메뉴 건너뛰기




Volumn 213, Issue 1, 2007, Pages 1-16

Heme as a magnificient molecule with multiple missions: Heme determines its own fate and governs cellular homeostasis

Author keywords

Aminolevulinate synthase; Bach1; CP motif; Heme; Heme oxygenase

Indexed keywords

5 AMINOLEVULINATE SYNTHASE; CATALASE; CYSTEINE; CYTOCHROME C; CYTOCHROME P450; HEME; HEME OXYGENASE 1; HEME OXYGENASE 2; HEMOGLOBIN; HEMOPROTEIN; IRON; IRON REGULATORY PROTEIN 2; ISOPROTEIN; MEMBRANE PROTEIN; MYOGLOBIN; PEROXIDASE; POTASSIUM CHANNEL; PROLINE; TRANSCRIPTION FACTOR; GLOBIN; HEME OXYGENASE;

EID: 34948858043     PISSN: 00408727     EISSN: 13493329     Source Type: Journal    
DOI: 10.1620/tjem.213.1     Document Type: Review
Times cited : (162)

References (116)
  • 2
  • 3
    • 34948835134 scopus 로고    scopus 로고
    • Anderson, K.E., Sassa, S., Bishop, D.F. & Desnick, R.J. (2001) Disorders of heme biosynthesis: X-linked sideroblastic anemia and the porphyrias. The Metabolic & Molecular Bases of Inherited Disease. C.R. Scriver, A.L. Beaudet, W.S. Sly & D. Valle, McGraw-Hill Medical Publishing Division, New York, pp. 2991-3062.
    • Anderson, K.E., Sassa, S., Bishop, D.F. & Desnick, R.J. (2001) Disorders of heme biosynthesis: X-linked sideroblastic anemia and the porphyrias. The Metabolic & Molecular Bases of Inherited Disease. C.R. Scriver, A.L. Beaudet, W.S. Sly & D. Valle, McGraw-Hill Medical Publishing Division, New York, pp. 2991-3062.
  • 4
    • 0035949630 scopus 로고    scopus 로고
    • Multiple autophosphorylation is essential for the formation of the active and stable homodimer of heme-regulated eIF2alpha kinase
    • Bauer, B.N., Rafie-Kolpin, M., Lu, L., Han, A. & Chen, J.J. (2001) Multiple autophosphorylation is essential for the formation of the active and stable homodimer of heme-regulated eIF2alpha kinase. Biochemistry, 40, 11543-11551.
    • (2001) Biochemistry , vol.40 , pp. 11543-11551
    • Bauer, B.N.1    Rafie-Kolpin, M.2    Lu, L.3    Han, A.4    Chen, J.J.5
  • 5
    • 0001598487 scopus 로고    scopus 로고
    • Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase
    • Berlanga, J.J., Santoyo, J. & De Haro, C. (1999) Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase. Eur. J. Biochem., 265, 754-762.
    • (1999) Eur. J. Biochem , vol.265 , pp. 754-762
    • Berlanga, J.J.1    Santoyo, J.2    De Haro, C.3
  • 7
    • 0015351748 scopus 로고
    • The nature of electron transfer and energy coupling reactions
    • Chance, B. (1972) The nature of electron transfer and energy coupling reactions. FEBS Lett., 23, 3-20.
    • (1972) FEBS Lett , vol.23 , pp. 3-20
    • Chance, B.1
  • 9
    • 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
  • 10
    • 0026535358 scopus 로고
    • Assignment of human erythroid delta-aminolevulinate synthase (ALAS2) to a distal subregion of band Xp11.21 by PCR analysis of somatic cell hybrids containing X; autosome translocations
    • Cotter, P.D., Willard, H.F., Gorski, J.L. & Bishop, D.F. (1992a) Assignment of human erythroid delta-aminolevulinate synthase (ALAS2) to a distal subregion of band Xp11.21 by PCR analysis of somatic cell hybrids containing X; autosome translocations. Genomics, 13, 211-212.
    • (1992) Genomics , vol.13 , pp. 211-212
    • Cotter, P.D.1    Willard, H.F.2    Gorski, J.L.3    Bishop, D.F.4
  • 11
    • 0026603687 scopus 로고
    • Enzymatic defect in "X-linked" sideroblastic anemia: Molecular evidence for erythroid delta-aminolevulinate synthase deficiency
    • Cotter, P.D., Baumann, M. & Bishop, D.F. (1992b) Enzymatic defect in "X-linked" sideroblastic anemia: molecular evidence for erythroid delta-aminolevulinate synthase deficiency. Proc. Natl. Acad. Sci. USA, 89, 4028-4032.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4028-4032
    • Cotter, P.D.1    Baumann, M.2    Bishop, D.F.3
  • 12
    • 0028899437 scopus 로고
    • Assignment of the human housekeeping delta-aminolevulinate synthase gene (ALAS1) to chromosome band 3p21.1 by PCR analysis of somatic cell hybrids
    • Cotter, P.D., Drabkin, H.A., Varkony, T., Smith, D.I. & Bishop, D.F. (1995) Assignment of the human housekeeping delta-aminolevulinate synthase gene (ALAS1) to chromosome band 3p21.1 by PCR analysis of somatic cell hybrids. Cytogenet. Cell Genet., 69, 207-208.
