메뉴 건너뛰기




Volumn 14, Issue 5, 2007, Pages 420-426

Iron-regulatory proteins limit hypoxia-inducible factor-2α expression in iron deficiency

Author keywords

[No Author keywords available]

Indexed keywords

FERRITIN; HYPOXIA INDUCIBLE FACTOR 2ALPHA; IRON; IRON REGULATORY FACTOR; MESSENGER RNA;

EID: 34247628002     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1222     Document Type: Article
Times cited : (244)

References (50)
  • 1
    • 28944455407 scopus 로고    scopus 로고
    • Regulation of erythropoietin production
    • Eckardt, K.U. & Kurtz, A. Regulation of erythropoietin production. Eur. J. Clin. Invest. 35 Suppl. 3, 13-19 (2005).
    • (2005) Eur. J. Clin. Invest , vol.35 , Issue.SUPPL. 3 , pp. 13-19
    • Eckardt, K.U.1    Kurtz, A.2
  • 2
    • 25444435160 scopus 로고    scopus 로고
    • Increased duodenal iron uptake and transfer in a rat model of chronic hypoxia is accompanied by reduced hepcidin expression
    • Leung, P.S., Srai, S.K., Mascarenhas, M., Churchill, L.J. & Debnam, E.S. Increased duodenal iron uptake and transfer in a rat model of chronic hypoxia is accompanied by reduced hepcidin expression. Gut 54, 1391-1395 (2005).
    • (2005) Gut , vol.54 , pp. 1391-1395
    • Leung, P.S.1    Srai, S.K.2    Mascarenhas, M.3    Churchill, L.J.4    Debnam, E.S.5
  • 3
    • 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. & Semenza, G.L. 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).
    • (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
  • 4
    • 0031000736 scopus 로고    scopus 로고
    • A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1alpha regulates the VEGF expression and is potentially involved in lung and vascular development
    • Ema, M. et al. A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1alpha regulates the VEGF expression and is potentially involved in lung and vascular development. Proc. Natl. Acad. Sci. USA 94, 4273-4278 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4273-4278
    • Ema, M.1
  • 5
    • 0343683375 scopus 로고    scopus 로고
    • HRF, a putative basic helix-loop-helix-PAS- domain transcription factor is closely related to hypoxia-inducible factor-1 alpha and developmentally expressed in blood vessels
    • Flamme, I. et al. HRF, a putative basic helix-loop-helix-PAS- domain transcription factor is closely related to hypoxia-inducible factor-1 alpha and developmentally expressed in blood vessels. Mech. Dev. 63, 51-60 (1997).
    • (1997) Mech. Dev , vol.63 , pp. 51-60
    • Flamme, I.1
  • 6
    • 0030887045 scopus 로고    scopus 로고
    • Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway
    • Hogenesch, J.B. et al. Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway. J. Biol. Chem. 272, 8581-8593 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 8581-8593
    • Hogenesch, J.B.1
  • 7
    • 0031020884 scopus 로고    scopus 로고
    • Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells
    • Tian, H., McKnight, S.L. & Russell, D.W. Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells. Genes Dev. 11, 72-82 (1997).
    • (1997) Genes Dev , vol.11 , pp. 72-82
    • Tian, H.1    McKnight, S.L.2    Russell, D.W.3
  • 8
    • 1842416574 scopus 로고    scopus 로고
    • Oxygen(es) and the hypoxia-inducible factor-1
    • Wenger, R.H. & Gassmann, M. Oxygen(es) and the hypoxia-inducible factor-1. Biol. Chem. 378, 609-616 (1997).
    • (1997) Biol. Chem , vol.378 , pp. 609-616
    • Wenger, R.H.1    Gassmann, M.2
  • 10
    • 0033525830 scopus 로고    scopus 로고
    • Regulation of the hypoxia-inducible transcription factor 1alpha by the ubiquitin-proteasome pathway
    • Kallio, P.J., Wilson, W.J., O'Brien, S., Makino, Y. & Poellinger, L. Regulation of the hypoxia-inducible transcription factor 1alpha by the ubiquitin-proteasome pathway. J. Biol. Chem. 274, 6519-6525 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 6519-6525
    • Kallio, P.J.1    Wilson, W.J.2    O'Brien, S.3    Makino, Y.4    Poellinger, L.5
  • 11
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch
    • Lando, D., Peet, D.J., Whelan, D.A., Gorman, J.J. & Whitelaw, M.L. Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch. Science 295, 858-861 (2002).
