메뉴 건너뛰기




Volumn 119, Issue 16, 2006, Pages 3467-3480

A computational model of intracellular oxygen sensing by hypoxia-inducible factor HIF1α

Author keywords

Computational modeling; Hypoxic response; Mathematical modeling; Oxygen sensing

Indexed keywords

2 OXOGLUTARIC ACID; ASCORBIC ACID; FERROUS ION; HYPOXIA INDUCIBLE FACTOR 1ALPHA; IRON; OXYGEN; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; VON HIPPEL LINDAU PROTEIN;

EID: 33748774664     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.03087     Document Type: Article
Times cited : (76)

References (74)
  • 1
    • 0018890003 scopus 로고
    • Metabolism of proline and the hydroxyprolines
    • Adams, E. and Frank, L. (1980). Metabolism of proline and the hydroxyprolines. Annu. Rev. Biochem. 49, 1005-1061.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 1005-1061
    • Adams, E.1    Frank, L.2
  • 2
    • 0018344726 scopus 로고
    • The mechanism of reduction of single-site redox proteins by ascorbic acid
    • Al-Ayash, A. I. and Wilson, M. T. (1979). The mechanism of reduction of single-site redox proteins by ascorbic acid. Biochem. J. 177, 641-648.
    • (1979) Biochem. J. , vol.177 , pp. 641-648
    • Al-Ayash, A.I.1    Wilson, M.T.2
  • 3
    • 4644318828 scopus 로고    scopus 로고
    • Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor
    • Appelhoff, R. J., Tian, Y. M., Raval, R. R., Turley, H., Harris, A. L., Pugh, C. W., Ratcliffe, P. J. and Gleadle, J. M. (2004). Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor. J. Biol. Chem. 279, 38458-38465.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38458-38465
    • Appelhoff, R.J.1    Tian, Y.M.2    Raval, R.R.3    Turley, H.4    Harris, A.L.5    Pugh, C.W.6    Ratcliffe, P.J.7    Gleadle, J.M.8
  • 4
    • 0030870020 scopus 로고    scopus 로고
    • Intracellular iron regulates iron absorption and IRP activity in intestinal epithelial (Caco-2) cells
    • Arredondo, M., Orellana, A., Garate, M. A. and Nunez, M. T. (1997). Intracellular iron regulates iron absorption and IRP activity in intestinal epithelial (Caco-2) cells. Am. J. Physiol. 273, G275-G280.
    • (1997) Am. J. Physiol. , vol.273
    • Arredondo, M.1    Orellana, A.2    Garate, M.A.3    Nunez, M.T.4
  • 6
    • 13944276440 scopus 로고    scopus 로고
    • OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha
    • Baek, J. H., Mahon, P. C., Oh, J., Kelly, B., Krishnamachary, B., Pearson, M., Chan, D. A., Giaccia, A. J. and Semenza, G. L. (2005). OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha. Mol. Cell 17, 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
  • 7
    • 0032474834 scopus 로고    scopus 로고
    • Fenton reagent advanced oxidation of polynuclear aromatic hydrocarbons in water
    • Beltran, F. J., Gonzalez, M., Rivas, F. J. and Alvarez, P. (1998). Fenton reagent advanced oxidation of polynuclear aromatic hydrocarbons in water. Water Air Soil Pollut. 105, 685-700.
    • (1998) Water Air Soil Pollut. , vol.105 , pp. 685-700
    • Beltran, F.J.1    Gonzalez, M.2    Rivas, F.J.3    Alvarez, P.4
  • 8
    • 0034904751 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 alpha (HIF-1 alpha) escapes O(2)-driven proteasomal degradation irrespective of its subcellular localization: Nucleus or cytoplasm
    • Berra, E., Roux, D., Richard, D. E. and Pouyssegur, J. (2001). Hypoxia-inducible factor-1 alpha (HIF-1 alpha) escapes O(2)-driven proteasomal degradation irrespective of its subcellular localization: nucleus or cytoplasm. EMBO Rep. 2, 615-620.