    • (1995) Cytogenet. Cell Genet , vol.69 , pp. 207-208
    • Cotter, P.D.1    Drabkin, H.A.2    Varkony, T.3    Smith, D.I.4    Bishop, D.F.5
  • 13
    • 0025811624 scopus 로고
    • Human erythroid 5-aminolevulinate synthase: Promoter analysis and identification of an iron-responsive element in the mRNA
    • Cox, T.C., Bawden, M.J., Martin, A. & May, B.K. (1991) Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA. EMBO J., 10, 1891-1902.
    • (1991) EMBO J , vol.10 , pp. 1891-1902
    • Cox, T.C.1    Bawden, M.J.2    Martin, A.3    May, B.K.4
  • 14
    • 0027976808 scopus 로고
    • X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase
    • Cox, T.C., Bottomley, S.S., Wiley, J.S., Bawden, M.J., Matthews, C.S. & May, B.K. (1994) X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase. N. Engl. J. Med., 330, 675-679.
    • (1994) N. Engl. J. Med , vol.330 , pp. 675-679
    • Cox, T.C.1    Bottomley, S.S.2    Wiley, J.S.3    Bawden, M.J.4    Matthews, C.S.5    May, B.K.6
  • 15
    • 0025822118 scopus 로고
    • Identification of a novel iron-responsive element in murine and human erythroid delta-aminolevulinic acid synthase mRNA
    • Dandekar, T., Stripecke, R., Gray, N.K., Goossen, B., Constable, A., Johansson, H.E. & Hentze, M.W. (1991) Identification of a novel iron-responsive element in murine and human erythroid delta-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
  • 17
    • 33751071823 scopus 로고    scopus 로고
    • Down-regulation of heme oxygenase-2 is associated with the increased expression of heme oxygenase-1 in human cell lines
    • Ding, Y., Zhang, Y.Z., Furuyama, K., Ogawa, K., Igarashi, K. & Shibahara, S. (2006) Down-regulation of heme oxygenase-2 is associated with the increased expression of heme oxygenase-1 in human cell lines. FEBS J., 273, 5333-5346.
    • (2006) FEBS J , vol.273 , pp. 5333-5346
    • Ding, Y.1    Zhang, Y.Z.2    Furuyama, K.3    Ogawa, K.4    Igarashi, K.5    Shibahara, S.6
  • 18
    • 0032990538 scopus 로고    scopus 로고
    • Phylogenetic analysis of the 5-aminolevulinate synthase gene
    • Duncan, R., Faggart, M.A., Roger, A.J. & Cornell, N.W. (1999) Phylogenetic analysis of the 5-aminolevulinate synthase gene. Mol. Biol. Evol., 16, 383-396.
    • (1999) Mol. Biol. Evol , vol.16 , pp. 383-396
    • Duncan, R.1    Faggart, M.A.2    Roger, A.J.3    Cornell, N.W.4
  • 19
    • 0032410688 scopus 로고    scopus 로고
    • Iron regulatory proteins, iron responsive elements and iron homeostasis
    • Eisenstein, R.S. & Blemings, K.P. (1998) Iron regulatory proteins, iron responsive elements and iron homeostasis. J. Nutr., 128, 2295-2298.
    • (1998) J. Nutr , vol.128 , pp. 2295-2298
    • Eisenstein, R.S.1    Blemings, K.P.2
  • 21
    • 33750838526 scopus 로고    scopus 로고
    • Heme oxygenase-1 as a potential therapeutic target for hepatoprotection
    • Farombi, E.O. & Surh, Y.J. (2006) Heme oxygenase-1 as a potential therapeutic target for hepatoprotection. J. Biochem. Mol. Biol., 39, 479-491.
    • (2006) J. Biochem. Mol. Biol , vol.39 , pp. 479-491
    • Farombi, E.O.1    Surh, Y.J.2
  • 22
    • 0030752517 scopus 로고    scopus 로고
    • Pyridoxine refractory X-linked sideroblastic anemia caused by a point mutation in the erythroid 5-aminolevulinate synthase gene
    • Furuyama, K., Fujita, H., Nagai, T., Yomogida, K., Munakata, H., Kondo, M., Kimura, A., Kuramoto, A., Hayashi, N. & Yamamoto, M. (1997) Pyridoxine refractory X-linked sideroblastic anemia caused by a point mutation in the erythroid 5-aminolevulinate synthase gene. Blood, 90, 822-830.
    • (1997) Blood , vol.90 , pp. 822-830
    • Furuyama, K.1    Fujita, H.2    Nagai, T.3    Yomogida, K.4    Munakata, H.5    Kondo, M.6    Kimura, A.7    Kuramoto, A.8    Hayashi, N.9    Yamamoto, M.10
  • 24
    • 0034068564 scopus 로고    scopus 로고
    • Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia
    • Furuyama, K. & Sassa, S. (2000) Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia. J. Clin. Invest., 105, 757-764.
    • (2000) J. Clin. Invest , vol.105 , pp. 757-764
    • Furuyama, K.1    Sassa, S.2
  • 25
    • 0036483546 scopus 로고    scopus 로고
    • Multiple mechanisms for hereditary sideroblastic anemia
    • Furuyama, K. & Sassa, S. (2002) Multiple mechanisms for hereditary sideroblastic anemia. Cell. Mol. Biol., 48, 5-10.
