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Oxygen-dependent regulation of mitochondrial respiration by hypoxia-inducible factor 1
Abstract
The survival of metazoan organisms is dependent upon the utilization of O2 as a substrate for COX (cytochrome c oxidase), which constitutes Complex IV of the mitochondrial respiratory chain. Premature transfer of electrons, either at Complex I or at Complex III, results in the increased generation of ROS (reactive oxygen species). Recent studies have identified two critical adaptations that may function to prevent excessive ROS production in hypoxic cells. First, expression of PDK1 [PDH (pyruvate dehydrogenase) kinase 1] is induced. PDK1 phosphorylates and inactivates PDH, the mitochondrial enzyme that converts pyruvate into acetyl-CoA. In combination with the hypoxia-induced expression of LDHA (lactate dehydrogenase A), which converts pyruvate into lactate, PDK1 reduces the delivery of acetyl-CoA to the tricarboxylic acid cycle, thus reducing the levels of NADH and FADH2 delivered to the electron-transport chain. Secondly, the subunit composition of COX is altered in hypoxic cells by increased expression of the COX4-2 subunit, which optimizes COX activity under hypoxic conditions, and increased degradation of the COX4-1 subunit, which optimizes COX activity under aerobic conditions. Hypoxia-inducible factor 1 controls the metabolic adaptation of mammalian cells to hypoxia by activating transcription of the genes encoding PDK1, LDHA, COX4-2 and LON, a mitochondrial protease that is required for the degradation of COX4-1. COX subunit switching occurs in yeast, but by a completely different regulatory mechanism, suggesting that selection for O2-dependent homoeostatic regulation of mitochondrial respiration is ancient and likely to be shared by all eukaryotic organisms.
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“For example, H2O2-induced oxidation of a cysteine residue located in its catalytic site precisely and rapidly inhibits tyrosine phosphatase (278, 315).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [278]
In the citing paper
“Mitochondria are essential regulators of cellular bioenergetics that respond to changes in environmental stimuli, such as hormones, nutrients, and oxygen tension (47, 94, 99, 109, 290, 301, 385).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [385]
In the citing paper
“HIF-1 coordinately upregulates many genes to regulate metabolism, energy production, and mitochondrial function (385).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [385]
In the citing paper
“Nonetheless, experimental evidence suggests that enhanced ROS production is not a sustained event in hypoxia (69, 385).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [385]
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Cites
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
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 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
Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1
Forsythe, J. A., Jiang, B.-H., Iyer, N. V., Agani, F., Leung, S. W., Koos, R. D., & Semenza, G. L. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.9.4604 · Cited by 3,981
Self-citationKim, J.-W., Tchernyshyov, I., Semenza, G. L., & Dang, C. V. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.002 · Cited by 3,905
Self-citationEpstein, 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
Semenza, G. L., & Wang, G. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5447 · Cited by 2,617
Self-citationProgenitor cell trafficking is regulated by hypoxic gradients through HIF-1 induction of SDF-1
Ceradini, D. J., Kulkarni, A. R., Callaghan, M. J., Tepper, O. M., Bastidas, N., Kleinman, M. E., Capla, J. M., Galiano, R. D., Levine, J. P., & Gurtner, G. C. (2004) · Nature Medicine · doi:10.1038/nm1075 · Cited by 2,600
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
Role of HIF-1α in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis
Carmeliet, P., Dor, Y., Herbert, J.-M., Fukumura, D., Brusselmans, K., Dewerchin, M., Neeman, M., Bono, F., Abramovitch, R., Maxwell, P., et al. (1998) · Nature · doi:10.1038/28867 · Cited by 2,502
Cellular and developmental control of O 2 homeostasis by hypoxia-inducible factor 1α
Iyer, N. V., Kotch, L. E., Agani, F., Leung, S. W., Laughner, E., Wenger, R. H., Gassmann, M., Gearhart, J. D., Lawler, A. M., Yu, A. Y., et al. (1998) · Genes & Development · doi:10.1101/gad.12.2.149 · Cited by 2,476
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Brahimi-Horn, M. C., Chiche, J., & Pouysségur, J. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-007-0281-3 · Cited by 765
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Eales, K. L., Hollinshead, K. E. R., & Tennant, D. A. (2016) · Oncogenesis · doi:10.1038/oncsis.2015.50 · Cited by 724
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Wallace, D. C., Fan, W., & Procaccio, V. (2010) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092314 · Cited by 747
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Ganapathy, V., Thangaraju, M., & Prasad, P. D. (2008) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2008.09.005 · Cited by 724
Chan, S. Y., Zhang, Y.-Y., Hemann, C., Mahoney, C. E., Zweier, J. L., & Loscalzo, J. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.08.015 · Cited by 702
“Thus, these coordinated changes allow HIF-1a to manipulate multiple targets and ensure precise, fail-safe control over energy production and cellular survival during hypoxic stress (Semenza, 2007).”
