메뉴 건너뛰기




Volumn 338, Issue 1, 2005, Pages 617-626

Signalling hypoxia by HIF hydroxylases

Author keywords

Hypoxia inducible factor; Iron; Oxygen; Oxygenase; Signalling; Transcription

Indexed keywords

2 OXOGLUTARIC ACID; ASPARAGINE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; IRON; OXYGENASE; PROLINE;

EID: 27544434803     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.111     Document Type: Review
Times cited : (302)

References (66)
  • 1
    • 0038037735 scopus 로고    scopus 로고
    • Regulation of angiogenesis by hypoxia: Role of the HIF system
    • C.W. Pugh, and P.J. Ratcliffe Regulation of angiogenesis by hypoxia: role of the HIF system Nat. Med. 9 2003 677 684
    • (2003) Nat. Med. , vol.9 , pp. 677-684
    • Pugh, C.W.1    Ratcliffe, P.J.2
  • 2
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • G.L. Semenza Targeting HIF-1 for cancer therapy Nat. Rev. Cancer 3 2003 721 732
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 721-732
    • Semenza, G.L.1
  • 4
    • 22244440847 scopus 로고    scopus 로고
    • Proline hydroxylation and gene expression
    • W.G. Kaelin Proline hydroxylation and gene expression Annu. Rev. Biochem. 74 2005 115 128
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 115-128
    • Kaelin, W.G.1
  • 5
    • 23444447955 scopus 로고    scopus 로고
    • Effect of desferrioxamine and metals on the hydroxylases in the oxygen sensing pathway
    • M. Hirsila, P. Koivunen, L. Xu, T. Seeley, K.I. Kivirikko, and J. Myllyharju Effect of desferrioxamine and metals on the hydroxylases in the oxygen sensing pathway FASEB J. 19 2005 1308 1310
    • (2005) FASEB J. , vol.19 , pp. 1308-1310
    • Hirsila, M.1    Koivunen, P.2    Xu, L.3    Seeley, T.4    Kivirikko, K.I.5    Myllyharju, J.6
  • 6
    • 1642315195 scopus 로고    scopus 로고
    • Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl-4-hydroxylases
    • P. Koivunen, M. Hirsila, V. Gunzler, K.I. Kivirikko, and J. Myllyharju Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl-4-hydroxylases J. Biol. Chem. 279 2003 9899 9904
    • (2003) J. Biol. Chem. , vol.279 , pp. 9899-9904
    • Koivunen, P.1    Hirsila, M.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 8
    • 0031893340 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases and their protein disulfide isomerase subunit
    • K.I. Kivirikko, and J. Myllyharju Prolyl 4-hydroxylases and their protein disulfide isomerase subunit Matrix Biol. 16 1998 357 368
    • (1998) Matrix Biol. , vol.16 , pp. 357-368
    • Kivirikko, K.I.1    Myllyharju, J.2
  • 9
    • 0032760945 scopus 로고    scopus 로고
    • Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes
    • C.J. Schofield, and Z. Zhang Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes Curr. Opin. Struct. Biol. 9 1999 722 731
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 722-731
    • Schofield, C.J.1    Zhang, Z.2
  • 10
    • 2442628211 scopus 로고    scopus 로고
    • Fe(II)/alpha-ketoglutarate-dependent hydroxylases and related enzymes
