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Volumn 16, Issue 7, 1996, Pages 3781-3788

Nitric oxide and oxidative stress (H2O2) control mammalian iron metabolism by different pathways

Author keywords

[No Author keywords available]

Indexed keywords

CHELATING AGENT; HYDROGEN PEROXIDE; IRON; IRON REGULATORY FACTOR; IRON SULFUR PROTEIN; MESSENGER RNA; NITRIC OXIDE; REACTIVE OXYGEN METABOLITE;

EID: 0029972895     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.7.3781     Document Type: Article
Times cited : (181)

References (50)
  • 1
    • 0027358877 scopus 로고
    • Endothelial-cell heme uptake from heme proteins: Induction of sensitization and desensitization to oxidative damage
    • Balla, J., H. S. Jacob, G. Balla, K. Nath, J. W. Eaton, and G. M. Vercellolti. 1993. Endothelial-cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidative damage. Proc. Natl. Acad. Sci. USA 90:9285-9289.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9285-9289
    • Balla, J.1    Jacob, H.S.2    Balla, G.3    Nath, K.4    Eaton, J.W.5    Vercellolti, G.M.6
  • 2
    • 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., J. A. Horowitz, J. P. Basilion, D. M. Koeller, R. D. Klausner, and J. B. Harford. 1994. 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) 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
  • 3
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • Boveris, A., and B. Chance. 1973. The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen. Biochem. J. 134:707-716.
    • (1973) Biochem. J. , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 5
    • 0028090219 scopus 로고
    • Aconitase is readily inactivated hy peroxynitrite, but not by its precursor, nitric oxide
    • Castro, L., M. Rodriguez, and R. Radi. 1994. Aconitase is readily inactivated hy peroxynitrite, but not by its precursor, nitric oxide. J. Biol. Chem. 269:29409-29415.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29409-29415
    • Castro, L.1    Rodriguez, M.2    Radi, R.3
  • 6
    • 0026511260 scopus 로고
    • Modulation of the RNA-binding activity of a regulatory protein by iron in vitro: Switching between enzymatic and genetic function?
    • Constable, A., S. Quick, N. K. Gray, and M. W. Hentze. 1992. Modulation of the RNA-binding activity of a regulatory protein by iron in vitro: switching between enzymatic and genetic function? Proc. Natl. Acad. Sci. USA 89:4554-4558.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4554-4558
    • Constable, A.1    Quick, S.2    Gray, N.K.3    Hentze, M.W.4
  • 7
    • 0025822118 scopus 로고
    • Identification of a novel iron-responsive element in murine and human erythroid δ-aminolevulinic acid synthase mRNA
    • Dandekar, T., R. Stripecke, N. K. Gray, B. Goossen, A. Constable, H. E. Johansson, and M. W. Hentze. 1991. Identification of a novel iron-responsive element in murine and human erythroid δ-aminolevulinic acid synthase mRNA. EMBO J. 10:1903-1909.
    • (1991) EMBO J. , vol.10 , pp. 1903-1909
    • Dandekar, T.1    Stripecke, R.2    Gray, N.K.3    Goossen, B.4    Constable, A.5    Johansson, H.E.6    Hentze, M.W.7
  • 8
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • Drapier, J. C., H. Hirling, J. Wietzerbin, P. Kaldy, and L. C. Kühn. 1993. Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. EMBO J. 12:3643-3649.