InfluentialSeyfried, T. N., & Shelton, L. M. (2010) · Nutrition & Metabolism · doi:10.1186/1743-7075-7-7 · Cited by 675
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Fuhrmann, D. C., & Brüne, B. (2017) · Redox Biology · doi:10.1016/j.redox.2017.02.012 · Cited by 665
Mitochondria in cancer cells: what is so special about them?
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Hypoxia and mitochondrial oxidative metabolism
Solaini, G., Baracca, A., Lenaz, G., & Sgarbi, G. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.011 · Cited by 628
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Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588
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Cesarz, Z., & Tamama, K. (2016) · Stem Cells International · doi:10.1155/2016/9176357 · Cited by 475
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Schwartz, A. L., & Ciechanover, A. J. (2008) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.051208.165340 · Cited by 498
Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471
Benita, Y., Kikuchi, H., Smith, A. D., Zhang, M. Q., Chung, D. C., & Xavier, R. J. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp425 · Cited by 485
What is really dangerous: anaemia or transfusion?
Shander, A., Javidroozi, M., Ozawa, S. J., & Hare, G. M. T. (2011) · British Journal of Anaesthesia · doi:10.1093/bja/aer350 · Cited by 460
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Wheaton, W. W., & Chandel, N. S. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00485.2010 · Cited by 426
Puisségur, M.-P., Mazure, N. M., Bertero, T., Pradelli, L. A., Grosso, S., Robbe-Sermesant, K., Maurin, T., Lebrigand, K., Cardinaud, B., Hofman, V., et al. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.119 · Cited by 430
Redzic, Z. B. (2011) · Fluids and Barriers of the CNS · doi:10.1186/2045-8118-8-3 · Cited by 455
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Ohta, A. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00109 · Cited by 385
Scarpulla, R. C. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.006 · Cited by 401
Hypoxia or in situ normoxia: The stem cell paradigm
Ivanovic, Z. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21690 · Cited by 406
Mustroph, A., Lee, S. C., Oosumi, T., Zanetti, M. E., Yang, H., Ma, K., Yaghoubi-Masihi, A., Fukao, T., & Bailey-Serres, J. N. (2010) · PLANT PHYSIOLOGY · doi:10.1104/pp.109.151845 · Cited by 378
MiR-210 – micromanager of the hypoxia pathway
Huang, X., Le, Q., & Giaccia, A. J. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.03.004 · Cited by 376
MicroRNA-210: A unique and pleiotropic hypoxamir
Chan, S. Y., & Loscalzo, J. (2010) · Cell Cycle · doi:10.4161/cc.9.6.11006 · Cited by 361
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Albadari, N. G., Deng, S., & Li, W. (2019) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2019.1613370 · Cited by 365
Beyer, S., Kristensen, M. M., Jensen, K. S., Johansen, J. V., & Staller, P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804578200 · Cited by 346
Favaro, E., Ramachandran, A., McCormick, R., Gee, H., Blancher, C., Crosby, M., Devlin, C., Blick, C., Buffa, F., Li, J.-L., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010345 · Cited by 324
“An emerging paradigm in hypoxia is that mitochondria produce reactive oxygen species, mediated by electron transport continuing in hypoxia [3].”