    • (2002) Science , vol.295 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 12
    • 0034901463 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1: Oxygen homeostasis and disease pathophysiology
    • Semenza, G.L. Hypoxia-inducible factor 1: oxygen homeostasis and disease pathophysiology. Trends Mol. Med. 7, 345-350 (2001).
    • (2001) Trends Mol. Med , vol.7 , pp. 345-350
    • Semenza, G.L.1
  • 13
    • 0345491599 scopus 로고    scopus 로고
    • Differential roles of hypoxia-inducible factor 1alpha (HIF-1alpha) and HIF-2alpha in hypoxic gene regulation
    • Hu, C.J., Wang, L.Y., Chodosh, L.A., Keith, B. & Simon, M.C. Differential roles of hypoxia-inducible factor 1alpha (HIF-1alpha) and HIF-2alpha in hypoxic gene regulation. Mol. Cell. Biol. 23, 9361-9374 (2003).
    • (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
  • 14
    • 9444283176 scopus 로고    scopus 로고
    • Differentiating the functional role of hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha (EPAS-1) by the use of RNA interference: Erythropoietin is a HIF-2alpha target gene in Hep3B and Kelly cells
    • Warnecke, C. et al. Differentiating the functional role of hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha (EPAS-1) by the use of RNA interference: erythropoietin is a HIF-2alpha target gene in Hep3B and Kelly cells. FASEB J. 18, 1462-1464 (2004).
    • (2004) FASEB J , vol.18 , pp. 1462-1464
    • Warnecke, C.1
  • 15
    • 20444485232 scopus 로고    scopus 로고
    • Silencing of epidermal growth factor receptor suppresses hypoxiainducible factor-2-driven VHL-/- renal cancer
    • Smith, K. et al. Silencing of epidermal growth factor receptor suppresses hypoxiainducible factor-2-driven VHL-/- renal cancer. Cancer Res. 65, 5221-5230 (2005).
    • (2005) Cancer Res , vol.65 , pp. 5221-5230
    • Smith, K.1
  • 16
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • Hentze, M.W., Muckenthaler, M.U. & Andrews, N.C. Balancing acts: molecular control of mammalian iron metabolism. Cell 117, 285-297 (2004).
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 17
    • 33746864096 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron homeostasis by iron regulatory proteins
    • Wallander, M.L., Leibold, E.A. & Eisenstein, R.S. Molecular control of vertebrate iron homeostasis by iron regulatory proteins. Biochim. Biophys. Acta 1763, 668-689 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 668-689
    • Wallander, M.L.1    Leibold, E.A.2    Eisenstein, R.S.3
  • 18
    • 33747349746 scopus 로고    scopus 로고
    • Iron regulation and the cell cycle: Identification of an iron-responsive element in the 3′-untranslated region of human cell division cycle 14A mRNA by a refined microarray-based screening strategy
    • Sanchez, M. et al. Iron regulation and the cell cycle: identification of an iron-responsive element in the 3′-untranslated region of human cell division cycle 14A mRNA by a refined microarray-based screening strategy. J. Biol. Chem. 281, 22865-22874 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 22865-22874
    • Sanchez, M.1
  • 19
    • 0032160381 scopus 로고    scopus 로고
    • IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F
    • Muckenthaler, M., Gray, N.K. & Hentze, M.W. IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F. Mol. Cell 2, 383-388 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 383-388
    • Muckenthaler, M.1    Gray, N.K.2    Hentze, M.W.3
  • 20
    • 0029899154 scopus 로고    scopus 로고
    • Translational regulation of mammalian and Drosophila citric acid cycle enzymes via iron-responsive elements
    • Gray, N.K., Pantopoulos, K., Dandekar, T., Ackrell, B.A. & Hentze, M.W. Translational regulation of mammalian and Drosophila citric acid cycle enzymes via iron-responsive elements. Proc. Natl. Acad. Sci. USA 93, 4925-4930 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4925-4930
    • Gray, N.K.1    Pantopoulos, K.2    Dandekar, T.3    Ackrell, B.A.4    Hentze, M.W.5
  • 21
    • 0344974223 scopus 로고    scopus 로고
    • Role of the ferroportin iron-responsive element in iron and nitric oxide dependent gene regulation
    • Liu, X.B., Hill, P. & Haile, D.J. Role of the ferroportin iron-responsive element in iron and nitric oxide dependent gene regulation. Blood Cells Mol. Dis. 29, 315-326 (2002).
