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Volumn 2015, Issue , 2015, Pages

Hypoxia Inducible Factor Pathway and Physiological Adaptation: A Cell Survival Pathway?

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CARBONATE DEHYDRATASE; CASPASE 9; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; CYCLOOXYGENASE 4; CYTOCHROME C; CYTOCHROME C1; HYPOXIA INDUCIBLE FACTOR; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; IRON SULFUR PROTEIN; MANGANESE SUPEROXIDE DISMUTASE; OXYGENASE; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROTEIN BAK; PROTEIN BAX; PROTEIN BNIP3; PYRUVATE DEHYDROGENASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; SODIUM PROTON EXCHANGE PROTEIN 1; SUPEROXIDE; UBIQUINOL CYTOCHROME C REDUCTASE; UNCLASSIFIED DRUG; VASCULOTROPIN; XANTHINE DEHYDROGENASE; XANTHINE OXIDASE; OXYGEN; TRANSCRIPTION FACTOR;

EID: 84944254470     PISSN: 09629351     EISSN: 14661861     Source Type: Journal    
DOI: 10.1155/2015/584758     Document Type: Review
Times cited : (134)

References (147)
  • 1
    • 0031020884 scopus 로고    scopus 로고
    • Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells
    • H. Tian, S. L. McKnight, and D. W. Russell, "Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells," Genes&Development, vol. 11, no. 1, pp. 72-82, 1997
    • (1997) Genes&Development , vol.11 , Issue.1 , pp. 72-82
    • Tian, H.1    McKnight, S.L.2    Russell, D.W.3
  • 2
    • 0031000736 scopus 로고    scopus 로고
    • A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1 regulates the VEGF expression and is potentially involved in lung and vascular development
    • M. Ema, S. Taya, N. Yokotani, K. Sogawa, Y. Matsuda, and Y. Fujii-Kuriyama, "A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1 regulates the VEGF expression and is potentially involved in lung and vascular development," Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 9, pp. 4273-4278, 1997
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , Issue.9 , pp. 4273-4278
    • Ema, M.1    Taya, S.2    Yokotani, N.3    Sogawa, K.4    Matsuda, Y.5    Fujii-Kuriyama, Y.6
  • 3
    • 0031733828 scopus 로고    scopus 로고
    • Molecular characterization and chromosomal localization of a third alpha-class hypoxia inducible factor subunit, HIF3alpha
    • Y. Z. Gu, S. M. Moran, J. B. Hogenesch, L. Wartman, and C. A. Bradfield, "Molecular characterization and chromosomal localization of a third alpha-class hypoxia inducible factor subunit, HIF3alpha," Gene Expression, vol. 7, no. 3, pp. 205-213, 1998
    • (1998) Gene Expression , vol.7 , Issue.3 , pp. 205-213
    • Gu, Y.Z.1    Moran, S.M.2    Hogenesch, J.B.3    Wartman, L.4    Bradfield, C.A.5
  • 4
    • 0033233243 scopus 로고    scopus 로고
    • Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1
    • G. L. Semenza, "Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1," Annual Review of Cell and Developmental Biology, vol. 15, pp. 551-578, 1999
    • (1999) Annual Review of Cell and Developmental Biology , vol.15 , pp. 551-578
    • Semenza, G.L.1
  • 5
    • 0036828845 scopus 로고    scopus 로고
    • Leu-574 of HIF-1 is essential for the von Hippel-Lindau (VHL)-mediated degradation pathway
    • L. E. Eric Huang, E. A. Pete, M. Schau, J. Milligan, and J. Gu, "Leu-574 of HIF-1 is essential for the von Hippel-Lindau (VHL)-mediated degradation pathway," The Journal of Biological Chemistry, vol. 277, no. 44, pp. 41750-41755, 2002
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.44 , pp. 41750-41755
    • Eric Huang, L.E.1    Pete, E.A.2    Schau, M.3    Milligan, J.4    Gu, J.5
  • 6
  • 7
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation
    • N. Masson, C. Willam, P. H. Maxwell, C. W. Pugh, and P. J. Ratcliffe, "Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation," The EMBO Journal, vol. 20, no. 18, pp. 5197-5206, 2001
    • (2001) The EMBO Journal , vol.20 , Issue.18 , pp. 5197-5206
    • Masson, N.1    Willam, C.2    Maxwell, P.H.3    Pugh, C.W.4    Ratcliffe, P.J.5
  • 8
    • 41149115123 scopus 로고    scopus 로고
    • The role of oxygen availability in embryonic development and stem cell function
    • M. C. Simon and B. Keith, "The role of oxygen availability in embryonic development and stem cell function," Nature Reviews Molecular Cell Biology, vol. 9, no. 4, pp. 285-296, 2008
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.4 , pp. 285-296
    • Simon, M.C.1    Keith, B.2
  • 9
    • 0032538797 scopus 로고    scopus 로고
    • Signal transduction in hypoxic cells: Inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1alpha
    • P. J. Kallio, K. Okamoto, S. O'Brien et al., "Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1alpha," The EMBO Journal, vol. 17, no. 22, pp. 6573-6586, 1998
    • (1998) The EMBO Journal , vol.17 , Issue.22 , pp. 6573-6586
    • Kallio, P.J.1    Okamoto, K.2    O'brien, S.3
  • 10
    • 0030937718 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible factor-1; Definition of regulatory domains within the subunit
    • C. W. Pugh, J. F. O'Rourke, M. Nagao, J. M. Gleadle, and P. J. Ratcliffe, "Activation of hypoxia-inducible factor-1; Definition of regulatory domains within the subunit," The Journal of Biological Chemistry, vol. 272, no. 17, pp. 11205-11214, 1997
    • (1997) The Journal of Biological Chemistry , vol.272 , Issue.17 , pp. 11205-11214
    • Pugh, C.W.1    O'rourke, J.F.2    Nagao, M.3    Gleadle, J.M.4    Ratcliffe, P.J.5
  • 11
    • 33947724515 scopus 로고    scopus 로고
    • HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells
    • R. Fukuda, H. Zhang, J. W. Kim, L. Shimoda, C. V. Dang, and G. Semenza, "HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells," Cell, vol. 129, no. 1, pp. 111-122, 2007
    • (2007) Cell , vol.129 , Issue.1 , pp. 111-122
    • Fukuda, R.1    Zhang, H.2    Kim, J.W.3    Shimoda, L.4    Dang, C.V.5    Semenza, G.6
  • 12
    • 9444283176 scopus 로고    scopus 로고
    • Differentiating the functional role of hypoxia-inducible factor (HIF)-1 and HIF-2 (EPAS-1) by the use of RNA interference: Erythropoietin is a HIF-2 target gene in Hep3B and Kelly cells
    • C. Warnecke, Z. Zaborowska, J. Kurreck et al., "Differentiating the functional role of hypoxia-inducible factor (HIF)-1 and HIF-2 (EPAS-1) by the use of RNA interference: erythropoietin is a HIF-2 target gene in Hep3B and Kelly cells," The FASEB Journal, vol. 18, no. 12, pp. 1462-1464, 2004
    • (2004) The FASEB Journal , vol.18 , Issue.12 , pp. 1462-1464
    • Warnecke, C.1    Zaborowska, Z.2    Kurreck, J.3
  • 13
    • 0345491599 scopus 로고    scopus 로고
    • Differential Roles of Hypoxia-Inducible Factor 1 (HIF-1) and HIF-2 in Hypoxic Gene Regulation
    • C.-J. Hu, L.-Y. Wang, L. A. Chodosh, B. Keith, and M. C. Simon, "Differential Roles of Hypoxia-Inducible Factor 1 (HIF-1) and HIF-2 in Hypoxic Gene Regulation," Molecular and Cellular Biology, vol. 23, no. 24, pp. 9361-9374, 2003
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.24 , pp. 9361-9374
    • Hu, C.-J.1    Wang, L.-Y.2    Chodosh, L.A.3    Keith, B.4    Simon, M.C.5
  • 14
    • 20744445650 scopus 로고    scopus 로고
    • Contrasting properties of hypoxia-inducible factor 1 (HIF-1) and HIF-2 in von Hippel-Lindau-associated renal cell carcinoma
    • R. R. Raval, K. W. Lau, M. G. B. Tran et al., "Contrasting properties of hypoxia-inducible factor 1 (HIF-1) and HIF-2 in von Hippel-Lindau-associated renal cell carcinoma," Molecular and Cellular Biology, vol. 25, no. 13, pp. 5675-5686, 2005