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Vachharajani, V., Liu, T., Wang, X., Hoth, J. J., Yoza, B. K., & McCall, C. E. (2016) · Journal of Immunology Research · doi:10.1155/2016/8167273 · Cited by 333
Yuan, G., Nanduri, J., Khan, S. A., Semenza, G. L., & Prabhakar, N. R. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21537 · Cited by 324
Self-citationMitochondrial gateways to cancer
Galluzzi, L., Morselli, E., Kepp, O., Vitale, I., Rigoni, A., Vacchelli, E., Michaud, M., Zischka, H., Castedo, M., & Kroemer, G. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.08.002 · Cited by 303
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Thompson, L. P., & Al-Hasan, Y. M. (2012) · Journal of Pregnancy · doi:10.1155/2012/582748 · Cited by 313
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Taylor, C. T. (2008) · Biochemical Journal · doi:10.1042/bj20071249 · Cited by 298
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Optical probes and techniques for O2 measurement in live cells and tissue
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Oxidative phosphorylation in cancer cells
Solaini, G., Sgarbi, G., & Baracca, A. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.09.003 · Cited by 233
Waves of gene regulation suppress and then restore oxidative phosphorylation in cancer cells
Smolková, K., Plecitá‐Hlavatá, L., Bellancé, N., Bénard, G., Rossignol, R., & Ježek, P. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.05.003 · Cited by 232
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Koyasu, S., Kobayashi, M., Gotö, Y., Hiraoka, M., & Harada, H. (2017) · Cancer Science · doi:10.1111/cas.13483 · Cited by 233
The Warburg effect and mitochondrial stability in cancer cells
Gogvadze, V. G., Zhivotovsky, B., & Orrenius, S. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.12.004 · Cited by 235
The role of declining adaptive homeostasis in ageing
Pomatto, L. C. D., & Davies, K. J. A. (2017) · The Journal of Physiology · doi:10.1113/jp275072 · Cited by 231
Oxidative Stress and MicroRNAs in Vascular Diseases
Magenta, A., Greco, S., Gaetano, C., & Martelli, F. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140917319 · Cited by 198
Regulation of respiration in plants: A role for alternative metabolic pathways
van Dongen, J. T., Gupta, K. J., Ramírez-Aguilar, S. J., Araújo, W. L., Nunes‐Nesi, A., & Fernie, A. R. (2010) · Journal of Plant Physiology · doi:10.1016/j.jplph.2010.11.004 · Cited by 194
Hypoxia and Adipocyte Physiology: Implications for Adipose Tissue Dysfunction in Obesity
Trayhurn, P. (2014) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071812-161156 · Cited by 194
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Telarović, I., Wenger, R. H., & Pruschy, M. N. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02000-x · Cited by 208
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Narsai, R., Rocha, M., Geigenberger, P., Whelan, J., & van Dongen, J. T. (2011) · New Phytologist · doi:10.1111/j.1469-8137.2010.03589.x · Cited by 185
Reactive oxygen and nitrogen species in pulmonary hypertension
Tabima, D. M., Frizzell, S. A., & Gladwin, M. T. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.041 · Cited by 194
Strogolova, V., Furness, A. I., Robb-McGrath, M., Garlich, J., & Stuart, R. A. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06369-11 · Cited by 185
Regulation of the Hypoxia-Inducible Factor (HIF) by Pro-Inflammatory Cytokines
Malkov, M. I., Lee, C. T., & Taylor, C. T. (2021) · Cells · doi:10.3390/cells10092340 · Cited by 190
Regulation of human metabolism by hypoxia-inducible factor
Formenti, F., Constantin‐Teodosiu, D., Emmanuel, Y., Cheeseman, J., Dorrington, K. L., Edwards, L. M., Humphreys, S. M., Lappin, T. R. J., McMullin, M. F., McNamara, C., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002339107 · Cited by 185
