메뉴 건너뛰기




Volumn 451, Issue 1, 2013, Pages 61-67

Nitrogen monoxide inhibits haem synthesis in mouse reticulocytes

Author keywords

Anaemia of infection; Haem synthesis; Iron metabolism; Nitric oxide (NO); Reticulocyte

Indexed keywords

5 AMINOLAEVULINIC ACID SYNTHASE 2; FERROCHELATASE; GLOBIN; HEME; HEMOGLOBIN; HYDROLYASE; INITIATION FACTOR 2ALPHA; IRON; NITRIC OXIDE; NITROPRUSSIDE SODIUM; SYNTHETASE; TRANSFERRIN; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 84875159215     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20121649     Document Type: Article
Times cited : (4)

References (51)
  • 1
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • Richardson, D. R. and Ponka, P. (1997) The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells. Biochim. Biophys. Acta 1331, 1-40
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 2
    • 0033511832 scopus 로고    scopus 로고
    • Cell biology of heme
    • Ponka, P. (1999) Cell biology of heme. Am. J. Med. Sci. 318, 241-256
    • (1999) Am. J. Med. Sci. , vol.318 , pp. 241-256
    • Ponka, P.1
  • 3
    • 0031963449 scopus 로고    scopus 로고
    • Function and regulation of transferrin and ferritin
    • Ponka, P., Beaumont, C. and Richardson, D. R. (1998) Function and regulation of transferrin and ferritin. Semin. Hematol. 35, 35-54
    • (1998) Semin. Hematol. , vol.35 , pp. 35-54
    • Ponka, P.1    Beaumont, C.2    Richardson, D.R.3
  • 4
    • 37549059612 scopus 로고    scopus 로고
    • Regulation of iron acquisition and storage: Consequences for iron-linked disorders
    • De Domenico, I., McVey Ward, D. and Kaplan, J. (2008) Regulation of iron acquisition and storage: consequences for iron-linked disorders. Nat. Rev. Mol. Cell Biol. 9, 72-81
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 72-81
    • De Domenico, I.1    McVey Ward, D.2    Kaplan, J.3
  • 5
    • 67349115201 scopus 로고    scopus 로고
    • Iron metabolism in the anemia of chronic disease
    • Weiss, G. (2008) Iron metabolism in the anemia of chronic disease. Biochim. Biophys. Acta 1790, 682-693
    • (2008) Biochim. Biophys. Acta , vol.1790 , pp. 682-693
    • Weiss, G.1
  • 6
    • 70349325941 scopus 로고    scopus 로고
    • Iron sequestration and anemia of inflammation
    • Ganz, T. and Nemeth, E. (2009) Iron sequestration and anemia of inflammation. Semin. Hematol. 46, 387-393
    • (2009) Semin. Hematol. , vol.46 , pp. 387-393
    • Ganz, T.1    Nemeth, E.2
  • 8
    • 33748102856 scopus 로고    scopus 로고
    • Hepcidin: A peptide hormone at the interface of innate immunity and iron metabolism
    • Ganz, T. (2006) Hepcidin: a peptide hormone at the interface of innate immunity and iron metabolism. Curr. Top. Microbiol. Immunol. 306, 183-198
    • (2006) Curr. Top. Microbiol. Immunol. , vol.306 , pp. 183-198
    • Ganz, T.1
  • 9
    • 24744438847 scopus 로고    scopus 로고
    • The macrophage: A cellular factory at the interphase between iron and immunity for the control of infections
    • Theurl, I., Fritsche, G., Ludwiczek, S., Garimorth, K., Bellmann-Weiler, R. and Weiss, G. (2005) The macrophage: a cellular factory at the interphase between iron and immunity for the control of infections. Biometals 18, 359-367
    • (2005) Biometals , vol.18 , pp. 359-367
    • Theurl, I.1    Fritsche, G.2    Ludwiczek, S.3    Garimorth, K.4    Bellmann-Weiler, R.5    Weiss, G.6
  • 10
    • 0026034432 scopus 로고
    • Role of nitric oxide synthesis in macrophage antimicrobial activity