    • (2002) Cell. Mol. Biol , vol.48 , pp. 5-10
    • Furuyama, K.1    Sassa, S.2
  • 27
    • 33644876018 scopus 로고    scopus 로고
    • Arg452 substitution of the erythroid-specific 5-aminolaevulinate synthase, a hot spot mutation in X-linked sideroblastic anaemia, does not itself affect enzyme activity
    • Furuyama, K., Harigae, H., Heller, T., Hamel, B.C., Minder, E.I., Shimizu, T., Kuribara, T., Blijlevens, N., Shibahara, S. & Sassa, S. (2006) Arg452 substitution of the erythroid-specific 5-aminolaevulinate synthase, a hot spot mutation in X-linked sideroblastic anaemia, does not itself affect enzyme activity. Eur J. Haematol., 76, 33-41.
    • (2006) Eur J. Haematol , vol.76 , pp. 33-41
    • Furuyama, K.1    Harigae, H.2    Heller, T.3    Hamel, B.C.4    Minder, E.I.5    Shimizu, T.6    Kuribara, T.7    Blijlevens, N.8    Shibahara, S.9    Sassa, S.10
  • 28
    • 0028059555 scopus 로고
    • Iron regulatory protein prevents binding of the 43S translation pre-initiation complex to ferritin and eALAS mRNAs
    • Gray, N.K. & Hentze, M.W. (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
  • 29
    • 0025307009 scopus 로고
    • Mechanisms of cytochrome P-450 catalysis
    • Guengerich, F.P. & MacDonald, T.L. (1990) Mechanisms of cytochrome P-450 catalysis. FASEB J., 4, 2453-2459.
    • (1990) FASEB J , vol.4 , pp. 2453-2459
    • Guengerich, F.P.1    MacDonald, T.L.2
  • 31
    • 0026045762 scopus 로고
    • Heme regulates hepatic 5-aminolevulinate synthase mRNA expression by decreasing mRNA half-life and not by altering its rate of transcription
    • Hamilton, J.W., Bement, W.J., Sinclair, P.R., Sinclair, J.F., Alcedo, J.A. & Wetterhahn, K.E. (1991) Heme regulates hepatic 5-aminolevulinate synthase mRNA expression by decreasing mRNA half-life and not by altering its rate of transcription. Arch. Biochem. Biophys., 289, 387-392.
    • (1991) Arch. Biochem. Biophys , vol.289 , pp. 387-392
    • Hamilton, J.W.1    Bement, W.J.2    Sinclair, P.R.3    Sinclair, J.F.4    Alcedo, J.A.5    Wetterhahn, K.E.6
  • 33
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding, H.P., Zhang, Y. & Ron, D. (1999) Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature, 397, 271-274.
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 35
    • 0032827236 scopus 로고    scopus 로고
    • A novel mutation of the erythroid-specific delta-Aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia
    • Harigae, H., Furuyama, K., Kudo, K., Hayashi, N., Yamamoto, M., Sassa, S. & Sasaki, T. (1999b) A novel mutation of the erythroid-specific delta-Aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia. Am. J. Hematol., 62, 112-114.
    • (1999) Am. J. Hematol , vol.62 , pp. 112-114
    • Harigae, H.1    Furuyama, K.2    Kudo, K.3    Hayashi, N.4    Yamamoto, M.5    Sassa, S.6    Sasaki, T.7
  • 36
    • 0037307754 scopus 로고    scopus 로고
    • Aberrant iron accumulation and oxidized status of erythroid-specific delta-aminolevulinate synthase (ALAS2)-deficient definitive erythroblasts
    • Harigae, H., Nakajima, O., Suwabe, N., Yokoyama, H., Furuyama, K., Sasaki, T., Kaku, M., Yamamoto, M. & Sassa, S. (2003) Aberrant iron accumulation and oxidized status of erythroid-specific delta-aminolevulinate synthase (ALAS2)-deficient definitive erythroblasts. Blood, 101, 1188-1193.
    • (2003) Blood , vol.101 , pp. 1188-1193
    • Harigae, H.1    Nakajima, O.2    Suwabe, N.3    Yokoyama, H.4    Furuyama, K.5    Sasaki, T.6    Kaku, M.7    Yamamoto, M.8    Sassa, S.9
  • 37
    • 0019126485 scopus 로고
    • Immunochemical studies of the turnover of delta-aminolevulinate synthase in rat liver mitochondria and the effect of hemin on it
    • Hayashi, N., Terasawa, M. & Kikuchi, G. (1980) Immunochemical studies of the turnover of delta-aminolevulinate synthase in rat liver mitochondria and the effect of hemin on it. J. Biochem., 88, 921-926.
    • (1980) J. Biochem , vol.88 , pp. 921-926
    • Hayashi, N.1    Terasawa, M.2    Kikuchi, G.3
  • 38
    • 0030249636 scopus 로고    scopus 로고
    • Iron regulatory proteins 1 and 2
    • Henderson, B.R. (1996) Iron regulatory proteins 1 and 2. Bioessays, 18, 739-746.
