메뉴 건너뛰기




Volumn 7, Issue 4-6, 1999, Pages 367-376

Regulation of the iron regulatory proteins by reactive nitrogen and oxygen species

Author keywords

Iron regulatory proteins; Reactive nitrogen species; Reactive oxygen species

Indexed keywords

ACONITATE HYDRATASE; HYDROGEN PEROXIDE; IRON; IRON REGULATORY FACTOR; ISOPROTEIN; NITRIC OXIDE; NITROGEN DERIVATIVE; OXYGEN; REACTIVE OXYGEN METABOLITE; SUPEROXIDE;

EID: 0032812762     PISSN: 10522166     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (82)

References (100)
  • 1
    • 0030660482 scopus 로고    scopus 로고
    • Structure and dynamics of the iron responsive element RNA: Implications for binding of the RNA by iron regulatory binding proteins
    • Addess, K. J.; Basilion, J. P.; Klausner, R. D.; Rouault, T. A.; Pardi, A. Structure and dynamics of the iron responsive element RNA: Implications for binding of the RNA by iron regulatory binding proteins. J. Mol. Biol. 274:72-83; 1997.
    • (1997) J. Mol. Biol. , vol.274 , pp. 72-83
    • Addess, K.J.1    Basilion, J.P.2    Klausner, R.D.3    Rouault, T.A.4    Pardi, A.5
  • 3
    • 0032530340 scopus 로고    scopus 로고
    • Iron is hot: An update on the pathophysiology of hemochromatosis
    • Andrews, N. C.; Levy, J. E. Iron is hot: An update on the pathophysiology of hemochromatosis. Blood 92: 1845-1851; 1998.
    • (1998) Blood , vol.92 , pp. 1845-1851
    • Andrews, N.C.1    Levy, J.E.2
  • 4
    • 0027141376 scopus 로고
    • Aconitase, a two-faced protein: Enzyme and iron regulatory factor
    • Beinert, H.; Kennedy, M. C. Aconitase, a two-faced protein: Enzyme and iron regulatory factor. FASEB J. 7:1442-1449; 1993.
    • (1993) FASEB J. , vol.7 , pp. 1442-1449
    • Beinert, H.1    Kennedy, M.C.2
  • 5
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett, B. S.; Stadtman, E. R. Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272:20313-20316; 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 6
    • 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.; Horowitz, J. A.; Basilion, J. P.; Koeller, D. M.; Klausner, R. D.; Harford, J. B. 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    Horowitz, J.A.2    Basilion, J.P.3    Koeller, D.M.4    Klausner, R.D.5    Harford, J.B.6
  • 7
    • 0032540274 scopus 로고    scopus 로고
    • Converse modulation of IRP1 and IRP2 by immunological stimuli in murine RAW 264.7 macrophages
    • Bouton, C.; Oliveira, L.; Drapier, J. Converse modulation of IRP1 and IRP2 by immunological stimuli in murine RAW 264.7 macrophages. J. Biol. Chem. 273:9403-9408; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9403-9408
    • Bouton, C.1    Oliveira, L.2    Drapier, J.3
  • 8
    • 0030752458 scopus 로고    scopus 로고
    • Redox modulation of iron regulatory proteins by peroxynitrite
    • Bouton, C.; Hirling, H.; Drapier, J. Redox modulation of iron regulatory proteins by peroxynitrite. J. Biol. Chem. 272:199969-199975; 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 199969-199975
    • Bouton, C.1    Hirling, H.2    Drapier, J.3
  • 9
    • 0002889135 scopus 로고    scopus 로고
    • Cellular sources and steady-state levels of reactive oxygen species
    • Biadasz Clerch, L.; Massaro, D. J., eds. New York: Marcel Dekker, Inc.
    • Boveris, A.; Cadenas, E. Cellular sources and steady-state levels of reactive oxygen species. In: Biadasz Clerch, L.; Massaro, D. J., eds. Oxygen gene expression and cellular function. New York: Marcel Dekker, Inc.; 1997:1-25.
    • (1997) Oxygen Gene Expression and Cellular Function , pp. 1-25
    • Boveris, A.1    Cadenas, E.2
  • 10
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • Boveris, A.; Oshino, N.; Chance, B. The cellular production of hydrogen peroxide. Biochem. J. 128:617-630; 1972.
    • (1972) Biochem. J. , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 11
    • 0029842459 scopus 로고    scopus 로고
    • Oxygen sensing and molecular adaptation to hypoxia
    • Bunn, H. F.; Poyton, R. O. Oxygen sensing and molecular adaptation to hypoxia. Physiol. Rev. 76:839-885; 1996.