    • (2002) Blood Cells Mol. Dis , vol.29 , pp. 315-326
    • Liu, X.B.1    Hill, P.2    Haile, D.J.3
  • 22
    • 0028266818 scopus 로고
    • Evidence that the pathway of transferrin receptor mRNA degradation involves an endonucleolytic cleavage within the 3′ UTR and does not involve poly(A) tail shortening
    • Binder, R. et al. Evidence that the pathway of transferrin receptor mRNA degradation involves an endonucleolytic cleavage within the 3′ UTR and does not involve poly(A) tail shortening. EMBO J. 13, 1969-1980 (1994).
    • (1994) EMBO J , vol.13 , pp. 1969-1980
    • Binder, R.1
  • 23
    • 33645307993 scopus 로고    scopus 로고
    • Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development
    • Smith, S.R., Ghosh, M.C., Ollivierre-Wilson, H., Hang Tong, W. & Rouault, T.A. Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development. Blood Cells Mol. Dis. 36, 283-287 (2006).
    • (2006) Blood Cells Mol. Dis , vol.36 , pp. 283-287
    • Smith, S.R.1    Ghosh, M.C.2    Ollivierre-Wilson, H.3    Hang Tong, W.4    Rouault, T.A.5
  • 24
    • 30944449709 scopus 로고    scopus 로고
    • Generation of conditional alleles of the murine Iron Regulatory Protein (IRP)-1 and -2 genes
    • Galy, B., Ferring, D. & Hentze, M.W. Generation of conditional alleles of the murine Iron Regulatory Protein (IRP)-1 and -2 genes. Genesis 43, 181-188 (2005).
    • (2005) Genesis , vol.43 , pp. 181-188
    • Galy, B.1    Ferring, D.2    Hentze, M.W.3
  • 25
    • 0024246416 scopus 로고
    • A model for the structure and functions of iron-responsive elements
    • Hentze, M.W. et al. A model for the structure and functions of iron-responsive elements. Gene 72, 201-208 (1988).
    • (1988) Gene , vol.72 , pp. 201-208
    • Hentze, M.W.1
  • 26
    • 18244389488 scopus 로고    scopus 로고
    • Iron-dependent regulation of the divalent metal ion transporter
    • Gunshin, H. et al. Iron-dependent regulation of the divalent metal ion transporter. FEBS Lett. 509, 309-316 (2001).
    • (2001) FEBS Lett , vol.509 , pp. 309-316
    • Gunshin, H.1
  • 27
    • 0026729483 scopus 로고
    • Position is the critical determinant for function of ironresponsive elements as translational regulators
    • Goossen, B. & Hentze, M.W. Position is the critical determinant for function of ironresponsive elements as translational regulators. Mol. Cell. Biol. 12, 1959-1966 (1992).
    • (1992) Mol. Cell. Biol , vol.12 , pp. 1959-1966
    • Goossen, B.1    Hentze, M.W.2
  • 28
    • 0032961171 scopus 로고    scopus 로고
    • Ribosomal pausing and scanning arrest as mechanisms of translational regulation from cap-distal iron-responsive elements
    • Paraskeva, E., Gray, N.K., Schlager, B., Wehr, K. & Hentze, M.W. Ribosomal pausing and scanning arrest as mechanisms of translational regulation from cap-distal iron-responsive elements. Mol. Cell. Biol. 19, 807-816 (1999).
    • (1999) Mol. Cell. Biol , vol.19 , pp. 807-816
    • Paraskeva, E.1    Gray, N.K.2    Schlager, B.3    Wehr, K.4    Hentze, M.W.5
  • 29
    • 0023612118 scopus 로고
    • Identification of the iron-responsive element for the translational regulation of human ferritin mRNA
    • Hentze, M.W. et al. Identification of the iron-responsive element for the translational regulation of human ferritin mRNA. Science 238, 1570-1573 (1987).
    • (1987) Science , vol.238 , pp. 1570-1573
    • Hentze, M.W.1
  • 30
    • 0033587146 scopus 로고    scopus 로고
    • The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
    • Maxwell, P.H. et al. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature 399, 271-275 (1999).