The effects of baicalein and baicalin on mitochondrial function and dynamics: A review
de Oliveira, M. R., Nabavi, S. F., Habtemariam, S., Orhan, İ., Daglia, M., & Nabavi, S. M. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.08.021 · Cited by 181
The Role of Osteoclast Energy Metabolism in the Occurrence and Development of Osteoporosis
Da, W., Tao, L., & Zhu, Y. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.675385 · Cited by 185
Maftouh, M., Avan, A., Sciarrillo, R., Granchi, C., Leon, L., Rani, R., Funel, N., Smid, K., Honeywell, R. J., Boggi, U., et al. (2013) · British Journal of Cancer · doi:10.1038/bjc.2013.681 · Cited by 183
Regulation of respiration when the oxygen availability changes
Gupta, K. J., Zabalza, A., & van Dongen, J. T. (2009) · Physiologia Plantarum · doi:10.1111/j.1399-3054.2009.01253.x · Cited by 179
Rapisarda, A., Hollingshead, M., Uranchimeg, B., Bonomi, C. A., Borgel, S. D., Carter, J. P., Gehrs, B., Raffeld, M., Kinders, R. J., Parchment, R., et al. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-0274 · Cited by 171
Suzuki, S. W., Onodera, J., & Ohsumi, Y. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017412 · Cited by 173
Molecular determinants of brown adipocyte formation and function: Figure 1.
Farmer, S. R. (2008) · Genes & Development · doi:10.1101/gad.1681308 · Cited by 165
Chung, S. S., Arrell, D. K., Faustino, R. S., Terzic, A., & Dzeja, P. P. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.12.014 · Cited by 164
Pyrimidine Biosynthesis Links Mitochondrial Respiration to the P53 Pathway
Khutornenko, A. A., Roudko, V. V., Chernyak, B. V., Vartapetian, A. B., Chumakov, P. M., & Evstafieva, A. G. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910885107 · Cited by 162
Molecular Mechanism of Proton Translocation by Cytochrome c Oxidase
Belevich, I. N., & Verkhovsky, M. I. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1705 · Cited by 160
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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
Mitochondria and Cancer: A Growing Role in Apoptosis, Cancer Cell Metabolism and Dedifferentiation
Scatena, R. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2869-1_13 · Cited by 152
Shander, A., Javidroozi, M., Naqvi, S., Aregbeyen, O., Caylan, M., Demir, S., & Juhl, A. (2014) · Transfusion · doi:10.1111/trf.12565 · Cited by 141
Nitric oxide, apoptosis and macrophage polarization during tumor progression
Weigert, A., & Brüne, B. (2008) · Nitric Oxide · doi:10.1016/j.niox.2008.04.021 · Cited by 150
Wang, B., Wood, I. S., & Trayhurn, P. (2008) · Journal of Endocrinology · doi:10.1677/joe-08-0156 · Cited by 153
Moderate Hypoxia Potentiates Interleukin-1β Production in Activated Human Macrophages
Folco, E. J. E., Sukhova, G. K., Quillard, T., & Libby, P. (2014) · Circulation Research · doi:10.1161/circresaha.115.304437 · Cited by 148
Ferini‐Strambi, L., Walters, A. S., & Sica, D. A. (2013) · Journal of Neurology · doi:10.1007/s00415-013-7065-1 · Cited by 145
Hypoxia inducible factor (HIF) in the tumor microenvironment: friend or foe?
Huang, Y., Lin, D., & Taniguchi, C. M. (2017) · Science China Life Sciences · doi:10.1007/s11427-017-9178-y · Cited by 150
Hypoglycemia and the Origin of Hypoxia-Induced Reduction in Human Fetal Growth
Zamudio, S., Torricos, T., Fik, E., Oyala, M., Echalar, L., Pullockaran, J., Tutino, E., Martin, B., Belliappa, S., Balanza, E., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008551 · Cited by 141
Nitrite–nitric oxide control of mitochondrial respiration at the frontier of anoxia
Benamar, A., Rolletschek, H., Borisjuk, L., Avelange‐Macherel, M., Curien, G., Mostefai, H. A., Andriantsitohaina, R., & Macherel, D. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.06.002 · Cited by 144
Metabolic rate depression: the biochemistry of mammalian hibernation.
