메뉴 건너뛰기




Volumn 2015, Issue , 2015, Pages

The Role of Oxygen Sensors, Hydroxylases, and HIF in Cardiac Function and Disease

Author keywords

[No Author keywords available]

Indexed keywords

CARDIOLOGY; DISEASES; HEART; OXYGEN SENSORS; PHYSIOLOGICAL MODELS; PROTEINS; SUBSTRATES;

EID: 84944246726     PISSN: 19420900     EISSN: 19420994     Source Type: Journal    
DOI: 10.1155/2015/676893     Document Type: Article
Times cited : (12)

References (137)
  • 1
    • 0003514452 scopus 로고    scopus 로고
    • World Health Organization, The Top 10 Causes of Death, Geneva, Switzerland
    • World Health Organization, The Top 10 Causes of Death, World Health Organization, Geneva, Switzerland, 2014, http: //www . who. int/mediacentre/factsheets/fs310/en/.
    • (2014) World Health Organization
  • 2
    • 84944237917 scopus 로고    scopus 로고
    • University TJH, ConditionsWe Treat: Coronary Artery Disease (Ischemic Heart Disease)
    • University TJH, ConditionsWe Treat: Coronary Artery Disease (Ischemic Heart Disease).
  • 3
    • 84872091789 scopus 로고    scopus 로고
    • Heart disease and stroke statistics-2013 update: A report from the American Heart Association
    • A. S. Go, D. Mozaffarian, V. L. Roger et al. , "Heart disease and stroke statistics-2013 update: A report from the American Heart Association," Circulation, vol. 127, no. 1,pp. e6-e245, 2013.
    • (2013) Circulation , vol.127 , Issue.1 , pp. e6-e245
    • Go, A.S.1    Mozaffarian, D.2    Roger, V.L.3
  • 5
    • 0032514228 scopus 로고    scopus 로고
    • Ventricularmyocytes are not terminally differentiated in the adult mammalian heart
    • P. Anversa and J. Kajstura, "Ventricularmyocytes are not terminally differentiated in the adult mammalian heart," Circulation Research, vol. 83, no. 1, pp. 1-14, 1998.
    • (1998) Circulation Research , vol.83 , Issue.1 , pp. 1-14
    • Anversa, P.1    Kajstura, J.2
  • 8
    • 14644442283 scopus 로고    scopus 로고
    • Oxygen, oxidative stress, hypoxia, and heart failure
    • F. J. Giordano, "Oxygen, oxidative stress, hypoxia, and heart failure," The Journal of Clinical Investigation, vol. 115, no. 3, pp. 500-508, 2005.
    • (2005) The Journal of Clinical Investigation , vol.115 , Issue.3 , pp. 500-508
    • Giordano, F.J.1
  • 10
    • 84944185086 scopus 로고    scopus 로고
    • Biomedical & pharmaceutical sciences with patient care correlations
    • R. Karimi, Biomedical & Pharmaceutical Sciences with Patient Care Correlations, Jones & Bartlett Learning, 2014.
    • (2014) Jones & Bartlett Learning
    • Karimi, R.1
  • 14
    • 0015292498 scopus 로고
    • Protocollagen proline hydroxylase activity in rat heart during experimental cardiac hypertrophy
    • S. Lindy, H. Turto, and J. Uitto, "Protocollagen proline hydroxylase activity in rat heart during experimental cardiac hypertrophy," Circulation Research, vol. 30, no. 2, pp. 205-209, 1972.
    • (1972) Circulation Research , vol.30 , Issue.2 , pp. 205-209
    • Lindy, S.1    Turto, H.2    Uitto, J.3
  • 15
    • 0035027828 scopus 로고    scopus 로고
    • Transcription factor HIF-1 is a necessary mediator of the pasteur effect in mammalian cells
    • T. N. Seagroves, H. E. Ryan, H. Lu et al. , "Transcription factor HIF-1 is a necessary mediator of the pasteur effect in mammalian cells," Molecular and Cellular Biology, vol. 21, no. 10, pp. 3436-3444, 2001.
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.10 , pp. 3436-3444
    • Seagroves, T.N.1    Ryan, H.E.2    Lu, H.3
  • 16
    • 0030659531 scopus 로고    scopus 로고
    • VSRC induces expression of hypoxia-inducible factor 1 (HIF-1) and transcription of genes encoding vascular endothelial growth factor and enolase 1: Involvement of HIF-1 in tumor progression
    • B. H. Jiang, F. Agani, A. Passaniti, and G. L. Semenza, "VSRC induces expression of hypoxia-inducible factor 1 (HIF-1) and transcription of genes encoding vascular endothelial growth factor and enolase 1: involvement of HIF-1 in tumor progression," Cancer Research, vol. 57, no. 23, pp. 5328-5335, 1997.
    • (1997) Cancer Research , vol.57 , Issue.23 , pp. 5328-5335
    • Jiang, B.H.1    Agani, F.2    Passaniti, A.3    Semenza, G.L.4
  • 17
    • 79953286300 scopus 로고    scopus 로고
    • Role of HIF-1in maternal hyperglycemia-induced embryonic vasculopathy
    • P. Yang and E. A. Reece, "Role of HIF-1in maternal hyperglycemia-induced embryonic vasculopathy," American Journal of Obstetrics and Gynecology, vol. 204, no. 4, pp. 332. e1-332. e7, 2011.
    • (2011) American Journal of Obstetrics and Gynecology , vol.204 , Issue.4 , pp. 332e1-332e7
    • Yang, P.1    Reece, E.A.2
  • 18
    • 0034682783 scopus 로고    scopus 로고
    • Hypoxia inducible factor-binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein
    • M. E. Cockman, N. Masson, D. R. Mole et al. , "Hypoxia inducible factor-binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein," The Journal of Biological Chemistry, vol. 275, no. 33, pp. 25733-25741, 2000.
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.33 , pp. 25733-25741
    • Cockman, M.E.1    Masson, N.2    Mole, D.R.3
  • 20
    • 0033776536 scopus 로고    scopus 로고
    • Ubiquitination of hypoxiainducible factor requires direct binding to the-domain of the vonHippel-Lindau protein
    • M. Ohh, C. W. Park,M. Ivan et al. , "Ubiquitination of hypoxiainducible factor requires direct binding to the-domain of the vonHippel-Lindau protein," Nature Cell Biology, vol. 2, no. 7,pp. 423-427, 2000.
    • (2000) Nature Cell Biology , vol.2 , Issue.7 , pp. 423-427
    • Ohh, M.1    Park, C.W.2    Ivan, M.3
  • 21
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: A novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity
    • P. C. Mahon, K. Hirota, and G. L. Semenza, "FIH-1: A novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity," Genes and Development, vol. 15, no. 20, pp. 2675-2686, 2001.
    • (2001) Genes and Development , vol.15 , Issue.20 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 22
    • 18544386401 scopus 로고    scopus 로고
    • Hypoxiainducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family
    • K. S. Hewitson, L. A. McNeill, M. V. Riordan et al. , "Hypoxiainducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family," Journal of Biological Chemistry, vol. 277, no. 29, pp. 26351-26355, 2002.
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.29 , pp. 26351-26355
    • Hewitson, K.S.1    McNeill, L.A.2    Riordan, M.V.3
  • 23
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • D. Lando, D. J. Peet, J. J. Gorman, D. A. Whelan,M. L. Whitelaw, and R. K. Bruick, "FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor," Genes and Development, vol. 16, no. 12, pp. 1466-1471, 2002.
    • (2002) Genes and Development , vol.16 , Issue.12 , pp. 1466-1471
    • Lando, D.1    Peet, D.J.2    Gorman, J.J.3    Whelan, D.A.4    Whitelaw, M.L.5    Bruick, R.K.6
  • 24
    • 4644370374 scopus 로고    scopus 로고
    • Signalling via the hypoxia-inducible factor-1alpha requires multiple posttranslationalmodifications
    • C. Brahimi-Horn, N. Mazure, and J. Pouysségur, "Signalling via the hypoxia-inducible factor-1alpha requires multiple posttranslationalmodifications," Cellular Signalling, vol. 17,no. 1, pp. 1-9, 2005.