    • (1999) Nature , vol.399 , pp. 271-275
    • Maxwell, P.H.1
  • 31
    • 33747488399 scopus 로고    scopus 로고
    • PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTOR
    • Bernardi, R. et al. PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTOR. Nature 442, 779-785 (2006).
    • (2006) Nature , vol.442 , pp. 779-785
    • Bernardi, R.1
  • 32
    • 0036000028 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha mRNA contains an internal ribosome entry site that allows efficient translation during normoxia and hypoxia
    • Lang, K.J., Kappel, A. & Goodall, G.J. Hypoxia-inducible factor-1alpha mRNA contains an internal ribosome entry site that allows efficient translation during normoxia and hypoxia. Mol. Biol. Cell 13, 1792-1801 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1792-1801
    • Lang, K.J.1    Kappel, A.2    Goodall, G.J.3
  • 33
    • 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
    • Kallio, P.J. et al. Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1alpha. EMBO J. 17, 6573-6586 (1998).
    • (1998) EMBO J , vol.17 , pp. 6573-6586
    • Kallio, P.J.1
  • 34
    • 0030460724 scopus 로고    scopus 로고
    • Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase A gene promoters contain essential binding sites for hypoxia-inducible factor 1
    • Semenza, G.L. et al. Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase A gene promoters contain essential binding sites for hypoxia-inducible factor 1. J. Biol. Chem. 271, 32529-32537 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 32529-32537
    • Semenza, G.L.1
  • 35
    • 0037315337 scopus 로고    scopus 로고
    • Widespread hypoxia-inducible expression of HIF-2alpha in distinct cell populations of different organs
    • Wiesener, M.S. et al. Widespread hypoxia-inducible expression of HIF-2alpha in distinct cell populations of different organs. FASEB J. 17, 271-273 (2003).
    • (2003) FASEB J , vol.17 , pp. 271-273
    • Wiesener, M.S.1
  • 36
    • 0032100732 scopus 로고    scopus 로고
    • HIF-1 alpha is required for solid tumor formation and embryonic vascularization
    • Ryan, H.E., Lo, J. & Johnson, R.S. HIF-1 alpha is required for solid tumor formation and embryonic vascularization. EMBO J. 17, 3005-3015 (1998).
    • (1998) EMBO J , vol.17 , pp. 3005-3015
    • Ryan, H.E.1    Lo, J.2    Johnson, R.S.3
  • 37
    • 0034682513 scopus 로고    scopus 로고
    • The transcription factor EPAS-1/hypoxiainducible factor 2alpha plays an important role in vascular remodeling
    • Peng, J., Zhang, L., Drysdale, L. & Fong, G.H. The transcription factor EPAS-1/hypoxiainducible factor 2alpha plays an important role in vascular remodeling. Proc. Natl. Acad. Sci. USA 97, 8386-8391 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8386-8391
    • Peng, J.1    Zhang, L.2    Drysdale, L.3    Fong, G.H.4
  • 38
    • 0032213236 scopus 로고    scopus 로고
    • The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development
    • Tian, H., Hammer, R.E., Matsumoto, A.M., Russell, D.W. & McKnight, S.L. The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development. Genes Dev. 12, 3320-3324 (1998).
    • (1998) Genes Dev , vol.12 , pp. 3320-3324
    • Tian, H.1    Hammer, R.E.2    Matsumoto, A.M.3    Russell, D.W.4    McKnight, S.L.5
  • 39
    • 0035983324 scopus 로고    scopus 로고
    • Loss of HIF-2alpha and inhibition of VEGF impair fetal lung maturation, whereas treatment with VEGF prevents fatal respiratory distress in premature mice
    • Compernolle, V. et al. Loss of HIF-2alpha and inhibition of VEGF impair fetal lung maturation, whereas treatment with VEGF prevents fatal respiratory distress in premature mice. Nat. Med. 8, 702-710 (2002).
    • (2002) Nat. Med , vol.8 , pp. 702-710
    • Compernolle, V.1
  • 40
    • 0041440036 scopus 로고    scopus 로고
    • The HIF family member EPAS1/HIF-2alpha is required for normal hematopoiesis in mice
    • Scortegagna, M., Morris, M.A., Oktay, Y., Bennett, M. & Garcia, J.A. The HIF family member EPAS1/HIF-2alpha is required for normal hematopoiesis in mice. Blood 102, 1634-1640 (2003).
