanisms to Drug Development
Recalcati, S., Minotti, G., & Cairo, G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2983 · Cited by 127
Hypoxia and the regulation of gene expression
Gleadle, J., & Ratcliffe, P. J. (1998) · Molecular Medicine Today · doi:10.1016/s1357-4310(97)01198-2 · Cited by 124
Minchenko, О. H., & Caro, J. (2000) · Molecular and Cellular Biochemistry · doi:10.1023/a:1007042729486 · Cited by 122
Oxygen sensing and oxidant/redox-related pathways
Haddad, J. J. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.02.162 · Cited by 123
Caveolin-1: a critical regulator of lung injury
Jin, Y., Lee, S., Minshall, R. D., & Choi, A. M. K. (2010) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00170.2010 · Cited by 120
Self-citationMense, S. M., Sengupta, A., Zhou, M., Lan, C., Bentsman, G., Volsky, D. J., & Li, Z. (2006) · Physiological Genomics · doi:10.1152/physiolgenomics.00315.2005 · Cited by 124
Regulation of Cyclooxygenase-2 by Hypoxia and Peroxisome Proliferators in the Corneal Epithelium
Bonazzi, A., Mastyugin, V., Mieyal, P. A., Dunn, M. W., & Schwartzman, M. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.4.2837 · Cited by 120
Xiao, H., Gu, Z.-Y., Wang, G., & Zhao, T. (2013) · International Journal of Medical Sciences · doi:10.7150/ijms.5630 · Cited by 125
Medina, M. V., Sapochnik, D., Solá, M. E. G., & Coso, O. A. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7991 · Cited by 119
Regulatory role of heme oxygenase 1 in inflammation of rheumatoid arthritis
Kobayashi, H., Takeno, M., Saito, T., Takeda, Y., Kirino, Y., Noyori, K., Hayashi, T., Ueda, A., & Ishigatsubo, Y. (2006) · Arthritis & Rheumatism · doi:10.1002/art.21754 · Cited by 119
Jögi, A., Vallon‐Christersson, J., Mengelbier, L. H., Axelson, H., Borg, Å., & Påhlman, S. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.01.013 · Cited by 120
Oxygen-sensing mechanisms across eukaryotic kingdoms and their roles in complex multicellularity
Hammarlund, E. U., Flashman, E., Mohlin, S., & Licausi, F. (2020) · Science · doi:10.1126/science.aba3512 · Cited by 120
Induction of T-type Calcium Channel Gene Expression by Chronic Hypoxia
Toro, R. D., Levitsky, K. L., López‐Barneo, J., & Chiara, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212576200 · Cited by 118
Regulation of Cardiovascular Development and Physiology by Hypoxia‐Inducible Factor 1a
Semenza, G. L., Agani, F. H., Iyer, N. V., Kotch, L. E., Laughner, E., Leung, S., & Yu, A. Y. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb09241.x · Cited by 116
Self-citationAnemia of Chronic Diseases: Wider Diagnostics—Better Treatment?
Wiciński, M., Liczner, G., Cadelski, K., Kołnierzak, T., Nowaczewska, M., & Malinowski, B. (2020) · Nutrients · doi:10.3390/nu12061784 · Cited by 122
HIF-1α and p53 Promote Hypoxia-Induced Delayed Neuronal Death in Models of CNS Ischemia
Halterman, M. W., & Federoff, H. J. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7160 · Cited by 114
Induction of heme oxygenase-1 by hypoxia and free radicals in human dermal fibroblasts
Panchenko, M. V., Farber, H. W., & Korn, J. H. (2000) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2000.278.1.c92 · Cited by 113
Distler, J. H. W., Wenger, R. H., Gassmann, M., Kurowska, W., Astrid, H., Gay, S., & Distler, O. (2004) · Arthritis & Rheumatism · doi:10.1002/art.11425 · Cited by 112
Metadata
- Authors
- Lee, P. J., Jiang, B.-H., Chin, B. Y., Iyer, N. V., Alam, J., Semenza, G. L., & Choi, A. K.
- Affiliations
- Johns Hopkins University (US)
- Ochsner Medical Center (US)
- Corresponding author
- Alam, Jawed
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-02
- Volume
- 272
- Issue
- 9
- Pages
- 5375-5381
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2081635255
- Cited by
- 782
- References
- 50
- Citations by year
- 2026: 8 · 2025: 13 · 2024: 26 · 2023: 17 · 2022: 22 · 2021: 27 · 2020: 31 · 2019: 21 · 2018: 14 · 2017: 17 · 2016: 19 · 2015: 16 · 2014: 18 · 2013: 28 · 2012: 21
- FWCI
- 12.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- American Heart Association
- National Institutes of Health (5k11ag000516-03, 5r01dk043135-07)
- National Institute on Aging
- National Heart, Lung, and Blood Institute (R01HL055338)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- 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
- HIF-1, heme oxygenase-1, hypoxia, transcriptional activation, vascular smooth muscle cells, HIF-1α, ARNT, promoter regulation, hepatoma cells, oxygen deprivation
- MeSH terms
- Animals, Hypoxia, Base Sequence, Dactinomycin, DNA-Binding Proteins, Heme Oxygenase (Decyclizing), Molecular Sequence Data, Muscle, Smooth, Vascular, Nuclear Proteins, RNA, Messenger, Transcription Factors, Restriction Mapping, Transcriptional Activation, Gene Expression Regulation, Enzymologic, Rats, Sprague-Dawley, Helix-Loop-Helix Motifs, Mice, Rats, Hypoxia-Inducible Factor 1, Hypoxia-Inducible Factor 1, alpha Subunit
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