    • R.P. Hausinger Fe(II)/alpha-ketoglutarate-dependent hydroxylases and related enzymes Crit. Rev. Biochem. Mol. Biol. 39 2004 21 68
    • (2004) Crit. Rev. Biochem. Mol. Biol. , vol.39 , pp. 21-68
    • Hausinger, R.P.1
  • 11
    • 1542378704 scopus 로고    scopus 로고
    • Dioxygen activation at mononuclear nonheme iron active sites: Enzymes, models, and intermediates
    • M. Costas, M.P. Mehn, M.P. Jensen, and L. Que Dioxygen activation at mononuclear nonheme iron active sites: Enzymes, models, and intermediates Chem. Rev. 104 2004 939 986
    • (2004) Chem. Rev. , vol.104 , pp. 939-986
    • Costas, M.1    Mehn, M.P.2    Jensen, M.P.3    Que, L.4
  • 12
    • 0021329173 scopus 로고
    • Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase
    • R. Myllyla, K. Majamaa, V. Gunzler, H.M. Hanauske-Abel, and K.I. Kivirikko Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase J. Biol. Chem. 259 1984 5403 5405 (communication)
    • (1984) J. Biol. Chem. , vol.259 , pp. 5403-5405
    • Myllyla, R.1    Majamaa, K.2    Gunzler, V.3    Hanauske-Abel, H.M.4    Kivirikko, K.I.5
  • 16
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor HIF
    • M. Hirsila, P. Koivunen, V. Gunzler, K.I. Kivirikko, and J. Myllyharju Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor HIF J. Biol. Chem. 278 2003 30772 30780
    • (2003) J. Biol. Chem. , vol.278 , pp. 30772-30780
    • Hirsila, M.1    Koivunen, P.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 17
    • 0035925098 scopus 로고    scopus 로고
    • Tumor hypoxia: Definitions and current clinical, biologic, and molecular aspects
    • M. Hockel, and P. Vaupel Tumor hypoxia: definitions and current clinical, biologic, and molecular aspects J. Nat. Cancer Inst. 93 2001 266 276
    • (2001) J. Nat. Cancer Inst. , vol.93 , pp. 266-276
    • Hockel, M.1    Vaupel, P.2
  • 20
    • 0024273450 scopus 로고
    • Regulation of the erythropoietin gene: Evidence that the oxygen sensor is a heme protein
    • M.A. Goldberg, S.P. Dunning, and H.F. Bunn Regulation of the erythropoietin gene: evidence that the oxygen sensor is a heme protein Science 242 1988 1412 1415
    • (1988) Science , vol.242 , pp. 1412-1415
    • Goldberg, M.A.1    Dunning, S.P.2    Bunn, H.F.3
  • 21
    • 0037844847 scopus 로고    scopus 로고
    • Cobalt inhibits the interaction between hypoxia inducible factor-α and von Hippel-Lindau protein by direct binding to hypoxia inducible factor-α
    • Y. Yuan, G. Hilliard, T. Ferguson, and D.E. Millhorn Cobalt inhibits the interaction between hypoxia inducible factor-α and von Hippel-Lindau protein by direct binding to hypoxia inducible factor-α J. Biol. Chem. 278 2003 15911 15916
    • (2003) J. Biol. Chem. , vol.278 , pp. 15911-15916
    • Yuan, Y.1    Hilliard, G.2    Ferguson, T.3    Millhorn, D.E.4
  • 22
    • 4644260710 scopus 로고    scopus 로고
    • Depletion of intracellular ascorbate by the carcinogenic metals nickel and cobalt results in the induction of hypoxic stress