    • Nathan, C. F. and Hibbs, Jr, J. B. (1991) Role of nitric oxide synthesis in macrophage antimicrobial activity. Curr. Opin. Immunol. 3, 65-70
    • (1991) Curr. Opin. Immunol. , vol.3 , pp. 65-70
    • Nathan, C.F.1    Hibbs Jr., J.B.2
  • 12
    • 0027184205 scopus 로고
    • Oxidation of nitric oxide in aqueous solution to nitrite but not nitrate: Comparison with enzymatically formed nitric oxide from L-arginine
    • Ignarro, L. J., Fukuto, J. M., Griscavage, J. M., Rogers, N. E. and Byrns, R. E. (1993) Oxidation of nitric oxide in aqueous solution to nitrite but not nitrate: comparison with enzymatically formed nitric oxide from L-arginine. Proc. Natl. Acad. Sci. U.S.A. 90, 8103-8107
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 8103-8107
    • Ignarro, L.J.1    Fukuto, J.M.2    Griscavage, J.M.3    Rogers, N.E.4    Byrns, R.E.5
  • 13
    • 0001509578 scopus 로고
    • Mammalian nitrate biosynthesis: Mouse macrophages produce nitrite and nitrate in response to Escherichia coli lipopolysaccharide
    • Stuehr, D. J. and Marletta, M. A. (1985) Mammalian nitrate biosynthesis: mouse macrophages produce nitrite and nitrate in response to Escherichia coli lipopolysaccharide. Proc. Natl. Acad. Sci. U.S.A. 82, 7738-7742
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 7738-7742
    • Stuehr, D.J.1    Marletta, M.A.2
  • 14
    • 0029763714 scopus 로고    scopus 로고
    • Inhibition of hemoglobin expression by heterologous production of nitric oxide synthase in the K562 erythroleukemic cell line
    • Rafferty, S. P., Domachowske, J. B. and Malech, H. L. (1996) Inhibition of hemoglobin expression by heterologous production of nitric oxide synthase in the K562 erythroleukemic cell line. Blood 88, 1070-1078
    • (1996) Blood , vol.88 , pp. 1070-1078
    • Rafferty, S.P.1    Domachowske, J.B.2    Malech, H.L.3
  • 15
    • 0028838664 scopus 로고
    • Nitric oxide-releasing agents and cGMP analogues inhibit murine erythroleukemia cell differentiation and suppress erythroid-specific gene expression: Correlation with decreased DNA binding of NF-E2 and altered c-myb mRNA expression
    • Suhasini, M., Boss, G. R., Pascual, F. E. and Pilz, R. B. (1995) Nitric oxide-releasing agents and cGMP analogues inhibit murine erythroleukemia cell differentiation and suppress erythroid-specific gene expression: correlation with decreased DNA binding of NF-E2 and altered c-myb mRNA expression. Cell Growth Differ. 6, 1559-1566
    • (1995) Cell Growth Differ , vol.6 , pp. 1559-1566
    • Suhasini, M.1    Boss, G.R.2    Pascual, F.E.3    Pilz, R.B.4
  • 16
    • 0345621625 scopus 로고    scopus 로고
    • Inhibitory effect of nitric oxide on chemically induced differentiation of human leukemic K562 cells
    • Chenais, B., Molle, I. and Jeannesson, P. (1999) Inhibitory effect of nitric oxide on chemically induced differentiation of human leukemic K562 cells. Biochem. Pharmacol. 58, 773-778
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 773-778
    • Chenais, B.1    Molle, I.2    Jeannesson, P.3
  • 17
    • 0029023937 scopus 로고
    • Nitric oxide-mediated inactivation of mammalian ferrochelatase in vivo and in vitro: Possible involvement of the iron-sulphur cluster of the enzyme
    • Furukawa, T., Kohno, H., Tokunaga, R. and Taketani, S. (1995) Nitric oxide-mediated inactivation of mammalian ferrochelatase in vivo and in vitro: possible involvement of the iron-sulphur cluster of the enzyme. Biochem. J. 310, 533-538