    • (1996) Physiol. Rev. , vol.76 , pp. 839-885
    • Bunn, H.F.1    Poyton, R.O.2
  • 13
    • 0029128256 scopus 로고
    • Nitric-oxide-mediated activation of iron-regulatory protein controls hepatic iron metabolism during acute inflammation
    • Cairo, G.; Pietrangelo, A. Nitric-oxide-mediated activation of iron-regulatory protein controls hepatic iron metabolism during acute inflammation. Eur. J. Biochem. 232:358-363; 1995.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 358-363
    • Cairo, G.1    Pietrangelo, A.2
  • 14
    • 0028090219 scopus 로고
    • Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide
    • Castro, L.; Rodriguez, M.; Radi, R. Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide. J. Biol. Chem. 269:29409-29415; 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29409-29415
    • Castro, L.1    Rodriguez, M.2    Radi, R.3
  • 16
    • 0031033532 scopus 로고    scopus 로고
    • Post-transcriptional regulation of tyrosine hydroxylase gene expression by oxygen in PC12 cells
    • Czyzyk-Krzeska, M. F.; Paulding, W. R.; Beresh, J. E.; Kroll, S. L. Post-transcriptional regulation of tyrosine hydroxylase gene expression by oxygen in PC12 cells. Kidney Int. 51:585-590; 1997.
    • (1997) Kidney Int. , vol.51 , pp. 585-590
    • Czyzyk-Krzeska, M.F.1    Paulding, W.R.2    Beresh, J.E.3    Kroll, S.L.4
  • 17
    • 0030058299 scopus 로고    scopus 로고
    • Molecular mechanisms of iron uptake in eukaryotes
    • De Silva, D.; Askwith, C. C.; Kaplan, J. Molecular mechanisms of iron uptake in eukaryotes. Physiol. Rev. 76:31-17; 1996.
    • (1996) Physiol. Rev. , vol.76 , pp. 31-117
    • De Silva, D.1    Askwith, C.C.2    Kaplan, J.3
  • 18
    • 0031068834 scopus 로고    scopus 로고
    • The role of nitric oxide in the regulation of cellular iron metabolism
    • Domachowske, J. B. The role of nitric oxide in the regulation of cellular iron metabolism. Biochem. Mol. Med. 60:1-7; 1997.
    • (1997) Biochem. Mol. Med. , vol.60 , pp. 1-7
    • Domachowske, J.B.1
  • 19
    • 0030197587 scopus 로고    scopus 로고
    • Modulation by nitric oxide metalloprotein regulatory activities
    • Drapier, J. C.; Bouton, C. Modulation by nitric oxide metalloprotein regulatory activities. Bioessays 18: 549-556; 1996.
    • (1996) Bioessays , vol.18 , pp. 549-556
    • Drapier, J.C.1    Bouton, C.2
  • 20
    • 0023940538 scopus 로고
    • Differentiation of murine macrophages to express nonspecific cytotoxicity for tumor cells results in L-arginine-dependent inhibition of mitochondrial iron-sulfur enzymes in the macrophage effector cells
    • Drapier, J. C.; Hibbs, J. B. Differentiation of murine macrophages to express nonspecific cytotoxicity for tumor cells results in L-arginine-dependent inhibition of mitochondrial iron-sulfur enzymes in the macrophage effector cells. J. Immunol. 140:2829-2838; 1988.
    • (1988) J. Immunol. , vol.140 , pp. 2829-2838
    • Drapier, J.C.1    Hibbs, J.B.2
  • 21
    • 0022461970 scopus 로고
    • Murine cytotoxic activated macrophages inhibit aconitase in tumor cells. Inhibition involves the iron-sulfur prosthetic group and is reversible
    • Drapier, J. C.; Hibbs, J. B. J. Murine cytotoxic activated macrophages inhibit aconitase in tumor cells. Inhibition involves the iron-sulfur prosthetic group and is reversible. J. Clin. Invest. 78:790-797; 1986.
    • (1986) J. Clin. Invest. , vol.78 , pp. 790-797
    • Drapier, J.C.1    Hibbs, J.B.J.2
  • 22
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • Drapier, J. C.; Hirling, H.; Wietzerbin, J.; Kaldy, P.; Kühn, L. C. Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. EMBO J. 12:3643-3649; 1993.