    • K. Salnikow, S.P. Donald, R.K. Bruick, A. Zhitkovich, J.M. Phang, and K.S. Kasprzak Depletion of intracellular ascorbate by the carcinogenic metals nickel and cobalt results in the induction of hypoxic stress J. Biol. Chem. 279 2004 40337 40344
    • (2004) J. Biol. Chem. , vol.279 , pp. 40337-40344
    • Salnikow, K.1    Donald, S.P.2    Bruick, R.K.3    Zhitkovich, A.4    Phang, J.M.5    Kasprzak, K.S.6
  • 23
    • 0037009846 scopus 로고    scopus 로고
    • The role of iron in cell cycle progression and the proliferation of neoplastic cells
    • N.T.V. Le, and D.R. Richardson The role of iron in cell cycle progression and the proliferation of neoplastic cells Biochim. Biophy. Acta 1603 2002 31 46
    • (2002) Biochim. Biophy. Acta , vol.1603 , pp. 31-46
    • Le, N.T.V.1    Richardson, D.R.2
  • 24
    • 0037131271 scopus 로고    scopus 로고
    • Role of prolyl hydroxylation in oncogenically stabilized hypoxia-inducible factor-1α
    • D.A. Chan, P.D. Sutphin, N.C. Denko, and A.J. Giaccia Role of prolyl hydroxylation in oncogenically stabilized hypoxia-inducible factor-1α J. Biol. Chem. 277 2002 40112 40117
    • (2002) J. Biol. Chem. , vol.277 , pp. 40112-40117
    • Chan, D.A.1    Sutphin, P.D.2    Denko, N.C.3    Giaccia, A.J.4
  • 25
    • 0037446983 scopus 로고    scopus 로고
    • Effect of ascorbate on the activity of hypoxia inducible factor (HIF) in cancer cells
    • H.J. Knowles, R.R. Raval, A.L. Harris, and P.J. Ratcliffe Effect of ascorbate on the activity of hypoxia inducible factor (HIF) in cancer cells Cancer Res. 63 2003 1764 1768
    • (2003) Cancer Res. , vol.63 , pp. 1764-1768
    • Knowles, H.J.1    Raval, R.R.2    Harris, A.L.3    Ratcliffe, P.J.4
  • 28
    • 24344438196 scopus 로고    scopus 로고
    • Reactive oxygen species in the control of hypoxia-inducible factor-mediated gene expression
    • Epub May 16, in press.
    • T. Kietzmann, A. Gorlach, Reactive oxygen species in the control of hypoxia-inducible factor-mediated gene expression, Semin. Cell Dev. Biol. (2005), Epub May 16, in press.
    • (2005) Semin. Cell Dev. Biol.
    • Kietzmann, T.1    Gorlach, A.2
  • 31
    • 24144447915 scopus 로고    scopus 로고
    • Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-α activation
    • K.D. Mansfield, R.D. Guzy, Y. Pan, R.M. Young, T.P. Cash, P.T. Schumacker, and M.C. Simon Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-α activation Cell Metab. 1 2005 393 399
    • (2005) Cell Metab. , vol.1 , pp. 393-399
    • Mansfield, K.D.1    Guzy, R.D.2    Pan, Y.3    Young, R.M.4    Cash, T.P.5    Schumacker, P.T.6    Simon, M.C.7
  • 32
    • 27144528715 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiration elevates oxygen concentration, but leaves regulation of hypoxia-inducible factor (HIF) intact
    • Epub June 9, in press.
    • K. Doege, S. Heine, I. Jensen, W. Jelkmann, E. Metzen, Inhibition of mitochondrial respiration elevates oxygen concentration, but leaves regulation of hypoxia-inducible factor (HIF) intact, Blood (2005), Epub June 9, in press.