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.13 , pp. 5675-5686
    • Raval, R.R.1    Lau, K.W.2    Tran, M.G.B.3
  • 15
    • 33744954065 scopus 로고    scopus 로고
    • Concordant regulation of gene expression by hypoxia and 2-oxoglutarate-dependent dioxygenase inhibition: The role of HIF-1, HIF-2, and other pathways
    • G. P. Elvidge, L. Glenny, R. J. Appelhoff, P. J. Ratcliffe, J. Ragoussis, and J. M. Gleadle, "Concordant regulation of gene expression by hypoxia and 2-oxoglutarate-dependent dioxygenase inhibition: the role of HIF-1, HIF-2, and other pathways,"The Journal of Biological Chemistry, vol. 281, no. 22, pp. 15215-15226, 2006
    • (2006) The Journal of Biological Chemistry , vol.281 , Issue.22 , pp. 15215-15226
    • Elvidge, G.P.1    Glenny, L.2    Appelhoff, R.J.3    Ratcliffe, P.J.4    Ragoussis, J.5    Gleadle, J.M.6
  • 18
    • 0037031808 scopus 로고    scopus 로고
    • Inhibitory PAS domain protein (IPAS) is a hypoxiainducible splicing variant of the hypoxia-inducible factor-3 locus
    • Y. Makino, A. Kanopka, W. J. Wilson, H. Tanaka, and L. Poellinger, "Inhibitory PAS domain protein (IPAS) is a hypoxiainducible splicing variant of the hypoxia-inducible factor-3 locus," The Journal of Biological Chemistry, vol. 277, no. 36, pp. 32405-32408, 2002
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 32405-32408
    • Makino, Y.1    Kanopka, A.2    Wilson, W.J.3    Tanaka, H.4    Poellinger, L.5
  • 19
    • 33750630119 scopus 로고    scopus 로고
    • Recruitment of HIF-1 and HIF-2 to common target genes is differentially regulated in neuroblastoma: HIF-2 promotes an aggressive phenotype
    • L. Holmquist-Mengelbier, E. Fredlund, T. Löfstedt et al., "Recruitment of HIF-1 and HIF-2 to common target genes is differentially regulated in neuroblastoma: HIF-2 promotes an aggressive phenotype," Cancer Cell, vol. 10, no. 5, pp. 413-423, 2006
    • (2006) Cancer Cell , vol.10 , Issue.5 , pp. 413-423
    • Holmquist-Mengelbier, L.1    Fredlund, E.2    Löfstedt, T.3
  • 20
    • 79957440998 scopus 로고    scopus 로고
    • The hypoxia-associated factor switches cells from HIF-1-to HIF-2-dependent signaling promoting stem cell characteristics, aggressive tumor growth and invasion
    • M. Y. Koh, R. Lemos Jr., X. Liu, and G. Powis, "The hypoxia-associated factor switches cells from HIF-1-to HIF-2-dependent signaling promoting stem cell characteristics, aggressive tumor growth and invasion," Cancer Research, vol. 71, no. 11, pp. 4015-4027, 2011
    • (2011) Cancer Research , vol.71 , Issue.11 , pp. 4015-4027
    • Koh, M.Y.1    Lemos, R.2    Liu, X.3    Powis, G.4
  • 21
    • 0035917808 scopus 로고    scopus 로고
    • Targeting of HIF- to the vonHippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation
    • P. Jaakkola, D. R. Mole, Y.-M. Tian et al., "Targeting of HIF- to the vonHippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation," Science, vol. 292, no. 5516, pp. 468-472, 2001
    • (2001) Science , vol.292 , Issue.5516 , pp. 468-472
    • Jaakkola, P.1    Mole, D.R.2    Tian, Y.-M.3
  • 22
    • 0035917313 scopus 로고    scopus 로고
    • HIF targeted for VHLmediated destruction by proline hydroxylation: Implications for O2 sensing
    • M. Ivan, K. Kondo, H. Yang et al., "HIF targeted for VHLmediated destruction by proline hydroxylation: implications for O2 sensing," Science, vol. 292, no. 5516, pp. 464-468, 2001
    • (2001) Science , vol.292 , Issue.5516 , pp. 464-468
    • Ivan, M.1    Kondo, K.2    Yang, H.3
  • 23
    • 0032493368 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 1 is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway
    • L. E. Huang, J. Gu, M. Schau, and H. F. Bunn, "Regulation of hypoxia-inducible factor 1 is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway," Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 14, pp. 7987-7992, 1998
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.14 , pp. 7987-7992
    • Huang, L.E.1    Gu, J.2    Schau, M.3    Bunn, H.F.4
  • 24
    • 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
  • 25
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1 in 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-1 in 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
  • 27
    • 67649980040 scopus 로고    scopus 로고
    • Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases
    • R. Chowdhury, M. A. McDonough, J. Mecinovíc et al., "Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases," Structure, vol. 17, no. 7, pp. 981-989, 2009
    • (2009) Structure , vol.17 , Issue.7 , pp. 981-989
    • Chowdhury, R.1    McDonough, M.A.2    Mecinovíc, J.3
  • 28
    • 0036433394 scopus 로고    scopus 로고
    • Mammalian EGLN genes have distinct patterns of mRNA expression and regulation
    • M. E. Lieb, K. Menzies, M. C. Moschella, R. Ni, and M. B. Taubman, "Mammalian EGLN genes have distinct patterns of mRNA expression and regulation," Biochemistry and Cell Biology, vol. 80, no. 4, pp. 421-426, 2002
    • (2002) Biochemistry and Cell Biology , vol.80 , Issue.4 , pp. 421-426
    • Lieb, M.E.1    Menzies, K.2    Moschella, M.C.3    Ni, R.4    Taubman, M.B.5
  • 29
    • 38649143118 scopus 로고    scopus 로고
    • Deficiency or inhibition of oxygen sensor Phd1 induces hypoxia tolerance by reprogramming basal metabolism
    • J. Aragonés, M. Schneider, K. van Geyte et al., "Deficiency or inhibition of oxygen sensor Phd1 induces hypoxia tolerance by reprogramming basal metabolism," Nature Genetics, vol. 40, no. 2, pp. 170-180, 2008
    • (2008) Nature Genetics , vol.40 , Issue.2 , pp. 170-180
    • Aragonés, J.1    Schneider, M.2    Van Geyte, K.3
  • 30
    • 77449090208 scopus 로고    scopus 로고
    • Loss or silencing of the PHD1 prolyl hydroxylase protects livers of mice against ischemia/reperfusion injury
    • e2-1154. e2
    • M. Schneider, K. van Geyte, P. Fraisl et al., "Loss or silencing of the PHD1 prolyl hydroxylase protects livers of mice against ischemia/reperfusion injury," Gastroenterology, vol. 138, no. 3, pp. 1143. e2-1154. e2, 2010
    • (2010) Gastroenterology , vol.138 , Issue.3 , pp. 1143
    • Schneider, M.1    Van Geyte, K.2    Fraisl, P.3
  • 31
    • 33750976389 scopus 로고    scopus 로고
    • Placental but not heart defects are associated with elevated hypoxia-inducible factor alpha levels in mice lacking prolyl hydroxylase domain protein 2
    • K. Takeda, V. C. Ho, H. Takeda, L.-J. Duan, A. Nagy, and G.-H. Fong, "Placental but not heart defects are associated with elevated hypoxia-inducible factor alpha levels in mice lacking prolyl hydroxylase domain protein 2," Molecular and Cellular Biology, vol. 26, no. 22, pp. 8336-8346, 2006
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.22 , pp. 8336-8346
    • Takeda, K.1    Ho, V.C.2    Takeda, H.3    Duan, L.-J.4    Nagy, A.5    Fong, G.-H.6
  • 32
    • 34547905406 scopus 로고    scopus 로고
    • Essential role for prolyl hydroxylase domain protein 2 in oxygen homeostasis of the adult vascular system
    • K. Takeda, A. Cowan, and G.-H. Fong, "Essential role for prolyl hydroxylase domain protein 2 in oxygen homeostasis of the adult vascular system," Circulation, vol. 116, no. 7, pp. 774-781, 2007
    • (2007) Circulation , vol.116 , Issue.7 , pp. 774-781
    • Takeda, K.1    Cowan, A.2    Fong, G.-H.3
  • 33
    • 42449163874 scopus 로고    scopus 로고
    • Somatic inactivation of the PHD2 prolyl hydroxylase causes polycythemia and congestive heart failure