    • (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
  • 9
    • 0025788509 scopus 로고
    • Generation of EPR-detectable nitrosyl-iron complexes in tumor target cells cocultured with activated macrophages
    • Drapier, J. C., C. Pellat, and Y. Henry. 1991. Generation of EPR-detectable nitrosyl-iron complexes in tumor target cells cocultured with activated macrophages. J. Biol. Chem. 266:10162-10167.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10162-10167
    • Drapier, J.C.1    Pellat, C.2    Henry, Y.3
  • 10
    • 0027297916 scopus 로고
    • Iron regulatory factor expressed from recombinant baculovirus: Conversion between the RNA-binding apoprotein and Fe-S cluster containing aconitase
    • Emery-Goodman, A., H. Hirling, L. Scarpellino, B. Henderson, and L. C. Kühn. 1993. Iron regulatory factor expressed from recombinant baculovirus: conversion between the RNA-binding apoprotein and Fe-S cluster containing aconitase. Nucleic Acids Res. 21:1457-1461.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1457-1461
    • Emery-Goodman, A.1    Hirling, H.2    Scarpellino, L.3    Henderson, B.4    Kühn, L.C.5
  • 11
    • 0025817680 scopus 로고
    • The biochemical pathways of nitric oxide formation from nitrovasodilators: Appropriate choise of exogenous NO donors and aspects of preparation and handling of aqueous NO solutions
    • Feelisch, M. 1991. The biochemical pathways of nitric oxide formation from nitrovasodilators: appropriate choise of exogenous NO donors and aspects of preparation and handling of aqueous NO solutions. J. Cardiovasc. Pharmacol. 17(Suppl. 3):S25-S33.
    • (1991) J. Cardiovasc. Pharmacol. , vol.17 , Issue.3 SUPPL.
    • Feelisch, M.1
  • 12
    • 0028059555 scopus 로고
    • Iron regulatory protein prevents binding of the 43S translation pre-initiation complex to ferritin and eALAS mRNAs
    • Gray, N. K., and M. W. Hentze. 1994. Iron regulatory protein prevents binding of the 43S translation pre-initiation complex to ferritin and eALAS mRNAs. EMBO J. 13:3882-3891.
    • (1994) EMBO J. , vol.13 , pp. 3882-3891
    • Gray, N.K.1    Hentze, M.W.2
  • 13
    • 0029899154 scopus 로고    scopus 로고
    • Translational regulation of mammalian and drosophila citric acid cycle enzymes via iron-responsive elements
    • Gray, N. K., K. Pantopoulos, T. Dandekar, B. A. C. Ackrell, and M. W. Hentze. 1996. Translational regulation of mammalian and drosophila citric acid cycle enzymes via iron-responsive elements. Proc. Natl. Acad. Sci. USA 93:4925-4930.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4925-4930
    • Gray, N.K.1    Pantopoulos, K.2    Dandekar, T.3    Ackrell, B.A.C.4    Hentze, M.W.5
  • 14
    • 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., S. Quick, B. Goossen, A. Constable, H. Hirling, L. C. Kuhn, and M. W. Hentze. 1993. 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) Eur. J. Biochem. , vol.218 , pp. 657-667
    • Gray, N.K.1    Quick, S.2    Goossen, B.3    Constable, A.4    Hirling, H.5    Kuhn, L.C.6    Hentze, M.W.7
  • 16
    • 0029034338 scopus 로고
    • Characterization and expression of iron regulatory protein 2 (IRP2). Presence of multiple IRP2 transcripts regulated by intracellular iron levels
    • Guo, B., F. M. Brown, J. D. Phillips, Y. Yu, and E. A. Leibold. 1995. Characterization and expression of iron regulatory protein 2 (IRP2). Presence of multiple IRP2 transcripts regulated by intracellular iron levels. J. Biol. Chem. 270:16529-16535.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16529-16535
    • Guo, B.1    Brown, F.M.2    Phillips, J.D.3    Yu, Y.4    Leibold, E.A.5
  • 17
    • 0028982262 scopus 로고
    • Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome
    • Guo, B., J. D. Phillips, Y. Yu, and E. A. Leibold. 1995. Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome. J. Biol. Chem. 270:21645-21651.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21645-21651
    • Guo, B.1    Phillips, J.D.2    Yu, Y.3    Leibold, E.A.4
  • 18
    • 0028131454 scopus 로고
    • Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity
    • Guo, B., Y. Yu, and E. A. Leibold. 1994. Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity. J. Biol. Chem. 269:24252-242611.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24252-242611
    • Guo, B.1    Yu, Y.2    Leibold, E.A.3
  • 19
    • 0027050315 scopus 로고
