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2-Oxoglutarate-dependent dioxygenases are sensors of energy metabolism, oxygen availability, and iron homeostasis: potential role in the regulation of aging process
Open accessAbstract
Recent studies have revealed that the members of an ancient family of nonheme Fe(2+)/2-oxoglutarate-dependent dioxygenases (2-OGDO) are involved in the functions associated with the aging process. 2-Oxoglutarate and O2 are the obligatory substrates and Fe(2+) a cofactor in the activation of 2-OGDO enzymes, which can induce the hydroxylation of distinct proteins and the demethylation of DNA and histones. For instance, ten-eleven translocation 1-3 (TET1-3) are the demethylases of DNA, whereas Jumonji C domain-containing histone lysine demethylases (KDM2-7) are the major epigenetic regulators of chromatin landscape, known to be altered with aging. The functions of hypoxia-inducible factor (HIF) prolyl hydroxylases (PHD1-3) as well as those of collagen hydroxylases are associated with age-related degeneration. Moreover, the ribosomal hydroxylase OGFOD1 controls mRNA translation, which is known to decline with aging. 2-OGDO enzymes are the sensors of energy metabolism, since the Krebs cycle intermediate 2-oxoglutarate is an activator whereas succinate and fumarate are the potent inhibitors of 2-OGDO enzymes. In addition, O2 availability and iron redox homeostasis control the activities of 2-OGDO enzymes in tissues. We will briefly elucidate the catalytic mechanisms of 2-OGDO enzymes and then review the potential functions of the above-mentioned 2-OGDO enzymes in the control of the aging process.
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“The cause of these so-called 2-hydroxyglutaric acidurias (2HGAs) was attributed to germline mutations in L-2-HG dehydrogenase (L2HGDH) and D-2-HG dehydrogenase (D2HGDH), the mitochondrial enzymes responsible for the conversion of 2-HG to α-KG and thus its breakdown107-109.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [109]
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1 retracted
Gilkes, D. M., Bajpai, S. K., Chaturvedi, P., Wirtz, D., & Semenza, G. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442939 · Cited by 473
RetractedRepertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756
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
Conversion of 5-Methylcytosine to 5-Hydroxymethylcytosine in Mammalian DNA by MLL Partner TET1
Tahiliani, M., Koh, K. P., Shen, Y., Pastor, W. A., Bandukwala, H., Brudno, Y., Agarwal, S., Iyer, L. M., Liu, D. R., Aravind, L., et al. (2009) · Science · doi:10.1126/science.1170116 · Cited by 5,836
Chen, X., Xiu, M., Xing, J., Yu, S., Min, D., & Guo, F. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479439 · Cited by 5,760
Cancer-associated IDH1 mutations produce 2-hydroxyglutarate
Dang, L., White, D. W., Gross, S., Bennett, B. D., Bittinger, M. A., Driggers, E. M., Fantin, V. R., Jang, H. G., Jin, S., Keenan, M. C., et al. (2009) · Nature · doi:10.1038/nature08617 · Cited by 4,154
Hypoxia-inducible factors in physiology and medicine
Semenza, G. L. (2012) · Cell · doi:10.1016/j.cell.2012.01.021 · Cited by 3,645
Epstein, A. C. R., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00507-4 · Cited by 3,333
Xu, W., Yang, H., Liu, Y., Yang, Y., Wang, P., Kim, S.-H., Ito, S., Yang, C., Wang, P., Xiao, M.-T., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2010.12.014 · Cited by 2,875
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
Hypoxia-inducible factors and the response to hypoxic stress
Majmundar, A. J., Wong, W. J., & Simon, M. C. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.022 · Cited by 2,380
Senescent cells, tumor suppression, and organismal aging: good citizens, bad neighbors
Campisi, J. (2005) · Cell · doi:10.1016/j.cell.2005.02.003 · Cited by 2,379
Histone methylation: a dynamic mark in health, disease and inheritance
Greer, E. L., & Shi, Y. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3173 · Cited by 2,241
Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-α prolyl hydroxylase
Selak, M. A., Armour, S. M., MacKenzie, E. D., Boulahbel, H., Watson, D. G., Mansfield, K. D., Pan, Y., Simon, M. C., Thompson, C. B., & Gottlieb, E. (2005) · Cancer Cell · doi:10.1016/j.ccr.2004.11.022 · Cited by 2,108
Oxygen sensing by HIF hydroxylases
Schofield, C. J., & Ratcliffe, P. J. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1366 · Cited by 2,068
Ward, P. S., Patel, J., Wise, D. R., Abdel-Wahab, O., Bennett, B. D., Coller, H. A., Cross, J. R., Fantin, V. R., Hedvat, C. V., Perl, A. E., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.01.020 · Cited by 2,020
Reductive glutamine metabolism by IDH1 mediates lipogenesis under hypoxia
Metallo, C. M., Gameiro, P. A., Bell, E. L., Mattaini, K. R., Yang, J., Hiller, K., Jewell, C. M., Johnson, Z. R., Irvine, D. J., Guarente, L., et al. (2012) · Nature · doi:10.1038/nature10602 · Cited by 1,791
TET enzymes, TDG and the dynamics of DNA demethylation
Kohli, R. M., & Zhang, Y. (2013) · Nature · doi:10.1038/nature12750 · Cited by 1,623
NF-κB links innate immunity to the hypoxic response through transcriptional regulation of HIF-1α