    • (2005) Cellular Signalling , vol.17 , Issue.1 , pp. 1-9
    • Brahimi-Horn, C.1    Mazure, N.2    Pouysségur, J.3
  • 25
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • G. L. Semenza, "Targeting HIF-1 for cancer therapy," Nature Reviews Cancer, vol. 3, no. 10, pp. 721-732, 2003.
    • (2003) Nature Reviews Cancer , vol.3 , Issue.10 , pp. 721-732
    • Semenza, G.L.1
  • 26
    • 38449121857 scopus 로고    scopus 로고
    • Hypoxia-Inducible Factor (HIF)-1 regulatory pathway and its potential for therapeutic intervention in malignancy and ischemia
    • J. E. Ziello, I. S. Jovin, andY. Huang, "Hypoxia-Inducible Factor (HIF)-1 regulatory pathway and its potential for therapeutic intervention in malignancy and ischemia," Yale Journal of Biology and Medicine, vol. 80, no. 2, pp. 51-60, 2007.
    • (2007) Yale Journal of Biology and Medicine , vol.80 , Issue.2 , pp. 51-60
    • Ziello, J.E.1    Jovin, I.S.2    Huang, Y.3
  • 28
    • 0038529602 scopus 로고    scopus 로고
    • Direct interactions between HIF-1 alpha and Mdm2 modulate p53 function
    • D. Chen,M. Li, J. Luo, andW. Gu, "Direct interactions between HIF-1 alpha and Mdm2 modulate p53 function," The Journal of Biological Chemistry, vol. 278, no. 16, pp. 13595-13598, 2003.
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 13595-13598
    • Chen, D.1    Li, M.2    Luo, J.3    Gu, W.4
  • 29
    • 11244315697 scopus 로고    scopus 로고
    • Transcriptional regulation of vascular endothelial cell responses to hypoxia by HIF-1
    • D. J. Manalo, A. Rowan, T. Lavoie et al. , "Transcriptional regulation of vascular endothelial cell responses to hypoxia by HIF-1," Blood, vol. 105, no. 2, pp. 659-669, 2005.
    • (2005) Blood , vol.105 , Issue.2 , pp. 659-669
    • Manalo, D.J.1    Rowan, A.2    Lavoie, T.3
  • 30
    • 73549088729 scopus 로고    scopus 로고
    • Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1enhances hypoxic gene expression and tumor growth
    • A. J. Krieg, E. B. Rankin,D. Chan,O. Razorenova, S. Fernandez, and A. J. Giaccia, "Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1enhances hypoxic gene expression and tumor growth," Molecular and Cellular Biology, vol. 30, no. 1, pp. 344-353, 2010.
    • (2010) Molecular and Cellular Biology , vol.30 , Issue.1 , pp. 344-353
    • Krieg, A.J.1    Rankin, E.B.2    Chan, D.3    Razorenova, O.4    Fernandez, S.5    Giaccia, A.J.6
  • 31
    • 79957567239 scopus 로고    scopus 로고
    • Pyruvate kinaseM2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1
    • W. Luo, H. Hu, R. Chang et al. , "Pyruvate kinaseM2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1," Cell, vol. 145, no. 5, pp. 732-744, 2011.
    • (2011) Cell , vol.145 , Issue.5 , pp. 732-744
    • Luo, W.1    Hu, H.2    Chang, R.3
  • 32
    • 70249122059 scopus 로고    scopus 로고
    • Oxygen-regulated 2-Adrenergic receptor hydroxylation by EGLN3 and ubiquitylation by pVHL
    • L. Xie, K. Xiao, E. J. Whalen et al. , "Oxygen-regulated 2-Adrenergic receptor hydroxylation by EGLN3 and ubiquitylation by pVHL," Science Signaling, vol. 2, no. 78, article ra33, 2009.
    • (2009) Science Signaling , vol.2 , Issue.78
    • Xie, L.1    Xiao, K.2    Whalen, E.J.3
  • 33
    • 33845321931 scopus 로고    scopus 로고
    • Prolyl hydroxylase-1 negatively regulates IkappaB kinase-beta, giving insight into hypoxia-induced NFkappaB activity
    • E. P. Cummins, E. Berra, K. M. Comerford et al. , "Prolyl hydroxylase-1 negatively regulates IkappaB kinase-beta, giving insight into hypoxia-induced NFkappaB activity," Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 48, pp. 18154-18159, 2006.
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.48 , pp. 18154-18159
    • Cummins, E.P.1    Berra, E.2    Comerford, K.M.3
  • 34
    • 34250376483 scopus 로고    scopus 로고
    • EGLN3 prolyl hydroxylase regulates skeletal muscle differentiation and myogenin protein stability
    • J. Fu, K. Menzies, R. S. Freeman, and M. B. Taubman, "EGLN3 prolyl hydroxylase regulates skeletal muscle differentiation and myogenin protein stability," The Journal of Biological Chemistry, vol. 282, no. 17, pp. 12410-12418, 2007.
    • (2007) The Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 12410-12418
    • Fu, J.1    Menzies, K.2    Freeman, R.S.3    Taubman, M.B.4
  • 36
    • 0033713239 scopus 로고    scopus 로고
    • CGMP-independent inotropic effects of nitric oxide and peroxynitrite donors: Potential role for nitrosylation
    • N. Paolocc, U. E. G. Ekelund, T. Isoda et al. , "cGMP-independent inotropic effects of nitric oxide and peroxynitrite donors: Potential role for nitrosylation," The American Journal of Physiology-Heart and Circulatory Physiology, vol. 279, no. 4, pp. H1982-H1988, 2000.
    • (2000) The American Journal of Physiology-Heart and Circulatory Physiology , vol.279 , Issue.4 , pp. H1982-H1988
    • Paolocc, N.1    Ekelund, U.E.G.2    Isoda, T.3
  • 37
    • 0029417335 scopus 로고
    • Activation of an H2O2-generating NADH oxidase in human lung fibroblasts by transforming growth factor beta1
    • V. J. Thannickal and B. L. Fanburg, "Activation of an H2O2-generating NADH oxidase in human lung fibroblasts by transforming growth factor beta1,"The Journal of Biological Chemistry, vol. 270, no. 51, pp. 30334-30338, 1995.
    • (1995) The Journal of Biological Chemistry , vol.270 , Issue.51 , pp. 30334-30338
    • Thannickal, V.J.1    Fanburg, B.L.2
  • 39
    • 0033035157 scopus 로고    scopus 로고
    • Reactive oxygen species modulate endothelin-I-induced c-fos gene expression in cardiomyocytes
    • T. H. Cheng, N. L. Shih, S. Y. Chen, D. L. Wang, and J. J. Chen, "Reactive oxygen species modulate endothelin-I-induced c-fos gene expression in cardiomyocytes," Cardiovascular Research, vol. 41, no. 3, pp. 654-662, 1999.
    • (1999) Cardiovascular Research , vol.41 , Issue.3 , pp. 654-662
    • Cheng, T.H.1    Shih, N.L.2    Chen, S.Y.3    Wang, D.L.4    Chen, J.J.5
  • 41
    • 0037453028 scopus 로고    scopus 로고
    • Oxidative stress mediates tumor necrosis factor-alpha-induced mitochondrial DNA damage and dysfunction in cardiac myocyte
    • N. Suematsu, H. Tsutsui, J. Wen et al. , "Oxidative stress mediates tumor necrosis factor-alpha-induced mitochondrial DNA damage and dysfunction in cardiac myocyte," Circulation, vol. 107, no. 10, pp. 1418-1423, 2003.
    • (2003) Circulation , vol.107 , Issue.10 , pp. 1418-1423
    • Suematsu, N.1    Tsutsui, H.2    Wen, J.3
  • 42
    • 0032189851 scopus 로고    scopus 로고
    • Lipid peroxidation and antioxidant enzymes in isoproterenol induced oxidative stress in rat tissues
    • N. Rathore, S. John, M. Kale, and D. Bhatnagar, "Lipid peroxidation and antioxidant enzymes in isoproterenol induced oxidative stress in rat tissues," Pharmacological Research, vol. 38, no. 4, pp. 297-303, 1998.