    • (1995) Biochem. J. , vol.310 , pp. 533-538
    • Furukawa, T.1    Kohno, H.2    Tokunaga, R.3    Taketani, S.4
  • 19
    • 0029970569 scopus 로고    scopus 로고
    • Function of the [2Fe-2S] cluster in mammalian ferrochelatase: A possible role as a nitric oxide sensor
    • Sellers, V. M., Johnson, M. K. and Dailey, H. A. (1996) Function of the [2Fe-2S] cluster in mammalian ferrochelatase: a possible role as a nitric oxide sensor. Biochemistry 35, 2699-2704
    • (1996) Biochemistry , vol.35 , pp. 2699-2704
    • Sellers, V.M.1    Johnson, M.K.2    Dailey, H.A.3
  • 20
    • 0033215094 scopus 로고    scopus 로고
    • Regulation of iron metabolism in murine J774 macrophages: Role of nitric oxide-dependent and -independent pathways following activation with γ interferon and lipopolysaccharide
    • Mulero, V. and Brock, J. H. (1999) Regulation of iron metabolism in murine J774 macrophages: role of nitric oxide-dependent and -independent pathways following activation with γ interferon and lipopolysaccharide. Blood 94, 2383-2389
    • (1999) Blood , vol.94 , pp. 2383-2389
    • Mulero, V.1    Brock, J.H.2
  • 21
    • 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. and Cairo, G. (1998) 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) Blood , vol.91 , pp. 1059-1066
    • Recalcati, S.1    Taramelli, D.2    Conte, D.3    Cairo, G.4
  • 22
    • 5644278790 scopus 로고    scopus 로고
    • Endogenous nitration of iron regulatory protein-1 (IRP-1) in nitric oxide-producing murine macrophages: Further insight into the mechanism of nitration in vivo and its impact on IRP-1 functions
    • Gonzalez, D., Drapier, J. C. and Bouton, C. (2004) Endogenous nitration of iron regulatory protein-1 (IRP-1) in nitric oxide-producing murine macrophages: further insight into the mechanism of nitration in vivo and its impact on IRP-1 functions. J. Biol. Chem. 279, 43345-43351
    • (2004) J. Biol. Chem. , vol.279 , pp. 43345-43351
    • Gonzalez, D.1    Drapier, J.C.2    Bouton, C.3
  • 23
    • 0032746973 scopus 로고    scopus 로고
    • Control of transferrin receptor expression via nitric oxide-mediated modulation of iron-regulatory protein 2
    • Kim, S. and Ponka, P. (1999) Control of transferrin receptor expression via nitric oxide-mediated modulation of iron-regulatory protein 2. J. Biol. Chem. 274, 33035-33042
    • (1999) J. Biol. Chem. , vol.274 , pp. 33035-33042
    • Kim, S.1    Ponka, P.2
  • 24
    • 0034089867 scopus 로고    scopus 로고
    • Effects of interferon-γ and lipopolysaccharide on macrophage iron metabolism are mediated by nitric oxide-induced degradation of iron regulatory protein 2
    • Kim, S. and Ponka, P. (2000) Effects of interferon-γ and lipopolysaccharide on macrophage iron metabolism are mediated by nitric oxide-induced degradation of iron regulatory protein 2. J. Biol. Chem. 275, 6220-6226
    • (2000) J. Biol. Chem. , vol.275 , pp. 6220-6226
    • Kim, S.1    Ponka, P.2
  • 25
    • 33746691267 scopus 로고    scopus 로고
    • Iron regulatory protein-independent regulation of ferritin synthesis by nitrogen monoxide
    • Mikhael, M., Kim, S. F., Schranzhofer, M., Soe-Lin, S., Sheftel, A. D., Mullner, E. W. and Ponka, P. (2006) Iron regulatory protein-independent regulation of ferritin synthesis by nitrogen monoxide. FEBS J. 273, 3828-3836
    • (2006) FEBS J , vol.273 , pp. 3828-3836
    • Mikhael, M.1    Kim, S.F.2    Schranzhofer, M.3    Soe-Lin, S.4    Sheftel, A.D.5    Mullner, E.W.6    Ponka, P.7