Rius, J., Guma, M., Schachtrup, C., Akassoglou, K., Zinkernagel, A. S., Nizet, V., Johnson, R. S., Haddad, G. G., & Karin, M. (2008) · Nature · doi:10.1038/nature06905 · Cited by 1,614
Lando, D., Peet, D. J., Gorman, J. J., Whelan, D. A., Whitelaw, M. L., & Bruick, R. K. (2002) · Genes & Development · doi:10.1101/gad.991402 · Cited by 1,550 · cited 1×
“[115] demonstrated that FIH-1 also was a 2-OGDO enzyme hydroxylating the asparagine residue”
BackgroundExtrachromosomal rDNA circles—a cause of aging in yeast
Sinclair, D. A., & Guarente, L. (1997) · Cell · doi:10.1016/s0092-8674(00)80493-6 · Cited by 1,500
Pyruvate Kinase M2 Is a PHD3-Stimulated Coactivator for Hypoxia-Inducible Factor 1
Luo, W., Hu, H., Chang, R., Zhong, J., Knabel, M., O'Meally, R., Cole, R. N., Pandey, A., & Semenza, G. L. (2011) · Cell · doi:10.1016/j.cell.2011.03.054 · Cited by 1,463
UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development
Agger, K., Cloos, P. A., Christensen, J. F., Pasini, D., Rose, S., Rappsilber, J., Issaeva, I., Canaani, E., Salcini, A. E., & Helin, K. (2007) · Nature · doi:10.1038/nature06145 · Cited by 1,392
Histone Lysine Methylation Dynamics: Establishment, Regulation, and Biological Impact
Black, J. C., Rechem, C. V., & Whetstine, J. R. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.006 · Cited by 1,391
Mahon, P. C., Hirota, K., & Semenza, G. L. (2001) · Genes & Development · doi:10.1101/gad.924501 · Cited by 1,385
Genetic pathways that regulate ageing in model organisms
Guarente, L., & Kenyon, C. J. (2000) · Nature · doi:10.1038/35041700 · Cited by 1,337
Reductive carboxylation supports growth in tumour cells with defective mitochondria
Mullen, A. R., Wheaton, W. W., Jin, E. S., Chen, P.-H., Sullivan, L. B., Cheng, T., Yang, Y., Linehan, W. M., Chandel, N. S., & DeBerardinis, R. J. (2012) · Nature · doi:10.1038/nature10642 · Cited by 1,328
JmjC-domain-containing proteins and histone demethylation
Klose, R. J., Kallin, E. M., & Zhang, Y. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1945 · Cited by 1,290
Xiao, M., Yang, H., Xu, W., Ma, S., Lin, H., Zhu, H., Liu, L., Liu, Y., Yang, C., Xu, Y., et al. (2012) · Genes & Development · doi:10.1101/gad.191056.112 · Cited by 1,188
The key role of anaplerosis and cataplerosis for citric acid cycle function
Owen, O. E., Kalhan, S. C., & Hanson, R. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.r200006200 · Cited by 1,172 · cited 1×
“, amino acid aminotransferases convert 2-oxoglutarate to glutamate and consequently glutamate can be metabolized to some other amino acids [29].”
BackgroundAppelhoff, R. J., Tian, Y.-M., Raval, R. R., Turley, H., Harris, A. L., Pugh, C. W., Ratcliffe, P. J., & Gleadle, J. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406026200 · Cited by 1,108
Christensen, B. C., Houseman, E. A., Marsit, C. J., Zheng, S., Wrensch, M., Wiemels, J. L., Nelson, H. H., Karagas, M. R., Padbury, J. F., Bueno, R., et al. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000602 · Cited by 1,102
Tanaka, M., Yamamoto, Y., Misawa, E., Nabeshima, K., Saito, M., Yamauchi, K., Abe, F., & Furukawa, F. (2016) · Skin Pharmacology and Physiology · doi:10.1159/000454718 · Cited by 1,092
Reversing DNA Methylation: Mechanisms, Genomics, and Biological Functions
Wu, H., & Zhang, Y. (2014) · Cell · doi:10.1016/j.cell.2013.12.019 · Cited by 1,065
Gao, X., Wu, G., Gu, X., Fu, L., & Mei, C. (2013) · Kidney & Blood Pressure Research · doi:10.1159/000355743 · Cited by 1,035
Kotake, Y., Nakagawa, T., Kitagawa, K., Suzuki, S., Liu, N., Kitagawa, M., & Xiong, Y. (2011) · Oncogene · doi:10.1038/onc.2010.568 · Cited by 1,001
Regulation of cellular iron metabolism
Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986
THE MAINTENANCE OF THE ACCURACY OF PROTEIN SYNTHESIS AND ITS RELEVANCE TO AGEING
Orgel, L. E. (1963) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.49.4.517 · Cited by 968
De Santa, F., Totaro, M. G., Prosperini, E., Notarbartolo, S., Testa, G., & Natoli, G. (2007) · Cell · doi:10.1016/j.cell.2007.08.019 · Cited by 965
Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes
Hausinger, R. P. (2004) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230490440541 · Cited by 937
Influence of Metabolism on Epigenetics and Disease
Kaelin, W. G., & McKnight, S. L. (2013) · Cell · doi:10.1016/j.cell.2013.03.004 · Cited by 920
Saito, M., & Marumo, K. (2009) · Osteoporosis International · doi:10.1007/s00198-009-1066-z · Cited by 914
Decreased Collagen Production in Chronologically Aged Skin
Varani, J., Dame, M. K., Rittie, L., Fligiel, S. E. G., Kang, S., Fisher, G. J., & Voorhees, J. J. (2006) · The American Journal of Pathology · doi:10.2353/ajpath.2006.051302 · Cited by 910
TETonic shift: biological roles of TET proteins in DNA demethylation and transcription
Pastor, W. A., Aravind, L., & Rao, A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3589 · Cited by 897 · cited 6×
“-dependent oxygenase domain-containing protein 1, P3H and P4H collagen prolyl 3-and 4-hydroxylases, PHD1-3 prolyl hydroxylase domain-containing proteins 1-3, ROS reactive oxygen species, TET1-3 ten-eleven translocation 1-3 maintenance of Fe 2? redox status.”