    • (1996) Bioessays , vol.18 , pp. 739-746
    • Henderson, B.R.1
  • 39
    • 33644643191 scopus 로고    scopus 로고
    • The heme-Bach1 pathway in the regulation of oxidative stress response and erythroid differentiation
    • Igarashi, K. & Sun, J. (2006) The heme-Bach1 pathway in the regulation of oxidative stress response and erythroid differentiation. Antioxid. Redox Signal., 8, 107-118.
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 107-118
    • Igarashi, K.1    Sun, J.2
  • 40
    • 34948848050 scopus 로고
    • Orientation of the haem group in myoglobin and its relation to the polypeptide chain detection
    • Ingram, D. & Kendrew, J. (1956) Orientation of the haem group in myoglobin and its relation to the polypeptide chain detection. Nature, 178, 905-906.
    • (1956) Nature , vol.178 , pp. 905-906
    • Ingram, D.1    Kendrew, J.2
  • 41
    • 22544452148 scopus 로고    scopus 로고
    • Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2
    • Ishikawa, H., Kato, M., Hori, H., Ishimori, K., Kirisako, T., Tokunaga, F. & Iwai, K. (2005) Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2. Mol. Cell, 19, 171-181.
    • (2005) Mol. Cell , vol.19 , pp. 171-181
    • Ishikawa, H.1    Kato, M.2    Hori, H.3    Ishimori, K.4    Kirisako, T.5    Tokunaga, F.6    Iwai, K.7
  • 43
    • 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. (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
  • 47
    • 0017147523 scopus 로고
    • Specificity of the protein kinase activity associated with the hemincontrolled repressor of rabbit reticulocyte
    • Kramer, G., Cimadevilla, J.M. & Hardesty, B. (1976) Specificity of the protein kinase activity associated with the hemincontrolled repressor of rabbit reticulocyte. Proc. Natl. Acad. Sci. USA, 73, 3078-3082.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3078-3082
    • Kramer, G.1    Cimadevilla, J.M.2    Hardesty, B.3
  • 49
    • 0028293023 scopus 로고
    • Chromosomal localization of the human heme oxygenase genes: Heme oxygenase-1 (FIMOX1) maps to chromosome 22q12 and heme oxygenase-2 (HMOX2) maps to chromosome 16p13.3
    • Kutty, R.K., Kutty, G., Rodriguez, I.R., Chader, G.J. & Wiggert, B. (1994) Chromosomal localization of the human heme oxygenase genes: heme oxygenase-1 (FIMOX1) maps to chromosome 22q12 and heme oxygenase-2 (HMOX2) maps to chromosome 16p13.3. Genomics, 20, 513-516.
    • (1994) Genomics , vol.20 , pp. 513-516
    • Kutty, R.K.1    Kutty, G.2    Rodriguez, I.R.3    Chader, G.J.4    Wiggert, B.5
  • 50
  • 51
    • 0027405813 scopus 로고
    • Regulation by heme of mitochondrial protein transport through a conserved amino acid motif
    • Lathrop, J.T. & Timko, M.P. (1993) Regulation by heme of mitochondrial protein transport through a conserved amino acid motif. Science, 259, 522-525.
    • (1993) Science , vol.259 , pp. 522-525
    • Lathrop, J.T.1    Timko, M.P.2
  • 53
    • 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. (2002) Role of the ferroportin iron-responsive element in iron and nitric oxide dependent gene regulation. Blood Cells Mol. Dis., 29, 315-326.
    • (2002) Blood Cells Mol. Dis , vol.29 , pp. 315-326
    • Liu, X.B.1    Hill, P.2    Haile, D.J.3
  • 54
    • 0029799191 scopus 로고    scopus 로고
    • Carbon monoxide and nitric oxide homology: Differential modulation of heme oxygenases in brain and detection of protein and activity
    • Maines, M.D. (1996) Carbon monoxide and nitric oxide homology: differential modulation of heme oxygenases in brain and detection of protein and activity. Methods Enzymol., 268, 473-488.
    • (1996) Methods Enzymol , vol.268 , pp. 473-488
    • Maines, M.D.1
  • 55
    • 0031906394 scopus 로고    scopus 로고
    • The molecular biology and pyridoxine responsiveness of X-linked sideroblastic anaemia
    • May, A. & Bishop, D.F. (1998) The molecular biology and pyridoxine responsiveness of X-linked sideroblastic anaemia. Haematologica, 83, 56-70.
    • (1998) Haematologica , vol.83 , pp. 56-70
    • May, A.1    Bishop, D.F.2
  • 56
    • 0026653813 scopus 로고
    • Human heme oxygenase-2: Characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal
    • McCoubrey, W.K., Jr., Ewing, J.F. & Maines, M.D. (1992) Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal. Arch. Biochem. Biophys., 295, 13-20.
    • (1992) Arch. Biochem. Biophys , vol.295 , pp. 13-20
    • McCoubrey Jr., W.K.1    Ewing, J.F.2    Maines, M.D.3
  • 57
    • 1842330947 scopus 로고    scopus 로고
    • Heme oxygenase-2 is a hemoprotein and binds heme through heme regulatory motifs that are not involved in heme catalysis
    • McCoubrey, W.K., Jr., Huang, T.J. & Maines, M.D. (1997) Heme oxygenase-2 is a hemoprotein and binds heme through heme regulatory motifs that are not involved in heme catalysis. J. Biol. Chem., 272, 12568-12574.