  • 26
    • 0344441629 scopus 로고
    • Regulation of protein synthesis in rabbit reticulocyte lysates: Characteristics of inhibition of protein synthesis by a translational inhibitor from heme-deficient lysates and its relationship to the initiation factor which binds Met-tRNAf
    • Ranu, R. S., Levin, D. H., Delaunay, J., Ernst, V. and London, I. M. (1976) Regulation of protein synthesis in rabbit reticulocyte lysates: characteristics of inhibition of protein synthesis by a translational inhibitor from heme-deficient lysates and its relationship to the initiation factor which binds Met-tRNAf. Proc. Natl. Acad. Sci. U.S.A. 73, 2720-2724
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 2720-2724
    • Ranu, R.S.1    Levin, D.H.2    Delaunay, J.3    Ernst, V.4    London, I.M.5
  • 27
    • 33947584856 scopus 로고    scopus 로고
    • Regulation of protein synthesis by the heme-regulated eIF2α kinase: Relevance to anemias
    • Chen, J. J. (2007) Regulation of protein synthesis by the heme-regulated eIF2α kinase: relevance to anemias. Blood 109, 2693-2699
    • (2007) Blood , vol.109 , pp. 2693-2699
    • Chen, J.J.1
  • 28
    • 0031902602 scopus 로고    scopus 로고
    • Inhibition of protein synthesis by nitric oxide correlates with cytostatic activity: Nitric oxide induces phosphorylation of initiation factor eIF-2α
    • Kim, Y. M., Son, K., Hong, S. J., Green, A., Chen, J. J., Tzeng, E., Hierholzer, C. and Billiar, T. R. (1998) Inhibition of protein synthesis by nitric oxide correlates with cytostatic activity: nitric oxide induces phosphorylation of initiation factor eIF-2α. Mol. Med. 4, 179-190
    • (1998) Mol. Med. , vol.4 , pp. 179-190
    • Kim, Y.M.1    Son, K.2    Hong, S.J.3    Green, A.4    Chen, J.J.5    Tzeng, E.6    Hierholzer, C.7    Billiar, T.R.8
  • 29
    • 0035805526 scopus 로고    scopus 로고
    • The heme-regulated eukaryotic initiation factor 2α kinase: A potential regulatory target for control of protein synthesis by diffusible gases
    • Uma, S., Yun, B. G. and Matts, R. L. (2001) The heme-regulated eukaryotic initiation factor 2α kinase: a potential regulatory target for control of protein synthesis by diffusible gases. J. Biol. Chem. 276, 14875-14883
    • (2001) J. Biol. Chem. , vol.276 , pp. 14875-14883
    • Uma, S.1    Yun, B.G.2    Matts, R.L.3
  • 30
    • 24344444080 scopus 로고    scopus 로고
    • Interdomain interactions regulate the activation of the heme-regulated eIF 2 α kinase
    • Yun, B. G., Matts, J. A. and Matts, R. L. (2005) Interdomain interactions regulate the activation of the heme-regulated eIF 2 α kinase. Biochim. Biophys. Acta 1725, 174-181
    • (2005) Biochim. Biophys. Acta , vol.1725 , pp. 174-181
    • Yun, B.G.1    Matts, J.A.2    Matts, R.L.3
  • 31
    • 0015518342 scopus 로고
    • The kinetics of iron and transferrin incorporation into rabbit erythroid cells and the nature of stromal-bound iron
    • Martinez-Medellin, J. and Schulman, H. M. (1972) The kinetics of iron and transferrin incorporation into rabbit erythroid cells and the nature of stromal-bound iron. Biochim. Biophys. Acta 264, 272-274
    • (1972) Biochim. Biophys. Acta , vol.264 , pp. 272-274
    • Martinez-Medellin, J.1    Schulman, H.M.2
  • 32
    • 0022406630 scopus 로고
    • Acquisition of iron from transferrin regulates reticulocyte heme synthesis