BackgroundInfluentialPollard, P. J., Brière, J. J., Alam, N. A., Barwell, J., Barclay, E., Wortham, N. C., Hunt, T., Mitchell, M., Olpin, S., Moat, S. J., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi227 · Cited by 865
Lifespan extension by conditions that inhibit translation in Caenorhabditis elegans
Hansen, M., Taubert, S., Crawford, D., Libina, N., Lee, S., & Kenyon, C. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2006.00267.x · Cited by 803
Interpreting the language of histone and DNA modifications
Rothbart, S. B., & Strahl, B. D. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.03.001 · Cited by 792
Cummins, E. P., Berra, E., Comerford, K. M., Ginouves, A., Fitzgerald, K. T., Seeballuck, F., Godson, C., Nielsen, J. E., Moynagh, P., Pouyssegur, J., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602235103 · Cited by 788
SDH mutations establish a hypermethylator phenotype in paraganglioma
Letouzé, E., Martinelli, C., Loriot, C., Burnichon, N., Abermil, N., Ottolenghi, C., Janin, M., Menara, M., Nguyen, A. T., Benit, P., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.04.018 · Cited by 776 · cited 1×
“Recent studies have revealed that distinct mutations in the SDH enzyme can provoke the accumulation of succinate and subsequently lead to carcinogenesis, probably due to the inhibition of TET enzymes since SDH mutations are associated with a robust hypermethylation of DNA [38, 39].”
BackgroundSirtuin 1 Modulates Cellular Responses to Hypoxia by Deacetylating Hypoxia-Inducible Factor 1α
Lim, J.-H., Lee, Y.-M., Chun, Y.-S., Chen, J., Kim, J.-E., & Park, J.-W. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.05.023 · Cited by 758
Bell, J. T., Tsai, P.-C., Yang, T.-P., Pidsley, R., Nisbet, J. P., Glass, D., Mangino, M., Zhai, G., Zhang, F., Valdes, A. M., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002629 · Cited by 700
Metabolic Regulation of Epigenetics
Lu, C., & Thompson, C. B. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.06.001 · Cited by 699
Erasing the methyl mark: histone demethylases at the center of cellular differentiation and diseasePreprint
Cloos, P. A., Christensen, J., Agger, K., & Helin, K. (2008) · Genes & Development · doi:10.1101/gad.1652908 · Cited by 679
Transgenerational epigenetic inheritance of longevity in Caenorhabditis elegans
Greer, E. L., Maures, T. J., Ucar, D., Hauswirth, A. G., Mancini, E., Lim, J. P., Benayoun, B. A., Shi, Y., & Brunet, A. (2011) · Nature · doi:10.1038/nature10572 · Cited by 660
Xu, Y., Wu, F., Tan, L., Kong, L., Xiong, L., Deng, J., Barbera, A. J., Zheng, L., Zhang, H., Huang, S., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.005 · Cited by 647
Dual functions of Tet1 in transcriptional regulation in mouse embryonic stem cells
Wu, H., D’Alessio, A. C., Ito, S., Xia, K., Wang, Z., Cui, K., Zhao, K., Eve Sun, Y., & Zhang, Y. (2011) · Nature · doi:10.1038/nature09934 · Cited by 646
Hypoxia-Inducible Factor 1 and Cardiovascular Disease
Semenza, G. L. (2013) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021113-170322 · Cited by 624
Yin, R., Mao, S.-Q., Zhao, B., Chong, Z., Yang, Y., Zhao, C., Zhang, D., Huang, H., Gao, J., Li, Z., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4028346 · Cited by 609
Wu, H., D’Alessio, A. C., Ito, S., Wang, Z., 崔凯荣, Zhao, K., Sun, Y. E., & Zhang, Y. (2011) · Genes & Development · doi:10.1101/gad.2036011 · Cited by 603
Passing the baton: the HIF switch
Koh, M. Y., & Powis, G. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.06.004 · Cited by 589
A cytosolic iron chaperone that delivers iron to ferritin
Shi, H., Bencze, K. Z., Stemmler, T. L., & Philpott, C. C. (2008) · Science · doi:10.1126/science.1157643 · Cited by 536
Inhibition of Hypoxia-inducible Factor (HIF) Hydroxylases by Citric Acid Cycle Intermediates
Koivunen, P., Hirsilä, M., Remes, A. M., Hassinen, I. E., Kivirikko, K. I., & Myllyharju, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610415200 · Cited by 521
Elastin and collagen fibre microstructure of the human aorta in ageing and disease: a review
Tsamis, A., Krawiec, J. T., & Vorp, D. A. (2013) · Journal of The Royal Society Interface · doi:10.1098/rsif.2012.1004 · Cited by 509
Land, S. C., & Tee, A. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611782200 · Cited by 507
Inhibition of mRNA translation extends lifespan in Caenorhabditis elegans
Pan, K. Z., Palter, J. E., Rogers, A. N., Olsen, A., Chen, D., Lithgow, G. J., & Kapahi, P. (2006) · Aging Cell · doi:10.1111/j.1474-9726.2006.00266.x · Cited by 500
5-Hydroxymethylcytosine is associated with enhancers and gene bodies in human embryonic stem cells
Stroud, H., Feng, S., Kinney, S. R. M., Pradhan, S., & Jacobsen, S. E. (2011) · Genome biology · doi:10.1186/gb-2011-12-6-r54 · Cited by 490
The Naked Mole-Rat: A New Long-Living Model for Human Aging Research
Buffenstein, R. (2005) · The Journals of Gerontology Series A · doi:10.1093/gerona/60.11.1369 · Cited by 474
Age-Specific Epigenetic Drift in Late-Onset Alzheimer's Disease
Wang, S.-C., Oelze, B., & Schumacher, A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002698 · Cited by 471