    • (1993) EMBO J. , vol.12 , pp. 3643-3649
    • Drapier, J.C.1    Hirling, H.2    Wietzerbin, J.3    Kaldy, P.4    Kühn, L.C.5
  • 23
    • 0032496159 scopus 로고    scopus 로고
    • Intracellular signaling by reactive oxygen species during hypoxia in cardiomyocytes
    • Duranteau, J.; Chandel, N. S.; Kulisz, A.; Shao, Z.; Schumacker, P. T. Intracellular signaling by reactive oxygen species during hypoxia in cardiomyocytes. J. Biol. Chem. 273:11619-11624; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11619-11624
    • Duranteau, J.1    Chandel, N.S.2    Kulisz, A.3    Shao, Z.4    Schumacker, P.T.5
  • 24
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by Superoxide
    • Flint, D. H.; Tuminello, J. F.; Emptage, M. H. The inactivation of Fe-S cluster containing hydro-lyases by Superoxide. J. Biol. Chem. 268:22369-22376; 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22369-22376
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.H.3
  • 25
    • 0030806863 scopus 로고    scopus 로고
    • .-), superoxide dismutases, and related matters
    • .-), superoxide dismutases, and related matters. J. Biol. Chem. 272:18515-18517; 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18515-18517
    • Fridovich, I.1
  • 26
    • 0029053451 scopus 로고
    • Superoxide radical and Superoxide dismutases
    • Fridovich, I. Superoxide radical and Superoxide dismutases. Annu. Rev. Biochem. 64:97-112; 1995.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 27
    • 0030993117 scopus 로고    scopus 로고
    • Superoxide-driven aconitase FE-S center cycling
    • Gardner, P. R. Superoxide-driven aconitase FE-S center cycling. Biosci. Rep. 17:33-42; 1997.
    • (1997) Biosci. Rep. , vol.17 , pp. 33-42
    • Gardner, P.R.1
  • 29
    • 0027274755 scopus 로고
    • Effect of glutathione on aconitase in Escherichia coli
    • Gardner, P. R.; Fridovich, I. Effect of glutathione on aconitase in Escherichia coli. Arch. Biochem. Biophys. 301:98-102; 1993.
    • (1993) Arch. Biochem. Biophys. , vol.301 , pp. 98-102
    • Gardner, P.R.1    Fridovich, I.2
  • 30
    • 0026806913 scopus 로고
    • Inactivation-reactivation of aconitase in Escherichia coli
    • Gardner, P. R.; Fridovich, I. Inactivation-reactivation of aconitase in Escherichia coli. J. Biol. Chem. 267: 8757-8763; 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8757-8763
    • Gardner, P.R.1    Fridovich, I.2
  • 31
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner, P. R.; Fridovich, I. Superoxide sensitivity of the Escherichia coli aconitase. J. Biol. Chem. 266: 19328-19333; 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 32
    • 0028075773 scopus 로고
    • Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs
    • Gardner, P. R.; Nguyen, D. H.; White, C. Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs. Proc. Natl. Acad. Sci. USA 91:12248-12252; 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12248-12252
    • Gardner, P.R.1    Nguyen, D.H.2    White, C.3
  • 33
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • Gardner, P. R.; Raineri, I.; Epstein, L. B.; White, C. W. Superoxide radical and iron modulate aconitase activity in mammalian cells. J. Biol. Chem. 270: 13399-133405; 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13399-133405
    • Gardner, P.R.1    Raineri, I.2    Epstein, L.B.3    White, C.W.4
  • 34
    • 0032501997 scopus 로고    scopus 로고
    • Iron regulatory element and internal loop/bulge structure for ferritin mRNA studied by cobalt(III) hexamine binding, molecular modeling, and NMR spectroscopy
    • Gdaniec, Z.; Sierzputowska-Gracz, H.; Theil, E. C. Iron regulatory element and internal loop/bulge structure for ferritin mRNA studied by cobalt(III) hexamine binding, molecular modeling, and NMR spectroscopy. Biochemistry 37:1505-1512; 1998.
    • (1998) Biochemistry , vol.37 , pp. 1505-1512
    • Gdaniec, Z.1    Sierzputowska-Gracz, H.2    Theil, E.C.3
  • 35
    • 0024273450 scopus 로고
    • Regulation of the erythropoietin gene: Evidence that the oxygen sensor is a heme protein
    • Goldberg, M. A.; Dunning, S. P.; Bunn, H. F. Regulation of the erythropoietin gene: Evidence that the oxygen sensor is a heme protein. Science 242:1412-1415; 1988.
    • (1988) Science , vol.242 , pp. 1412-1415
    • Goldberg, M.A.1    Dunning, S.P.2    Bunn, H.F.3
  • 36
    • 0031033691 scopus 로고    scopus 로고
    • The aconitase family: Three structural variations on a common theme
    • Gruer, M. J.; Artymiuk, P. J.; Guest, J. R. The aconitase family: Three structural variations on a common theme. Trends Biochem. Sci. 22:3-6; 1997.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 3-6
    • Gruer, M.J.1    Artymiuk, P.J.2    Guest, J.R.3
  • 37
    • 0030963616 scopus 로고    scopus 로고
    • The hypoxic response: Huffing and HIFFing
    • Guillemin, K.; Krasnow, M. A. The hypoxic response: Huffing and HIFFing. Cell 89:9-12; 1997.