    • (1998) Pharmacological Research , vol.38 , Issue.4 , pp. 297-303
    • Rathore, N.1    John, S.2    Kale, M.3    Bhatnagar, D.4
  • 43
    • 0038544188 scopus 로고    scopus 로고
    • Oxidative stress, chromatin remodeling and gene transcription in inflammation and chronic lung diseases
    • I. Rahman, "Oxidative stress, chromatin remodeling and gene transcription in inflammation and chronic lung diseases," Journal of Biochemistry andMolecular Biology, vol. 36, no. 1, pp. 95-109, 2003.
    • (2003) Journal of Biochemistry AndMolecular Biology , vol.36 , Issue.1 , pp. 95-109
    • Rahman, I.1
  • 44
    • 0034707049 scopus 로고    scopus 로고
    • G(i) and G(o) are target proteins of reactive oxygen species
    • M. Nishida, Y. Maruyama, R. Tanaka, K. Kontani, T. Nagao, and H. Kurose, "G(i) and G(o) are target proteins of reactive oxygen species," Nature, vol. 408, no. 6811, pp. 492-495, 2000.
    • (2000) Nature , vol.408 , Issue.6811 , pp. 492-495
    • Nishida, M.1    Maruyama, Y.2    Tanaka, R.3    Kontani, K.4    Nagao, T.5    Kurose, H.6
  • 45
    • 6344277918 scopus 로고    scopus 로고
    • Essential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development, and heart function
    • M. Conrad, C. Jakupoglu, S. G. Moreno et al. , "Essential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development, and heart function,"Molecular and Cellular Biology, vol. 24, no. 21, pp. 9414-9423, 2004.
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.21 , pp. 9414-9423
    • Conrad, M.1    Jakupoglu, C.2    Moreno, S.G.3
  • 46
    • 0029781555 scopus 로고    scopus 로고
    • The protective role of manganese superoxide dismutase against adriamycin-induced acute cardiac toxicity in transgenic mice
    • H. C. Yen, T. D. Oberley, S. Vichitbandha, Y.-S. Ho, and D. K. St. Clair, "The protective role of manganese superoxide dismutase against adriamycin-induced acute cardiac toxicity in transgenic mice," The Journal of Clinical Investigation, vol. 98, no. 5, pp. 1253-1260, 1996.
    • (1996) The Journal of Clinical Investigation , vol.98 , Issue.5 , pp. 1253-1260
    • Yen, H.C.1    Oberley, T.D.2    Vichitbandha, S.3    Ho, Y.-S.4    St. Clair, D.K.5
  • 47
    • 0010117025 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase transgene overexpression preserves postischemic myocardial function in isolated murine hearts
    • E. P. Chen, H. B. Bittner, R. D. Davis, R. J. Folz, and P. van Trigt, "Extracellular superoxide dismutase transgene overexpression preserves postischemic myocardial function in isolated murine hearts," Circulation, vol. 94, no. 9, pp. II412-II417, 1996.
    • (1996) Circulation , vol.94 , Issue.9 , pp. II412-II417
    • Chen, E.P.1    Bittner, H.B.2    Davis, R.D.3    Folz, R.J.4    Van Trigt, P.5
  • 48
    • 77649162855 scopus 로고    scopus 로고
    • Sent to destroy: The ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease
    • M. S. Willis,W. H. D. Townley-Tilson,E. Y. Kang, J. W. Homeister, and C. Patterson, "Sent to destroy: The ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease," Circulation Research, vol. 106, no. 3, pp. 463-478, 2010.
    • (2010) Circulation Research , vol.106 , Issue.3 , pp. 463-478
    • Willis, M.S.1    Townley-Tilson, W.H.D.2    Kang, E.Y.3    Homeister, J.W.4    Patterson, C.5
  • 49
    • 73349093117 scopus 로고    scopus 로고
    • Cytochrome P450 enzymes and the heart
    • K. R. Chaudhary, S. N. Batchu, and J. M. Seubert, "Cytochrome P450 enzymes and the heart," IUBMB Life, vol. 61, no. 10, pp. 954-960, 2009.
    • (2009) IUBMB Life , vol.61 , Issue.10 , pp. 954-960
    • Chaudhary, K.R.1    Batchu, S.N.2    Seubert, J.M.3
  • 50
    • 0034681719 scopus 로고    scopus 로고
    • Cytochrome P450 enzymes in the heart
    • B. K. Park, "Cytochrome P450 enzymes in the heart," The Lancet, vol. 355, no. 9208, pp. 945-946, 2000.
    • (2000) The Lancet , vol.355 , Issue.9208 , pp. 945-946
    • Park, B.K.1
  • 51
    • 41549153249 scopus 로고    scopus 로고
    • Modulation of cardiac and hepatic cytochrome P450 enzymes during heart failure
    • B. N. M. Zordoky and A. O. S. El-Kadi, "Modulation of cardiac and hepatic cytochrome P450 enzymes during heart failure," Current Drug Metabolism, vol. 9, no. 2, pp. 122-128, 2008.
    • (2008) Current Drug Metabolism , vol.9 , Issue.2 , pp. 122-128
    • Zordoky, B.N.M.1    El-Kadi, A.O.S.2
  • 52
    • 0034725724 scopus 로고    scopus 로고
    • Phagocytes and oxidative stress
    • B. M. Babior, "Phagocytes and oxidative stress," The American Journal of Medicine, vol. 109, no. 1, pp. 33-44, 2000.
    • (2000) The American Journal of Medicine , vol.109 , Issue.1 , pp. 33-44
    • Babior, B.M.1
  • 53
    • 0029162591 scopus 로고
    • Hydrogen peroxide changes in ischemic and reperfused heart: Cytochemistry and biochemical and X-ray microanalysis
    • J. Slezak, N. Tribulova, J. Pristacova et al. , "Hydrogen peroxide changes in ischemic and reperfused heart: cytochemistry and biochemical and X-ray microanalysis," The American Journal of Pathology, vol. 147, no. 3, pp. 772-781, 1995.
    • (1995) The American Journal of Pathology , vol.147 , Issue.3 , pp. 772-781
    • Slezak, J.1    Tribulova, N.2    Pristacova, J.3
  • 54
    • 0034659164 scopus 로고    scopus 로고
    • Myeloperoxidase-generated oxidants and atherosclerosis
    • E. A. Podrez, H. M. Abu-Soud, and S. L. Hazen, "Myeloperoxidase-generated oxidants and atherosclerosis," Free Radical Biology and Medicine, vol. 28, no. 12, pp. 1717-1725, 2000.
    • (2000) Free Radical Biology and Medicine , vol.28 , Issue.12 , pp. 1717-1725
    • Podrez, E.A.1    Abu-Soud, H.M.2    Hazen, S.L.3
  • 55
    • 68149168582 scopus 로고    scopus 로고
    • Myeloperoxidase: A useful biomarker for cardiovascular disease risk stratification?
    • R. K. Schindhelm, L. P. van der Zwan, T. Teerlink, and P. G. Scheffer, "Myeloperoxidase: A useful biomarker for cardiovascular disease risk stratification?" Clinical Chemistry, vol. 55, no. 8, pp. 1462-1470, 2009.
    • (2009) Clinical Chemistry , vol.55 , Issue.8 , pp. 1462-1470
    • Schindhelm, R.K.1    Van Der Zwan, L.P.2    Teerlink, T.3    Scheffer, P.G.4
  • 57
    • 0037195783 scopus 로고    scopus 로고
    • Myeloperoxidase functions as a major enzymatic catalyst for initiation of lipid peroxidation at sites of inflammation
    • R. Zhang, M.-L. Brennan, Z. Shen et al. , "Myeloperoxidase functions as a major enzymatic catalyst for initiation of lipid peroxidation at sites of inflammation," The Journal of Biological Chemistry, vol. 277, no. 48, pp. 46116-46122, 2002.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.48 , pp. 46116-46122
    • Zhang, R.1    Brennan, M.-L.2    Shen, Z.3
  • 58
    • 0035824162 scopus 로고    scopus 로고
    • Association between myeloperoxidase levels and risk of coronary artery disease
    • R. Zhang, M.-L. Brennan, X. Fu et al. , "Association between myeloperoxidase levels and risk of coronary artery disease," The Journal of the AmericanMedical Association, vol. 286, no. 17, pp. 2136-2142, 2001.