Crystal Structure of TET2-DNA Complex: Insight into TET-Mediated 5mC Oxidation
Hu, L., Li, Z., Cheng, J., Rao, Q., Gong, W., Liu, M., Shi, Y. G., Zhu, J., Wang, P., & Xu, Y. (2013) · Cell · doi:10.1016/j.cell.2013.11.020 · Cited by 467
The PHD finger: a versatile epigenome reader
Sánchez, R., & Zhou, M. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.03.005 · Cited by 457
Koivunen, P., Hirsilä, M., Günzler, V., Kivirikko, K. I., & Myllyharju, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312254200 · Cited by 447
Structural studies on 2-oxoglutarate oxygenases and related double-stranded β-helix fold proteins
Clifton, I. J., McDonough, M. A., Ehrismann, D., Kershaw, N. J., Granatino, N., & Schofield, C. J. (2006) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2006.01.024 · Cited by 444
Oncometabolites: linking altered metabolism with cancer
Yang, M. H., Soga, T., & Pollard, P. J. (2013) · Journal of Clinical Investigation · doi:10.1172/jci67228 · Cited by 441
Genetic links between diet and lifespan: shared mechanisms from yeast to humans
Bishop, N. A., & Guarente, L. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2188 · Cited by 426
Tissue type is a major modifier of the 5-hydroxymethylcytosine content of human genesPreprint
Nestor, C. E., Ottaviano, R., Reddington, J. P., Sproul, D., Reinhardt, D., Dunican, D. S., Katz, E., Dixon, J. M., Harrison, D. J., & Meehan, R. R. (2011) · Genome Research · doi:10.1101/gr.126417.111 · Cited by 415
Nitric Oxide Impairs Normoxic Degradation of HIF-1α by Inhibition of Prolyl Hydroxylases
Metzen, E., Zhou, J., Jelkmann, W., Fandrey, J., & Brüne, B. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-12-0791 · Cited by 414
Chromatin dynamics during cellular reprogramming
Apostolou, E., & Hochedlinger, K. (2013) · Nature · doi:10.1038/nature12749 · Cited by 414
Minor, E. A., Court, B. L., Young, J. I., & Wang, G. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.464800 · Cited by 413
Xia, X., Lemieux, M. E., Li, W., Carroll, J. S., Brown, M., Liu, X. S., & Kung, A. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810067106 · Cited by 410
Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes
Schofield, C. J., & Zhang, Z. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00036-6 · Cited by 408
Inhibition of 2-oxoglutarate dependent oxygenases
Rose, N. R., McDonough, M. A., King, O. N. F., Kawamura, A., & Schofield, C. J. (2011) · Chemical Society Reviews · doi:10.1039/c0cs00203h · Cited by 405
Evolution and diversity of the 2–oxoglutarate‐dependent dioxygenase superfamily in plants
Kawai, Y., Ono, E., & Mizutani, M. (2014) · The Plant Journal · doi:10.1111/tpj.12479 · Cited by 390
MARXSEN, J. H., STENGEL, P., DOEGE, K., HEIKKINEN, P., JOKILEHTO, T., WAGNER, T., JELKMANN, W., JAAKKOLA, P., & METZEN, E. (2004) · Biochemical Journal · doi:10.1042/bj20040620 · Cited by 386
Peterkofsky, B. (1991) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/54.6.1135s · Cited by 383
Distinct DNA methylation changes highly correlated with chronological age in the human brain
Hernandez, D. G., Nalls, M. A., Gibbs, J. R., Arepalli, S., van der Brug, M., Chong, S., Moore, M., Longo, D. L., Cookson, M., Traynor, B. J., et al. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddq561 · Cited by 382
Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)
McDonough, M. A., Li, V., Flashman, E., Chowdhury, R., Mohr, C., Liénard, B. M. R., Zondlo, J., Oldham, N. J., Clifton, I. J., Lewis, J. K., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601283103 · Cited by 370
Human high-altitude adaptation: forward genetics meets the HIF pathwayPreprint
Bigham, A. W., & Lee, F. S. (2014) · Genes & Development · doi:10.1101/gad.250167.114 · Cited by 364
MacKenzie, E. D., Selak, M. A., Tennant, D. A., Payne, L. J., Crosby, S., Frederiksen, C. M., Watson, D. G., & Gottlieb, E. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01927-06 · Cited by 359
Role of Vitamin C in the Function of the Vascular Endothelium
May, J. M., & Harrison, F. E. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5205 · Cited by 358
Killian, J. K., Kim, S. Y., Miettinen, M., Smith, C., Merino, M., Tsokos, M., Quezado, M., Smith, W. I., Jahromi, M. S., Xekouki, P., et al. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0092 · Cited by 356
Histone demethylase JMJD3 contributes to epigenetic control of INK4a/ARF by oncogenic RAS
Barradas, M., Anderton, E., Acosta, J. C., Li, S., Banito, A., Rodriguez-Niedenführ, M., Maertens, G., Banck, M., Zhou, M.-M., Walsh, M. J., et al. (2009) · Genes & Development · doi:10.1101/gad.511109 · Cited by 352
Hon, G. C., Song, C., Du, T., Jin, F., Selvaraj, S., Lee, A. Y., Yen, C., Ye, Z., Mao, S.-Q., Wang, B.-A., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.08.026 · Cited by 349
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
Dauer-independent insulin/IGF-1-signalling implicates collagen remodelling in longevity
Ewald, C. Y., Landis, J. N., Abate, J. P., Murphy, C. T., & Blackwell, T. K. (2014) · Nature · doi:10.1038/nature14021 · Cited by 331
Age-associated epigenetic drift: implications, and a case of epigenetic thrift?