    • (1997) Cell , vol.89 , pp. 9-12
    • Guillemin, K.1    Krasnow, M.A.2
  • 39
    • 0028982262 scopus 로고
    • Iron regulates the intracellular degradation of iron regula-tory protein 2 by the proteasome
    • Guo, B.; Phillips, J. D.; Yu, Y.; Leibold, E. A. Iron regulates the intracellular degradation of iron regula-tory protein 2 by the proteasome. J. Biol. Chem. 270: 21645-21651; 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21645-21651
    • Guo, B.1    Phillips, J.D.2    Yu, Y.3    Leibold, E.A.4
  • 40
    • 0030697289 scopus 로고    scopus 로고
    • Functional expression cloning and characterization of SFT, a stimulator of Fe transport
    • Gutierrez, J. A.; Yu, J.; Rivera, S.; Wessling-Resnick, M. Functional expression cloning and characterization of SFT, a stimulator of Fe transport. J. Cell Biol. 139:895-905; 1997.
    • (1997) J. Cell Biol. , vol.139 , pp. 895-905
    • Gutierrez, J.A.1    Yu, J.2    Rivera, S.3    Wessling-Resnick, M.4
  • 41
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing
    • Hampton, M. B.; Kettle, A. J.; Winterbourn, C. C. Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing. Blood 92:3007-3017; 1998.
    • (1998) Blood , vol.92 , pp. 3007-3017
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 42
    • 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
  • 43
    • 0032571304 scopus 로고    scopus 로고
    • Regulation of iron regulatory protein 1 during hypoxia and hypoxia/reoxygenation
    • Hanson, E. S.; Leibold, E. A. Regulation of iron regulatory protein 1 during hypoxia and hypoxia/reoxygenation. J. Biol. Chem. 273:7588-7593; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7588-7593
    • Hanson, E.S.1    Leibold, E.A.2
  • 44
    • 0027960215 scopus 로고
    • Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not
    • Hausladen, A.; Fridovich, I. Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not. J. Biol. Chem. 269:29405-29408; 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29405-29408
    • Hausladen, A.1    Fridovich, I.2
  • 45
    • 0028321733 scopus 로고
    • Optimal sequence and structure of iron-responsive elements
    • Henderson, B. R.; Menotti, E.; Bonnard, C.; Kühn, L. C. Optimal sequence and structure of iron-responsive elements. J. Biol. Chem. 269:17481-17489; 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17481-17489
    • Henderson, B.R.1    Menotti, E.2    Bonnard, C.3    Kühn, L.C.4
  • 46
    • 0014198972 scopus 로고
    • Purification and kinetic studies of beef liver cytoplasmic aconitase
    • Henson, C. P.; Cleland, W. W. Purification and kinetic studies of beef liver cytoplasmic aconitase. J. Biol. Chem. 242:3833-3838; 1967.
    • (1967) J. Biol. Chem. , vol.242 , pp. 3833-3838
    • Henson, C.P.1    Cleland, W.W.2
  • 47
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze, M. W.; Kühn, L. C. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc. Natl. Acad. Sci. USA 93:8175-8182; 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 48
    • 0021128761 scopus 로고
    • Iron depletion: Possible cause of tumor cell cytotoxicity induced by activated macrophages
    • Hibbs, J. B.; Taintor, R. R.; Vavrin, Z. Iron depletion: Possible cause of tumor cell cytotoxicity induced by activated macrophages. Biochem. Biophys. Res. Commun. 123:716-723; 1984.
    • (1984) Biochem. Biophys. Res. Commun. , vol.123 , pp. 716-723
    • Hibbs, J.B.1    Taintor, R.R.2    Vavrin, Z.3
  • 49
    • 0029753008 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit
    • Huang, L.; Arany, Z.; Livingston, D.; Bunn, H. Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit. J. Biol. Chem. 271:32253-32259; 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32253-32259
    • Huang, L.1    Arany, Z.2    Livingston, D.3    Bunn, H.4
  • 51
    • 0028788316 scopus 로고
    • Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2
    • Iwai, K.; Klausner, R. D.; Rouault, T. A. Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2. EMBO J. 14:5350-5357; 1995.
    • (1995) EMBO J. , vol.14 , pp. 5350-5357
    • Iwai, K.1    Klausner, R.D.2    Rouault, T.A.3
  • 52
    • 0017700831 scopus 로고
    • Low molecular weight intracellular iron transport compounds
    • Jacobs, A. Low molecular weight intracellular iron transport compounds. Blood 50:433-439; 1977.
    • (1977) Blood , vol.50 , pp. 433-439
    • Jacobs, A.1
  • 53
    • 0029744741 scopus 로고    scopus 로고
    • Suppression of TCA cycle activity in the cardiac muscle cell by hydroperoxideinduced oxidant stress
    • Janero, D. R.; Hreniuk, D. Suppression of TCA cycle activity in the cardiac muscle cell by hydroperoxideinduced oxidant stress. Am. J. Physiol. 270:C1735-1742; 1996.