    • (2001) The Journal of the AmericanMedical Association , vol.286 , Issue.17 , pp. 2136-2142
    • Zhang, R.1    Brennan, M.-L.2    Fu, X.3
  • 59
    • 34248374428 scopus 로고    scopus 로고
    • Plasma concentrations of myeloperoxidase predict mortality after myocardial infarction
    • T. J. Mocatta, A. P. Pilbrow, V. A. Cameron et al. , "Plasma concentrations of myeloperoxidase predict mortality after myocardial infarction," Journal of the American College of Cardiology, vol. 49, no. 20, pp. 1993-2000, 2007.
    • (2007) Journal of the American College of Cardiology , vol.49 , Issue.20 , pp. 1993-2000
    • Mocatta, T.J.1    Pilbrow, A.P.2    Cameron, V.A.3
  • 61
  • 63
    • 0023030627 scopus 로고
    • A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor
    • M. E. Martin, B. R. Byers, M. O. J. Olson, M. L. Salin, J. E. Arceneaux, and C. Tolbert, "A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor," Journal of Biological Chemistry, vol. 261, no. 20, pp. 9361-9367, 1986.
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.20 , pp. 9361-9367
    • Martin, M.E.1    Byers, B.R.2    Olson, M.O.J.3    Salin, M.L.4    Arceneaux, J.E.5    Tolbert, C.6
  • 64
    • 0037210467 scopus 로고    scopus 로고
    • Oxygenases without requirement for cofactors or metal ions
    • S. Fetzner, "Oxygenases without requirement for cofactors or metal ions," AppliedMicrobiology and Biotechnology, vol. 60,no. 3, pp. 243-257, 2003.
    • (2003) AppliedMicrobiology and Biotechnology , vol.60 , Issue.3 , pp. 243-257
    • Fetzner, S.1
  • 65
    • 0035221419 scopus 로고    scopus 로고
    • The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate-and iron-dependent dioxygenases
    • L. Aravind and E. V. Koonin, "The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate-and iron-dependent dioxygenases," Genome Biology, vol. 2, no. 3, Article ID RESEARCH0007, 2001.
    • (2001) Genome Biology , vol.2 , Issue.3
    • Aravind, L.1    Koonin, E.V.2
  • 66
    • 23244445988 scopus 로고    scopus 로고
    • Cyclooxygenase inhibition and cardiovascular risk
    • E. M. Antman, D. DeMets, and J. Loscalzo, "Cyclooxygenase inhibition and cardiovascular risk," Circulation, vol. 112, no. 5, pp. 759-770, 2005.
    • (2005) Circulation , vol.112 , Issue.5 , pp. 759-770
    • Antman, E.M.1    DeMets, D.2    Loscalzo, J.3
  • 67
    • 0037437765 scopus 로고    scopus 로고
    • Advances in the pathophysiology of constitutive and inducible cyclooxygenases: Two enzymes in the spotlight
    • L. Parente and M. Perretti, "Advances in the pathophysiology of constitutive and inducible cyclooxygenases: Two enzymes in the spotlight," Biochemical Pharmacology, vol. 65,no. 2, pp. 153-159, 2003.
    • (2003) Biochemical Pharmacology , vol.65 , Issue.2 , pp. 153-159
    • Parente, L.1    Perretti, M.2
  • 68
    • 0037047092 scopus 로고    scopus 로고
    • Cyclooxygenase-2 inhibition and cardiovascular events
    • B. Pitt, C. Penine, and J. T. Willerson, "Cyclooxygenase-2 inhibition and cardiovascular events," Circulation, vol. 106, no. 2,pp. 167-169, 2002.
    • (2002) Circulation , vol.106 , Issue.2 , pp. 167-169
    • Pitt, B.1    Penine, C.2    Willerson, J.T.3
  • 69
    • 0035928784 scopus 로고    scopus 로고
    • Overexpression of functionally coupled cyclooxygenase-2 and prostaglandin e synthase in symptomatic atherosclerotic plaques as a basis of prostaglandin E2-dependent plaque instability
    • F. Cipollone, C. Prontera, B. Pini et al. , "Overexpression of functionally coupled cyclooxygenase-2 and prostaglandin E synthase in symptomatic atherosclerotic plaques as a basis of prostaglandin E2-dependent plaque instability," Circulation, vol. 104, no. 8, pp. 921-927, 2001.
    • (2001) Circulation , vol.104 , Issue.8 , pp. 921-927
    • Cipollone, F.1    Prontera, C.2    Pini, B.3
  • 70
    • 0042232709 scopus 로고    scopus 로고
    • Selective cyclo-oxygenase-2 inhibition with parecoxib acutely impairs endothelium-dependent vasodilatation in patients with essential hypertension
    • D. Bulut, S. Liaghat, C. Hanefeld, R. Koll, T. Miebach, and A. Mügge, "Selective cyclo-oxygenase-2 inhibition with parecoxib acutely impairs endothelium-dependent vasodilatation in patients with essential hypertension," Journal of Hypertension, vol. 21, no. 9, pp. 1663-1667, 2003.
    • (2003) Journal of Hypertension , vol.21 , Issue.9 , pp. 1663-1667
    • Bulut, D.1    Liaghat, S.2    Hanefeld, C.3    Koll, R.4    Miebach, T.5    Mügge, A.6
  • 71
    • 0037117652 scopus 로고    scopus 로고
    • Cyclooxygenase-2 promotes early atherosclerotic lesion formation in LDL receptor-deficient mice
    • M. E. Burleigh, V. R. Babaev, J. A. Oates et al. , "Cyclooxygenase-2 promotes early atherosclerotic lesion formation in LDL receptor-deficient mice," Circulation, vol. 105, no. 15, pp. 1816-1823, 2002.
    • (2002) Circulation , vol.105 , Issue.15 , pp. 1816-1823
    • Burleigh, M.E.1    Babaev, V.R.2    Oates, J.A.3
  • 72
    • 0037028635 scopus 로고    scopus 로고
    • Why do cyclo-oxygenase-2 inhibitors cause cardiovascular events?
    • R. J. Bing and M. Lomnicka, "Why do cyclo-oxygenase-2 inhibitors cause cardiovascular events?" Journal of theAmerican College of Cardiology, vol. 39, no. 3, pp. 521-522, 2002.
    • (2002) Journal of TheAmerican College of Cardiology , vol.39 , Issue.3 , pp. 521-522
    • Bing, R.J.1    Lomnicka, M.2
  • 73
    • 33846315497 scopus 로고    scopus 로고
    • Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay
    • D. Ehrismann, E. Flashman, D. N. Genn et al. , "Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay," Biochemical Journal, vol. 401, no. 1, pp. 227-234, 2007.
    • (2007) Biochemical Journal , vol.401 , Issue.1 , pp. 227-234
    • Ehrismann, D.1    Flashman, E.2    Genn, D.N.3
  • 74
    • 33846400822 scopus 로고    scopus 로고
    • The most versatile of all reactive intermediates?
    • E. Flashman and C. J. Schofield, "The most versatile of all reactive intermediates?" Nature Chemical Biology, vol. 3, no. 2, pp. 86-87, 2007.
    • (2007) Nature Chemical Biology , vol.3 , Issue.2 , pp. 86-87
    • Flashman, E.1    Schofield, C.J.2
  • 76
    • 1542378704 scopus 로고    scopus 로고
    • Dioxygen activation at mononuclear nonheme iron active sites: Enzymes, models, and intermediate
    • M. Costas, M. P. Mehn,M. P. Jensen, and L. Que Jr. , "Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediate," Chemical Reviews, vol. 104, no. 2, pp. 939-986, 2004.