    • (1997) J. Biol. Chem , vol.272 , pp. 12568-12574
    • McCoubrey Jr., W.K.1    Huang, T.J.2    Maines, M.D.3
  • 59
    • 0027254988 scopus 로고
    • Purification and structure of rat erythroid- specific delta-aminolevulinate synthase
    • Munakata, H., Yamagami, T., Nagai, T., Yamamoto, M. & Hayashi, N. (1993) Purification and structure of rat erythroid- specific delta-aminolevulinate synthase. J. Biochem., 114, 103-111.
    • (1993) J. Biochem , vol.114 , pp. 103-111
    • Munakata, H.1    Yamagami, T.2    Nagai, T.3    Yamamoto, M.4    Hayashi, N.5
  • 60
    • 4644371570 scopus 로고    scopus 로고
    • Role of the heme regulatory motif in the heme-mediated inhibition of mitochondrial import of 5-aminolevulinate synthase
    • Munakata, H., Sun, J.Y., Yoshida, K., Nakatani, T., Honda, E., Hayakawa, S., Furuyama, K. & Hayashi, N. (2004) Role of the heme regulatory motif in the heme-mediated inhibition of mitochondrial import of 5-aminolevulinate synthase. J. Biochem., 136, 233-238.
    • (2004) J. Biochem , vol.136 , pp. 233-238
    • Munakata, H.1    Sun, J.Y.2    Yoshida, K.3    Nakatani, T.4    Honda, E.5    Hayakawa, S.6    Furuyama, K.7    Hayashi, N.8
  • 61
    • 0031002833 scopus 로고    scopus 로고
    • 5-Aminolevulinate synthase expression and hemoglobin synthesis in a human myelogenous leukemia cell line
    • Nagai, T., Harigae, H., Furuyama, K., Munakata, H., Hayashi, N., Endo, K., Sassa, S. & Yamamoto, M. (1997) 5-Aminolevulinate synthase expression and hemoglobin synthesis in a human myelogenous leukemia cell line. J. Biochem., 121, 487-495.
    • (1997) J. Biochem , vol.121 , pp. 487-495
    • Nagai, T.1    Harigae, H.2    Furuyama, K.3    Munakata, H.4    Hayashi, N.5    Endo, K.6    Sassa, S.7    Yamamoto, M.8
  • 62
    • 0033571237 scopus 로고    scopus 로고
    • Heme deficiency in erythroid lineage causes differentiation arrest and cytoplasmic iron overload
    • Nakajima, O., Takahashi, S., Harigae, H., Furuyama, K., Hayashi, N., Sassa, S. & Yamamoto, M. (1999) Heme deficiency in erythroid lineage causes differentiation arrest and cytoplasmic iron overload. EMBO J., 18, 6282-6289.
    • (1999) EMBO J , vol.18 , pp. 6282-6289
    • Nakajima, O.1    Takahashi, S.2    Harigae, H.3    Furuyama, K.4    Hayashi, N.5    Sassa, S.6    Yamamoto, M.7
  • 65
    • 23944509741 scopus 로고    scopus 로고
    • Preventive strategies for aspiration pneumonia in elderly disabled persons
    • Ohrui, T. (2005) Preventive strategies for aspiration pneumonia in elderly disabled persons. Tohoku J. Exp. Med., 207, 3-12.
    • (2005) Tohoku J. Exp. Med , vol.207 , pp. 3-12
    • Ohrui, T.1
  • 67
    • 0031749286 scopus 로고    scopus 로고
    • Differentiation-specific increase in ALA-induced protoporphyrin IX accumulation in primary mouse keratinocytes
    • Ortel, B., Chen, N., Brissette, J., Dotto, G.P., Maytin, E. & Hasan, T. (1998) Differentiation-specific increase in ALA-induced protoporphyrin IX accumulation in primary mouse keratinocytes. Br. J. Cancer, 77, 1744-1751.
    • (1998) Br. J. Cancer , vol.77 , pp. 1744-1751
    • Ortel, B.1    Chen, N.2    Brissette, J.3    Dotto, G.P.4    Maytin, E.5    Hasan, T.6
  • 68
    • 0029805130 scopus 로고    scopus 로고
    • Bach proteins belong to a novel family of BTB-basic leucine zipper transcription factors that interact with MafK and regulate transcription through the NF-E2 site
    • Oyake, T., Itoh, K., Motohashi, H., Hayashi, N., Hoshino, H., Nishizawa, M., Yamamoto, M. & Igarashi, K. (1996) Bach proteins belong to a novel family of BTB-basic leucine zipper transcription factors that interact with MafK and regulate transcription through the NF-E2 site. Mol. Cell. Biol., 16, 6083-6095.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 6083-6095
    • Oyake, T.1    Itoh, K.2    Motohashi, H.3    Hayashi, N.4    Hoshino, H.5    Nishizawa, M.6    Yamamoto, M.7    Igarashi, K.8
  • 70
    • 0030600134 scopus 로고    scopus 로고
    • Iron-sulphur clusters as genetic regulatory switches: The bifunctional iron regulatory protein-1
    • Paraskeva, E. & Hentze, M.W. (1996) Iron-sulphur clusters as genetic regulatory switches: the bifunctional iron regulatory protein-1. FEBS Lett., 389, 40-43.