    • (2001) EMBO Rep. , vol.2 , pp. 615-620
    • Berra, E.1    Roux, D.2    Richard, D.E.3    Pouyssegur, J.4
  • 9
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia
    • Berra, E., Benizri, E., Ginouves, A., Volmat, V., Roux, D. and Pouyssegur, J. (2003). HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia. EMBO J. 22, 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
  • 11
    • 13244284943 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha is associated with angiogenesis, and expression of bFGF, PDGF-BB, and EGFR in invasive breast cancer
    • Bos, R., van Diest, P. J., de Jong, J. S., van der Groep, P., van der Valk, P. and van der Wall, E. (2005). Hypoxia-inducible factor-1alpha is associated with angiogenesis, and expression of bFGF, PDGF-BB, and EGFR in invasive breast cancer. Histopathology 46, 31-36.
    • (2005) Histopathology , vol.46 , pp. 31-36
    • Bos, R.1    van Diest, P.J.2    de Jong, J.S.3    van der Groep, P.4    van der Valk, P.5    van der Wall, E.6
  • 12
    • 0000292524 scopus 로고
    • A note on the kinetics of enzyme action
    • Briggs, G. E. and Haldane, J. B. S. (1925). A note on the kinetics of enzyme action. Biochem. J. 19, 339.
    • (1925) Biochem. J. , vol.19 , pp. 339
    • Briggs, G.E.1    Haldane, J.B.S.2
  • 13
    • 0027469054 scopus 로고
    • Ascorbate free radical as a marker of oxidative stress: An EPR study
    • Buettner, G. R. and Jurkiewicz, B. A. (1993). Ascorbate free radical as a marker of oxidative stress: an EPR study. Free Radic. Biol. Med. 14, 49-55.
    • (1993) Free Radic. Biol. Med. , vol.14 , pp. 49-55
    • Buettner, G.R.1    Jurkiewicz, B.A.2
  • 14
    • 0029939394 scopus 로고    scopus 로고
    • Catalytic metals, ascorbate and free radicals: Combinations to avoid
    • Buettner, G. R. and Jurkiewicz, B. A. (1996). Catalytic metals, ascorbate and free radicals: combinations to avoid. Radiat. Res. 145, 532-541.
    • (1996) Radiat. Res. , vol.145 , pp. 532-541
    • Buettner, G.R.1    Jurkiewicz, B.A.2
  • 16
    • 22544464403 scopus 로고    scopus 로고
    • Coordinate regulation of the oxygen-dependent degradation domains of Hypoxia-inducible factor 1{alpha}
    • Chan, D. A., Sutphin, P. D., Yen, S. E. and Giaccia, A. J. (2005). Coordinate regulation of the oxygen-dependent degradation domains of Hypoxia-inducible factor 1{alpha}. Mol. Cell. Biol. 25, 6415-6426.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6415-6426
    • Chan, D.A.1    Sutphin, P.D.2    Yen, S.E.3    Giaccia, A.J.4
  • 17
    • 0029833706 scopus 로고    scopus 로고
    • The relationship of intracellular iron chelation to the inhibition and regeneration of human ribonucleotide reductase
    • Cooper, C. E., Lynagh, G. R., Hoyes, K. P., Hider, R. C., Cammack, R. and Porter, J. B. (1996). The relationship of intracellular iron chelation to the inhibition and regeneration of human ribonucleotide reductase. J. Biol. Chem. 271, 20291-20299.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20291-20299
    • Cooper, C.E.1    Lynagh, G.R.2    Hoyes, K.P.3    Hider, R.C.4    Cammack, R.5    Porter, J.B.6
  • 19
    • 0141643358 scopus 로고    scopus 로고
    • Hypoxia upregulates prolyl hydroxylase activity: A feedback mechanism that limits HIF-1 responses during reoxygenation
    • D'Angelo, G., Duplan, E., Boyer, N., Vigne, P. and Frelin, C. (2003). Hypoxia upregulates prolyl hydroxylase activity: a feedback mechanism that limits HIF-1 responses during reoxygenation. J. Biol. Chem. 278, 38183-38187.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38183-38187
    • D'Angelo, G.1    Duplan, E.2    Boyer, N.3    Vigne, P.4    Frelin, C.5
  • 21
    • 0036570964 scopus 로고    scopus 로고
    • A review of fluorescence methods for assessing labile iron in cells and biological fluids
    • Esposito, B. P., Epsztejn, S., Breuer, W. and Cabantchik, Z. I. (2002). A review of fluorescence methods for assessing labile iron in cells and biological fluids. Anal. Biochem. 304, 1-18.