    • (2005) Blood
    • Doege, K.1    Heine, S.2    Jensen, I.3    Jelkmann, W.4    Metzen, E.5
  • 33
    • 0348134741 scopus 로고    scopus 로고
    • Redistribution of intracellular oxygen in hypoxia by nitric oxide: Effect on HIF-1α
    • T. Hagen, C.T. Taylor, F. Lam, and S. Moncada Redistribution of intracellular oxygen in hypoxia by nitric oxide: effect on HIF-1α Science 302 2003 1975 1978
    • (2003) Science , vol.302 , pp. 1975-1978
    • Hagen, T.1    Taylor, C.T.2    Lam, F.3    Moncada, S.4
  • 35
    • 0037165643 scopus 로고    scopus 로고
    • Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate- substrate-NO complex: Evidence for metal centred rearrangements
    • Z. Zhang, J.-S. Ren, K. Harlos, C.H. McKinnon, I.J. Clifton, and C.J. Schofield Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate- substrate-NO complex: evidence for metal centred rearrangements FEBS Lett. 517 2002 7 12
    • (2002) FEBS Lett. , vol.517 , pp. 7-12
    • Zhang, Z.1    Ren, J.-S.2    Harlos, K.3    McKinnon, C.H.4    Clifton, I.J.5    Schofield, C.J.6
  • 36
    • 0042469448 scopus 로고    scopus 로고
    • Nitric oxide impairs normoxic degradation of HIF-1alpha by inhibition of prolyl hydroxylases
    • E. Metzen, J. Zhou, W. Jelkmann, J. Fandrey, and B. Brune Nitric oxide impairs normoxic degradation of HIF-1alpha by inhibition of prolyl hydroxylases Mol. Biol. Cell 14 2003 3470 3481
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3470-3481
    • Metzen, E.1    Zhou, J.2    Jelkmann, W.3    Fandrey, J.4    Brune, B.5
  • 39
    • 0037364314 scopus 로고    scopus 로고
    • A role for mitochondrial enzymes in inherited neoplasia and beyond
    • C. Eng, M. Kiuru, M.J. Fernandez, and L.A. Aaltonen A role for mitochondrial enzymes in inherited neoplasia and beyond Nat. Rev. Cancer 3 2003 193 202
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 193-202
    • Eng, C.1    Kiuru, M.2    Fernandez, M.J.3    Aaltonen, L.A.4
  • 43
    • 0017697003 scopus 로고
    • Mechanism of the prolyl hydroxylase reaction. 1. Role of co-substrates
    • L. Tuderman, R. Myllyla, and K.I. Kivirikko Mechanism of the prolyl hydroxylase reaction. 1. Role of co-substrates Eur. J. Biochem. 80 1977 341 348
    • (1977) Eur. J. Biochem. , vol.80 , pp. 341-348
    • Tuderman, L.1    Myllyla, R.2    Kivirikko, K.I.3
  • 44
    • 2642542967 scopus 로고    scopus 로고
    • Endogenous 2-oxoacids differentially regulate expression of oxygen sensors
    • C.L. Dalgard, H. Lu, A. Mohyeldin, and A. Verma Endogenous 2-oxoacids differentially regulate expression of oxygen sensors Biochem. J. 380 2004 419 424
    • (2004) Biochem. J. , vol.380 , pp. 419-424
    • Dalgard, C.L.1    Lu, H.2    Mohyeldin, A.3    Verma, A.4
  • 45
    • 0037131159 scopus 로고    scopus 로고
    • Sequence determinants in hypoxia inducible factor-1a for hydroxylation by the prolyl hydroxylases PHD1, PHD2 and PHD3
    • J. Huang, Q. Zhao, S.M. Mooney, and F.S. Lee Sequence determinants in hypoxia inducible factor-1a for hydroxylation by the prolyl hydroxylases PHD1, PHD2 and PHD3 J. Biol. Chem. 277 2002 39792 39800