    • Y. A. Minamishima, J. Moslehi, N. Bardeesy, D. Cullen, R. T. Bronson, and W. G. Kaelin Jr., "Somatic inactivation of the PHD2 prolyl hydroxylase causes polycythemia and congestive heart failure," Blood, vol. 111, no. 6, pp. 3236-3244, 2008
    • (2008) Blood , vol.111 , Issue.6 , pp. 3236-3244
    • Minamishima, Y.A.1    Moslehi, J.2    Bardeesy, N.3    Cullen, D.4    Bronson, R.T.5    Kaelin, W.G.6
  • 34
    • 43249108443 scopus 로고    scopus 로고
    • Abnormal sympathoadrenal development and systemic hypotension in PHD3/ mice
    • T. Bishop, D. Gallagher, A. Pascual et al., "Abnormal sympathoadrenal development and systemic hypotension in PHD3/ mice," Molecular and Cellular Biology, vol. 28, no. 10, pp. 3386-3400, 2008
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.10 , pp. 3386-3400
    • Bishop, T.1    Gallagher, D.2    Pascual, A.3
  • 35
    • 84896350565 scopus 로고    scopus 로고
    • Targeted gene deletion of prolyl hydroxylase domain protein 3 triggers angiogenesis and preserves cardiac function by stabilizing hypoxia inducible factor 1 alpha following myocardial infarction
    • B. Oriowo, M. Thirunavukkarasu, V. Selvaraju et al., "Targeted gene deletion of prolyl hydroxylase domain protein 3 triggers angiogenesis and preserves cardiac function by stabilizing hypoxia inducible factor 1 alpha following myocardial infarction," Current Pharmaceutical Design, vol. 20, no. 9, pp. 1305-1310, 2014
    • (2014) Current Pharmaceutical Design , vol.20 , Issue.9 , pp. 1305-1310
    • Oriowo, B.1    Thirunavukkarasu, M.2    Selvaraju, V.3
  • 36
    • 0034458228 scopus 로고    scopus 로고
    • The NADPH oxidase of endothelial cells
    • B. M. Babior, "The NADPH oxidase of endothelial cells," IUBMB Life, vol. 50, no. 4-5, pp. 267-269, 2000
    • (2000) IUBMB Life , vol.50 , Issue.4-5 , pp. 267-269
    • Babior, B.M.1
  • 38
    • 0026564816 scopus 로고
    • Cytochrome P450: Progress and predictions
    • M. J. Coon, X. Ding, S. J. Pernecky, and A. D. N. Vaz, "Cytochrome P450: progress and predictions," The FASEB Journal, vol. 6, no. 2, pp. 669-673, 1992
    • (1992) The FASEB Journal , vol.6 , Issue.2 , pp. 669-673
    • Coon, M.J.1    Ding, X.2    Pernecky, S.J.3    Vaz, A.D.N.4
  • 40
    • 0030969868 scopus 로고    scopus 로고
    • Superoxide production by the mitochondrial respiratory chain
    • J. F. Turrens, "Superoxide production by the mitochondrial respiratory chain," Bioscience Reports, vol. 17, no. 1, pp. 3-8, 1997
    • (1997) Bioscience Reports , vol.17 , Issue.1 , pp. 3-8
    • Turrens, J.F.1
  • 41
    • 0035929367 scopus 로고    scopus 로고
    • The site of production of superoxide radical in mitochondrial Complex i is not a bound ubisemiquinone but presumably iron-sulfur cluster N2
    • M. L. Genova, B. Ventura, G. Giuliano et al., "The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron-sulfur cluster N2," FEBS Letters, vol. 505, no. 3, pp. 364-368, 2001
    • (2001) FEBS Letters , vol.505 , Issue.3 , pp. 364-368
    • Genova, M.L.1    Ventura, B.2    Giuliano, G.3
  • 43
    • 0037158626 scopus 로고    scopus 로고
    • O2 sensing in hypoxic pulmonary vasoconstriction: Themitochondrial door re-opens
    • G. B. Waypa and P. T. Schumacker, "O2 sensing in hypoxic pulmonary vasoconstriction: themitochondrial door re-opens," Respiratory Physiology and Neurobiology, vol. 132, no. 1, pp. 81-91, 2002
    • (2002) Respiratory Physiology and Neurobiology , vol.132 , Issue.1 , pp. 81-91
    • Waypa, G.B.1    Schumacker, P.T.2
  • 47
    • 0034680825 scopus 로고    scopus 로고
    • The role of mitochondria in the regulation of hypoxia-inducible factor 1 expression during hypoxia
    • F. H. Agani, P. Pichiule, J. C. Chavez, and J. C. LaManna, "The role of mitochondria in the regulation of hypoxia-inducible factor 1 expression during hypoxia," The Journal of Biological Chemistry, vol. 275, no. 46, pp. 35863-35867, 2000
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.46 , pp. 35863-35867
    • Agani, F.H.1    Pichiule, P.2    Chavez, J.C.3    Lamanna, J.C.4
  • 48
    • 84875472017 scopus 로고    scopus 로고
    • The role of free radicals in the aging brain and Parkinson's disease: Convergence and parallelism
    • H. Kumar, H. W. Lim, S. V. More et al., "The role of free radicals in the aging brain and Parkinson's disease: convergence and parallelism," International Journal of Molecular Sciences, vol. 13, no. 8, pp. 10478-10504, 2012
    • (2012) International Journal of Molecular Sciences , vol.13 , Issue.8 , pp. 10478-10504
    • Kumar, H.1    Lim, H.W.2    More, S.V.3
  • 50
    • 24144447915 scopus 로고    scopus 로고
    • Mitochondrial dysfunction resulting fromloss of cytochrome c impairs cellular oxygen sensing and hypoxicHIF- Activation
    • K. D. Mansfield, R. D. Guzy, Y. Pan et al., "Mitochondrial dysfunction resulting fromloss of cytochrome c impairs cellular oxygen sensing and hypoxicHIF- Activation," CellMetabolism, vol. 1, no. 6, pp. 393-399, 2005
    • (2005) CellMetabolism , vol.1 , Issue.6 , pp. 393-399
    • Mansfield, K.D.1    Guzy, R.D.2    Pan, Y.3
  • 51
    • 24144493814 scopus 로고    scopus 로고
    • Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing
    • R. D. Guzy, B. Hoyos, E. Robin et al., "Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing," Cell Metabolism, vol. 1, no. 6, pp. 401-408, 2005
    • (2005) Cell Metabolism , vol.1 , Issue.6 , pp. 401-408
    • Guzy, R.D.1    Hoyos, B.2    Robin, E.3
  • 52
    • 0034682786 scopus 로고    scopus 로고
    • Reactive oxygen species generated at mitochondrial Complex III stabilize hypoxia-inducible factor-1 during hypoxia: A mechanism of O2 sensing
    • N. S. Chandel, D. S. McClintock, C. E. Feliciano et al., "Reactive oxygen species generated at mitochondrial Complex III stabilize hypoxia-inducible factor-1 during hypoxia: a mechanism of O2 sensing," The Journal of Biological Chemistry, vol. 275, no. 33, pp. 25130-25138, 2000
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.33 , pp. 25130-25138
    • Chandel, N.S.1    McClintock, D.S.2    Feliciano, C.E.3
  • 53
    • 34250745912 scopus 로고    scopus 로고
    • The site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production
    • E. L. Bell, T. A. Klimova, J. Eisenbart et al., "The site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production," The Journal of Cell Biology, vol. 177, no. 6, pp. 1029-1036, 2007
    • (2007) The Journal of Cell Biology , vol.177 , Issue.6 , pp. 1029-1036
    • Bell, E.L.1    Klimova, T.A.2    Eisenbart, J.3
  • 54
    • 0034282388 scopus 로고    scopus 로고
    • Nonhypoxic pathway mediates the induction of hypoxia-inducible factor 1 in vascular smooth muscle cells
    • D. E. Richard, E. Berra, and J. Pouyssegur, "Nonhypoxic pathway mediates the induction of hypoxia-inducible factor 1 in vascular smooth muscle cells," The Journal of Biological Chemistry, vol. 275, no. 35, pp. 26765-26771, 2000
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.35 , pp. 26765-26771
    • Richard, D.E.1    Berra, E.2    Pouyssegur, J.3
  • 55
    • 0033562569 scopus 로고    scopus 로고
    • Defective vascularization of HIF-1-null embryos is not associated with VEGF deficiency but with mesenchymal cell death
    • L. E. Kotch, N. V. Iyer, E. Laughner, and G. L. Semenza, "Defective vascularization of HIF-1-null embryos is not associated with VEGF deficiency but with mesenchymal cell death," Developmental Biology, vol. 209, no. 2, pp. 254-267, 1999