    • (2002) Anal. Biochem. , vol.304 , pp. 1-18
    • Esposito, B.P.1    Epsztejn, S.2    Breuer, W.3    Cabantchik, Z.I.4
  • 22
    • 22744447648 scopus 로고    scopus 로고
    • HIF-1alpha and p53: The ODD couple?
    • Fels, D. R. and Koumenis, C. (2005). HIF-1alpha and p53: the ODD couple? Trends Biochem. Sci. 30, 426-429.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 426-429
    • Fels, D.R.1    Koumenis, C.2
  • 23
    • 0042763564 scopus 로고    scopus 로고
    • HIF-1 in cell cycle regulation, apoptosis, and tumor progression
    • Goda, N., Dozier, S. J. and Johnson, R. S. (2003). HIF-1 in cell cycle regulation, apoptosis, and tumor progression. Antioxid. Redox Signal. 5, 467-473.
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 467-473
    • Goda, N.1    Dozier, S.J.2    Johnson, R.S.3
  • 24
    • 0031025115 scopus 로고    scopus 로고
    • Homeostatic regulation of intracellular hydrogen peroxide concentration in aerobically growing Escherichia coli
    • Gonzalez-Flecha, B. and Demple, B. (1997). Homeostatic regulation of intracellular hydrogen peroxide concentration in aerobically growing Escherichia coli. J. Bacteriol. 179, 382-388.
    • (1997) J. Bacteriol. , vol.179 , pp. 382-388
    • Gonzalez-Flecha, B.1    Demple, B.2
  • 25
    • 0036314978 scopus 로고    scopus 로고
    • Oxygen-dependent ubiquitination and degradation of hypoxia-inducible factor requires nuclear-cytoplasmic trafficking of the von Hippel-Lindau tumor suppressor protein
    • Groulx, I. and Lee, S. (2002). Oxygen-dependent ubiquitination and degradation of hypoxia-inducible factor requires nuclear-cytoplasmic trafficking of the von Hippel-Lindau tumor suppressor protein. Mol. Cell. Biol. 22, 5319-5336.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5319-5336
    • Groulx, I.1    Lee, S.2
  • 27
    • 4043119692 scopus 로고    scopus 로고
    • The HIF pathway as a therapeutic target
    • Hewitson, K. S. and Schofield, C. J. (2004). The HIF pathway as a therapeutic target. Drug Discov. Today 9, 704-711.