    • (2002) J. Biol. Chem. , vol.277 , pp. 39792-39800
    • Huang, J.1    Zhao, Q.2    Mooney, S.M.3    Lee, F.S.4
  • 46
    • 11244279649 scopus 로고    scopus 로고
    • Many amino acid substitutions in a hypoxia-inducible transcription factor (HIF)-1alpha-like peptide cause only minor changes in its hydroxylation by the HIF prolyl 4-hydroxylases: Substitution of 3,4-dehydroproline or azetidine-2-carboxylic acid for the proline leads to a high rate of uncoupled 2-oxoglutarate decarboxylation
    • D. Li, M. Hirsila, P. Koivunen, M.C. Brenner, L. Xu, C. Yang, K.I. Kivirikko, and J. Myllyharju Many amino acid substitutions in a hypoxia-inducible transcription factor (HIF)-1alpha-like peptide cause only minor changes in its hydroxylation by the HIF prolyl 4-hydroxylases: substitution of 3,4-dehydroproline or azetidine-2-carboxylic acid for the proline leads to a high rate of uncoupled 2-oxoglutarate decarboxylation J. Biol. Chem. 279 2004 55051 55059
    • (2004) J. Biol. Chem. , vol.279 , pp. 55051-55059
    • Li, D.1    Hirsila, M.2    Koivunen, P.3    Brenner, M.C.4    Xu, L.5    Yang, C.6    Kivirikko, K.I.7    Myllyharju, J.8
  • 48
    • 1842639126 scopus 로고    scopus 로고
    • Substrate requirements of the oxygen-sensing asparaginyl hydroxylase Factor-inhibiting Hypoxia-inducible Factor
    • S. Linke, C. Stojkoski, R.J. Kewley, G.W. Booker, M.L. Whitelaw, and D.J. Peet Substrate requirements of the oxygen-sensing asparaginyl hydroxylase Factor-inhibiting Hypoxia-inducible Factor J. Biol. Chem. 279 2004 14391 14397
    • (2004) J. Biol. Chem. , vol.279 , pp. 14391-14397
    • Linke, S.1    Stojkoski, C.2    Kewley, R.J.3    Booker, G.W.4    Whitelaw, M.L.5    Peet, D.J.6
  • 49
    • 0030937718 scopus 로고    scopus 로고
    • Activation of hypoxia inducible factor-1; Definition of regulatory domains within the α 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 α subunit J. Biol. Chem. 272 1997 11205 11214
    • (1997) J. Biol. Chem. , vol.272 , pp. 11205-11214
    • Pugh, C.W.1    O'Rourke, J.F.2    Nagao, M.3    Gleadle, J.M.4    Ratcliffe, P.J.5
  • 52
    • 20544431636 scopus 로고    scopus 로고
    • Analysis of ARD1 function in hypoxia response using retroviral RNA interference
    • T.S. Fisher, S.D. Etages, L. Hayes, K. Crimin, and B. Li Analysis of ARD1 function in hypoxia response using retroviral RNA interference J. Biol. Chem. 280 2005 17749 17757
    • (2005) J. Biol. Chem. , vol.280 , pp. 17749-17757
    • Fisher, T.S.1    Etages, S.D.2    Hayes, L.3    Crimin, K.4    Li, B.5
  • 53
    • 24744460523 scopus 로고    scopus 로고
    • ARD1, an acetyltransferase, does not alter stability of hypoxia-inducible factor-1alpha and is not induced by hypoxia or HIF
    • Epub July 1, in press.
    • R. Bilton, N. Mazure, E. Trottier, M. Hattab, M.A. Dery, D.E. Richard, J. Pouyssegur, M.C. Brahimi-Horn, ARD1, an acetyltransferase, does not alter stability of hypoxia-inducible factor-1alpha and is not induced by hypoxia or HIF, J. Biol. Chem. (2005), Epub July 1, in press.
    • (2005) J. Biol. Chem.