    • (2004) Chemical Reviews , vol.104 , Issue.2 , pp. 939-986
    • Costas, M.1    Mehn, M.P.2    Jensen, M.P.3    Que, L.4
  • 77
    • 0018889924 scopus 로고
    • Studies on the lysyl hydroxylase reaction. II. Inhibition kinetics and the reaction mechanism
    • U. Puistola, T. M. Turpeeniemi Hujanen, R. Myllyla, and K. I. Kivirikko, "Studies on the lysyl hydroxylase reaction. II. Inhibition kinetics and the reaction mechanism," Biochimica et Biophysica Acta, vol. 611, no. 1, pp. 51-60, 1980.
    • (1980) Biochimica et Biophysica Acta , vol.611 , Issue.1 , pp. 51-60
    • Puistola, U.1    Turpeeniemi Hujanen, T.M.2    Myllyla, R.3    Kivirikko, K.I.4
  • 78
    • 85003598105 scopus 로고    scopus 로고
    • Contrasting effects of ascorbate and iron on the pulmonary vascular response to hypoxia in humans
    • N. P. Talbot, Q. P. Croft,M. K. Curtis et al. , "Contrasting effects of ascorbate and iron on the pulmonary vascular response to hypoxia in humans," Physiological Reports, vol. 2, no. 12, Article ID e12220, 2014.
    • (2014) Physiological Reports , vol.2 , Issue.12
    • Talbot, N.P.1    Croft, Q.P.2    Curtis, M.K.3
  • 79
    • 70449527373 scopus 로고    scopus 로고
    • Hypoxia, hypoxiainducible factors (HIF), HIF hydroxylases and oxygen sensing
    • J. D. Webb,M. L. Coleman, andC. W. Pugh, "Hypoxia, hypoxiainducible factors (HIF), HIF hydroxylases and oxygen sensing," Cellular and Molecular Life Sciences, vol. 66, no. 22, pp. 3539-3554, 2009.
    • (2009) Cellular and Molecular Life Sciences , vol.66 , Issue.22 , pp. 3539-3554
    • Webb, J.D.1    Coleman, M.L.2    Pugh, C.W.3
  • 81
    • 0037386143 scopus 로고    scopus 로고
    • Intracellular localisation of human HIF-1hydroxylases: Implications for oxygen sensing
    • E. Metzen, U. Berchner-Pfannschmidt, P. Stengel et al. , "Intracellular localisation of human HIF-1hydroxylases: implications for oxygen sensing," Journal of Cell Science, vol. 116, no. 7, pp. 1319-1326, 2003.
    • (2003) Journal of Cell Science , vol.116 , Issue.7 , pp. 1319-1326
    • Metzen, E.1    Berchner-Pfannschmidt, U.2    Stengel, P.3
  • 82
    • 32844454603 scopus 로고    scopus 로고
    • Histone demethylation by a family of JmjC domain-containing proteins
    • Y.-I. Tsukada, J. Fang, H. Erdjument-Bromage et al. , "Histone demethylation by a family of JmjC domain-containing proteins," Nature, vol. 439, no. 7078, pp. 811-816, 2006.
    • (2006) Nature , vol.439 , Issue.7078 , pp. 811-816
    • Tsukada, Y.-I.1    Fang, J.2    Erdjument-Bromage, H.3
  • 83
    • 0037068433 scopus 로고    scopus 로고
    • AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
    • P. Ø. Falnes, R. F. Johansen, and E. Seeberg, "AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli," Nature, vol. 419, no. 6903, pp. 178-182, 2002.
    • (2002) Nature , vol.419 , Issue.6903 , pp. 178-182
    • Falnes, P.Ø.1    Johansen, R.F.2    Seeberg, E.3
  • 84
    • 77952779747 scopus 로고    scopus 로고
    • Themitochondrial 2-oxoglutarate carrier is part of a metabolic pathway that mediates glucose-and glutamine-stimulated insulin secretion
    • M. L. Odegaard, J. W. Joseph, M. V. Jensen et al. , "Themitochondrial 2-oxoglutarate carrier is part of a metabolic pathway that mediates glucose-and glutamine-stimulated insulin secretion," The Journal of Biological Chemistry, vol. 285, no. 22, pp. 16530-16537, 2010.
    • (2010) The Journal of Biological Chemistry , vol.285 , Issue.22 , pp. 16530-16537
    • Odegaard, M.L.1    Joseph, J.W.2    Jensen, M.V.3
  • 85
    • 77950686223 scopus 로고    scopus 로고
    • OGFOD1, a novel modulator of eukaryotic translation initiation factor 2phosphorylation and the cellular response to stress
    • K. A. Wehner, S. Schütz, and P. Sarnow, "OGFOD1, a novel modulator of eukaryotic translation initiation factor 2phosphorylation and the cellular response to stress," Molecular and Cellular Biology, vol. 30, no. 8, pp. 2006-2016, 2010.
    • (2010) Molecular and Cellular Biology , vol.30 , Issue.8 , pp. 2006-2016
    • Wehner, K.A.1    Schütz, S.2    Sarnow, P.3
  • 86
    • 33747691662 scopus 로고    scopus 로고
    • Transforming growth factor 1 induces hypoxia-inducible factor-1 stabilization through selective inhibition of PHD2 expression
    • S. McMahon, M. Charbonneau, S. Grandmont, D. E. Richard, and C. M. Dubois, "Transforming growth factor 1 induces hypoxia-inducible factor-1 stabilization through selective inhibition of PHD2 expression," Journal of Biological Chemistry, vol. 281, no. 34, pp. 24171-24181, 2006.
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.34 , pp. 24171-24181
    • McMahon, S.1    Charbonneau, M.2    Grandmont, S.3    Richard, D.E.4    Dubois, C.M.5
  • 87
    • 54749094325 scopus 로고    scopus 로고
    • Autohydroxylation of FIH-1: An Fe(II),-ketoglutarate-dependent human hypoxia sensor
    • Y.-H. Chen, L. M. Comeaux, S. J. Eyles, and M. J. Knapp, "Autohydroxylation of FIH-1: An Fe(II),-ketoglutarate-dependent human hypoxia sensor," Chemical Communications, no. 39, pp. 4768-4770, 2008.
    • (2008) Chemical Communications , Issue.39 , pp. 4768-4770
    • Chen, Y.-H.1    Comeaux, L.M.2    Eyles, S.J.3    Knapp, M.J.4
  • 88
    • 17944375360 scopus 로고    scopus 로고
    • C. Elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation
    • A. C. R. Epstein, J. M. Gleadle, L. A. McNeill et al. , "C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation," Cell, vol. 107, no. 1, pp. 43-54, 2001.
    • (2001) Cell , vol.107 , Issue.1 , pp. 43-54
    • Epstein, A.C.R.1    Gleadle, J.M.2    McNeill, L.A.3
  • 89
    • 27544477748 scopus 로고    scopus 로고
    • The von Hippel-Lindau protein, HIF hydroxylation, and oxygen sensing
    • W. G. Kaelin Jr. , "The von Hippel-Lindau protein, HIF hydroxylation, and oxygen sensing," Biochemical and Biophysical Research Communications, vol. 338, no. 1, pp. 627-628, 2005.
    • (2005) Biochemical and Biophysical Research Communications , vol.338 , Issue.1 , pp. 627-628
    • Kaelin, W.G.1
  • 90
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
    • M. Hirsilä, P. Koivunen, V. Günzler, K. I. Kivirikko, and J. Myllyharju, "Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor," The Journal of Biological Chemistry, vol. 278, no. 33, pp. 30772-30780, 2003.
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 30772-30780
    • Hirsilä, M.1    Koivunen, P.2    Günzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 91
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1in normoxia
    • E. Berra, E. Benizri, A. Ginouvès, V. Volmat, D. Roux, and J. Pouysségur, "HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1in normoxia," The EMBO Journal, vol. 22, no. 16, pp. 4082-4090, 2003.