    • (2004) Drug Discov. Today , vol.9 , pp. 704-711
    • Hewitson, K.S.1    Schofield, C.J.2
  • 28
    • 0042818299 scopus 로고    scopus 로고
    • The peptide-substrate-binding domain of human collagen prolyl 4-hydroxylases. Backbone assignments, secondary structure, and binding of proline-rich peptides
    • Hieta, R., Kukkola, L., Permi, P., Pirila, P., Kivirikko, K. I., Kilpelainen, I. and Myllyharju, J. (2003). The peptide-substrate-binding domain of human collagen prolyl 4-hydroxylases. Backbone assignments, secondary structure, and binding of proline-rich peptides. J. Biol. Chem. 278, 34966-34974.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34966-34974
    • Hieta, R.1    Kukkola, L.2    Permi, P.3    Pirila, P.4    Kivirikko, K.I.5    Kilpelainen, I.6    Myllyharju, J.7
  • 29
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
    • Hirsila, M., Koivunen, P., Gunzler, V., Kivirikko, K. I. and Myllyharju, J. (2003). Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor. J. Biol. Chem. 278, 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
  • 30
    • 23444447955 scopus 로고    scopus 로고
    • Effect of desferrioxamine and metals on the hydroxylases in the oxygen sensing pathway
    • Hirsila, M., Koivunen, P., Xu, L., Seeley, T., Kivirikko, K. I. and Myllyharju, J. (2005). Effect of desferrioxamine and metals on the hydroxylases in the oxygen sensing pathway. FASEB J. 19, 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
  • 32
    • 0032493368 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway
    • Huang, L. E., Gu, J., Schau, M. and Bunn, H. F. (1998). Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway. Proc. Natl. Acad. Sci. USA 95, 7987-7992.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7987-7992
    • Huang, L.E.1    Gu, J.2    Schau, M.3    Bunn, H.F.4
  • 35
    • 0029859510 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 levels vary exponentially over a physiologically relevant range of O2 tension
    • Jiang, B. H., Semenza, G. L., Bauer, C. and Marti, H. H. (1996). Hypoxia-inducible factor 1 levels vary exponentially over a physiologically relevant range of O2 tension. Am. J. Physiol. 271, C1172-C1180.
    • (1996) Am. J. Physiol. , vol.271
    • Jiang, B.H.1    Semenza, G.L.2    Bauer, C.3    Marti, H.H.4
  • 36
    • 33645066360 scopus 로고    scopus 로고
    • Effects of transferrin receptor blockade on cancer cell proliferation and hypoxia-inducible factor function and their differential regulation by ascorbate
    • Jones, D. T., Trowbridge, I. S. and Harris, A. L. (2006). Effects of transferrin receptor blockade on cancer cell proliferation and hypoxia-inducible factor function and their differential regulation by ascorbate. Cancer Res. 66, 2749-2756.
    • (2006) Cancer Res. , vol.66 , pp. 2749-2756
    • Jones, D.T.1    Trowbridge, I.S.2    Harris, A.L.3
  • 37
    • 1942502894 scopus 로고    scopus 로고
    • Transcription factors having impact on vascular endothelial growth factor (VEGF) gene expression in angiogenesis
    • Josko, J. and Mazurek, M. (2004). Transcription factors having impact on vascular endothelial growth factor (VEGF) gene expression in angiogenesis. Med. Sci. Monit. 10, RA89-RA98.
    • (2004) Med. Sci. Monit. , vol.10
    • Josko, J.1    Mazurek, M.2
  • 39
    • 0034641615 scopus 로고    scopus 로고
    • Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex
    • Kamura, T., Sato, S., Iwai, K., Czyzyk-Krzeska, M., Conaway, R. C. and Conaway, J. W. (2000). Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex. Proc. Natl. Acad. Sci. USA 97, 10430-10435.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10430-10435
    • Kamura, T.1    Sato, S.2    Iwai, K.3    Czyzyk-Krzeska, M.4    Conaway, R.C.5    Conaway, J.W.6
  • 40
    • 8844224950 scopus 로고    scopus 로고
    • Production of human prolyl 4-hydroxylase in Escherichia coli
    • Kersteen, E. A., Higgin, J. J. and Raines, R. T. (2004). Production of human prolyl 4-hydroxylase in Escherichia coli. Protein Expr. Purif. 38, 279-291.