    • (1996) FEBS Lett , vol.389 , pp. 40-43
    • Paraskeva, E.1    Hentze, M.W.2
  • 71
    • 0009765487 scopus 로고
    • X-ray analysis of haemoglobin
    • Perutz, M. (1942) X-ray analysis of haemoglobin. Nature, 149, 491-494.
    • (1942) Nature , vol.149 , pp. 491-494
    • Perutz, M.1
  • 72
    • 0028880959 scopus 로고
    • Hippocampal long-term potentiation is normal in heme oxygenase-2 mutant mice
    • Poss, K.D., Thomas, M.J., Ebralidze, A.K., O'Dell, T.J. & Tonegawa, S. (1995) Hippocampal long-term potentiation is normal in heme oxygenase-2 mutant mice. Neuron, 15, 867-873.
    • (1995) Neuron , vol.15 , pp. 867-873
    • Poss, K.D.1    Thomas, M.J.2    Ebralidze, A.K.3    O'Dell, T.J.4    Tonegawa, S.5
  • 73
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • Poss, K.D. & Tonegawa, S. (1997) Heme oxygenase 1 is required for mammalian iron reutilization. Proc. Natl. Acad. Sci. USA., 94, 10919-10924.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 75
    • 0038728800 scopus 로고    scopus 로고
    • Autophosphorylation of threonine'485 in the activation loop is essential for attaining eIF2alpha kinase activity of HRI
    • Rafie-Kolpin, M., Han, A.P. & Chen, J.J. (2003) Autophosphorylation of threonine'485 in the activation loop is essential for attaining eIF2alpha kinase activity of HRI. Biochemistry, 42, 6536-6544.
    • (2003) Biochemistry , vol.42 , pp. 6536-6544
    • Rafie-Kolpin, M.1    Han, A.P.2    Chen, J.J.3
  • 76
    • 0344010398 scopus 로고
    • Regulation of protein synthesis in rabbit reticulocyte lysates: Purification and initial characterization of the cyclic 3′:5′-AMP independent protein kinase of the heme-regulated translational inhibitor
    • Ranu, R.S. & London, I.M. (1976) Regulation of protein synthesis in rabbit reticulocyte lysates: purification and initial characterization of the cyclic 3′:5′-AMP independent protein kinase of the heme-regulated translational inhibitor. Proc. Natl. Acad. Sci. USA, 73, 4349-4353.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 4349-4353
    • Ranu, R.S.1    London, I.M.2
  • 77
    • 2042452756 scopus 로고
    • Expression of delta-aminolevulinate synthase in avian cells: Separate genes encode erythroid-specific and nonspecific isozymes
    • Riddle, R.D., Yamamoto, M. & Engel, J.D. (1989) Expression of delta-aminolevulinate synthase in avian cells: separate genes encode erythroid-specific and nonspecific isozymes. Proc. Natl. Acad. Sci. USA, 86, 792-796.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 792-796
    • Riddle, R.D.1    Yamamoto, M.2    Engel, J.D.3
  • 78
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • Rouault, T.A. (2006) The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat. Chem. Biol., 2, 406-414.
    • (2006) Nat. Chem. Biol , vol.2 , pp. 406-414
    • Rouault, T.A.1
  • 79
    • 0040350202 scopus 로고
    • Mechanism of interferon action: Phosphorylation of protein synthesis initiation factor eIF-2 in interferon-treated human cells by a ribosome-associated kinase processing site specificity similar to hemin-regulated rabbit reticulocyte kinase
    • Samuel, C.E. (1979) Mechanism of interferon action: phosphorylation of protein synthesis initiation factor eIF-2 in interferon-treated human cells by a ribosome-associated kinase processing site specificity similar to hemin-regulated rabbit reticulocyte kinase. Proc. Natl. Acad. Sci. USA, 76, 600-604.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 600-604
    • Samuel, C.E.1
  • 80
    • 0014856880 scopus 로고
    • Induction of delta-aminolevuclinic acid synthetase in chick embryo liver cells in culture
    • Sassa, S. & Granick, S. (1970) Induction of delta-aminolevuclinic acid synthetase in chick embryo liver cells in culture. Proc. Natl. Acad. Sci. USA, 67, 517-522.
    • (1970) Proc. Natl. Acad. Sci. USA , vol.67 , pp. 517-522
    • Sassa, S.1    Granick, S.2
  • 81
    • 33644537718 scopus 로고    scopus 로고
    • Kidney dysfunction and hypertension: Role for cadmium, p450 and heme oxygenases?
    • Satarug, S., Nishijo, M., Lasker, J.M., Edwards, R.J. & Moore, M.R. (2006) Kidney dysfunction and hypertension: role for cadmium, p450 and heme oxygenases? Tohoku J. Exp. Med., 208, 179-202.
    • (2006) Tohoku J. Exp. Med , vol.208 , pp. 179-202
    • Satarug, S.1    Nishijo, M.2    Lasker, J.M.3    Edwards, R.J.4    Moore, M.R.5
  • 82
    • 0018637428 scopus 로고
    • Mechanism of increase of heme oxygenase activity induced by hemin in cultured pig alveolar macrophages
    • Shibahara, S., Yoshida, T. & Kikuchi, G. (1979) Mechanism of increase of heme oxygenase activity induced by hemin in cultured pig alveolar macrophages. Arch. Biochem. Biophys., 197, 607-617.