    • (2003) The EMBO Journal , vol.22 , Issue.16 , pp. 4082-4090
    • Berra, E.1    Benizri, E.2    Ginouvès, A.3    Volmat, V.4    Roux, D.5    Pouysségur, J.6
  • 92
    • 22544464403 scopus 로고    scopus 로고
    • Coordinate regulation of the oxygen-dependent degradation domains of hypoxia-inducible factor 1
    • D. A. Chan, P. D. Sutphin, S.-E. Yen, and A. J. Giaccia, "Coordinate regulation of the oxygen-dependent degradation domains of hypoxia-inducible factor 1,"Molecular and Cellular Biology, vol. 25, no. 15, pp. 6415-6426, 2005.
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.15 , pp. 6415-6426
    • Chan, D.A.1    Sutphin, P.D.2    Yen, S.-E.3    Giaccia, A.J.4
  • 93
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: A delay of lethal cell injury in ischemic myocardium
    • C. E. Murry, R. B. Jennings, and K. A. Reimer, "Preconditioning with ischemia: A delay of lethal cell injury in ischemic myocardium," Circulation, vol. 74, no. 5, pp. 1124-1136, 1986.
    • (1986) Circulation , vol.74 , Issue.5 , pp. 1124-1136
    • Murry, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 94
    • 38849182762 scopus 로고    scopus 로고
    • Complete loss of ischaemic preconditioning-induced cardioprotection in mice with partial deficiency of HIF-1
    • Z. Cai, H. Zhong, M. Bosch-Marce et al. , "Complete loss of ischaemic preconditioning-induced cardioprotection in mice with partial deficiency of HIF-1," Cardiovascular Research, vol. 77, no. 3, pp. 463-470, 2008.
    • (2008) Cardiovascular Research , vol.77 , Issue.3 , pp. 463-470
    • Cai, Z.1    Zhong, H.2    Bosch-Marce, M.3
  • 95
    • 0027163384 scopus 로고
    • Cardiac stress protein elevation 24 hours after brief ischemia or heat stress is associated with resistance to myocardial infarction
    • M. S. Marber, D. S. Latchman, J. M. Walker, and D. M. Yellon, "Cardiac stress protein elevation 24 hours after brief ischemia or heat stress is associated with resistance to myocardial infarction," Circulation, vol. 88, no. 3, pp. 1264-1272, 1993.
    • (1993) Circulation , vol.88 , Issue.3 , pp. 1264-1272
    • Marber, M.S.1    Latchman, D.S.2    Walker, J.M.3    Yellon, D.M.4
  • 96
    • 77956388934 scopus 로고    scopus 로고
    • Hypoxia inducible factor 1 (HIF-1) and cardioprotection
    • D. Tekin, A. D. Dursun, and L. Xi, "Hypoxia inducible factor 1 (HIF-1) and cardioprotection," Acta Pharmacologica Sinica, vol. 31, no. 9, pp. 1085-1094, 2010.
    • (2010) Acta Pharmacologica Sinica , vol.31 , Issue.9 , pp. 1085-1094
    • Tekin, D.1    Dursun, A.D.2    Xi, L.3
  • 97
    • 69449087752 scopus 로고    scopus 로고
    • Lower mortality from coronary heart disease and stroke at higher altitudes in Switzerland
    • Swiss National Cohort Study G
    • D. Faeh, F. Gutzwiller, M. Bopp, and Swiss National Cohort Study G, "Lower mortality from coronary heart disease and stroke at higher altitudes in Switzerland," Circulation, vol. 120, no. 6, pp. 495-501, 2009.
    • (2009) Circulation , vol.120 , Issue.6 , pp. 495-501
    • Faeh, D.1    Gutzwiller, F.2    Bopp, M.3
  • 98
    • 84859095540 scopus 로고    scopus 로고
    • Unfavourable consequences of chronic cardiacHIF-1alpha stabilization
    • M. Hölscher, K. Schäfer, S. Krull et al. , "Unfavourable consequences of chronic cardiacHIF-1alpha stabilization," Cardiovascular Research, vol. 94, no. 1, pp. 77-86, 2012.
    • (2012) Cardiovascular Research , vol.94 , Issue.1 , pp. 77-86
    • Hölscher, M.1    Schäfer, K.2    Krull, S.3
  • 99
    • 84865426294 scopus 로고    scopus 로고
    • Activation of the prolyl-hydroxylase oxygen-sensing signal cascade leads to AMPK activation in cardiomyocytes
    • H. Yan, D.-X. Zhang, X. Shi, Q. Zhang, and Y.-S. Huang, "Activation of the prolyl-hydroxylase oxygen-sensing signal cascade leads to AMPK activation in cardiomyocytes," Journal of Cellular andMolecularMedicine, vol. 16,no. 9, pp. 2049-2059, 2012.
    • (2012) Journal of Cellular AndMolecularMedicine , vol.16 , Issue.9 , pp. 2049-2059
    • Yan, H.1    Zhang, D.-X.2    Shi, X.3    Zhang, Q.4    Huang, Y.-S.5
  • 100
    • 0038165466 scopus 로고    scopus 로고
    • Activation of the prolyl hydroxylase oxygen-sensor results in induction of GLUT1, heme oxygenase-1, and nitricoxide synthase proteins and confers protection from metabolic inhibition to cardiomyocytes
    • G. Wright, J. J. Higgin, R. T. Raines, C. Steenbergen, and E. Murphy, "Activation of the prolyl hydroxylase oxygen-sensor results in induction of GLUT1, heme oxygenase-1, and nitricoxide synthase proteins and confers protection from metabolic inhibition to cardiomyocytes," The Journal of Biological Chemistry, vol. 278, no. 22, pp. 20235-20239, 2003.
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.22 , pp. 20235-20239
    • Wright, G.1    Higgin, J.J.2    Raines, R.T.3    Steenbergen, C.4    Murphy, E.5
  • 101
    • 33847028349 scopus 로고    scopus 로고
    • The prolyl hydroxylase oxygensensing pathway is cytoprotective and allows maintenance of mitochondrial membrane potential during metabolic inhibition
    • V. Sridharan, J. Guichard, R. M. Bailey, H. Kasiganesan, C. Beeson, and G. L. Wright, "The prolyl hydroxylase oxygensensing pathway is cytoprotective and allows maintenance of mitochondrial membrane potential during metabolic inhibition," The American Journal of Physiology-Cell Physiology, vol. 292, no. 2, pp. C719-C728, 2007.
    • (2007) The American Journal of Physiology-Cell Physiology , vol.292 , Issue.2 , pp. C719-C728
    • Sridharan, V.1    Guichard, J.2    Bailey, R.M.3    Kasiganesan, H.4    Beeson, C.5    Wright, G.L.6
  • 102
    • 84895899655 scopus 로고    scopus 로고
    • Prolonged Hypoxia Increases Survival even in Zebrafish (Danio rerio) Showing Cardiac Arrhythmia
    • R. Kopp, I. Bauer, A. Ramalingam, M. Egg, T. Schwerte, and V. Lionetti, "Prolonged Hypoxia Increases Survival Even in Zebrafish (Danio rerio) Showing Cardiac Arrhythmia," PLoS ONE, vol. 9, no. 2,Article ID e89099, 2014.
    • (2014) PLoS ONE , vol.9 , Issue.2
    • Kopp, R.1    Bauer, I.2    Ramalingam, A.3    Egg, M.4    Schwerte, T.5    Lionetti, V.6
  • 103
    • 0242637601 scopus 로고    scopus 로고
    • What is the role of-adrenergic signaling in heart failure?
    • M. J. Lohse, S. Engelhardt, andT. Eschenhagen, "What is the role of-adrenergic signaling in heart failure?" Circulation Research, vol. 93, no. 10, pp. 896-906, 2003.
    • (2003) Circulation Research , vol.93 , Issue.10 , pp. 896-906
    • Lohse, M.J.1    Engelhardt, S.2    Eschenhagen, T.3
  • 104
    • 33749518516 scopus 로고    scopus 로고
    • Posttranslational hydroxylation of ankyrin repeats in IB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)
    • M. E. Cockman, D. E. Lancaster, I. P. Stolze et al. , "Posttranslational hydroxylation of ankyrin repeats in IB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)," Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 40, pp. 14767-14772, 2006.