    • Cellular regulation of the iron-responsive element binding protein: Disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding
    • Halle, D. J., T. A. Rouault, J. B. Harford, M. C. Kennedy, G. A. Blondin, H. Beinert, and R. D. Klausner. 1992. Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding. Proc. Natl. Acad. Sci. USA 89:11735-11739.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11735-11739
    • Halle, D.J.1    Rouault, T.A.2    Harford, J.B.3    Kennedy, M.C.4    Blondin, G.A.5    Beinert, H.6    Klausner, R.D.7
  • 20
    • 0026756095 scopus 로고
    • Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: Role of the iron-sulfur cluster
    • Haile, D. J., T. A. Rouault, C. K. Tang, J. Chin, J. B. Harford, and R. D. Klausner. 1992. Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: role of the iron-sulfur cluster. Proc. Natl. Acad. Sci. USA 89:7536-7540.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7536-7540
    • Haile, D.J.1    Rouault, T.A.2    Tang, C.K.3    Chin, J.4    Harford, J.B.5    Klausner, R.D.6
  • 21
    • 0027960215 scopus 로고
    • Superoxide and peroxynitrite inactivates aconitases, but nitric oxide does not
    • Hausladen, A., and I. Fridovich. 1994. Superoxide and peroxynitrite inactivates aconitases, but nitric oxide does not. J. Biol. Chem. 269:29405-29408.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29405-29408
    • Hausladen, A.1    Fridovich, I.2
  • 22
    • 0029132168 scopus 로고
    • Differential modulation of the RNA-binding proteins IRP-1 and 1RP-2 in response to iron. 1RP-2 inactivation requires translation of another protein
    • Henderson, B. R., and L. C. Kühn. 1995. Differential modulation of the RNA-binding proteins IRP-1 and 1RP-2 in response to iron. 1RP-2 inactivation requires translation of another protein. J. Biol. Chem. 270:20509-20515.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20509-20515
    • Henderson, B.R.1    Kühn, L.C.2
  • 23
    • 0027717217 scopus 로고
    • Characterization of a second RNA-binding protein in rodents with specificity for iron-responsive elements
    • Henderson, B. R., C. Seiser, and L. C. Kühn. 1993. Characterization of a second RNA-binding protein in rodents with specificity for iron-responsive elements. J. Biol. Chem. 268:27327-27334.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27327-27334
    • Henderson, B.R.1    Seiser, C.2    Kühn, L.C.3
  • 24
    • 0024516594 scopus 로고
    • Oxidation-reduction and the molecular mechanism of a regulated RNA-protein interaction
    • Hentze, M. W., T. A. Rouault, J. B. Harford, and R. D. Klausner. 1989. Oxidation-reduction and the molecular mechanism of a regulated RNA-protein interaction. Science 244:357-359.
    • (1989) Science , vol.244 , pp. 357-359
    • Hentze, M.W.1    Rouault, T.A.2    Harford, J.B.3    Klausner, R.D.4
  • 25
    • 0028586693 scopus 로고
    • Control of disease by selective iron depletion: A novel therapeutic strategy utilizing iron chelators
    • Hershko, C. 1994. Control of disease by selective iron depletion: a novel therapeutic strategy utilizing iron chelators. Baillieres Clin. Haematol. 7:965-1000.
    • (1994) Baillieres Clin. Haematol. , vol.7 , pp. 965-1000
    • Hershko, C.1
  • 26
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter, T. 1995. Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80:225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 27
    • 0028788316 scopus 로고
    • Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2
    • Iwai, K., R. D. Klausner, and T. A. Rouault. 1995. Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2. EMBO J. 14:5350-5357.
    • (1995) EMBO J. , vol.14 , pp. 5350-5357
    • Iwai, K.1    Klausner, R.D.2    Rouault, T.A.3
  • 28
    • 0027081042 scopus 로고
    • Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein
    • Kennedy, M. C., L. Mende-Mueller, G. A. Blondin, and H. Beinert. 1992. Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein. Proc. Natl. Acad. Sci. USA 89:11730-11734.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11730-11734
    • Kennedy, M.C.1    Mende-Mueller, L.2    Blondin, G.A.3    Beinert, H.4
  • 29
    • 0029328437 scopus 로고
    • Reactive oxygen species as cellular messengers
    • Khan, A. U., and T. Wilson. 1995. Reactive oxygen species as cellular messengers. Chem. Biol. 2:437-445.