Teschendorff, A. E., West, J., & Beck, S. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt375 · Cited by 330
Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity
Ng, S. S., Kavanagh, K. L., McDonough, M. A., Butler, D. S., Pilka, E. S., Liénard, B. M. R., Bray, J. E., Savitsky, P. A., Gileadi, O., von Delft, F., et al. (2007) · Nature · doi:10.1038/nature05971 · Cited by 329
Inhibition of oxygen sensors as a therapeutic strategy for ischaemic and inflammatory disease
Fraisl, P., Aragonés, J., & Carmeliet, P. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2761 · Cited by 326
Kivirikko, K. I., Myllylä, R., & Pihlajaniemi, T. (1989) · The FASEB Journal · doi:10.1096/fasebj.3.5.2537773 · Cited by 320
Regulation of Jumonji-domain-containing histone demethylases by hypoxia-inducible factor (HIF)-1α
Pollard, P. J., Loenarz, C., Mole, D. R., McDonough, M. A., Gleadle, J., Schofield, C. J., & Ratcliffe, P. J. (2008) · Biochemical Journal · doi:10.1042/bj20081238 · Cited by 298
Oxygen sensing and hypoxia signalling pathways in animals: The implications of physiology for cancer
Ratcliffe, P. J. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.251470 · Cited by 294
Oxygen Sensors at the Crossroad of Metabolism
Aragonés, J., Fraisl, P., Baes, M. I., & Carmeliet, P. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2008.10.001 · Cited by 293
Prolyl 4-hydroxylases and their protein disulfide isomerase subunit
Kivirikko, K. I., & Myllyharju, J. (1998) · Matrix Biology · doi:10.1016/s0945-053x(98)90009-9 · Cited by 285
Cockman, M. E., Lancaster, D. E., Stolze, I. P., Hewitson, K. S., McDonough, M. A., Coleman, M. L., Coles, C. H., Yu, X., Hay, R. T., Ley, S. C., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606877103 · Cited by 285
JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes
Frescas, D., Guardavaccaro, D., Bassermann, F., Koyama-Nasu, R., & Pagano, M. (2007) · Nature · doi:10.1038/nature06255 · Cited by 284
Heterochromatin formation promotes longevity and represses ribosomal RNA synthesis
Larson, K., Yan, S.-J., Tsurumi, A., Liu, J., Zhou, J., Gaur, K., Guo, D., Eickbush, T. H., & Li, W. X. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002473 · Cited by 284
Structural studies on human 2-oxoglutarate dependent oxygenases
McDonough, M. A., Loenarz, C., Chowdhury, R., Clifton, I. J., & Schofield, C. J. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.08.006 · Cited by 280
Zheng, X., Linke, S., Dias, J. M., Zheng, X., Gradin, K., Wallis, T. P., Hamilton, B. R., Gustafsson, M. V., Ruas, J. L., Wilkins, S. E., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711591105 · Cited by 271
Mechanism of the Prolyl Hydroxylase Reaction: 2. Kinetic Analysis of the Reaction Sequence
MYLLYLÄ, R., TUDERMAN, L., & KIVIRIKKO, K. I. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11889.x · Cited by 263
Hypoxia, hypoxia-inducible factors (HIF), HIF hydroxylases and oxygen sensing
Webb, J. D., Coleman, M. L., & Pugh, C. W. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0147-7 · Cited by 261
The hypoxia-inducible factors: key transcriptional regulators of hypoxic responses
Bracken, C. P., Whitelaw, M. L., & Peet, D. J. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-2370-y · Cited by 259
Jin, C., Li, J., Green, C. D., Yu, X., Tang, X., Han, D., Xian, B., Wang, D., Huang, X., Cao, X., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.07.001 · Cited by 258
Maures, T. J., Greer, E. L., Hauswirth, A. G., & Brunet, A. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00738.x · Cited by 256
Carcinogenic metals and the epigenome: understanding the effect of nickel, arsenic, and chromium
Chervona, Y., Arita, A., & Costa, M. (2012) · Metallomics · doi:10.1039/c2mt20033c · Cited by 245
Loenarz, C., Coleman, M. L., Boleininger, A., Schierwater, B., Holland, P. W. H., Ratcliffe, P. J., & Schofield, C. J. (2010) · EMBO Reports · doi:10.1038/embor.2010.170 · Cited by 239
PHD fingers in human diseases: Disorders arising from misinterpreting epigenetic marks
Baker, L. A., Allis, C. D., & Wang, G. G. (2008) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2008.07.004 · Cited by 227
Emerling, B. M., Weinberg, F. D., Liu, J.-L., Mak, T. W., & Chandel, N. S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706790105 · Cited by 220
Role of the jelly-roll fold in substrate binding by 2-oxoglutarate oxygenases
Aik, W. S., McDonough, M. A., Thalhammer, A., Chowdhury, R., & Schofield, C. J. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.10.001 · Cited by 219
Exposito, J., Cluzel, C., Garrone, R., & Lethias, C. (2002) · The Anatomical Record · doi:10.1002/ar.10162 · Cited by 213
Involvement of Hypoxia-Inducible Factor 1 in Human Cancer.