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.40 , pp. 14767-14772
    • Cockman, M.E.1    Lancaster, D.E.2    Stolze, I.P.3
  • 105
    • 34548239264 scopus 로고    scopus 로고
    • Asparaginyl hydroxylation of the notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor
    • M. L. Coleman, M. A. McDonough, K. S. Hewitson et al. , "Asparaginyl hydroxylation of the notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor," The Journal of Biological Chemistry, vol. 282, no. 33, pp. 24027-24038, 2007.
    • (2007) The Journal of Biological Chemistry , vol.282 , Issue.33 , pp. 24027-24038
    • Coleman, M.L.1    McDonough, M.A.2    Hewitson, K.S.3
  • 106
    • 34548794831 scopus 로고    scopus 로고
    • ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism
    • J. E. Ferguson III, Y. Wu, K. Smith et al. , "ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism," Molecular and Cellular Biology, vol. 27, no. 18, pp. 6407-6419, 2007.
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.18 , pp. 6407-6419
    • Ferguson, J.E.1    Wu, Y.2    Smith, K.3
  • 107
    • 80052761451 scopus 로고    scopus 로고
    • Double knockdown of prolyl hydroxylase and factor-inhibiting hypoxia-inducible factor with nonviral minicircle gene therapy enhances stem cell mobilization and angiogenesis after myocardial infarction
    • M. Huang, P. Nguyen, F. Jia et al. , "Double knockdown of prolyl hydroxylase and factor-inhibiting hypoxia-inducible factor with nonviral minicircle gene therapy enhances stem cell mobilization and angiogenesis after myocardial infarction," Circulation, vol. 124, no. 11, pp. S46-S54, 2011.
    • (2011) Circulation , vol.124 , Issue.11 , pp. S46-S54
    • Huang, M.1    Nguyen, P.2    Jia, F.3
  • 108
    • 84908577860 scopus 로고    scopus 로고
    • FIH-1, a novel interactor of mindbomb, functions as an essential anti-angiogenic factor during zebrafish vascular development
    • J. H. So, J. D. Kim, K. W. Yoo et al. , "FIH-1, a novel interactor of mindbomb, functions as an essential anti-angiogenic factor during zebrafish vascular development," PLoS ONE, vol. 9, Article ID e109517, 2014.
    • (2014) PLoS ONE , vol.9
    • So, J.H.1    Kim, J.D.2    Yoo, K.W.3
  • 109
    • 79958803246 scopus 로고    scopus 로고
    • Regulation of ankyrin repeat and suppressor of cytokine signalling box protein 4 expression in the immortalizedmurine endothelial cell linesMS1 and SVR: A role for tumour necrosis factor alpha and oxygen
    • M. Bode, Y. Wu, X. Pi et al. , "Regulation of ankyrin repeat and suppressor of cytokine signalling box protein 4 expression in the immortalizedmurine endothelial cell linesMS1 and SVR: A role for tumour necrosis factor alpha and oxygen," Cell Biochemistry and Function, vol. 29, no. 4, pp. 334-341, 2011.
    • (2011) Cell Biochemistry and Function , vol.29 , Issue.4 , pp. 334-341
    • Bode, M.1    Wu, Y.2    Pi, X.3
  • 110
    • 77955916842 scopus 로고    scopus 로고
    • NF-kappaB balances vascular regression and angiogenesis via chromatin remodeling and NFAT displacement
    • A. B. Aurora, D. Biyashev, Y. Mirochnik et al. , "NF-kappaB balances vascular regression and angiogenesis via chromatin remodeling and NFAT displacement," Blood, vol. 116, no. 3, pp. 475-484, 2010.
    • (2010) Blood , vol.116 , Issue.3 , pp. 475-484
    • Aurora, A.B.1    Biyashev, D.2    Mirochnik, Y.3
  • 112
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • C. M. Grozinger and S. L. Schreiber, "Deacetylase enzymes: biological functions and the use of small-molecule inhibitors," Chemistry and Biology, vol. 9, no. 1, pp. 3-16, 2002.
    • (2002) Chemistry and Biology , vol.9 , Issue.1 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 114
    • 82155192318 scopus 로고    scopus 로고
    • Functional regulation of HIF-1under normoxia-is there more than post-translational regulation?
    • A. Kuschel, P. Simon, and S. Tug, "Functional regulation of HIF-1under normoxia-is there more than post-translational regulation?" Journal of Cellular Physiology, vol. 227, no. 2, pp. 514-524, 2012.
    • (2012) Journal of Cellular Physiology , vol.227 , Issue.2 , pp. 514-524
    • Kuschel, A.1    Simon, P.2    Tug, S.3
  • 115
    • 77953688069 scopus 로고    scopus 로고
    • High glucose activates HIF-1-mediated signal transduction in glomerular mesangial cells through a carbohydrate response element binding protein
    • T. Isoe, Y. Makino, K. Mizumoto et al. , "High glucose activates HIF-1-mediated signal transduction in glomerular mesangial cells through a carbohydrate response element binding protein," Kidney International, vol. 78, no. 1, pp. 48-59, 2010.
    • (2010) Kidney International , vol.78 , Issue.1 , pp. 48-59
    • Isoe, T.1    Makino, Y.2    Mizumoto, K.3
  • 116
    • 65249185780 scopus 로고    scopus 로고
    • Downregulation of miR-199a derepresses hypoxia-inducible factor-1alpha and Sirtuin 1 and recapitulates hypoxia preconditioning in cardiacmyocytes
    • S. Rane, M. He, D. Sayed et al. , "Downregulation of miR-199a derepresses hypoxia-inducible factor-1alpha and Sirtuin 1 and recapitulates hypoxia preconditioning in cardiacmyocytes," Circulation Research, vol. 104, no. 7, pp. 879-886, 2009.
    • (2009) Circulation Research , vol.104 , Issue.7 , pp. 879-886
    • Rane, S.1    He, M.2    Sayed, D.3
  • 117
    • 34147113316 scopus 로고    scopus 로고
    • Akyrin repeat and SOCS box containing protein 4 (Asb-4) interacts with GPS1 (CSN1) and inhibits c-Jun NH2-terminal kinase activity
    • J.-Y. Li,B.-X. Chai,W. Zhang,Y.-Q. Liu, J. B. Ammori, and M. W. Mulholland, "Akyrin repeat and SOCS box containing protein 4 (Asb-4) interacts with GPS1 (CSN1) and inhibits c-Jun NH2-terminal kinase activity," Cellular Signalling, vol. 19, no. 6, pp. 1185-1192, 2007.
    • (2007) Cellular Signalling , vol.19 , Issue.6 , pp. 1185-1192
    • Li, J.-Y.1    Chai, B.-X.2    Zhang, W.3    Liu, Y.-Q.4    Ammori, J.B.5    Mulholland, M.W.6
  • 118
    • 84896769273 scopus 로고    scopus 로고
    • The ubiquitin ligase ASB4 promotes trophoblast differentiation through the degradation of ID2
    • W. H. D. Townley-Tilson, Y. Wu, J. E. Ferguson III, and C. Patterson, "The ubiquitin ligase ASB4 promotes trophoblast differentiation through the degradation of ID2," PLoS ONE, vol. 9, no. 2, Article ID e89451, 2014.
    • (2014) PLoS ONE , vol.9 , Issue.2
    • Townley-Tilson, W.H.D.1    Wu, Y.2    Ferguson, J.E.3    Patterson, C.4
  • 119
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • G. Xu, J. S. Paige, and S. R. Jaffrey, "Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling," Nature Biotechnology, vol. 28, no. 8, pp. 868-873, 2010.
    • (2010) Nature Biotechnology , vol.28 , Issue.8 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 120
    • 84865726581 scopus 로고    scopus 로고
    • Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns
    • A. Lundby, K. Lage, B. T. Weinert et al. , "Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns," Cell Reports, vol. 2, no. 2,pp. 419-431, 2012.