    • (1995) Chem. Biol. , vol.2 , pp. 437-445
    • Khan, A.U.1    Wilson, T.2
  • 30
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: The control of cellular iron metabolism
    • Klausner, R. D., T. Rouault, and J. B. Harford. 1993. Regulating the fate of mRNA: the control of cellular iron metabolism. Cell 72:19-28.
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.2    Harford, J.B.3
  • 31
    • 0028589014 scopus 로고
    • Molecular regulation of iron proteins
    • Kühn, L. C. 1994. Molecular regulation of iron proteins. Baillieres Clin. Haematol. 7:763-785.
    • (1994) Baillieres Clin. Haematol. , vol.7 , pp. 763-785
    • Kühn, L.C.1
  • 32
    • 0025117611 scopus 로고
    • EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages
    • Lancaster, J. R., Jr., and J. B. Hibbs, Jr. 1990. EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages. Proc. Natl. Acad. Sci. USA 87:1223-1227.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1223-1227
    • Lancaster Jr., J.R.1    Hibbs Jr., J.B.2
  • 33
    • 0021813287 scopus 로고
    • Cellular pharmacology of deferrioxamine B and derivatives in cultured rat hepatocytes in relation to iron mobilization
    • Laub, R., Y.-J. Schneider, J.-N. Octave, A. Trouet, and R. R. Crichton. 1985. Cellular pharmacology of deferrioxamine B and derivatives in cultured rat hepatocytes in relation to iron mobilization. Biochem. Pharmacol. 34:1175-1183.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 1175-1183
    • Laub, R.1    Schneider, Y.-J.2    Octave, J.-N.3    Trouet, A.4    Crichton, R.R.5
  • 34
    • 0024121621 scopus 로고
    • Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated regions of ferritin heavy-and light-subunit mRNAs
    • Leibold, E. A., and H. N. Munro. 1988. Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated regions of ferritin heavy-and light-subunit mRNAs. Proc. Natl. Acad. Sci. USA 85:2171-2175.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2171-2175
    • Leibold, E.A.1    Munro, H.N.2
  • 36
    • 0028799569 scopus 로고
    • Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake
    • Martins, E. A. L., R. L. Robalinho, and R. Meneghini. 1995. Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake. Arch. Biochem. Biophys. 316:128-134.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 128-134
    • Martins, E.A.L.1    Robalinho, R.L.2    Meneghini, R.3
  • 37
    • 0027503294 scopus 로고
    • Translational control of 5-aminolevulinate synthase mRNA by iron-responsive elements in erythroid cells
    • Melefors. Ö., B. Goossen, H. E. Johansson, R. Stripecke, N. K. Gray, and M. W. Hentze. 1993. Translational control of 5-aminolevulinate synthase mRNA by iron-responsive elements in erythroid cells. J. Biol. Chem. 268:5974-5978.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5974-5978
    • Melefors, Ö.1    Goossen, B.2    Johansson, H.E.3    Stripecke, R.4    Gray, N.K.5    Hentze, M.W.6
  • 38
    • 0027549047 scopus 로고
    • Translational regulation by mRNA, protein interactions in eukaryotic cells: Ferritin and beyond
    • Melefors, Ö., and M. W. Hentze. 1993. Translational regulation by mRNA, protein interactions in eukaryotic cells: ferritin and beyond. Bioessays 15:85-90.
    • (1993) Bioessays , vol.15 , pp. 85-90
    • Melefors, Ö.1    Hentze, M.W.2
  • 39
    • 0024365045 scopus 로고
    • A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA
    • Müllner, E. W., B. Neupert, and L. C. Kühn. 1989. A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA. Cell 58:373-382.
    • (1989) Cell , vol.58 , pp. 373-382
    • Müllner, E.W.1    Neupert, B.2    Kühn, L.C.3
  • 40
    • 0029054681 scopus 로고
    • Effect of nitric oxide on expression of transferrin receptor and ferritin and on cellular iron metabolism in K562 human erythroleukemia cells
    • Oria, R., L. Sanchez, T. Houston, M. W. Hentze, F. Y. Liew, and J. H. Brock. 1995. Effect of nitric oxide on expression of transferrin receptor and ferritin and on cellular iron metabolism in K562 human erythroleukemia cells. Blood 85:2962-2966.