    • (2004) Protein Expr. Purif. , vol.38 , pp. 279-291
    • Kersteen, E.A.1    Higgin, J.J.2    Raines, R.T.3
  • 41
    • 0037446983 scopus 로고    scopus 로고
    • Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells
    • Knowles, H. J., Raval, R. R., Harris, A. L. and Ratcliffe, P. J. (2003). Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells. Cancer Res. 63, 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
  • 42
    • 33645080666 scopus 로고    scopus 로고
    • Normoxic stabilization of hypoxia-inducible factor-1alpha by modulation of the labile iron pool in differentiating U937 macrophages: Effect of natural resistance-associated macrophage protein 1
    • Knowles, H. J., Mole, D. R., Ratcliffe, P. J. and Harris, A. L. (2006). Normoxic stabilization of hypoxia-inducible factor-1alpha by modulation of the labile iron pool in differentiating U937 macrophages: effect of natural resistance-associated macrophage protein 1. Cancer Res. 66, 2600-2607.
    • (2006) Cancer Res. , vol.66 , pp. 2600-2607
    • Knowles, H.J.1    Mole, D.R.2    Ratcliffe, P.J.3    Harris, A.L.4
  • 43
    • 3042808208 scopus 로고    scopus 로고
    • Properties of switch-like bioregulatory networks studied by simulation of the hypoxia response control system
    • Kohn, K. W., Riss, J., Aprelikova, O., Weinstein, J. N., Pommier, Y. and Barrett, J. C. (2004). Properties of switch-like bioregulatory networks studied by simulation of the hypoxia response control system. Mol. Biol. Cell 15, 3042-3052.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3042-3052
    • Kohn, K.W.1    Riss, J.2    Aprelikova, O.3    Weinstein, J.N.4    Pommier, Y.5    Barrett, J.C.6
  • 44
    • 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
    • Koivunen, P., Hirsila, M., Gunzler, V., Kivirikko, K. I. and Myllyharju, J. (2004). 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, 9899-9904.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9899-9904
    • Koivunen, P.1    Hirsila, M.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 45
    • 13144275217 scopus 로고    scopus 로고
    • Dynamic balancing of the dual nature of HIF-1alpha for cell survival
    • Koshiji, M. and Huang, L. E. (2004). Dynamic balancing of the dual nature of HIF-1alpha for cell survival. Cell Cycle 3, 853-854.
    • (2004) Cell Cycle , vol.3 , pp. 853-854
    • Koshiji, M.1    Huang, L.E.2
  • 46
    • 33747821181 scopus 로고    scopus 로고
    • Ascorbate enhances the toxicity of the photodynamic action of Verteporfin in HL-60 cells
    • Kramarenko, G. G., Wilke, W. W., Dayal, D., Buettner, G. R. and Schafer, F. Q. (2006). Ascorbate enhances the toxicity of the photodynamic action of Verteporfin in HL-60 cells. Free Radic. Biol. Med. 40, 1615-1627.
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 1615-1627
    • Kramarenko, G.G.1    Wilke, W.W.2    Dayal, D.3    Buettner, G.R.4    Schafer, F.Q.5
  • 47
    • 27944445890 scopus 로고    scopus 로고
    • Differential responses of two degradation domains of HIF-1alpha to hypoxia and iron deficiency
    • Lee, K. H., Choi, E., Chun, Y. S., Kim, M. S. and Park, J. W. (2005). Differential responses of two degradation domains of HIF-1alpha to hypoxia and iron deficiency. Biochimie 88, 163-169.
    • (2005) Biochimie , vol.88 , pp. 163-169
    • Lee, K.H.1    Choi, E.2    Chun, Y.S.3    Kim, M.S.4    Park, J.W.5
  • 48
    • 17644421091 scopus 로고    scopus 로고
    • VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF-1alpha
    • Li, Z., Wang, D., Messing, E. M. and Wu, G. (2005). VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF-1alpha. EMBO Rep. 6, 373-378.