    • (1996) Am. J. Physiol. , vol.270
    • Janero, D.R.1    Hreniuk, D.2
  • 54
    • 0030914648 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible factor 1alpha: Posttranscriptional regulation and conformational change by recruitment of the Amt transcription factor
    • Kallio, P. J.; Pongratz, I.; Gradin, K.; McGuire, J.; Poellinger, L. Activation of hypoxia-inducible factor 1alpha: Posttranscriptional regulation and conformational change by recruitment of the Amt transcription factor. Proc. Natl. Acad. Sci. USA 94:5667-5672; 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5667-5672
    • Kallio, P.J.1    Pongratz, I.2    Gradin, K.3    McGuire, J.4    Poellinger, L.5
  • 55
    • 0031825424 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase cascades as regulators of stress responses
    • Karin, M. Mitogen-activated protein kinase cascades as regulators of stress responses. Ann. NY Acad. Sci. 851:139-146; 1998.
    • (1998) Ann. NY Acad. Sci. , vol.851 , pp. 139-146
    • Karin, M.1
  • 56
    • 0032508548 scopus 로고    scopus 로고
    • Loops and bulge/loops in iron-responsive element isoforms influence iron regulatory protein binding. Fine-tuning of mRNA regulation?
    • Ke, Y.; Wu, J.; Leibold, E. A.; Walden, W. E.; Theil, E. C. Loops and bulge/loops in iron-responsive element isoforms influence iron regulatory protein binding. Fine-tuning of mRNA regulation? J. Biol. Chem. 273:23637-23640; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23637-23640
    • Ke, Y.1    Wu, J.2    Leibold, E.A.3    Walden, W.E.4    Theil, E.C.5
  • 57
    • 0029686707 scopus 로고    scopus 로고
    • Role of iron-sulfur proteins in gene regualtion
    • Kennedy, M. C. Role of iron-sulfur proteins in gene regualtion. Met. Ions Biol. Syst. 32:579-602; 1996.
    • (1996) Met. Ions Biol. Syst. , vol.32 , pp. 579-602
    • Kennedy, M.C.1
  • 58
    • 0030873539 scopus 로고    scopus 로고
    • An EPR investigation of the products of the reaction of cytosolic and mitochondrial aconitases with nitric oxide
    • Kennedy, M. C.; Antholine, W. E.; Beinert, H. An EPR investigation of the products of the reaction of cytosolic and mitochondrial aconitases with nitric oxide. J. Biol. Chem. 272:20340-20347; 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20340-20347
    • Kennedy, M.C.1    Antholine, W.E.2    Beinert, H.3
  • 59
    • 0032513043 scopus 로고    scopus 로고
    • Hypoxic stabilization of vascular endothelial growth factor mRNA by the RNA-binding protein HuR
    • Levy, N. S.; Chung, S.; Furneaux, H.; Levy, A. P. Hypoxic stabilization of vascular endothelial growth factor mRNA by the RNA-binding protein HuR. J. Biol. Chem. 273:6417-6423; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6417-6423
    • Levy, N.S.1    Chung, S.2    Furneaux, H.3    Levy, A.P.4
  • 62
    • 0028799569 scopus 로고
    • Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake
    • Martins, E. A.; Robalinho, R. L.; Meneghini, R. Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake. Arch. Biochem. Biophys. 316:128-134; 1995.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 128-134
    • Martins, E.A.1    Robalinho, R.L.2    Meneghini, R.3
  • 63
    • 0014410114 scopus 로고
    • The reduction of cytochrome c by milk xanthine oxidase
    • McCord, J. M.; Fridovich, I. The reduction of cytochrome c by milk xanthine oxidase. J. Biol. Chem. 243:5753-5760; 1968.
    • (1968) J. Biol. Chem. , vol.243 , pp. 5753-5760
    • McCord, J.M.1    Fridovich, I.2
  • 64
    • 0031917173 scopus 로고    scopus 로고
    • Translational regulation of mRNAs with distinct IRE sequences by iron regulatory proteins 1 and 2
    • Menotti, E.; Henderson, B. R.; Kuhn, L. C. Translational regulation of mRNAs with distinct IRE sequences by iron regulatory proteins 1 and 2. J. Biol. Chem. 273:1821-1824; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1821-1824
    • Menotti, E.1    Henderson, B.R.2    Kuhn, L.C.3
  • 65
    • 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.; Hentze, M. 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.2    Hentze, M.3
  • 66
    • 0040204710 scopus 로고    scopus 로고
    • Study of gene regulation by NF-kappa B and AP-1 in response to reactive oxygen intermediates
    • Muller, J. M.; Rupee, R. A.; Baeuerle, P. A. Study of gene regulation by NF-kappa B and AP-1 in response to reactive oxygen intermediates. Methods 11:301-312; 1997.
    • (1997) Methods , vol.11 , pp. 301-312
    • Muller, J.M.1    Rupee, R.A.2    Baeuerle, P.A.3
  • 67
    • 0028092958 scopus 로고
    • Nitric oxide synthases: Roles, tolls, and controls
    • Nathan, C.; Xie, Q. Nitric oxide synthases: Roles, tolls, and controls. Cell 78:915-918; 1994.