    • (1999) Developmental Biology , vol.209 , Issue.2 , pp. 254-267
    • Kotch, L.E.1    Iyer, N.V.2    Laughner, E.3    Semenza, G.L.4
  • 56
    • 0032213236 scopus 로고    scopus 로고
    • The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development
    • H. Tian, R. E. Hammer, A. M. Matsumoto, D. W. Russell, and S. L. McKnight, "The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development," Genes and Development, vol. 12, no. 21, pp. 3320-3324, 1998
    • (1998) Genes and Development , vol.12 , Issue.21 , pp. 3320-3324
    • Tian, H.1    Hammer, R.E.2    Matsumoto, A.M.3    Russell, D.W.4    McKnight, S.L.5
  • 57
    • 0035159670 scopus 로고    scopus 로고
    • HIF-1 is expressed in normoxic tissue and displays an organ-specific regulation under systemic hypoxia
    • D. M. Stroka, T. Burkhardt, I. Desbaillets et al., "HIF-1 is expressed in normoxic tissue and displays an organ-specific regulation under systemic hypoxia," The FASEB Journal, vol. 15, no. 13, pp. 2445-2453, 2001
    • (2001) The FASEB Journal , vol.15 , Issue.13 , pp. 2445-2453
    • Stroka, D.M.1    Burkhardt, T.2    Desbaillets, I.3
  • 59
    • 0035914436 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-2 (HIF-2) is involved in the apoptotic response to hypoglycemia but not to hypoxia
    • K. Brusselmans, F. Bono, P. Maxwell et al., "Hypoxia-inducible factor-2 (HIF-2) is involved in the apoptotic response to hypoglycemia but not to hypoxia," The Journal of Biological Chemistry, vol. 276, no. 42, pp. 39192-39196, 2001
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.42 , pp. 39192-39196
    • Brusselmans, K.1    Bono, F.2    Maxwell, P.3
  • 60
    • 0035203884 scopus 로고    scopus 로고
    • Hypoxia affects expression of circadian genes PER1 and CLOCK in mouse brain
    • D. Chilov, T. Hofer, C. Bauer, R. H. Wenger, and M. Gassmann, "Hypoxia affects expression of circadian genes PER1 and CLOCK in mouse brain," The FASEB Journal, vol. 15, no. 14, pp. 2613-2622, 2001
    • (2001) The FASEB Journal , vol.15 , Issue.14 , pp. 2613-2622
    • Chilov, D.1    Hofer, T.2    Bauer, C.3    Wenger, R.H.4    Gassmann, M.5
  • 61
    • 0036162264 scopus 로고    scopus 로고
    • Isoform-specific expression of hypoxia-inducible factor-1alpha during the late stages ofmouse spermiogenesis
    • H. H. Marti, D. M. Katschinski, K. F. Wagner, L. Schäffer, B. Stier, and R. H. Wenger, "Isoform-specific expression of hypoxia-inducible factor-1alpha during the late stages ofmouse spermiogenesis," Molecular Endocrinology, vol. 16, no. 2, pp. 234-243, 2002
    • (2002) Molecular Endocrinology , vol.16 , Issue.2 , pp. 234-243
    • Marti, H.H.1    Katschinski, D.M.2    Wagner, K.F.3    Schäffer, L.4    Stier, B.5    Wenger, R.H.6
  • 62
    • 0035966119 scopus 로고    scopus 로고
    • Differential Regulation of two alternatively spliced isoforms of hypoxia-inducible factor-1alpha in activated T lymphocytes
    • D. Lukashev, C. Caldwell, A. Ohta, P. Chen, and M. Sitkovsky, "Differential Regulation of two alternatively spliced isoforms of hypoxia-inducible factor-1alpha in activated T lymphocytes," The Journal of Biological Chemistry, vol. 276, no. 52, pp. 48754-48763, 2001
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.52 , pp. 48754-48763
    • Lukashev, D.1    Caldwell, C.2    Ohta, A.3    Chen, P.4    Sitkovsky, M.5
  • 63
    • 0037088576 scopus 로고    scopus 로고
    • Heat induction of the unphosphorylated form of hypoxia-inducible factor-1alpha is dependent on heat shock protein-90 activity
    • D. M. Katschinski, L. Le, D. Heinrich et al., "Heat induction of the unphosphorylated form of hypoxia-inducible factor-1alpha is dependent on heat shock protein-90 activity," Journal of Biological Chemistry, vol. 277, no. 11, pp. 9262-9267, 2002
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.11 , pp. 9262-9267
    • Katschinski, D.M.1    Le, L.2    Heinrich, D.3
  • 64
    • 84898052710 scopus 로고    scopus 로고
    • Low-dose radiation exposure induces a HIF-1-mediated adaptive and protective metabolic response
    • R. Lall, S. Ganapathy, M. Yang et al., "Low-dose radiation exposure induces a HIF-1-mediated adaptive and protective metabolic response," Cell Death and Differentiation, vol. 21, no. 5, pp. 836-844, 2014
    • (2014) Cell Death and Differentiation , vol.21 , Issue.5 , pp. 836-844
    • Lall, R.1    Ganapathy, S.2    Yang, M.3
  • 65
    • 84901373499 scopus 로고    scopus 로고
    • The role of the HIF-1 transcription factor in increased cell division at physiological oxygen tensions
    • S. Carrera, J. Senra, M. I. Acosta et al., "The role of the HIF-1 transcription factor in increased cell division at physiological oxygen tensions," PLoS ONE, vol. 9, no. 5, Article ID e97938, 2014
    • (2014) PLoS ONE , vol.9 , Issue.5
    • Carrera, S.1    Senra, J.2    Acosta, M.I.3
  • 66
    • 0013199207 scopus 로고    scopus 로고
    • Early expression ofmyocardialHIF-1 in response to mechanical stresses: Regulation by stretch-activated channels and the phosphatidylinositol 3-kinase signaling pathway
    • C.-H. Kim, Y.-S. Cho, Y.-S. Chun, J.-W. Park, and M.-S. Kim, "Early expression ofmyocardialHIF-1 in response to mechanical stresses: regulation by stretch-activated channels and the phosphatidylinositol 3-kinase signaling pathway," Circulation Research, vol. 90, no. 2, pp. e25-e33, 2002
    • (2002) Circulation Research , vol.90 , Issue.2 , pp. e25-e33
    • Kim, C.-H.1    Cho, Y.-S.2    Chun, Y.-S.3    Park, J.-W.4    Kim, M.-S.5
  • 67
    • 15444342958 scopus 로고    scopus 로고
    • Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1
    • N. V. Iyer, L. E. Kotch, F. Agani et al., "Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1," Genes and Development, vol. 12, no. 2, pp. 149-162, 1998
    • (1998) Genes and Development , vol.12 , Issue.2 , pp. 149-162
    • Iyer, N.V.1    Kotch, L.E.2    Agani, F.3
  • 68
    • 0032100732 scopus 로고    scopus 로고
    • HIF-1 is required for solid tumor formation and embryonic vascularization
    • H. E. Ryan, J. Lo, and R. S. Johnson, "HIF-1 is required for solid tumor formation and embryonic vascularization," The EMBO Journal, vol. 17, no. 11, pp. 3005-3015, 1998
    • (1998) The EMBO Journal , vol.17 , Issue.11 , pp. 3005-3015
    • Ryan, H.E.1    Lo, J.2    Johnson, R.S.3
  • 69
    • 84917736664 scopus 로고    scopus 로고
    • Moderate hypoxia potentiates interleukin-1beta production in activated human macrophages
    • E. J. Folco, G. K. Sukhova, T. Quillard, and P. Libby, "Moderate hypoxia potentiates interleukin-1beta production in activated human macrophages," Circulation Research, vol. 115, no. 10, pp. 875-883, 2014
    • (2014) Circulation Research , vol.115 , Issue.10 , pp. 875-883
    • Folco, E.J.1    Sukhova, G.K.2    Quillard, T.3    Libby, P.4
  • 70
    • 0033104847 scopus 로고    scopus 로고
    • Impaired physiological responses to chronic hypoxia in mice partially deficient for hypoxia-inducible factor 1
    • A. Y. Yu, L. A. Shimoda,N. V. Iyer et al., "Impaired physiological responses to chronic hypoxia in mice partially deficient for hypoxia-inducible factor 1," The Journal of Clinical Investigation, vol. 103, no. 5, pp. 691-696, 1999
    • (1999) The Journal of Clinical Investigation , vol.103 , Issue.5 , pp. 691-696
    • Yu, A.Y.1    Shimoda, L.A.2    Iyer, N.V.3
  • 72
    • 22044436344 scopus 로고    scopus 로고
    • Developmental changes in HIF transcription factor in carotid body: Relevance for O2 sensing by chemoreceptors