    • (1995) Blood , vol.85 , pp. 2962-2966
    • Oria, R.1    Sanchez, L.2    Houston, T.3    Hentze, M.W.4    Liew, F.Y.5    Brock, J.H.6
  • 42
    • 0028929741 scopus 로고
    • Nitric oxide signaling to iron-regulatory protein (IRP): Direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts
    • Pantopoulos, K., and M. W. Hentze. 1995. Nitric oxide signaling to iron-regulatory protein (IRP): direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts. Proc. Natl. Acad. Sci. USA 92:1267-1271.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1267-1271
    • Pantopoulos, K.1    Hentze, M.W.2
  • 43
    • 0029055581 scopus 로고
    • Rapid responses to oxidative stress mediated by iron regulatory protein
    • Pantopoulos, K., and M. W. Hentze. 1995. Rapid responses to oxidative stress mediated by iron regulatory protein. EMBO J. 14:2917-2924.
    • (1995) EMBO J. , vol.14 , pp. 2917-2924
    • Pantopoulos, K.1    Hentze, M.W.2
  • 44
    • 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., V. Neumannova, E. Nagy, and P. Ponka. 1995. 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) Blood , vol.86 , pp. 3211-3219
    • Richardson, D.R.1    Neumannova, V.2    Nagy, E.3    Ponka, P.4
  • 45
    • 0028143071 scopus 로고
    • Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2
    • Samaniego, F., J. Chin, K. Iwai, T. A. Renault, and R. D. Klausner. 1994. Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. J. Biol. Chem. 269:30904-30910.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30904-30910
    • Samaniego, F.1    Chin, J.2    Iwai, K.3    Renault, T.A.4    Klausner, R.D.5
  • 46
    • 0026483360 scopus 로고
    • Iron regulates the activity of the iron-responsive element binding protein without changing its rate of synthesis or degradation
    • Tang, C. K., J. Chin, J. B. Harford, R. D. Klausner, and T. A. Rouault. 1992 Iron regulates the activity of the iron-responsive element binding protein without changing its rate of synthesis or degradation. J. Biol. Chem. 267:24466-24470.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24466-24470
    • Tang, C.K.1    Chin, J.2    Harford, J.B.3    Klausner, R.D.4    Rouault, T.A.5
  • 47
    • 0024369974 scopus 로고
    • Purification of a specific represser of ferritin mRNA translation from rabbit liver
    • Walden, W. E., M. M. Patino, and L. Gafiield. 1989. Purification of a specific represser of ferritin mRNA translation from rabbit liver. J. Biol. Chem. 264:13765-13769.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13765-13769
    • Walden, W.E.1    Patino, M.M.2    Gafiield, L.3
  • 48
    • 0030065261 scopus 로고    scopus 로고
    • Protein phosphatase 2A positively and negatively regulates Rasl-mediated photoreceptor development in Drosophila
    • Wassarman, D. A., N. M. Solomon, H. C. Chang, F. D. Karim, M. Therrien, and G. M. Rubin. 1996. Protein phosphatase 2A positively and negatively regulates Rasl-mediated photoreceptor development in Drosophila. Genes Dev. 10:272-278.
    • (1996) Genes Dev. , vol.10 , pp. 272-278
    • Wassarman, D.A.1    Solomon, N.M.2    Chang, H.C.3    Karim, F.D.4    Therrien, M.5    Rubin, G.M.6
  • 50
    • 0000104045 scopus 로고
    • Measurement of endothelial cell free radical generation: Evidence for a central mechanism of free radical injury in postischemic tissues
    • Zweier, J. L., P. Kuppusamy, and G. A. Lutty. 1988. Measurement of endothelial cell free radical generation: evidence for a central mechanism of free radical injury in postischemic tissues. Proc. Natl. Acad. Sci. USA 85:4046-4050.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4046-4050
    • Zweier, J.L.1    Kuppusamy, P.2    Lutty, G.A.3


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