    • Ponka, P. and Schulman, H. M. (1985) Acquisition of iron from transferrin regulates reticulocyte heme synthesis. J. Biol. Chem. 260, 14717-14721
    • (1985) J. Biol. Chem. , vol.260 , pp. 14717-14721
    • Ponka, P.1    Schulman, H.M.2
  • 33
    • 0020050144 scopus 로고
    • Iron utilization in rabbit reticulocytes: A study using succinylacetone as an inhibitor or heme synthesis
    • Ponka, P., Wilczynska, A. and Schulman, H. M. (1982) Iron utilization in rabbit reticulocytes: a study using succinylacetone as an inhibitor or heme synthesis. Biochim. Biophys. Acta 720, 96-105
    • (1982) Biochim. Biophys. Acta , vol.720 , pp. 96-105
    • Ponka, P.1    Wilczynska, A.2    Schulman, H.M.3
  • 34
    • 0015893042 scopus 로고
    • Study of intracellular iron distribution in rabbit reticulocytes with normal and inhibited heme synthesis
    • Borova, J., Ponka, P. and Neuwirt, J. (1973) Study of intracellular iron distribution in rabbit reticulocytes with normal and inhibited heme synthesis. Biochim. Biophys. Acta 320, 143-156
    • (1973) Biochim. Biophys. Acta , vol.320 , pp. 143-156
    • Borova, J.1    Ponka, P.2    Neuwirt, J.3
  • 35
    • 11144226961 scopus 로고    scopus 로고
    • Intracellular kinetics of iron in reticulocytes: Evidence for endosome involvement in iron targeting to mitochondria
    • Zhang, A. S., Sheftel, A. D. and Ponka, P. (2005) Intracellular kinetics of iron in reticulocytes: evidence for endosome involvement in iron targeting to mitochondria. Blood 105, 368-375
    • (2005) Blood , vol.105 , pp. 368-375
    • Zhang, A.S.1    Sheftel, A.D.2    Ponka, P.3
  • 36
    • 0036525943 scopus 로고    scopus 로고
    • Nitric oxide donors: Chemical activities and biological applications
    • Wang, P. G., Xian, M., Tang, X., Wu, X., Wen, Z., Cai, T. and Janczuk, A. J. (2002) Nitric oxide donors: chemical activities and biological applications. Chem. Rev. 102, 1091-1134
    • (2002) Chem. Rev. , vol.102 , pp. 1091-1134
    • Wang, P.G.1    Xian, M.2    Tang, X.3    Wu, X.4    Wen, Z.5    Cai, T.6    Janczuk, A.J.7
  • 37
    • 0014506913 scopus 로고
    • Regulation of iron entry into reticulocytes. I. Feedback inhibitory effect of heme on iron entry into reticulocytes and on heme synthesis
    • Ponka, P. and Neuwirt, J. (1969) Regulation of iron entry into reticulocytes. I. Feedback inhibitory effect of heme on iron entry into reticulocytes and on heme synthesis. Blood 33, 690-707
    • (1969) Blood , vol.33 , pp. 690-707
    • Ponka, P.1    Neuwirt, J.2
  • 38
    • 0016192663 scopus 로고
    • The role of heme in the release of iron from transferrin in reticulocytes
    • Ponka, P., Neuwirt, J. and Borova, J. (1974) The role of heme in the release of iron from transferrin in reticulocytes. Enzyme 17, 91-99
    • (1974) Enzyme , vol.17 , pp. 91-99
    • Ponka, P.1    Neuwirt, J.2    Borova, J.3
  • 39
    • 0016208405 scopus 로고
    • The reticulocyte-mediated release of iron and bicarbonate from transferrin: Effect of metabolic inhibitors
    • Schulman, H. M., Martinez-Medellin, J. and Sidloi, R. (1974) The reticulocyte-mediated release of iron and bicarbonate from transferrin: effect of metabolic inhibitors. Biochim. Biophys. Acta 343, 529-534
    • (1974) Biochim. Biophys. Acta , vol.343 , pp. 529-534
    • Schulman, H.M.1    Martinez-Medellin, J.2    Sidloi, R.3
  • 40
    • 0021993655 scopus 로고
    • Regulation of heme synthesis in erythroid cells: Hemin inhibits transferrin iron utilization but not protoporphyrin synthesis