    • J.-C. Roux, H. Brismar, A. Aperia, and H. Lagercrantz, "Developmental changes in HIF transcription factor in carotid body: relevance for O2 sensing by chemoreceptors," Pediatric Research, vol. 58, no. 1, pp. 53-57, 2005
    • (2005) Pediatric Research , vol.58 , Issue.1 , pp. 53-57
    • Roux, J.-C.1    Brismar, H.2    Aperia, A.3    Lagercrantz, H.4
  • 74
    • 79952609061 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 2 (HIF-2) heterozygous-null mice exhibit exaggerated carotid body sensitivity to hypoxia, breathing instability, and hypertension
    • Y.-J. Peng, J. Nanduri, S. A. Khan et al., "Hypoxia-inducible factor 2 (HIF-2) heterozygous-null mice exhibit exaggerated carotid body sensitivity to hypoxia, breathing instability, and hypertension," Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 7, pp. 3065-3070, 2011
    • (2011) Proceedings of the National Academy of Sciences of the United States of America , vol.108 , Issue.7 , pp. 3065-3070
    • Peng, Y.-J.1    Nanduri, J.2    Khan, S.A.3
  • 75
    • 84877347155 scopus 로고    scopus 로고
    • Mutual antagonism between hypoxia-inducible factors 1 and 2 regulates oxygen sensing and cardio-respiratory homeostasis
    • G. Yuan, Y.-J. Peng, V. D. Reddy et al., "Mutual antagonism between hypoxia-inducible factors 1 and 2 regulates oxygen sensing and cardio-respiratory homeostasis," Proceedings of the National Academy of Sciences of the United States of America, vol. 110, no. 19, pp. E1788-E1796, 2013
    • (2013) Proceedings of the National Academy of Sciences of the United States of America , vol.110 , Issue.19 , pp. E1788-E1796
    • Yuan, G.1    Peng, Y.-J.2    Reddy, V.D.3
  • 76
    • 0035499204 scopus 로고    scopus 로고
    • Hypoxia in cartilage: HIF-1 is essential for chondrocyte growth arrest and survival
    • E. Schipani,H. E. Ryan, S. Didrickson, T. Kobayashi,M. Knight, and R. S. Johnson, "Hypoxia in cartilage: HIF-1 is essential for chondrocyte growth arrest and survival," Genes&Development, vol. 15, no. 21, pp. 2865-2876, 2001
    • (2001) Genes&Development , vol.15 , Issue.21 , pp. 2865-2876
    • Schipani, E.1    Ryan, H.E.2    Didrickson, S.3    Kobayashi, T.4    Knight, M.5    Johnson, R.S.6
  • 77
    • 0030879909 scopus 로고    scopus 로고
    • Regulation of human placental development by oxygen tension
    • O. Genbacev,Y. Zhou, J. W. Ludlow, and S. J. Fisher, "Regulation of human placental development by oxygen tension," Science, vol. 277, no. 5332, pp. 1669-1672, 1997
    • (1997) Science , vol.277 , Issue.5332 , pp. 1669-1672
    • Genbacev, O.1    Zhou, Y.2    Ludlow, J.W.3    Fisher, S.J.4
  • 78
    • 0034671706 scopus 로고    scopus 로고
    • Placental cell fates are regulated in vivo by HIFmediated hypoxia responses
    • D. M. Adelman, M. Gertsenstein, A. Nagy, M. C. Simon, and E. Maltepe, "Placental cell fates are regulated in vivo by HIFmediated hypoxia responses," Genes and Development, vol. 14, no. 24, pp. 3191-3203, 2000
    • (2000) Genes and Development , vol.14 , Issue.24 , pp. 3191-3203
    • Adelman, D.M.1    Gertsenstein, M.2    Nagy, A.3    Simon, M.C.4    Maltepe, E.5
  • 79
    • 24344502368 scopus 로고    scopus 로고
    • Hypoxiainducible factor-dependent histone deacetylase activity determines stem cell fate in the placenta
    • E. Maltepe, G. W. Krampitz, K. M. Okazaki et al., "Hypoxiainducible factor-dependent histone deacetylase activity determines stem cell fate in the placenta," Development, vol. 132, no. 15, pp. 3393-3403, 2005
    • (2005) Development , vol.132 , Issue.15 , pp. 3393-3403
    • Maltepe, E.1    Krampitz, G.W.2    Okazaki, K.M.3
  • 80
    • 0034100836 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 mediates the biological effects of oxygen on human trophoblast differentiation through TGF3
    • I. Caniggia, H. Mostachfi, J. Winter et al., "Hypoxia-inducible factor-1 mediates the biological effects of oxygen on human trophoblast differentiation through TGF3," Journal of Clinical Investigation, vol. 105, no. 5, pp. 577-587, 2000
    • (2000) Journal of Clinical Investigation , vol.105 , Issue.5 , pp. 577-587
    • Caniggia, I.1    Mostachfi, H.2    Winter, J.3
  • 81
    • 0036511366 scopus 로고    scopus 로고
    • Physiologically low oxygen concentrations in fetal skin regulate hypoxia-inducible factor 1 and transforming growth factor-beta3
    • A. Scheid, R. H. Wenger, L. Schäffer et al., "Physiologically low oxygen concentrations in fetal skin regulate hypoxia-inducible factor 1 and transforming growth factor-beta3," The FASEB Journal, vol. 16, no. 3, pp. 411-413, 2002
    • (2002) The FASEB Journal , vol.16 , Issue.3 , pp. 411-413
    • Scheid, A.1    Wenger, R.H.2    Schäffer, L.3
  • 82
    • 79957510410 scopus 로고    scopus 로고
    • A central role for hypoxic signaling in cartilage, bone, and hematopoiesis
    • E. B. Rankin, A. J. Giaccia, and E. Schipani, "A central role for hypoxic signaling in cartilage, bone, and hematopoiesis," Current Osteoporosis Reports, vol. 9, no. 2, pp. 46-52, 2011
    • (2011) Current Osteoporosis Reports , vol.9 , Issue.2 , pp. 46-52
    • Rankin, E.B.1    Giaccia, A.J.2    Schipani, E.3
  • 83
    • 70349758284 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1alpha inhibits the fibroblast-like markers type i and type III collagen during hypoxia-induced chondrocyte redifferentiation: Hypoxia not only induces type II collagen and aggrecan, but it also inhibits type i and type III collagen in the hypoxia-inducible factor 1alpha-dependent redifferentiation of chondrocytes
    • E. Duval, S. Leclercq, J.-M. Elissalde, M. Demoor, P. Galéra, and K. Boumédiene, "Hypoxia-inducible factor 1alpha inhibits the fibroblast-like markers type I and type III collagen during hypoxia-induced chondrocyte redifferentiation: hypoxia not only induces type II collagen and aggrecan, but it also inhibits type I and type III collagen in the hypoxia-inducible factor 1alpha-dependent redifferentiation of chondrocytes," Arthritis and Rheumatism, vol. 60, no. 10, pp. 3038-3048, 2009
    • (2009) Arthritis and Rheumatism , vol.60 , Issue.10 , pp. 3038-3048
    • Duval, E.1    Leclercq, S.2    Elissalde, J.-M.3    Demoor, M.4    Galéra, P.5    Boumédiene, K.6
  • 84
    • 34248532510 scopus 로고    scopus 로고
    • HIF-1 regulation of chondrocyte apoptosis: Induction of the autophagic pathway
    • J. Bohensky, I. M. Shapiro, S. Leshinsky, S. P. Terkhorn, C. S. Adams, and V. Srinivas, "HIF-1 regulation of chondrocyte apoptosis: induction of the autophagic pathway," Autophagy, vol. 3, no. 3, pp. 207-214, 2007
    • (2007) Autophagy , vol.3 , Issue.3 , pp. 207-214
    • Bohensky, J.1    Shapiro, I.M.2    Leshinsky, S.3    Terkhorn, S.P.4    Adams, C.S.5    Srinivas, V.6
  • 85
    • 77953208836 scopus 로고    scopus 로고
    • Transcriptional regulation of endochondral ossification by HIF-2 during skeletal growth and osteoarthritis development
    • T. Saito, A. Fukai, A. Mabuchi et al., "Transcriptional regulation of endochondral ossification by HIF-2 during skeletal growth and osteoarthritis development," Nature Medicine, vol. 16, no. 6, pp. 678-686, 2010
    • (2010) Nature Medicine , vol.16 , Issue.6 , pp. 678-686
    • Saito, T.1    Fukai, A.2    Mabuchi, A.3
  • 86
    • 77953183739 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-2alpha is a catabolic regulator of osteoarthritic cartilage destruction
    • S. Yang, J. Kim, J. H. Ryu et al., "Hypoxia-inducible factor-2alpha is a catabolic regulator of osteoarthritic cartilage destruction," Nature Medicine, vol. 16, no. 6, pp. 687-693, 2010