    • (1979) Arch. Biochem. Biophys , vol.197 , pp. 607-617
    • Shibahara, S.1    Yoshida, T.2    Kikuchi, G.3
  • 84
    • 0023665016 scopus 로고
    • Transcriptional control of rat heme oxygenase by heat shock
    • Shibahara, S., Muller, R.M. & Taguchi, H. (1987) Transcriptional control of rat heme oxygenase by heat shock. J. Biol. Chem., 262, 12889-12892.
    • (1987) J. Biol. Chem , vol.262 , pp. 12889-12892
    • Shibahara, S.1    Muller, R.M.2    Taguchi, H.3
  • 85
    • 0024100201 scopus 로고
    • Regulation of heme oxygenase gene expression
    • Shibahara, S. (1988) Regulation of heme oxygenase gene expression. Sem. Hematol., 25, 370-376.
    • (1988) Sem. Hematol , vol.25 , pp. 370-376
    • Shibahara, S.1
  • 86
    • 0027532668 scopus 로고
    • Functional analysis of cDNAs for two types of human heme oxygenase and evidence for their separate regulation
    • Shibahara, S., Yoshizawa, M., Suzuki, H., Takeda, K., Meguro, K. & Endo, K. (1993) Functional analysis of cDNAs for two types of human heme oxygenase and evidence for their separate regulation. J. Biochem., 113, 214-218.
    • (1993) J. Biochem , vol.113 , pp. 214-218
    • Shibahara, S.1    Yoshizawa, M.2    Suzuki, H.3    Takeda, K.4    Meguro, K.5    Endo, K.6
  • 87
    • 0036671624 scopus 로고    scopus 로고
    • Heme degradation and human disease: Diversity is the soul of life
    • Shibahara, S., Kitamuro, T. & Takahashi, K. (2002) Heme degradation and human disease: diversity is the soul of life. Antioxid. Redox Signal., 4, 593-602.
    • (2002) Antioxid. Redox Signal , vol.4 , pp. 593-602
    • Shibahara, S.1    Kitamuro, T.2    Takahashi, K.3
  • 88
    • 0242525192 scopus 로고    scopus 로고
    • The heme oxygenase dilemma in cellular homeostasis: New insights for the feedback regulation of heme catabolism
    • Shibahara, S. (2003) The heme oxygenase dilemma in cellular homeostasis: new insights for the feedback regulation of heme catabolism. Tohoku J. Exp. Med., 200, 167-186.
    • (2003) Tohoku J. Exp. Med , vol.200 , pp. 167-186
    • Shibahara, S.1
  • 89
    • 0025368527 scopus 로고
    • Induction of haem oxygenase as a defence against oxidative stress
    • Stocker, R. (1990) Induction of haem oxygenase as a defence against oxidative stress. Free. Radic. Res. Commun., 9, 101-112.
    • (1990) Free. Radic. Res. Commun , vol.9 , pp. 101-112
    • Stocker, R.1
  • 92
    • 4744356825 scopus 로고    scopus 로고
    • Heme-dependent up-regulation of the alpha-globin gene expression by transcriptional repressor Bach1 in erythroid cells
    • Tahara, T., Sun, J., Igarashi, K. & Taketani, S. (2004a) Heme-dependent up-regulation of the alpha-globin gene expression by transcriptional repressor Bach1 in erythroid cells. Biochem. Biophys. Res. Commun., 324, 77-85.
    • (2004) Biochem. Biophys. Res. Commun , vol.324 , pp. 77-85
    • Tahara, T.1    Sun, J.2    Igarashi, K.3    Taketani, S.4
  • 93
    • 1242317026 scopus 로고    scopus 로고
    • Heme positively regulates the expression of beta-globin at the locus control region via the transcriptional factor Bach1 in erythroid cells
    • Tahara, T., Sun, J., Nakanishi, K., Yamamoto, M., Mori, H., Saito, T., Fujita, H., Igarashi, K. & Taketani, S. (2004b) Heme positively regulates the expression of beta-globin at the locus control region via the transcriptional factor Bach1 in erythroid cells. J. Biol. Chem., 279, 5480-5487.
    • (2004) J. Biol. Chem , vol.279 , pp. 5480-5487
    • Tahara, T.1    Sun, J.2    Nakanishi, K.3    Yamamoto, M.4    Mori, H.5    Saito, T.6    Fujita, H.7    Igarashi, K.8    Taketani, S.9
  • 94
    • 0030056221 scopus 로고    scopus 로고
    • Expression of heme oxygenase isozyme mRNA in the human brain and induction of heme oxgenase-1 by nitric oxide donors
    • Takahashi, K., Hara, E., Suzuki, H. & Shibahara, S. (1996) Expression of heme oxygenase isozyme mRNA in the human brain and induction of heme oxgenase-1 by nitric oxide donors. J. Neurochem., 67, 482-489.
    • (1996) J. Neurochem , vol.67 , pp. 482-489
    • Takahashi, K.1    Hara, E.2    Suzuki, H.3    Shibahara, S.4
  • 95
    • 0033006381 scopus 로고    scopus 로고
    • Suppression of heme oxygenase-1 mRNA expression by interferon-γ in human glioblastoma cells
    • Takahashi, K., Nakayama, M., Takeda, K., Fujita, H. & Shibahara, S. (1999) Suppression of heme oxygenase-1 mRNA expression by interferon-γ in human glioblastoma cells. J. Neurochem., 72, 2356-2361.