    • (2005) EMBO Rep. , vol.6 , pp. 373-378
    • Li, Z.1    Wang, D.2    Messing, E.M.3    Wu, G.4
  • 50
    • 17344377672 scopus 로고    scopus 로고
    • A kinetic study on iron stimulation of the xanthine oxidase dependent oxidation of ascorbate
    • Lovstad, R. A. (2003). A kinetic study on iron stimulation of the xanthine oxidase dependent oxidation of ascorbate. Biometals 16, 435-439.
    • (2003) Biometals , vol.16 , pp. 435-439
    • Lovstad, R.A.1
  • 51
    • 0023021512 scopus 로고
    • Partial identity of the 2-oxoglutarate and ascorbate binding sites of prolyl 4-hydroxylase
    • Majamaa, K., Gunzler, V., Hanauske-Abel, H. M., Myllyla, R. and Kivirikko, K. I. (1986). Partial identity of the 2-oxoglutarate and ascorbate binding sites of prolyl 4-hydroxylase. J. Biol. Chem. 261, 7819-7823.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7819-7823
    • Majamaa, K.1    Gunzler, V.2    Hanauske-Abel, H.M.3    Myllyla, R.4    Kivirikko, K.I.5
  • 52
    • 4644318784 scopus 로고    scopus 로고
    • Erythropoietin and the hypoxic brain
    • Marti, H. H. (2004). Erythropoietin and the hypoxic brain. J. Exp. Biol. 207, 3233-3242.
    • (2004) J. Exp. Biol. , vol.207 , pp. 3233-3242
    • Marti, H.H.1
  • 53
    • 0345598876 scopus 로고    scopus 로고
    • Turning an 'Achilles' Heel' into an asset-activation of HIF-1alpha during angiostatic therapy will increase tumor sensitivity to iron-catalyzed oxidative damage
    • McCarty, M. F. (2003). Turning an 'Achilles' Heel' into an asset-activation of HIF-1alpha during angiostatic therapy will increase tumor sensitivity to iron-catalyzed oxidative damage. Med. Hypotheses 61, 509-511.
    • (2003) Med. Hypotheses , vol.61 , pp. 509-511
    • McCarty, M.F.1
  • 54
    • 0141992249 scopus 로고    scopus 로고
    • Differential expression of Flk-1 and Flt-1 in rat skeletal muscle in response to chronic ischaemia: Favourable effect of muscle activity
    • Milkiewicz, M., Hudlicka, O., Verhaeg, J., Egginton, S. and Brown, M. D. (2003). Differential expression of Flk-1 and Flt-1 in rat skeletal muscle in response to chronic ischaemia: favourable effect of muscle activity. Clin. Sci. 105, 473-482.
    • (2003) Clin. Sci. , vol.105 , pp. 473-482
    • Milkiewicz, M.1    Hudlicka, O.2    Verhaeg, J.3    Egginton, S.4    Brown, M.D.5
  • 56
    • 0017742181 scopus 로고
    • Mechanism of the prolyl hydroxylase reaction. 2. Kinetic analysis of the reaction sequence
    • Myllyla, R., Tuderman, L. and Kivirikko, K. I. (1977). Mechanism of the prolyl hydroxylase reaction. 2. Kinetic analysis of the reaction sequence. Eur. J. Biochem. 80, 349-357.
    • (1977) Eur. J. Biochem. , vol.80 , pp. 349-357
    • Myllyla, R.1    Tuderman, L.2    Kivirikko, K.I.3
  • 57
    • 0021329173 scopus 로고
    • Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase
    • Myllyla, R., Majamaa, K., Gunzler, V., Hanauske-Abel, H. M. and Kivirikko, K. I. (1984). Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase. J. Biol. Chem. 259, 5403-5405.