    • (2010) Nature Medicine , vol.16 , Issue.6 , pp. 687-693
    • Yang, S.1    Kim, J.2    Ryu, J.H.3
  • 87
    • 33644622570 scopus 로고    scopus 로고
    • HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
    • I. Papandreou, R. A. Cairns, L. Fontana, A. L. Lim, and N. C. Denko, "HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption," Cell Metabolism, vol. 3, no. 3, pp. 187-197, 2006
    • (2006) Cell Metabolism , vol.3 , Issue.3 , pp. 187-197
    • Papandreou, I.1    Cairns, R.A.2    Fontana, L.3    Lim, A.L.4    Denko, N.C.5
  • 88
    • 0029942862 scopus 로고    scopus 로고
    • The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2. 8 A
    • T. Tsukihara, H. Aoyama, E. Yamashita et al., "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2. 8 A," Science, vol. 272, no. 5265, pp. 1136-1144, 1996
    • (1996) Science , vol.272 , Issue.5265 , pp. 1136-1144
    • Tsukihara, T.1    Aoyama, H.2    Yamashita, E.3
  • 90
    • 0031924141 scopus 로고    scopus 로고
    • Extramitochondrial ATP/ADP-ratios regulate cytochrome c oxidase activity via binding to the cytosolic domain of subunit IV
    • J. Napiwotzki and B. Kadenbach, "Extramitochondrial ATP/ADP-ratios regulate cytochrome c oxidase activity via binding to the cytosolic domain of subunit IV," Biological Chemistry, vol. 379, no. 3, pp. 335-339, 1998
    • (1998) Biological Chemistry , vol.379 , Issue.3 , pp. 335-339
    • Napiwotzki, J.1    Kadenbach, B.2
  • 91
    • 43649104579 scopus 로고    scopus 로고
    • Mitochondrial autophagy is an HIF-1-dependent adaptivemetabolic response to hypoxia
    • H. Zhang, M. Bosch-Marce, L. A. Shimoda et al., "Mitochondrial autophagy is an HIF-1-dependent adaptivemetabolic response to hypoxia," Journal of Biological Chemistry, vol. 283, no. 16, pp. 10892-10903, 2008
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.16 , pp. 10892-10903
    • Zhang, H.1    Bosch-Marce, M.2    Shimoda, L.A.3
  • 92
    • 0015239454 scopus 로고
    • The turnover of mitochondria in a variety of tissues of young adult and aged rats
    • R. A. Menzies and P. H. Gold, "The turnover of mitochondria in a variety of tissues of young adult and aged rats," The Journal of Biological Chemistry, vol. 246, no. 8, pp. 2425-2429, 1971
    • (1971) The Journal of Biological Chemistry , vol.246 , Issue.8 , pp. 2425-2429
    • Menzies, R.A.1    Gold, P.H.2
  • 93
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • B. Levine and D. J. Klionsky, "Development by self-digestion: molecular mechanisms and biological functions of autophagy," Developmental Cell, vol. 6, no. 4, pp. 463-477, 2004
    • (2004) Developmental Cell , vol.6 , Issue.4 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 94
    • 27644575235 scopus 로고    scopus 로고
    • Macroautophagy versus mitochondrial autophagy: A question of fate
    • M. Kundu and C. B. Thompson, "Macroautophagy versus mitochondrial autophagy: a question of fate" Cell Death & Differentiation, vol. 12, supplement 2, pp. 1484-1489, 2005
    • (2005) Cell Death & Differentiation , vol.12 , pp. 1484-1489
    • Kundu, M.1    Thompson, C.B.2
  • 96
    • 34447133404 scopus 로고    scopus 로고
    • Cardiac autophagy is a maladaptive response to hemodynamic stress
    • H. Zhu, P. Tannous, J. L. Johnstone et al., "Cardiac autophagy is a maladaptive response to hemodynamic stress," The Journal of Clinical Investigation, vol. 117, no. 7, pp. 1782-1793, 2007
    • (2007) The Journal of Clinical Investigation , vol.117 , Issue.7 , pp. 1782-1793
    • Zhu, H.1    Tannous, P.2    Johnstone, J.L.3
  • 97
    • 0018827202 scopus 로고
    • Lysosomal alterations in hypoxic and reoxygenated hearts. I. Ultrastructural and cytochemical changes
    • R. S. Decker and K. Wildenthal, "Lysosomal alterations in hypoxic and reoxygenated hearts. I. Ultrastructural and cytochemical changes," The American Journal of Pathology, vol. 98, no. 2, pp. 425-444, 1980
    • (1980) The American Journal of Pathology , vol.98 , Issue.2 , pp. 425-444
    • Decker, R.S.1    Wildenthal, K.2
  • 98
    • 33845511362 scopus 로고    scopus 로고
    • Response to myocardial ischemia/reperfusion injury involves Bnip3 and autophagy
    • A. Hamacher-Brady, N. R. Brady, S. E. Logue et al., "Response to myocardial ischemia/reperfusion injury involves Bnip3 and autophagy," Cell Death & Differentiation, vol. 14, no. 1, pp. 146-157, 2007
    • (2007) Cell Death & Differentiation , vol.14 , Issue.1 , pp. 146-157
    • Hamacher-Brady, A.1    Brady, N.R.2    Logue, S.E.3
  • 100
    • 0033566693 scopus 로고    scopus 로고
    • Reciprocal positive regulation of hypoxia-inducible factor 1alpha and insulin-like growth factor 2
    • D. Feldser, F. Agani, N. V. Iyer, B. Pak, G. Ferreira, and G. L. Semenza, "Reciprocal positive regulation of hypoxia-inducible factor 1alpha and insulin-like growth factor 2," Cancer Research, vol. 59, no. 16, pp. 3915-3918, 1999
    • (1999) Cancer Research , vol.59 , Issue.16 , pp. 3915-3918
    • Feldser, D.1    Agani, F.2    Iyer, N.V.3    Pak, B.4    Ferreira, G.5    Semenza, G.L.6
  • 101
    • 34248998801 scopus 로고    scopus 로고
    • Functional and physical interaction between Bcl-X and a BH3-like domain in Beclin-1
    • M. C. Maiuri, G. Le Toumelin, A. Criollo et al., "Functional and physical interaction between Bcl-X and a BH3-like domain in Beclin-1," The EMBO Journal, vol. 26, no. 10, pp. 2527-2539, 2007
    • (2007) The EMBO Journal , vol.26 , Issue.10 , pp. 2527-2539
    • Maiuri, M.C.1    Le Toumelin, G.2    Criollo, A.3
  • 102
    • 0038185378 scopus 로고    scopus 로고
    • Genomic targets of the human c-Myc protein
    • P. C. Fernandez, S. R. Frank, L. Wang et al., "Genomic targets of the human c-Myc protein," Genes and Development, vol. 17, no. 9, pp. 1115-1129, 2003
    • (2003) Genes and Development , vol.17 , Issue.9 , pp. 1115-1129
    • Fernandez, P.C.1    Frank, S.R.2    Wang, L.3
  • 104
    • 34247614521 scopus 로고    scopus 로고
    • HIF-1 inhibits mitochondrial biogenesis and cellular respiration in VHL-deficient renal cell carcinoma by repression of C-MYC activity
    • H. Zhang, P. Gao, R. Fukuda et al., "HIF-1 inhibits mitochondrial biogenesis and cellular respiration in VHL-deficient renal cell carcinoma by repression of C-MYC activity," Cancer Cell, vol. 11, no. 5, pp. 407-420, 2007
    • (2007) Cancer Cell , vol.11 , Issue.5 , pp. 407-420
    • Zhang, H.1    Gao, P.2    Fukuda, R.3
  • 105
    • 34547580590 scopus 로고    scopus 로고
    • HIF and c-Myc: Sibling rivals for control of cancer cell metabolism and proliferation
    • J. D. Gordan, C. B. Thompson, and M. C. Simon, "HIF and c-Myc: sibling rivals for control of cancer cell metabolism and proliferation," Cancer Cell, vol. 12, no. 2, pp. 108-113, 2007
    • (2007) Cancer Cell , vol.12 , Issue.2 , pp. 108-113
    • Gordan, J.D.1    Thompson, C.B.2    Simon, M.C.3
  • 106
    • 37549032776 scopus 로고    scopus 로고
    • The interplay between MYC and HIF in cancer
    • C. V. Dang, J.-W. Kim, P. Gao, and J. Yustein, "The interplay between MYC and HIF in cancer," Nature Reviews Cancer, vol. 8, no. 1, pp. 51-56, 2008
    • (2008) Nature Reviews Cancer , vol.8 , Issue.1 , pp. 51-56
    • Dang, C.V.1    Kim, J.-W.2    Gao, P.3    Yustein, J.4
  • 107
    • 0032581277 scopus 로고    scopus 로고
    • Role of HIF-1alpha in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis
    • P. Carmeliet, Y. Dor, J. M. Herbert et al., "Role of HIF-1alpha in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis," Nature, vol. 394, pp. 485-490, 1998
    • (1998) Nature , vol.394 , pp. 485-490
    • Carmeliet, P.1    Dor, Y.2    Herbert, J.M.3
  • 108
    • 0035418621 scopus 로고    scopus 로고
    • Constitutive expression of hypoxia-inducible factor-l renders pancreatic cancer cells resistant to apoptosis induced by hypoxia and nutrient deprivation
    • N. Akakura, M. Kobayashi, I. Horiuchi et al., "Constitutive expression of hypoxia-inducible factor-l renders pancreatic cancer cells resistant to apoptosis induced by hypoxia and nutrient deprivation," Cancer Research, vol. 61, no. 17, pp. 6548-6554, 2001
    • (2001) Cancer Research , vol.61 , Issue.17 , pp. 6548-6554
    • Akakura, N.1    Kobayashi, M.2    Horiuchi, I.3
  • 110
    • 0036006511 scopus 로고    scopus 로고
    • Bc1-2 family members and functional electron transport chain regulate oxygen deprivation-induced cell death
    • D. S. McClintock, M. T. Santore, V. Y. Lee et al., "Bc1-2 family members and functional electron transport chain regulate oxygen deprivation-induced cell death,"Molecular and Cellular Biology, vol. 22, no. 1, pp. 94-104, 2002
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.1 , pp. 94-104
    • McClintock, D.S.1    Santore, M.T.2    Lee, V.Y.3
  • 111
    • 0032585644 scopus 로고    scopus 로고
    • Role of hypoxia-induced Bax translocation and cytochrome c release in reoxygenation injury
    • P. Saikumar, Z. Dong, Y. Patel et al., "Role of hypoxia-induced Bax translocation and cytochrome c release in reoxygenation injury," Oncogene, vol. 17, no. 26, pp. 3401-3415, 1998
    • (1998) Oncogene , vol.17 , Issue.26 , pp. 3401-3415
    • Saikumar, P.1    Dong, Z.2    Patel, Y.3
  • 112
    • 0035957653 scopus 로고    scopus 로고
    • ProapoptoticBAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • M. C. Wei,W. X. Zong, E. H. Y. Cheng et al., "ProapoptoticBAX and BAK: a requisite gateway to mitochondrial dysfunction and death," Science, vol. 292, no. 5517, pp. 727-730, 2001
    • (2001) Science , vol.292 , Issue.5517 , pp. 727-730
    • Wei, M.C.1    Zong, W.X.2    Cheng, E.H.Y.3
  • 113
    • 0028950645 scopus 로고
    • Prevention of hypoxia-induced cell death by Bcl-2 and Bcl-xL
    • S. Shimizu, Y. Eguchi, H. Kosaka,W. Kamiike, H. Matsuda, and Y. Tsujimoto, "Prevention of hypoxia-induced cell death by Bcl-2 and Bcl-xL," Nature, vol. 374, no. 6525, pp. 811-813, 1995
    • (1995) Nature , vol.374 , Issue.6525 , pp. 811-813
    • Shimizu, S.1    Eguchi, Y.2    Kosaka, H.3    Kamiike, W.4    Matsuda, H.5    Tsujimoto, Y.6
  • 114
    • 0030025773 scopus 로고    scopus 로고
    • Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours
    • T. G. Graeber, C. Osmanian, T. Jacks et al., "Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours," Nature, vol. 379, pp. 88-91, 1996
    • (1996) Nature , vol.379 , pp. 88-91
    • Graeber, T.G.1    Osmanian, C.2    Jacks, T.3
  • 115
    • 0037072937 scopus 로고    scopus 로고
    • An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome -independent activation of caspase-9 by caspase-12
    • N. Morishima, K. Nakanishi, H. Takenouchi, T. Shibata, and Y. Yasuhiko, "An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome -independent activation of caspase-9 by caspase-12," The Journal of Biological Chemistry, vol. 277, no. 37, pp. 34287-34294, 2002
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.37 , pp. 34287-34294
    • Morishima, N.1    Nakanishi, K.2    Takenouchi, H.3    Shibata, T.4    Yasuhiko, Y.5
  • 116
    • 0032411879 scopus 로고    scopus 로고
    • Stress signals for apoptosis: Ceramide and c-Jun kinase
    • S. Basu and R. Kolesnick, "Stress signals for apoptosis: ceramide and c-Jun kinase," Oncogene, vol. 17, no. 25, pp. 3277-3285, 1998
    • (1998) Oncogene , vol.17 , Issue.25 , pp. 3277-3285
    • Basu, S.1    Kolesnick, R.2
  • 117
    • 0142120661 scopus 로고    scopus 로고
    • Hypoxia-inducible factors 1 and 2 are related to vascular endothelial growth factor expression and a poorer prognosis in nodular malignant melanomas of the skin
    • A. Giatromanolaki, E. Sivridis, C. Kouskoukis, K. C. Gatter, A. L. Harris, and M. I. Koukourakis, "Hypoxia-inducible factors 1 and 2 are related to vascular endothelial growth factor expression and a poorer prognosis in nodular malignant melanomas of the skin," Melanoma Research, vol. 13,no. 5, pp. 493-501,2003
    • (2003) Melanoma Research , vol.13 , Issue.5 , pp. 493-501
    • Giatromanolaki, A.1    Sivridis, E.2    Kouskoukis, C.3    Gatter, K.C.4    Harris, A.L.5    Koukourakis, M.I.6
  • 118
    • 84877101126 scopus 로고    scopus 로고
    • HIF1 and HIF2 independently activate SRC to promote melanoma metastases
    • S. C. Hanna, B. Krishnan, S. T. Bailey et al., "HIF1 and HIF2 independently activate SRC to promote melanoma metastases," Journal of Clinical Investigation, vol. 123, no. 5, pp. 2078-2093, 2013
    • (2013) Journal of Clinical Investigation , vol.123 , Issue.5 , pp. 2078-2093
    • Hanna, S.C.1    Krishnan, B.2    Bailey, S.T.3
  • 119
    • 79952760563 scopus 로고    scopus 로고
    • VEGF as a biomarker for metastatic uveal melanoma in humans
    • V. Barak, J. Pe'er, I. Kalickman, and S. Frenkel, "VEGF as a biomarker for metastatic uveal melanoma in humans," Current Eye Research, vol. 36, no. 4, pp. 386-390, 2011
    • (2011) Current Eye Research , vol.36 , Issue.4 , pp. 386-390
    • Barak, V.1    Pe'er, J.2    Kalickman, I.3    Frenkel, S.4
  • 120
    • 33747873394 scopus 로고    scopus 로고
    • Hypoxia inducible factors 1alpha and 2alpha are associated with VEGF expression and angiogenesis in gallbladder carcinomas
    • A. Giatromanolaki, E. Sivridis, C. Simopoulos et al., "Hypoxia inducible factors 1alpha and 2alpha are associated with VEGF expression and angiogenesis in gallbladder carcinomas," Journal of Surgical Oncology, vol. 94, no. 3, pp. 242-247, 2006
    • (2006) Journal of Surgical Oncology , vol.94 , Issue.3 , pp. 242-247
    • Giatromanolaki, A.1    Sivridis, E.2    Simopoulos, C.3
  • 121
    • 0037617447 scopus 로고    scopus 로고
    • Loss of von Hippel-Lindau protein causes cell density dependent deregulation of CyclinD1 expression through Hypoxia-inducible factor
    • M. Baba, S. Hirai, H. Yamada-Okabe et al., "Loss of von Hippel-Lindau protein causes cell density dependent deregulation of CyclinD1 expression through Hypoxia-inducible factor," Oncogene, vol. 22, no. 18, pp. 2728-2738, 2003
    • (2003) Oncogene , vol.22 , Issue.18 , pp. 2728-2738
    • Baba, M.1    Hirai, S.2    Yamada-Okabe, H.3
  • 123
    • 0025083389 scopus 로고
    • Cerebral energy metabolism and intracellular pH during severe hypoxia and recovery: A study using 1H, 31P, and 1H [13C] nuclear magnetic resonance spectroscopy in the guinea pig cerebral cortex in vitro
    • R. A. Kauppinen and S. R. Williams, "Cerebral energy metabolism and intracellular pH during severe hypoxia and recovery: a study using 1H, 31P, and 1H [13C] nuclear magnetic resonance spectroscopy in the guinea pig cerebral cortex in vitro," Journal of Neuroscience Research, vol. 26, no. 3, pp. 356-369, 1990
    • (1990) Journal of Neuroscience Research , vol.26 , Issue.3 , pp. 356-369
    • Kauppinen, R.A.1    Williams, S.R.2
  • 125
    • 0036174658 scopus 로고    scopus 로고
    • The changing face of the Na+/H+ exchanger, NHE1: Structure, regulation, and cellular actions