Storey, K. B., & Storey, J. M. (2010) · PubMed · Cited by 139
Baracca, A., Chiaradonna, F., Sgarbi, G., Solaini, G., Alberghina, L., & Lenaz, G. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.11.006 · Cited by 143
Human placental glucose transport in fetoplacental growth and metabolism
Illsley, N. P., & Baumann, M. U. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.12.010 · Cited by 145
Rani, R., & Kumar, V. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00168 · Cited by 136
Oxygen dependence of metabolic fluxes and energy generation of Saccharomyces cerevisiae CEN.PK113-1A
Jouhten, P., Rintala, E., Huuskonen, A., Tamminen, A., Toivari, M., Wiebe, M., Ruohonen, L., Penttilä, M., & Maaheimo, H. (2008) · BMC Systems Biology · doi:10.1186/1752-0509-2-60 · Cited by 131
Metabolic Tumor Imaging Using Magnetic Resonance Spectroscopy
Glunde, K., & Bhujwalla, Z. M. (2011) · Seminars in Oncology · doi:10.1053/j.seminoncol.2010.11.001 · Cited by 135
The Key Role of Nitric Oxide in Hypoxia: Hypoxic Vasodilation and Energy Supply–Demand Matching
Umbrello, M., Dyson, A., Feelisch, M., & Singer, M. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4979 · Cited by 138
Intestinal hypoxia and hypoxia-induced signalling as therapeutic targets for IBD
Welden, S. V., Selfridge, A. C., & Hindryckx, P. (2017) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2017.101 · Cited by 128
PGC-1α is Dispensable for Exercise-Induced Mitochondrial Biogenesis in Skeletal Muscle
Rowe, G. C., El‐Khoury, R., Patten, I. S., Rustin, P., & Arany, Z. P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041817 · Cited by 132
Proteins modulation in human skeletal muscle in the early phase of adaptation to hypobaric hypoxia
Viganò, A., Ripamonti, M., Palma, S. D., Capitanio, D., Vasso, M., Wait, R., Lundby, C., Cerretelli, P., & Gelfi, C. (2008) · PROTEOMICS · doi:10.1002/pmic.200800232 · Cited by 126
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Metadata
- Authors
- Semenza, G. L.
- Affiliations
- Johns Hopkins University (US)
- Corresponding author
- Semenza, Gregg L.
- ORCID
- Semenza, Gregg L.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2007-06-13
- Volume
- 405
- Issue
- 1
- Pages
- 1-9
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1799768544
- Cited by
- 541
- References
- 113
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 15 · 2023: 16 · 2022: 19 · 2021: 37 · 2020: 25 · 2019: 27 · 2018: 29 · 2017: 27 · 2016: 29 · 2015: 29 · 2014: 29 · 2013: 36 · 2012: 37
- FWCI
- 3.75
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Journal (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (n01hv28180-13-0-0)
- National Heart, Lung, and Blood Institute (N01 HV-28180, R01HL055338)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- HIF-1, mitochondrial respiration, cytochrome c oxidase, PDK1, pyruvate dehydrogenase, LDHA, reactive oxygen species, electron transport chain, TCA cycle, Lon protease, oxygen homeostasis
- MeSH terms
- Pyruvate Dehydrogenase Acetyl-Transferring Kinase, Electron Transport Complex IV, Electron Transport, Gene Expression Regulation, Glucose, Glycolysis, Homeostasis, Mitochondria, Oxidative Phosphorylation, Oxygen, Protein Kinases, Protein Serine-Threonine Kinases, Cell Respiration, Hypoxia-Inducible Factor 1
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