    • (2003) Blood , vol.102 , pp. 1634-1640
    • Scortegagna, M.1    Morris, M.A.2    Oktay, Y.3    Bennett, M.4    Garcia, J.A.5
  • 41
    • 17044378251 scopus 로고    scopus 로고
    • HIF-2alpha regulates murine hematopoietic development in an erythropoietin-dependent manner
    • Scortegagna, M. et al. HIF-2alpha regulates murine hematopoietic development in an erythropoietin-dependent manner. Blood 105, 3133-3140 (2005).
    • (2005) Blood , vol.105 , pp. 3133-3140
    • Scortegagna, M.1
  • 42
    • 0037416792 scopus 로고    scopus 로고
    • HLF/HIF-2alpha is a key factor in retinopathy of prematurity in association with erythropoietin
    • Morita, M. et al. HLF/HIF-2alpha is a key factor in retinopathy of prematurity in association with erythropoietin. EMBO J. 22, 1134-1146 (2003).
    • (2003) EMBO J , vol.22 , pp. 1134-1146
    • Morita, M.1
  • 44
    • 18444380862 scopus 로고    scopus 로고
    • Expression of hypoxia-inducible factor-1alpha and -2alpha in hypoxic and ischemic rat kidneys
    • Rosenberger, C. et al. Expression of hypoxia-inducible factor-1alpha and -2alpha in hypoxic and ischemic rat kidneys. J. Am. Soc. Nephrol. 13, 1721-1732 (2002).
    • (2002) J. Am. Soc. Nephrol , vol.13 , pp. 1721-1732
    • Rosenberger, C.1
  • 45
    • 0027131432 scopus 로고
    • Recombinant iron-regulatory factor functions as an iron-responsive-element-binding protein, a translational repressor and an aconitase. A functional assay for translational repression and direct demonstration of the iron switch
    • Gray, N.K. et al. Recombinant iron-regulatory factor functions as an iron-responsive-element-binding protein, a translational repressor and an aconitase. A functional assay for translational repression and direct demonstration of the iron switch. Eur. J. Biochem. 218, 657-667 (1993).
    • (1993) Eur. J. Biochem , vol.218 , pp. 657-667
    • Gray, N.K.1
  • 46
    • 0040126630 scopus 로고    scopus 로고
    • The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes
    • Korner, C.G. et al. The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes. EMBO J. 17, 5427-5437 (1998).
    • (1998) EMBO J , vol.17 , pp. 5427-5437
    • Korner, C.G.1
  • 47
    • 0038403678 scopus 로고    scopus 로고
    • Standardization of protocols in cDNA microarray analysis
    • Benes, V. & Muckenthaler, M. Standardization of protocols in cDNA microarray analysis. Trends Biochem. Sci. 28, 244-249 (2003).
    • (2003) Trends Biochem. Sci , vol.28 , pp. 244-249
    • Benes, V.1    Muckenthaler, M.2
  • 48
    • 0033582451 scopus 로고    scopus 로고
    • Hypoxia post-translationally activates iron-regulatory protein 2
    • Hanson, E.S., Foot, L.M. & Leibold, E.A. Hypoxia post-translationally activates iron-regulatory protein 2. J. Biol. Chem. 274, 5047-5052 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 5047-5052
    • Hanson, E.S.1    Foot, L.M.2    Leibold, E.A.3
  • 49
    • 0033548251 scopus 로고    scopus 로고
    • Hypoxia alters ironregulatory protein-1 binding capacity and modulates cellular iron homeostasis in human hepatoma and erythroleukemia cells
    • Toth, I., Yuan, L., Rogers, J.T., Boyce, H. & Bridges, K.R. Hypoxia alters ironregulatory protein-1 binding capacity and modulates cellular iron homeostasis in human hepatoma and erythroleukemia cells. J. Biol. Chem. 274, 4467-4473 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 4467-4473
    • Toth, I.1    Yuan, L.2    Rogers, J.T.3    Boyce, H.4    Bridges, K.R.5
  • 50
    • 34247564616 scopus 로고    scopus 로고
    • Effect of hypoxia on the binding and subcellular distribution of iron regulatory proteins
    • published online 3 January
    • Christova, T. & Templeton, D.M. Effect of hypoxia on the binding and subcellular distribution of iron regulatory proteins. Mol. Cell. Biochem., published online 3 January 2007.
    • (2007) Mol. Cell. Biochem
    • Christova, T.1    Templeton, D.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.