    • Bilton, R.1    Mazure, N.2    Trottier, E.3    Hattab, M.4    Dery, M.A.5    Richard, D.E.6    Pouyssegur, J.7    Brahimi-Horn, M.C.8
  • 56
    • 0035783192 scopus 로고    scopus 로고
    • Review: Cellular substrates of the eukaryotic chaperonin TRiIC/CCT
    • A.Y. Dunn, M.W. Melville, and J. Frydman Review: cellular substrates of the eukaryotic chaperonin TRiIC/CCT J. Struct. Biol. 135 2001 176 184
    • (2001) J. Struct. Biol. , vol.135 , pp. 176-184
    • Dunn, A.Y.1    Melville, M.W.2    Frydman, J.3
  • 58
    • 13944276440 scopus 로고    scopus 로고
    • OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha
    • J.H. Baek, P.C. Mahon, J. Oh, B. Kelly, B. Krishnamachary, M. Pearson, D.A. Chan, A.J. Giaccia, and G.L. Semenza OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha Mol. Cell 17 2005 503 512
    • (2005) Mol. Cell , vol.17 , pp. 503-512
    • Baek, J.H.1    Mahon, P.C.2    Oh, J.3    Kelly, B.4    Krishnamachary, B.5    Pearson, M.6    Chan, D.A.7    Giaccia, A.J.8    Semenza, G.L.9
  • 59
    • 19644376763 scopus 로고    scopus 로고
    • The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF)
    • A. Ozer, L.C. Wu, and R.K. Bruick The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF) Proc. Natl. Acad. Sci. 102 2005 7481 7486
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 7481-7486
    • Ozer, A.1    Wu, L.C.2    Bruick, R.K.3
  • 61
    • 0035936886 scopus 로고    scopus 로고
    • HIF-1-dependent transcriptional activity is required for oxygen-mediated HIF-1α degradation
    • E. Berra, D.E. Richard, E. Gothie, and J. Pouyssegur HIF-1-dependent transcriptional activity is required for oxygen-mediated HIF-1α degradation FEBS Lett. 491 2001 85 90
    • (2001) FEBS Lett. , vol.491 , pp. 85-90
    • Berra, E.1    Richard, D.E.2    Gothie, E.3    Pouyssegur, J.4
  • 62
    • 1542300383 scopus 로고    scopus 로고
    • The von Hippel Lindau/hypoxia-inducible factor (HIF) pathway regulates the transcription of the HIF-proline hydroxylase genes in response to low oxygen
    • L. del Peso, M.C. Castellanos, E. Temes, S. Martin-Puig, Y. Cuevas, G. Olmos, and M.O. Landazuri The von Hippel Lindau/hypoxia-inducible factor (HIF) pathway regulates the transcription of the HIF-proline hydroxylase genes in response to low oxygen J. Biol. Chem. 278 2003 48690 48695
    • (2003) J. Biol. Chem. , vol.278 , pp. 48690-48695
    • Del Peso, L.1    Castellanos, M.C.2    Temes, E.3    Martin-Puig, S.4    Cuevas, Y.5    Olmos, G.6    Landazuri, M.O.7
  • 63
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1α in normoxia
    • E. Berra, E. Benizri, A. Ginouves, V. Volmat, D. Roux, and J. Pouyssegur HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1α in normoxia EMBO J. 22 2003 4082 4090
    • (2003) EMBO J. , vol.22 , pp. 4082-4090
    • Berra, E.1    Benizri, E.2    Ginouves, A.3    Volmat, V.4    Roux, D.5    Pouyssegur, J.6
  • 64
    • 5644240828 scopus 로고    scopus 로고
    • Genetic analysis of the role of the asparaginyl hydroxylase FIH in regulating HIF transcriptional target genes
    • I.P. Stolze, Y.M. Tian, R.J. Appelhoff, H. Turley, C.C. Wykoff, J.M. Gleadle, and P.J. Ratcliffe Genetic analysis of the role of the asparaginyl hydroxylase FIH in regulating HIF transcriptional target genes J. Biol. Chem. 279 2004 42719 42725
    • (2004) J. Biol. Chem. , vol.279 , pp. 42719-42725
    • Stolze, I.P.1    Tian, Y.M.2    Appelhoff, R.J.3    Turley, H.4    Wykoff, C.C.5    Gleadle, J.M.6    Ratcliffe, P.J.7
  • 65
    • 0345491599 scopus 로고    scopus 로고
    • Differential roles of hypoxia-inducible factor 1α (HIF-1α) and HIF-2α 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 1α (HIF-1α) and HIF-2α in hypoxic gene regulation Mol. Cell. Biol. 23 2003 9361 9374
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 9361-9374
    • Hu, C.-J.1    Wang, L.-Y.2    Chodosh, L.A.3    Keith, B.4    Simon, M.C.5
  • 66
    • 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 Biochem. Cell Biol. 80 2002 421 426
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 421-426
    • Lieb, M.E.1    Menzies, K.2    Moschella, M.C.3    Ni, R.4    Taubman, M.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.