Semenza, G. L. (2002) · Internal Medicine · doi:10.2169/internalmedicine.41.79 · Cited by 211
The HIF-1 Hypoxia-Inducible Factor Modulates Lifespan in C. elegans
Zhang, Y., Shao, Z., Zhai, Z., Shen, C., & Powell-Coffman, J. A. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006348 · Cited by 211
Synthesis, modifications, and turnover of proteins during aging
Rattan, S. I. S. (1996) · Experimental Gerontology · doi:10.1016/0531-5565(95)02022-5 · Cited by 208
Lineage-specific distribution of high levels of genomic
Ruzov, A. S., Tsenkina, Y., Serio, A., Dudnakova, T., Fletcher, J. M., Bai, Y., Chebotareva, T., Pells, S., Hannoun, Z., Sullivan, G. J., et al. (2011) · Cell Research · doi:10.1038/cr.2011.113 · Cited by 206
Maynard, M. A., Evans, A. J., Hosomi, T., Hara, S., Jewett, M. A. S., & Ohh, M. (2005) · The FASEB Journal · doi:10.1096/fj.05-3788com · Cited by 205
Histone methylation makes its mark on longevity
Han, S., & Brunet, A. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.11.001 · Cited by 204
Activation of the HIF Prolyl Hydroxylase by the Iron Chaperones PCBP1 and PCBP2
Nandal, A., Ruiz, J. C., Subramanian, P., Ghimire-Rijal, S., Sinnamon, R. A., Stemmler, T. L., Bruick, R. K., & Philpott, C. C. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.015 · Cited by 204
Prolyl 3-Hydroxylase 1, Enzyme Characterization and Identification of a Novel Family of Enzymes
Vranka, J. A., Sakai, L. Y., & Bächinger, H. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312807200 · Cited by 200
Roles of jumonji and jumonji family genes in chromatin regulation and development
Takeuchi, T., Watanabe, Y., Takano‐Shimizu, T., & Kondo, S. (2006) · Developmental Dynamics · doi:10.1002/dvdy.20851 · Cited by 197
The DNMT3 Family of Mammalian De Novo DNA Methyltransferases
Chedin, F. L. (2011) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-387685-0.00007-x · Cited by 196
Chromatin remodeling in the aging genome of Drosophila
Wood, J. G., Hillenmeyer, S., Lawrence, C., Chang, C., Hosier, S., Lightfoot, W., Mukherjee, E., Jiang, N., Schorl, C., Brodsky, A. S., et al. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00624.x · Cited by 192
Tudor: a versatile family of histone methylation ‘readers’
Lu, R., & Wang, G. G. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.08.002 · Cited by 190
Chua, Y. L., Dufour, E., Dassa, E. P., Rustin, P., Jacobs, H. T., Taylor, C. T., & Hagen, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.158485 · Cited by 189
Neri, F., Incarnato, D., Krepelova, A., Rapelli, S., Pagnani, A., Zecchina, R., Parlato, C., & Oliviero, S. (2013) · Genome Biology · doi:10.1186/gb-2013-14-8-r91 · Cited by 179
Functional regulation of HIF‐1α under normoxia—is there more than post‐translational regulation?
Kuschel, A., Simon, P. D., & Tug, S. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22798 · Cited by 174
Hepcidin Is Involved in Iron Regulation in the Ischemic Brain
Ding, H., Yan, C.-Z., Shi, H., Zhao, Y., Chang, S., Yu, P., Wu, W., Zhao, C., Chang, Y., & Duan, X. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025324 · Cited by 172
ENZYMATIC HYDROXYLATION OF PROLINE AND LYSINE IN PROTOCOLLAGEN
Kivirikko, K. I., & Prockop, D. J. (1967) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.57.3.782 · Cited by 171
Leonardi, R., Subramanian, C., Jackowski, S., & Rock, C. O. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.c112.353946 · Cited by 171
The Roles of Jumonji-Type Oxygenases in Human Disease
Johansson, C., Tumber, A., Che, K., Cain, P., Nowak, R. P., Gileadi, C., & Oppermann, U. C. T. (2014) · Epigenomics · doi:10.2217/epi.13.79 · Cited by 167
Fitzpatrick, S. F., Tambuwala, M. M., Brüning, U., Schaible, B., Scholz, C. C., Byrne, A. T., O’Connor, A. E., Gallagher, W. M., Lenihan, C. R., Garvey, J., et al. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1002256 · Cited by 156
Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells
Cervera, A. M., Bayley, J.-P., Devilee, P., & McCreath, K. J. (2009) · Molecular Cancer · doi:10.1186/1476-4598-8-89 · Cited by 156
Regulatory role of HIF-1α in the pathogenesis of age-related macular degeneration (AMD)
Arjamaa, O., Nikinmaa, M., Salminen, A., & Kaarniranta, K. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.06.002 · Cited by 150
Self-citationChinopoulos, C. (2013) · Journal of Neuroscience Research · doi:10.1002/jnr.23196 · Cited by 148
Salminen, A., Kaarniranta, K., Hiltunen, M. O., & Kauppinen, A. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1182-x · Cited by 148
Self-citationThe FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity
Masson, N., Singleton, R. S., Sekirnik, R., Trudgian, D. C., Ambrose, L. J. A., Miranda, M. X., Tian, Y., Kessler, B. M., Schofield, C. J., & Ratcliffe, P. J. (2012) · EMBO Reports · doi:10.1038/embor.2012.9 · Cited by 148
Salminen, A., Kauppinen, A., Hiltunen, M. O., & Kaarniranta, K. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.05.004 · Cited by 145
Self-citationEmerging novel functions of the oxygen-sensing prolyl hydroxylase domain enzymes
Wong, B. W., Kuchnio, A., Brüning, U., & Carmeliet, P. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.10.004 · Cited by 144
Agherbi, H., Gaussmann-Wenger, A., Verthuy, C., Chasson, L., Serrano, M., & Djabali, M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005622 · Cited by 142
Shams, I., Avivi, A., & Nevo, E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403540101 · Cited by 140
Breathing-in epigenetic change with vitamin C
Monfort, A., & Wutz, A. (2013) · The EMBO Reports · doi:10.1038/embor.2013.29 · Cited by 140
Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy
Loenarz, C., Sekirnik, R., Thalhammer, A., Ge, W., Spivakovsky, E., Mackeen, M. M., McDonough, M. A., Cockman, M. E., Kessler, B. M., Ratcliffe, P. J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311750111 · Cited by 134
Hypoxia induces trimethylated H3 lysine 4 by inhibition of JARID1A demethylase
Zhou, X., Sun, H., Chen, H., Zavadil, J., Kluz, T., Arita, A., & Costa, M. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-2942 · Cited by 134
Zhao, B., Yang, Y., Wang, X., Chong, Z., Yin, R., Song, S.-H., Zhao, C., Li, C., Huang, H., Sun, B.-F., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1090 · Cited by 133
Flashman, E., Davies, S. L., Yeoh, K. K., & Schofield, C. J. (2010) · Biochemical Journal · doi:10.1042/bj20091609 · Cited by 133
Wu, H., & Zhang, Y. (2011) · Cell Cycle · doi:10.4161/cc.10.15.16930 · Cited by 132
Masters of Longevity: Lessons from Long-Lived Bivalves – A Mini-Review
Philipp, E. E. R., & Abele, D. (2009) · Gerontology · doi:10.1159/000221004 · Cited by 131
Schneider, M. A., Geyte, K. V., Fraisl, P., Kiss, J., Aragonés, J., Mazzone, M., Mairbäurl, H., Bock, K. D., Jeoung, N. H., Mollenhauer, M., et al. (2009) · Gastroenterology · doi:10.1053/j.gastro.2009.09.057 · Cited by 131
Ageing and the regulation of protein synthesis: a balancing act?