    • (1994) Cell , vol.78 , pp. 915-918
    • Nathan, C.1    Xie, Q.2
  • 68
    • 0026034432 scopus 로고
    • Role of nitric oxide synthesis in macrophage antimicrobial activity
    • Nathan, C. F.; Hibbs, J. B. Role of nitric oxide synthesis in macrophage antimicrobial activity. Curr. Opin. Immunol. 3:65-70; 1991.
    • (1991) Curr. Opin. Immunol. , vol.3 , pp. 65-70
    • Nathan, C.F.1    Hibbs, J.B.2
  • 69
    • 0032167632 scopus 로고    scopus 로고
    • Activation of iron regulatory protein-1 by oxidative stress in vitro
    • Pantopoulos, K.; Hentze, M. W. Activation of iron regulatory protein-1 by oxidative stress in vitro. Proc. Natl. Acad. Sci. USA 95:10559-10563; 1998.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10559-10563
    • Pantopoulos, K.1    Hentze, M.W.2
  • 70
    • 0028929741 scopus 로고
    • Nitric oxide signaling to iron regulatory protein: Direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts
    • Pantopoulos, K.; Hentze, M. W. Nitric oxide signaling to iron regulatory protein: Direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts. Proc. Natl. Acad. Sci. USA 92:1267-1271; 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1267-1271
    • Pantopoulos, K.1    Hentze, M.W.2
  • 71
    • 0029055581 scopus 로고
    • Rapid responses to oxidative stress mediated by iron regulatory protein
    • Pantopoulos, K.; Hentze, M. W. Rapid responses to oxidative stress mediated by iron regulatory protein. EMBO J. 14:2917-2924; 1995.
    • (1995) EMBO J. , vol.14 , pp. 2917-2924
    • Pantopoulos, K.1    Hentze, M.W.2
  • 72
    • 0030942257 scopus 로고    scopus 로고
    • Differences in the regulation of iron regulatory protein-1 (IRP-1) by extra- And intracellular oxidative stress
    • Pantopoulos, K.; Mueller, S.; Atzberger, A.; Ansorge, W.; Stremmel, W.; Hentze, M. W. Differences in the regulation of iron regulatory protein-1 (IRP-1) by extra- and intracellular oxidative stress. J. Biol. Chem. 272:9802-9808; 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9802-9808
    • Pantopoulos, K.1    Mueller, S.2    Atzberger, A.3    Ansorge, W.4    Stremmel, W.5    Hentze, M.W.6
  • 75
    • 2642659737 scopus 로고    scopus 로고
    • Differential regulation of iron-regulatory proteins 1 and 2 by nitric oxide in hepatoma cells
    • Phillips, J. D.; Guo, B.; Yu, Y.; Brown, F. M.; Leibold, E. A. Differential regulation of iron-regulatory proteins 1 and 2 by nitric oxide in hepatoma cells. Blood 50:1-10; 1996.
    • (1996) Blood , vol.50 , pp. 1-10
    • Phillips, J.D.1    Guo, B.2    Yu, Y.3    Brown, F.M.4    Leibold, E.A.5
  • 76
    • 0032053169 scopus 로고    scopus 로고
    • Oxygen sensing, hypoxia-inducible factor-1 and the regulation of mammalian gene expression
    • Ratcliffe, P. J.; O'Rourke, J. F.; Maxwell, P. H.; Pugh, C. W. Oxygen sensing, hypoxia-inducible factor-1 and the regulation of mammalian gene expression. J. Exp. Biol. 201(Pt. 8):1153-1162; 1998.
    • (1998) J. Exp. Biol. , vol.201 , Issue.8 PT , pp. 1153-1162
    • Ratcliffe, P.J.1    O'Rourke, J.F.2    Maxwell, P.H.3    Pugh, C.W.4
  • 77
    • 0032006692 scopus 로고    scopus 로고
    • Nitric oxide-mediated induction of ferritin synthesis in J774 macrophages by inflammatory cytokines: Role of selective iron regulatory protein-2 downregulation
    • Recalcati, S.; Taramelli, D.; Conte, D.; Cairo, G. Nitric oxide-mediated induction of ferritin synthesis in J774 macrophages by inflammatory cytokines: Role of selective iron regulatory protein-2 downregulation. Blood 91:1059-1066: 1998.
    • (1998) Blood , vol.91 , pp. 1059-1066
    • Recalcati, S.1    Taramelli, D.2    Conte, D.3    Cairo, G.4
  • 78
    • 0028784211 scopus 로고
    • The effect of redox-related species of nitrogen monoxide on transferrin and iron uptake and cellular proliferation of erythroleukemia (K562) cells
    • Richardson, D. R.; Neumannova, V.; Nagy, E.; Ponka, P. The effect of redox-related species of nitrogen monoxide on transferrin and iron uptake and cellular proliferation of erythroleukemia (K562) cells. Blood 86:3211-3219. 1995.