    • Ponka, P. and Schulman, H. M. (1985) Regulation of heme synthesis in erythroid cells: hemin inhibits transferrin iron utilization but not protoporphyrin synthesis. Blood 65, 850-857
    • (1985) Blood , vol.65 , pp. 850-857
    • Ponka, P.1    Schulman, H.M.2
  • 41
    • 0018646107 scopus 로고
    • Succinylacetone, a potent inhibitor of heme biosynthesis: Effect on cell growth, heme content and δ-aminolevulinic acid dehydratase activity of malignant murine erythroleukemia cells
    • Ebert, P. S., Hess, R. A., Frykholm, B. C. and Tschudy, D. P. (1979) Succinylacetone, a potent inhibitor of heme biosynthesis: effect on cell growth, heme content and δ-aminolevulinic acid dehydratase activity of malignant murine erythroleukemia cells. Biochem. Biophys. Res. Commun. 88, 1382-1390
    • (1979) Biochem. Biophys. Res. Commun. , vol.88 , pp. 1382-1390
    • Ebert, P.S.1    Hess, R.A.2    Frykholm, B.C.3    Tschudy, D.P.4
  • 43
    • 0000072402 scopus 로고
    • Iron metabolism in the bone marrow as seen by electron microscopy: A critical review
    • Bessis, M. C. and Breton-Gorius, J. (1962) Iron metabolism in the bone marrow as seen by electron microscopy: a critical review. Blood 19, 635-663
    • (1962) Blood , vol.19 , pp. 635-663
    • Bessis, M.C.1    Breton-Gorius, J.2
  • 44
    • 50949089311 scopus 로고    scopus 로고
    • Erythroblastic islands: Niches for erythropoiesis
    • Chasis, J. A. and Mohandas, N. (2008) Erythroblastic islands: niches for erythropoiesis. Blood 112, 470-478
    • (2008) Blood , vol.112 , pp. 470-478
    • Chasis, J.A.1    Mohandas, N.2
  • 45
    • 84856834347 scopus 로고    scopus 로고
    • Regulation by S-nitrosylation of protein post-translational modification
    • Hess, D. T. and Stamler, J. S. (2012) Regulation by S-nitrosylation of protein post-translational modification. J. Biol. Chem. 287, 4411-4418
    • (2012) J. Biol. Chem. , vol.287 , pp. 4411-4418
    • Hess, D.T.1    Stamler, J.S.2
  • 46
    • 0342873589 scopus 로고
    • The effect of hemin on the synthesis of globin
    • Bruns, G. P. and London, I. M. (1965) The effect of hemin on the synthesis of globin. Biochem. Biophys. Res. Commun. 18, 236-242
    • (1965) Biochem. Biophys. Res. Commun. , vol.18 , pp. 236-242
    • Bruns, G.P.1    London, I.M.2
  • 47
    • 0014252635 scopus 로고
    • Stimulation of globin-chain initiation by hemin in the reticulocyte cell-free system
    • Zucker, W. V. and Schulman, H. M. (1968) Stimulation of globin-chain initiation by hemin in the reticulocyte cell-free system. Proc. Natl. Acad. Sci. U.S.A. 59, 582-589
    • (1968) Proc. Natl. Acad. Sci. U.S.A. , vol.59 , pp. 582-589
    • Zucker, W.V.1    Schulman, H.M.2
  • 48
    • 0028935374 scopus 로고
    • Regulation of protein synthesis by heme-regulated eIF-2 α kinase
    • Chen, J. J. and London, I. M. (1995) Regulation of protein synthesis by heme-regulated eIF-2 α kinase. Trends Biochem. Sci. 20, 105-108
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 105-108
    • Chen, J.J.1    London, I.M.2
  • 50
    • 0028356915 scopus 로고
    • Erythroid expression of the heme-regulated eIF-2 α kinase
    • Crosby, J. S., Lee, K., London, I. M. and Chen, J. J. (1994) Erythroid expression of the heme-regulated eIF-2 α kinase. Mol. Cell. Biol. 14, 3906-3914
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3906-3914
    • Crosby, J.S.1    Lee, K.2    London, I.M.3    Chen, J.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.