Tavernarakis, N. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.02.004 · Cited by 129
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
Ruotsalainen, H. J., Sipilä, L., Vapola, M. H., Sormunen, R. T., Salo, A. M., Uitto, L., Mercer, D. K., Robins, S. P., Risteli, M., Aszódi, A., et al. (2006) · Journal of Cell Science · doi:10.1242/jcs.02780 · Cited by 126
Oxygen Activation at Mononuclear Nonheme Iron Centers: A Superoxo Perspective
Mukherjee, A., Cranswick, M. A., Chakrabarti, M., Paine, T. K., Fujisawa, K., Münck, E., & QUE, L. J. (2010) · Inorganic Chemistry · doi:10.1021/ic901891n · Cited by 123
Singleton, R. S., Liu-Yi, P., Formenti, F., Ge, W., Sekirnik, R., Fischer, R., Adam, J., Pollard, P. J., Wolf, A., Thalhammer, A., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314482111 · Cited by 122
Hickok, J. R., Vasudevan, D., Antholine, W. E., & Thomas, D. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.432294 · Cited by 120
JmjC enzyme KDM2A is a regulator of rRNA transcription in response to starvation
Tanaka, Y., Okamoto, K., Teye, K., Umata, T., Yamagiwa, N., Suto, Y., Zhang, Y., & Tsuneoka, M. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.56 · Cited by 118
Kuiper, C., Dachs, G. U., Currie, M. J., & Vissers, M. C. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.01.033 · Cited by 117
Ye, S., Riplinger, C., Hansen, A., Krebs, C., Bollinger, J. M., Jr., & Neese, F. (2012) · Chemistry - A European Journal · doi:10.1002/chem.201102829 · Cited by 114
Myllylä, R., Wang, C., Heikkinen, J., Juffer, A. H., Lampela, O., Risteli, M., Ruotsalainen, H. J., Salo, A. M., & Sipilä, L. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21036 · Cited by 111
Putiri, E. L., Tiedemann, R. L., Thompson, J. J., Liu, C., Ho, T. H., Choi, J.-H., & Robertson, K. D. (2014) · Genome biology · doi:10.1186/gb-2014-15-6-r81 · Cited by 111
Ribosomal oxygenases are structurally conserved from prokaryotes to humans
Chowdhury, R., Sekirnik, R., Brissett, N. C., Krojer, T., Ho, C.-H., Ng, S. S., Clifton, I. J., Ge, W., Kershaw, N. J., Fox, G. C., et al. (2014) · Nature · doi:10.1038/nature13263 · Cited by 105
Heyn, H., Morán, S., & Esteller, M. (2012) · Epigenetics · doi:10.4161/epi.23366 · Cited by 105
The paradox of mitochondrial dysfunction and extended longevity
Munkácsy, E., & Rea, S. L. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.03.016 · Cited by 104
Stress resistance in long-lived mouse models
Murakami, S. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.06.061 · Cited by 104
Yu, C., Li, Y., Holmes, A., Szafranski, K., Faulkes, C. G., Coen, C. W., Buffenstein, R., Platzer, M., de Magalhães, J. P., & Church, G. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026729 · Cited by 103
Polycomb silencing: from linear chromatin domains to 3D chromosome folding
Cheutin, T., & Cavalli, G. (2014) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2013.11.016 · Cited by 102
Oxygen versus Reactive Oxygen in the Regulation of HIF-1α: The Balance Tips
Hagen, T. (2012) · Biochemistry Research International · doi:10.1155/2012/436981 · Cited by 100
Chromatin and oxygen sensing in the context of JmjC histone demethylases
Shmakova, A., Batie, M., Druker, J., & Rocha, S. (2014) · Biochemical Journal · doi:10.1042/bj20140754 · Cited by 99 · cited 1×
“The functional differences between KDMs can be attributed to the fact that the proteins of distinct KDM subgroups have unique binding domains, which target enzymes to specific complexes [9, 47, 96, 98].”