    • (1995) Blood , vol.86 , pp. 3211-3219
    • Richardson, D.R.1    Neumannova, V.2    Nagy, E.3    Ponka, P.4
  • 79
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • Richardson, D. R.; Ponka, P. The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells. Biochim. Biophys. Acta 1331:1-10; 1997.
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 1-10
    • Richardson, D.R.1    Ponka, P.2
  • 80
    • 0029683776 scopus 로고    scopus 로고
    • The impact of oxidative stress on eukaryotic iron metabolism
    • Rouault, T. A.; Klausner, R. D. The impact of oxidative stress on eukaryotic iron metabolism. EXS 77: 183-197; 1996.
    • (1996) EXS , vol.77 , pp. 183-197
    • Rouault, T.A.1    Klausner, R.D.2
  • 81
    • 0029930904 scopus 로고    scopus 로고
    • Iron-sulfur clusters as biosensors of oxidants and iron
    • Rouault, T. A.; Klausner, R. D. Iron-sulfur clusters as biosensors of oxidants and iron. Trends Biochem. Sci. 121:174-177; 1996.
    • (1996) Trends Biochem. Sci. , vol.121 , pp. 174-177
    • Rouault, T.A.1    Klausner, R.D.2
  • 82
    • 0030961006 scopus 로고    scopus 로고
    • Hypoxia-inducible factor lalpha (HIF-1 alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes
    • Salceda, S.; Caro, J. Hypoxia-inducible factor lalpha (HIF-1 alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes. J. Biol. Chem. 272:22642-22647; 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22642-22647
    • Salceda, S.1    Caro, J.2
  • 83
    • 0028143071 scopus 로고
    • Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2
    • Samaniego, F.; Chin, J.; Iwai, K.; Rouault, T. A.; Klausner, R. D. Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. J. Biol. Chem. 49:30904-30910; 1994.
    • (1994) J. Biol. Chem. , vol.49 , pp. 30904-30910
    • Samaniego, F.1    Chin, J.2    Iwai, K.3    Rouault, T.A.4    Klausner, R.D.5
  • 84
    • 0031002851 scopus 로고    scopus 로고
    • The iron-sulfur cluster of iron regulatory protein 1 modulates the accessibilty of RNA binding and phosphorylation sites
    • Schalinske, K. L.; Anderson, S. A.; Tuazon, P. T.; Chen, O. S.; Kennedy, M. C.; Eisenstein, R. S. The iron-sulfur cluster of iron regulatory protein 1 modulates the accessibilty of RNA binding and phosphorylation sites. Biochemistry 36:3950-3958; 1997.
    • (1997) Biochemistry , vol.36 , pp. 3950-3958
    • Schalinske, K.L.1    Anderson, S.A.2    Tuazon, P.T.3    Chen, O.S.4    Kennedy, M.C.5    Eisenstein, R.S.6
  • 85
    • 0030961083 scopus 로고    scopus 로고
    • Iron regulatory protein 1 is not required for the modulation of ferritin and transferrin receptor expression by iron in a murine pro-B lymphocyte cell line
    • Schalinske, K. L.; Blemings, K. P.; Steffen, D. W.; Chen, O. S.; Eisenstein, R. S. Iron regulatory protein 1 is not required for the modulation of ferritin and transferrin receptor expression by iron in a murine pro-B lymphocyte cell line. Proc. Natl. Acad. Sci. USA 30:10681-10686; 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.30 , pp. 10681-10686
    • Schalinske, K.L.1    Blemings, K.P.2    Steffen, D.W.3    Chen, O.S.4    Eisenstein, R.S.5
  • 86
    • 0029914953 scopus 로고    scopus 로고
    • Phosphorylation and activation of both iron regulatory proteins 1 and 2 in HL-60 cells
    • Schalinske, K. L.; Eisenstein, R. S. Phosphorylation and activation of both iron regulatory proteins 1 and 2 in HL-60 cells. J. Biol. Chem. 271:7168-7176; 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7168-7176
    • Schalinske, K.L.1    Eisenstein, R.S.2
  • 87
    • 0032033086 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 and the molecular physiology of oxygen homeostasis
    • Semenza, G. L. Hypoxia-inducible factor 1 and the molecular physiology of oxygen homeostasis. J. Lab. Clin. Med. 131:207-214; 1998.
    • (1998) J. Lab. Clin. Med. , vol.131 , pp. 207-214
    • Semenza, G.L.1
  • 88
    • 0029437799 scopus 로고
    • 15N NMR and CD studies of the IRE (iron regulatory element) in ferntin mRNA with single base substitution in the hairpin loop
    • Sierzputowska-Gracz, H.; Theil, E. C. 15N NMR and CD studies of the IRE (iron regulatory element) in ferntin mRNA with single base substitution in the hairpin loop. Nucleic Acids Symp. Ser. 33:203-206; 1995.