    • L. K. Putney, S. P. Denker, and D. L. Barber, "The changing face of the Na+/H+ exchanger, NHE1: structure, regulation, and cellular actions," Annual Review of Pharmacology and Toxicology, vol. 42, pp. 527-552, 2002
    • (2002) Annual Review of Pharmacology and Toxicology , vol.42 , pp. 527-552
    • Putney, L.K.1    Denker, S.P.2    Barber, D.L.3
  • 129
    • 27144433158 scopus 로고    scopus 로고
    • Chronic hypoxia elevates intracellular pH and activates Na+/H+ exchange in pulmonary arterial smoothmuscle cells
    • E. J. Rios, M. Fallon, J. Wang, and L. A. Shimoda, "Chronic hypoxia elevates intracellular pH and activates Na+/H+ exchange in pulmonary arterial smoothmuscle cells," American Journal of Physiology-Lung Cellular and Molecular Physiology, vol. 289, no. 5, pp. L867-L874, 2005
    • (2005) American Journal of Physiology-Lung Cellular and Molecular Physiology , vol.289 , Issue.5 , pp. L867-L874
    • Rios, E.J.1    Fallon, M.2    Wang, J.3    Shimoda, L.A.4
  • 131
    • 1242283850 scopus 로고    scopus 로고
    • Involvement of Na+/H+ exchanger in hypoxia/re-oxygenation-induced neonatal rat cardiomyocyte apoptosis
    • H.-Y. Sun, N.-P. Wang, M. E. Halkos et al., "Involvement of Na+/H+ exchanger in hypoxia/re-oxygenation-induced neonatal rat cardiomyocyte apoptosis," European Journal of Pharmacology, vol. 486, no. 2, pp. 121-131, 2004
    • (2004) European Journal of Pharmacology , vol.486 , Issue.2 , pp. 121-131
    • Sun, H.-Y.1    Wang, N.-P.2    Halkos, M.E.3
  • 132
    • 0033986761 scopus 로고    scopus 로고
    • Causes and consequences of tumour acidity and implications for treatment
    • M. Stubbs, P. M. J. McSheehy, J. R. Griffiths, and C. L. Bashford, "Causes and consequences of tumour acidity and implications for treatment,"MolecularMedicine Today, vol. 6, no. 1, pp. 15-19, 2000
    • (2000) MolecularMedicine Today , vol.6 , Issue.1 , pp. 15-19
    • Stubbs, M.1    McSheehy, P.M.J.2    Griffiths, J.R.3    Bashford, C.L.4
  • 133
    • 0035881307 scopus 로고    scopus 로고
    • Hypoxia and acidosis independently up-regulate vascular endothelial growth factor transcription in brain tumors in vivo
    • D. Fukumura, L. Xu, Y. Chen, T. Gohongi, B. Seed, and R. K. Jain, "Hypoxia and acidosis independently up-regulate vascular endothelial growth factor transcription in brain tumors in vivo," Cancer Research, vol. 61, no. 16, pp. 6020-6024, 2001
    • (2001) Cancer Research , vol.61 , Issue.16 , pp. 6020-6024
    • Fukumura, D.1    Xu, L.2    Chen, Y.3    Gohongi, T.4    Seed, B.5    Jain, R.K.6
  • 134
    • 8844249356 scopus 로고    scopus 로고
    • Hypoxia activates the capacity of tumor-associated carbonic anhydrase IX to acidify extracellular pH
    • E. Svastová, A. Hulíková, M. Rafajová et al., "Hypoxia activates the capacity of tumor-associated carbonic anhydrase IX to acidify extracellular pH," FEBS Letters, vol. 577, no. 3, pp. 439-445, 2004
    • (2004) FEBS Letters , vol.577 , Issue.3 , pp. 439-445
    • Svastová, E.1    Hulková, A.2    Rafajová, M.3
  • 135
    • 58249094845 scopus 로고    scopus 로고
    • Hypoxia-inducible carbonic anhydrase IX and XII promote tumor cell growth by counteracting acidosis through the regulation of the intracellular pH
    • J. Chiche, K. Ilc, J. Laferrière et al., "Hypoxia-inducible carbonic anhydrase IX and XII promote tumor cell growth by counteracting acidosis through the regulation of the intracellular pH," Cancer Research, vol. 69, no. 1, pp. 358-368, 2009
    • (2009) Cancer Research , vol.69 , Issue.1 , pp. 358-368
    • Chiche, J.1    Ilc, K.2    Laferrière, J.3
  • 137
    • 0016888751 scopus 로고
    • Biochemical adaptations to endurance exercise inmuscle
    • J. O. Holloszy and F. W. Booth, "Biochemical adaptations to endurance exercise inmuscle,"Annual Reviewof Physiology, vol. 38, pp. 273-291, 1976
    • (1976) Annual Reviewof Physiology , vol.38 , pp. 273-291
    • Holloszy, J.O.1    Booth, F.W.2
  • 139
    • 85003441266 scopus 로고    scopus 로고
    • Effects of systemic hypoxia on humanmuscular adaptations to resistance exercise training
    • M. Kon, N. Ohiwa, A. Honda et al., "Effects of systemic hypoxia on humanmuscular adaptations to resistance exercise training," Physiological Reports, vol. 2, no. 6,Article ID e12033, 2014
    • (2014) Physiological Reports , vol.2 , Issue.6
    • Kon, M.1    Ohiwa, N.2    Honda, A.3
  • 140
    • 33745756977 scopus 로고    scopus 로고
    • Endothelin-1, vascular endothelial growth factor and systolic pulmonary artery pressure in patients with Chuvash polycythemia
    • V. I. Bushuev, G. Y. Miasnikova, A. I. Sergueeva et al., "Endothelin-1, vascular endothelial growth factor and systolic pulmonary artery pressure in patients with Chuvash polycythemia," Haematologica, vol. 91, no. 6, pp. 744-749, 2006
    • (2006) Haematologica , vol.91 , Issue.6 , pp. 744-749
    • Bushuev, V.I.1    Miasnikova, G.Y.2    Sergueeva, A.I.3
  • 141
    • 18744373593 scopus 로고    scopus 로고
    • Disruption of oxygen homeostasis underlies congenital Chuvash polycythemia
    • S. O. Ang, H. Chen, K. Hirota et al., "Disruption of oxygen homeostasis underlies congenital Chuvash polycythemia," Nature Genetics, vol. 32, no. 4, pp. 614-621, 2002
    • (2002) Nature Genetics , vol.32 , Issue.4 , pp. 614-621
    • Ang, S.O.1    Chen, H.2    Hirota, K.3
  • 143
    • 80054960235 scopus 로고    scopus 로고
    • Effect of hypoxiainducible factor-1 gene therapy on walking performance in patients with intermittent claudication
    • M. A. Creager, J. W. Olin, J. J. F. Belch et al., "Effect of hypoxiainducible factor-1 gene therapy on walking performance in patients with intermittent claudication," Circulation, vol. 124, no. 16, pp. 1765-1773, 2011
    • (2011) Circulation , vol.124 , Issue.16 , pp. 1765-1773
    • Creager, M.A.1    Olin, J.W.2    Belch, J.J.F.3
  • 145
    • 59549107216 scopus 로고    scopus 로고
    • Effect of intermittent hypoxic training on HIF gene expression in human skeletal muscle and leukocytes
    • R. Mounier, V. Pialoux, B. Roels et al., "Effect of intermittent hypoxic training on HIF gene expression in human skeletal muscle and leukocytes," European Journal of Applied Physiology, vol. 105, no. 4, pp. 515-524, 2009
    • (2009) European Journal of Applied Physiology , vol.105 , Issue.4 , pp. 515-524
    • Mounier, R.1    Pialoux, V.2    Roels, B.3
  • 146
    • 84908665955 scopus 로고    scopus 로고
    • HIF-1alpha and HIF-2alpha induce angiogenesis and improve muscle energy recovery
    • H. Niemi, K. Honkonen, P. Korpisalo et al., "HIF-1alpha and HIF-2alpha induce angiogenesis and improve muscle energy recovery," European Journal of Clinical Investigation, vol. 44, no. 10, pp. 989-999, 2014
    • (2014) European Journal of Clinical Investigation , vol.44 , Issue.10 , pp. 989-999
    • Niemi, H.1    Honkonen, K.2    Korpisalo, P.3
  • 147
    • 84865407427 scopus 로고    scopus 로고
    • HIF-3 mRNA expression changes in different tissues and their role in adaptation to intermittent hypoxia and physical exercise
    • T. Drevytska, B. Gavenauskas, S. Drozdovska, V. Nosar, V. Dosenko, and I. Mankovska, "HIF-3 mRNA expression changes in different tissues and their role in adaptation to intermittent hypoxia and physical exercise," Pathophysiology, vol. 19, no. 3, pp. 205-214, 2012.
    • (2012) Pathophysiology , vol.19 , Issue.3 , pp. 205-214
    • Drevytska, T.1    Gavenauskas, B.2    Drozdovska, S.3    Nosar, V.4    Dosenko, V.5    Mankovska, I.6


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