    • (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
  • 58
    • 7544243762 scopus 로고    scopus 로고
    • Geldanamycin induces mitotic catastrophe and subsequent apoptosis in human glioma cells
    • Nomura, M., Nomura, N., Newcomb, E. W., Lukyanov, Y., Tamasdan, C. and Zagzag, D. (2004). Geldanamycin induces mitotic catastrophe and subsequent apoptosis in human glioma cells. J. Cell Physiol. 201, 374-384.
    • (2004) J. Cell Physiol. , vol.201 , pp. 374-384
    • Nomura, M.1    Nomura, N.2    Newcomb, E.W.3    Lukyanov, Y.4    Tamasdan, C.5    Zagzag, D.6
  • 59
    • 13244260964 scopus 로고    scopus 로고
    • Nitric oxide signalling and cellular adaptations to changes in oxygenation
    • Postovit, L. M., Sullivan, R., Adams, M. A. and Graham, C. H. (2005). Nitric oxide signalling and cellular adaptations to changes in oxygenation. Toxicology 208, 235-248.
    • (2005) Toxicology , vol.208 , pp. 235-248
    • Postovit, L.M.1    Sullivan, R.2    Adams, M.A.3    Graham, C.H.4
  • 60
    • 0037974523 scopus 로고    scopus 로고
    • Functional genomics and the comparative physiology of hypoxia
    • Powell, F. L. (2003). Functional genomics and the comparative physiology of hypoxia. Annu. Rev. Physiol. 65, 203-230.
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 203-230
    • Powell, F.L.1
  • 62
    • 8344237449 scopus 로고    scopus 로고
    • Hydroxylation of HIF-1: Oxygen sensing at the molecular level
    • Semenza, G. L. (2004). Hydroxylation of HIF-1: oxygen sensing at the molecular level. Physiology Bethesda 19, 176-182.
    • (2004) Physiology Bethesda , vol.19 , pp. 176-182
    • Semenza, G.L.1
  • 65
    • 0017697003 scopus 로고
    • Mechanism of the prolyl hydroxylase reaction. 1. Role of co-substrates
    • Tuderman, L., Myllyla, R. and Kivirikko, K. I. (1977). Mechanism of the prolyl hydroxylase reaction. 1. Role of co-substrates. Eur. J. Biochem. 80, 341-348.
    • (1977) Eur. J. Biochem. , vol.80 , pp. 341-348
    • Tuderman, L.1    Myllyla, R.2    Kivirikko, K.I.3
  • 66
    • 0344667645 scopus 로고    scopus 로고
    • Endogenous markers of tumor hypoxia predictors of clinical radiation resistance? Strahlenther
    • Vordermark, D. and Brown, J. M. (2003). Endogenous markers of tumor hypoxia predictors of clinical radiation resistance? Strahlenther. Onkol. 179, 801-811.
    • (2003) Onkol. , vol.179 , pp. 801-811
    • Vordermark, D.1    Brown, J.M.2
  • 67
    • 1542316344 scopus 로고    scopus 로고
    • Cell type-specific association of hypoxia-inducible factor-1 alpha (HIF-1 alpha) protein accumulation and radiobiologic tumor hypoxia
    • Vordermark, D., Katzer, A., Baier, K., Kraft, P. and Flentje, M. (2004). Cell type-specific association of hypoxia-inducible factor-1 alpha (HIF-1 alpha) protein accumulation and radiobiologic tumor hypoxia. Int. J. Radiat. Oncol. Biol. Phys. 58, 1242-1250.