    • (1995) Nucleic Acids Symp. Ser. , vol.33 , pp. 203-206
    • Sierzputowska-Gracz, H.1    Theil, E.C.2
  • 89
    • 0028132836 scopus 로고
    • Redox signaling: Nitrosylation and related target interactions of nitric oxide
    • Stamler, J. S. Redox signaling: Nitrosylation and related target interactions of nitric oxide. Cell 78:931-936; 1994.
    • (1994) Cell , vol.78 , pp. 931-936
    • Stamler, J.S.1
  • 90
    • 0032553445 scopus 로고    scopus 로고
    • Suppressors of Superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly
    • Strain, J.; Lorenz, C. R.; Bode, J.; Garland, S.; Smolen, G. A.; Ta, D. T.; Vickery, L. E.; Culotta, V. C. Suppressors of Superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly. J. Biol. Chem. 273:31138-31144; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31138-31144
    • Strain, J.1    Lorenz, C.R.2    Bode, J.3    Garland, S.4    Smolen, G.A.5    Ta, D.T.6    Vickery, L.E.7    Culotta, V.C.8
  • 92
    • 0032493381 scopus 로고    scopus 로고
    • Lower intracellular hydrogen peroxide levels in cells overexpressing CuZn-superoxide dismutase
    • Teixeira, H.; Schumacher, R.; Meneghini, R. Lower intracellular hydrogen peroxide levels in cells overexpressing CuZn-superoxide dismutase. Proc. Natl. Acad. Sci. USA 95:7872-7875; 1998.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7872-7875
    • Teixeira, H.1    Schumacher, R.2    Meneghini, R.3
  • 93
    • 0032541173 scopus 로고    scopus 로고
    • Reactive oxygen species released from mitochondria during brief hypoxia induce pre-conditioning in cardiomyocytes
    • Vanden-Hoek, T. L.; Becker, L. B.; Shao, Z.; Li, C.; Schumacker, P. T. Reactive oxygen species released from mitochondria during brief hypoxia induce pre-conditioning in cardiomyocytes. J. Biol. Chem. 273: 18092-18098; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18092-18098
    • Vanden-Hoek, T.L.1    Becker, L.B.2    Shao, Z.3    Li, C.4    Schumacker, P.T.5
  • 95
    • 0027136260 scopus 로고
    • Desferrioxamine induces erythropoietin gene expression and hypoxia-inducible factor 1 DNA-binding activity: Implications for models of hypoxia signal transduction
    • Wang, G. L.; Semenza, G. L. Desferrioxamine induces erythropoietin gene expression and hypoxia-inducible factor 1 DNA-binding activity: Implications for models of hypoxia signal transduction. Blood 82: 3610-3615; 1993.
    • (1993) Blood , vol.82 , pp. 3610-3615
    • Wang, G.L.1    Semenza, G.L.2
  • 96
    • 0030639030 scopus 로고    scopus 로고
    • Pathways for the regulation of macrophage iron metabolism by the anti-inflammatory cytokines IL-4 and IL-13
    • Weiss, G.; Bogdan, C.; Hentze, M. W. Pathways for the regulation of macrophage iron metabolism by the anti-inflammatory cytokines IL-4 and IL-13. J. Immunol. 158:420-425; 1997.
    • (1997) J. Immunol. , vol.158 , pp. 420-425
    • Weiss, G.1    Bogdan, C.2    Hentze, M.W.3
  • 98
    • 0032561328 scopus 로고    scopus 로고
    • Increased oxidative damage is correlated to altered mitochondrial function in heterozygous manganese Superoxide dismutase knockout mice
    • Williams, M. D.; Van Remmen, H.; Conrad, C. C.; Huang, T. T.; Epstein, C. J.; Richardson, A. Increased oxidative damage is correlated to altered mitochondrial function in heterozygous manganese Superoxide dismutase knockout mice. J. Biol. Chem. 273:28510-28515; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28510-28515
    • Williams, M.D.1    Van Remmen, H.2    Conrad, C.C.3    Huang, T.T.4    Epstein, C.J.5    Richardson, A.6
  • 99
    • 0031002421 scopus 로고    scopus 로고
    • Superoxide and peroxynitrite generation from inducible nitric oxide synthase in macrophages
    • Xia, Y.; Zweier, J. L. Superoxide and peroxynitrite generation from inducible nitric oxide synthase in macrophages. Proc. Natl. Acad. Sci. USA 94:6954-6958; 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6954-6958
    • Xia, Y.1    Zweier, J.L.2
  • 100
    • 0030881686 scopus 로고    scopus 로고
    • Oxidative damage during aging targets mitochondrial aconitase
    • Yan, L.-J.; Levine, R. L.; Sohal, R. S. Oxidative damage during aging targets mitochondrial aconitase. Proc. Natl. Acad. Sci. USA 94:11168-11172; 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11168-11172
    • Yan, L.-J.1    Levine, R.L.2    Sohal, R.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.