BackgroundGardi, C., Arezzini, B., Fortino, V., & Comporti, M. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01257-1 · Cited by 94
Vranka, J. A., Pokidysheva, E. N., Hayashi, L., Zientek, K. D., Mizuno, K., Ishikawa, Y., Maddox, K., Tufa, S. F., Keene, D. R., Klein, R. F., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.102228 · Cited by 94
Less is more: improving proteostasis by translation slow down
Sherman, M. Y., & Qian, S. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.09.003 · Cited by 93
HIF-1-Dependent Induction of Jumonji Domain-Containing Protein (JMJD) 3 under Hypoxic Conditions
Lee, H.-Y., Choi, K. Y., Oh, H., Park, Y.-K., & Park, H. (2014) · Molecules and Cells · doi:10.14348/molcells.2014.2250 · Cited by 86
Defective Tibetan PHD2 Binding to p23 Links High Altitude Adaption to Altered Oxygen Sensing
Song, D., Li, L.-S., Arsenault, P. R., Tan, Q., Bigham, A. W., Heaton-Johnson, K. J., Master, S. R., & Lee, F. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.541227 · Cited by 81
Hypoxia-inducible factor prolyl 4-hydroxylases: common and specific roles
Myllyharju, J., & Koivunen, P. (2013) · Biological Chemistry · doi:10.1515/hsz-2012-0328 · Cited by 80
Iron Homeostasis and Its Interaction with Prolyl Hydroxylases
Mole, D. R. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2790 · Cited by 80
The hypoxia-inducible factor HIF-1 functions as both a positive and negative modulator of aging
Leiser, S. F., & Kaeberlein, M. R. (2010) · Biological Chemistry · doi:10.1515/bc.2010.123 · Cited by 79
Risteli, J., & Kivirikko, K. I. (1976) · Biochemical Journal · doi:10.1042/bj1580361 · Cited by 78
Salo, A. M., Wang, C., Sipilä, L., Sormunen, R. T., Vapola, M. H., Kervinen, P., Ruotsalainen, H. J., Heikkinen, J., & Myllylä, R. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20596 · Cited by 76
Wehner, K. A., Schütz, S., & Sarnow, P. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01350-09 · Cited by 72
Oxidation by 2-oxoglutarate oxygenases: non-haem iron systems in catalysis and signalling
Hewitson, K. S., Granatino, N., Welford, R. W. D., McDonough, M. A., & Schofield, C. J. (2005) · Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences · doi:10.1098/rsta.2004.1540 · Cited by 64
Koch, S., Gonzalez, O. G., Assfalg, R., Schelling, A., Schäfer, P., Scharffetter‐Kochanek, K., & Iben, S. (2014) · Cell Cycle · doi:10.4161/cc.29018 · Cited by 61
The mitochondrial oxoglutarate carrier: from identification to mechanism
Monné, M., Miniero, D. V., Bisaccia, F., & Fiermonte, G. (2012) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-012-9475-7 · Cited by 59
Keeling, K. M., Salas-Marco, J., Osherovich, L. Z., & Bedwell, D. M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02448-05 · Cited by 58
Estarás, C., Fueyo, R., Akizu, N., Beltrán, S., & Martínez‐Balbás, M. A. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-07-0561 · Cited by 56
Rat Brain Protein Synthesis Declines During Postdevelopmental Aging
Dwyer, B. E., Fando, J. L., & Wasterlain, C. G. (1980) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1980.tb03717.x · Cited by 55
Investigations on the oxygen dependence of a 2-oxoglutarate histone demethylase
Sánchez‐Fernández, E. M., Tarhonskaya, H., Al‐Qahtani, K., Hopkinson, R. J., McCullagh, J., Schofield, C. J., & Flashman, E. (2012) · Biochemical Journal · doi:10.1042/bj20121155 · Cited by 55
Effects of the mitochondrial respiratory chain on longevity in C. elegans
Rabbitts, B. M., Sedensky, M. M., & Morgan, P. G. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.03.028 · Cited by 54
Triantafyllou, A., Liakos, P., Tsakalof, A. K., Chachami, G., Paraskeva, E., Molyvdas, P.-A., Georgatsou, E., Simos, G., & Bonanou, S. (2006) · Free Radical Research · doi:10.1080/10715760601055324 · Cited by 54
Katz, M. J., Acevedo, J. M., Loenarz, C., Galagovsky, D., Liu-Yi, P., Pérez-Pepe, M., Thalhammer, A., Sekirnik, R., Ge, W., Melani, M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314485111 · Cited by 52
Nijwening, J. H., Geutjes, E.-J., Bernards, R., & Beijersbergen, R. L. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025235 · Cited by 50
The regulation, localization, and functions of oxygen-sensing prolyl hydroxylase PHD3
Jaakkola, P., & Rantanen, K. (2013) · Biological Chemistry · doi:10.1515/hsz-2012-0330 · Cited by 50
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Metadata
- Authors
- Salminen, A., Kauppinen, A., & Kaarniranta, K.
- Affiliations
- University of Eastern Finland (FI)
- Corresponding author
- Kaarniranta, Kai
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2015-06-29
- Volume
- 72
- Issue
- 20
- Pages
- 3897-3914
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC11114064
- OpenAlex
- W1010999108
- Cited by
- 99
- References
- 216
- Citations by year
- 2026: 6 · 2025: 4 · 2024: 9 · 2023: 12 · 2022: 11 · 2021: 7 · 2020: 12 · 2019: 6 · 2018: 10 · 2017: 10 · 2016: 9 · 2015: 3
- FWCI
- 0.42
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cellular and Molecular Life Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Kuopion Yliopistollinen Sairaala
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- 2-oxoglutarate-dependent dioxygenase, aging, energy metabolism, oxygen availability, iron homeostasis, histone demethylation, DNA demethylation, mRNA translation, epigenetic regulation
- MeSH terms
- Aging, Animals, Hypoxia, Energy Metabolism, Homeostasis, Iron, Oxygen, Protein Biosynthesis, DNA Methylation, Epigenesis, Genetic, Dioxygenases
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