    • (2004) Int. J. Radiat. Oncol. Biol. Phys. , vol.58 , pp. 1242-1250
    • Vordermark, D.1    Katzer, A.2    Baier, K.3    Kraft, P.4    Flentje, M.5
  • 68
    • 0029051439 scopus 로고
    • Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension
    • Wang, G. L., Jiang, B. H., Rue, E. A. and Semenza, G. L. (1995). Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc. Natl. Acad. Sci. USA 92, 5510-5514.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5510-5514
    • Wang, G.L.1    Jiang, B.H.2    Rue, E.A.3    Semenza, G.L.4
  • 69
    • 0033167931 scopus 로고    scopus 로고
    • The effect of intracellular iron concentration and nitrogen monoxide on Nramp2 expression and non-transferrin-bound iron uptake
    • Wardrop, S. L. and Richardson, D. R. (1999). The effect of intracellular iron concentration and nitrogen monoxide on Nramp2 expression and non-transferrin-bound iron uptake. Eur. J. Biochem. 263, 41-49.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 41-49
    • Wardrop, S.L.1    Richardson, D.R.2
  • 70
    • 0242413711 scopus 로고    scopus 로고
    • The antimalaria agent artemisinin exerts antiangiogenic effects in mouse embryonic stem cell-derived embryoid bodies
    • Wartenberg, M., Wolf, S., Budde, P., Grunheck, F., Acker, H., Hescheler, J., Wartenberg, G. and Sauer, H. (2003). The antimalaria agent artemisinin exerts antiangiogenic effects in mouse embryonic stem cell-derived embryoid bodies. Lab. Invest. 83, 1647-1655.
    • (2003) Lab. Invest. , vol.83 , pp. 1647-1655
    • Wartenberg, M.1    Wolf, S.2    Budde, P.3    Grunheck, F.4    Acker, H.5    Hescheler, J.6    Wartenberg, G.7    Sauer, H.8
  • 71
    • 9644283362 scopus 로고    scopus 로고
    • The prolyl hydroxylase enzymes that act as oxygen sensors regulating destruction of hypoxia-inducible factor alpha
    • Willam, C., Nicholls, L. G., Ratcliffe, P. J., Pugh, C. W. and Maxwell, P. H. (2004). The prolyl hydroxylase enzymes that act as oxygen sensors regulating destruction of hypoxia-inducible factor alpha. Adv. Enzyme Regul. 44, 75-92.
    • (2004) Adv. Enzyme Regul. , vol.44 , pp. 75-92
    • Willam, C.1    Nicholls, L.G.2    Ratcliffe, P.J.3    Pugh, C.W.4    Maxwell, P.H.5
  • 72
    • 84970583204 scopus 로고
    • Outer-sphere electron transfer of ascorbate anions
    • Williams, N. and Yandell, J. (1982). Outer-sphere electron transfer of ascorbate anions. Aust. J. Chem. 35, 1133-1144.
    • (1982) Aust. J. Chem. , vol.35 , pp. 1133-1144
    • Williams, N.1    Yandell, J.2
  • 73
    • 0031753986 scopus 로고    scopus 로고
    • Temporal, spatial, and oxygen-regulated expression of hypoxia-inducible factor-1 in the lung
    • Yu, A. Y., Frid, M. G., Shimoda, L. A., Wiener, C. M., Stenmark, K. and Semenza, G. L. (1998). Temporal, spatial, and oxygen-regulated expression of hypoxia-inducible factor-1 in the lung. Am. J. Physiol. 275, L818-L826.
    • (1998) Am. J. Physiol. , vol.275
    • Yu, A.Y.1    Frid, M.G.2    Shimoda, L.A.3    Wiener, C.M.4    Stenmark, K.5    Semenza, G.L.6
  • 74
    • 0034213146 scopus 로고    scopus 로고
    • Expression of hypoxia-inducible factor 1alpha in brain tumors: Association with angiogenesis, invasion, and progression
    • Zagzag, D., Zhong, H., Scalzitti, J. M., Laughner, E., Simons, J. W. and Semenza, G. L. (2000). Expression of hypoxia-inducible factor 1alpha in brain tumors: association with angiogenesis, invasion, and progression. Cancer 88, 2606-2618.
    • (2000) Cancer , vol.88 , pp. 2606-2618
    • Zagzag, D.1    Zhong, H.2    Scalzitti, J.M.3    Laughner, E.4    Simons, J.W.5    Semenza, G.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.