    • (2012) Cell Reports , vol.2 , Issue.2 , pp. 419-431
    • Lundby, A.1    Lage, K.2    Weinert, B.T.3
  • 122
    • 21244432831 scopus 로고    scopus 로고
    • Experimental determination of proline hydroxylation and hydroxyproline arabinogalactosylation motifs in secretory proteins
    • M. Shimizu, T. Igasaki, M. Yamada et al. , "Experimental determination of proline hydroxylation and hydroxyproline arabinogalactosylation motifs in secretory proteins," Plant Journal, vol. 42, no. 6, pp. 877-889, 2005.
    • (2005) Plant Journal , vol.42 , Issue.6 , pp. 877-889
    • Shimizu, M.1    Igasaki, T.2    Yamada, M.3
  • 124
    • 84898734084 scopus 로고    scopus 로고
    • Lysine-targeting specificity in ubiquitin and ubiquitin-like modification pathways
    • F. Mattiroli and T. K. Sixma, "Lysine-targeting specificity in ubiquitin and ubiquitin-like modification pathways," Nature Structural and Molecular Biology, vol. 21, no. 4, pp. 308-316, 2014.
    • (2014) Nature Structural and Molecular Biology , vol.21 , Issue.4 , pp. 308-316
    • Mattiroli, F.1    Sixma, T.K.2
  • 125
    • 79953891392 scopus 로고    scopus 로고
    • Differential sensitivity of hypoxia inducible factor hydroxylation sites to hypoxia and hydroxylase inhibitors
    • Y.-M. Tian, K. K. Yeoh, M. K. Lee et al. , "Differential sensitivity of hypoxia inducible factor hydroxylation sites to hypoxia and hydroxylase inhibitors," Journal of Biological Chemistry, vol. 286, no. 15, pp. 13041-13051, 2011.
    • (2011) Journal of Biological Chemistry , vol.286 , Issue.15 , pp. 13041-13051
    • Tian, Y.-M.1    Yeoh, K.K.2    Lee, M.K.3
  • 126
    • 84872638319 scopus 로고
    • The action of tyrosinase on proteins
    • I. W. Sizer, "The action of tyrosinase on proteins," Federation proceedings, vol. 5, article 96, 1946.
    • (1946) Federation Proceedings , vol.5
    • Sizer, I.W.1
  • 127
    • 9344262366 scopus 로고    scopus 로고
    • Cobalt chloride induces delayed cardiac preconditioning in mice through selective activation of HIF-1and AP-1 and iNOS signaling
    • L. Xi, M. Taher, C. Yin, F. Salloum, and R. C. Kukreja, "Cobalt chloride induces delayed cardiac preconditioning in mice through selective activation of HIF-1and AP-1 and iNOS signaling," The American Journal of Physiology-Heart and Circulatory Physiology, vol. 287, no. 6, pp. H2369-H2375, 2004.
    • (2004) The American Journal of Physiology-Heart and Circulatory Physiology , vol.287 , Issue.6 , pp. H2369-H2375
    • Xi, L.1    Taher, M.2    Yin, C.3    Salloum, F.4    Kukreja, R.C.5
  • 129
    • 23744443462 scopus 로고    scopus 로고
    • HIF-1 activation attenuates postischemic myocardial injury: Role for heme oxygenase-1 in modulating microvascular chemokine generation
    • R. Ockaili, R. Natarajan, F. Salloum et al. , "HIF-1 activation attenuates postischemic myocardial injury: role for heme oxygenase-1 in modulating microvascular chemokine generation," American Journal of Physiology-Heart and Circulatory Physiology, vol. 289, no. 2, pp. H542-H548, 2005.
    • (2005) American Journal of Physiology-Heart and Circulatory Physiology , vol.289 , Issue.2 , pp. H542-H548
    • Ockaili, R.1    Natarajan, R.2    Salloum, F.3
  • 130
    • 47649128513 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 is central to cardioprotection a new paradigm for ischemic preconditioning
    • T. Eckle, D. Kohler, R. Lehmann, K. C. E. Kasmi, and H. K. Eltzschig, "Hypoxia-inducible factor-1 is central to cardioprotection a new paradigm for ischemic preconditioning," Circulation, vol. 118, no. 2, pp. 166-175, 2008.
    • (2008) Circulation , vol.118 , Issue.2 , pp. 166-175
    • Eckle, T.1    Kohler, D.2    Lehmann, R.3    Kasmi, K.C.E.4    Eltzschig, H.K.5
  • 131
    • 79960920655 scopus 로고    scopus 로고
    • Systemic pretreatment with dimethyloxalylglycine increases myocardial HIF-1alpha and VEGF production and improves functional recovery after acute ischemia/reperfusion
    • J. A. Poynter, M. C. Manukyan, Y. Wang et al. , "Systemic pretreatment with dimethyloxalylglycine increases myocardial HIF-1alpha and VEGF production and improves functional recovery after acute ischemia/reperfusion," Surgery, vol. 150, no. 2, pp. 278-283, 2011.
    • (2011) Surgery , vol.150 , Issue.2 , pp. 278-283
    • Poynter, J.A.1    Manukyan, M.C.2    Wang, Y.3
  • 132
    • 84858733754 scopus 로고    scopus 로고
    • The HIF1A C85T single nucleotide polymorphism influences the number of branches of the human coronary tree
    • J. Duran, V. Götzens, J. Carballo et al. , "The HIF1A C85T single nucleotide polymorphism influences the number of branches of the human coronary tree," Cardiology, vol. 121, no. 3,pp. 156-159, 2012.
    • (2012) Cardiology , vol.121 , Issue.3 , pp. 156-159
    • Duran, J.1    Götzens, V.2    Carballo, J.3
  • 133
    • 81555205783 scopus 로고    scopus 로고
    • Study on the role of environmental parameters and HIF-1A gene polymorphism in coronary collateral formation among patients with ischemic heart disease
    • M. Alidoosti,M. Ghaedi, A. Soleimani et al. , "Study on the role of environmental parameters and HIF-1A gene polymorphism in coronary collateral formation among patients with ischemic heart disease," Clinical Biochemistry, vol. 44, no. 17-18, pp. 1421-1424, 2011.
    • (2011) Clinical Biochemistry , vol.44 , Issue.17-18 , pp. 1421-1424
    • Alidoosti, M.1    Ghaedi, M.2    Soleimani, A.3
  • 134
    • 77951738011 scopus 로고    scopus 로고
    • Myocardial transfection of hypoxia inducible factor-1via an adenoviral vector during coronary artery bypass grafting -A multicenter phase i and safety study
    • E. G. Kilian, S. Sadoni, C. Vicol et al. , "Myocardial transfection of hypoxia inducible factor-1via an adenoviral vector during coronary artery bypass grafting-a multicenter phase I and safety study," Circulation Journal, vol. 74, no. 5, pp. 916-924, 2010.
    • (2010) Circulation Journal , vol.74 , Issue.5 , pp. 916-924
    • Kilian, E.G.1    Sadoni, S.2    Vicol, C.3
  • 135
    • 78649876180 scopus 로고    scopus 로고
    • Inhibition of prolyl hydroxylases increases erythropoietin production in ESRD
    • W. M. Bernhardt, M. S. Wiesener, P. Scigalla et al. , "Inhibition of prolyl hydroxylases increases erythropoietin production in ESRD," Journal of the American Society of Nephrology, vol. 21, no. 12, pp. 2151-2156, 2010.
    • (2010) Journal of the American Society of Nephrology , vol.21 , Issue.12 , pp. 2151-2156
    • Bernhardt, W.M.1    Wiesener, M.S.2    Scigalla, P.3
  • 137
    • 84887011365 scopus 로고    scopus 로고
    • FG-4592, an oral hypoxia-inducible factor prolyl hydroxylase-inhibitor, corrects anemia without iron supplementation in incident dialysis patients
    • M. A. Besarab, E. N. Chernyavskaya, I. Motylev et al. , "FG-4592, an oral hypoxia-inducible factor prolyl hydroxylase-inhibitor, corrects anemia without iron supplementation in incident dialysis patients," Journal of the American Society of Nephrology, vol. 23, p. 428A, 2012.
    • (2012) Journal of the American Society of Nephrology , vol.23 , pp. 428A
    • Besarab, M.A.1    Chernyavskaya, E.N.2    Motylev, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.