    • (1999) J. Neurochem , vol.72 , pp. 2356-2361
    • Takahashi, K.1    Nakayama, M.2    Takeda, K.3    Fujita, H.4    Shibahara, S.5
  • 96
    • 2942555358 scopus 로고    scopus 로고
    • Heme oxygenase-1: A novel therapeutic target in oxidative tissue injuries
    • Takahashi, T., Morita, K. Akagi, R. & Sassa, S. (2004) Heme oxygenase-1: a novel therapeutic target in oxidative tissue injuries. Curr. Med. Chem., 11, 1545-1561.
    • (2004) Curr. Med. Chem , vol.11 , pp. 1545-1561
    • Takahashi, T.1    Morita, K.2    Akagi, R.3    Sassa, S.4
  • 97
    • 0028133168 scopus 로고
    • Identification of a cis-acting element that is responsible for cadmium-mediated induction of the human heme oxygenase
    • Takeda, K., Ishizawa, S., Sato, M., Yoshida, T. & Shibahara, S. (1994) Identification of a cis-acting element that is responsible for cadmium-mediated induction of the human heme oxygenase. J. Biol. Chem., 269, 22858-22867.
    • (1994) J. Biol. Chem , vol.269 , pp. 22858-22867
    • Takeda, K.1    Ishizawa, S.2    Sato, M.3    Yoshida, T.4    Shibahara, S.5
  • 98
    • 27744595458 scopus 로고    scopus 로고
    • Microsatellite polymorphism in the heme oxygenase-1 gene promoter is associated with susceptibility to cerebral malaria in Myanmar
    • Takeda, M., Kikuchi, M., Ubalee, R., Na-Bangchang, K., Ruangweerayut, R., Shibahara, S., Imai, S. & Hirayama, K. (2005) Microsatellite polymorphism in the heme oxygenase-1 gene promoter is associated with susceptibility to cerebral malaria in Myanmar. Jpn. J. Infect. Dis., 58, 268-271.
    • (2005) Jpn. J. Infect. Dis , vol.58 , pp. 268-271
    • Takeda, M.1    Kikuchi, M.2    Ubalee, R.3    Na-Bangchang, K.4    Ruangweerayut, R.5    Shibahara, S.6    Imai, S.7    Hirayama, K.8
  • 99
    • 23944443759 scopus 로고    scopus 로고
    • Prevalence of chronic obstructive pulmonary disease in Japanese people on medical check-up
    • Takemura, H., Hida, W., Sasaki, T., Sugawara, T. & Sen, T. (2005) Prevalence of chronic obstructive pulmonary disease in Japanese people on medical check-up. Tohoku J. Exp. Med., 207, 41-50.
    • (2005) Tohoku J. Exp. Med , vol.207 , pp. 41-50
    • Takemura, H.1    Hida, W.2    Sasaki, T.3    Sugawara, T.4    Sen, T.5
  • 100
    • 17844393421 scopus 로고    scopus 로고
    • Aquisition, mobilization and utilization of cellular iron and heme: Endless findings and growing evidence of fight regulation
    • Taketani, S. (2005) Aquisition, mobilization and utilization of cellular iron and heme: endless findings and growing evidence of fight regulation. Tohoku J. Exp. Med., 205, 297-318.
    • (2005) Tohoku J. Exp. Med , vol.205 , pp. 297-318
    • Taketani, S.1
  • 101
    • 0141963861 scopus 로고    scopus 로고
    • Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels
    • Tang, X.D., Xu, R., Reynolds, M.F., Garcia, M.L., Heinemann, S.H. & Hoshi, T. (2003) Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels. Nature, 425, 531-535.
    • (2003) Nature , vol.425 , pp. 531-535
    • Tang, X.D.1    Xu, R.2    Reynolds, M.F.3    Garcia, M.L.4    Heinemann, S.H.5    Hoshi, T.6
  • 102
    • 0028114730 scopus 로고
    • Iron regulatory elementsi IREs): A family of mRNA non-coding sequences
    • Theil, E.C. (1994) Iron regulatory elementsi IREs): a family of mRNA non-coding sequences. Biochem. J., 304 (Pt 1), 1-11.
    • (1994) Biochem. J , vol.304 , Issue.PART 1 , pp. 1-11
    • Theil, E.C.1
  • 103
    • 3242767645 scopus 로고    scopus 로고
    • Expression of heme oxygenase-1 is repressed by interferon-γ and induced by hypoxia in human retinal pigment epithelial cells
    • Udono-Fujimori, R., Takahashi, K., Takeda, K., Furuyama, K., Kaneko, K., Takahashi, S., Tamai, M. & Shibahara, S. (2004) Expression of heme oxygenase-1 is repressed by interferon-γ and induced by hypoxia in human retinal pigment epithelial cells. Eur. J. Biochem., 271, 3076-3084.
    • (2004) Eur. J. Biochem , vol.271 , pp. 3076-3084
    • Udono-Fujimori, R.1    Takahashi, K.2    Takeda, K.3    Furuyama, K.4    Kaneko, K.5    Takahashi, S.6    Tamai, M.7    Shibahara, S.8
  • 106
    • 0033925281 scopus 로고    scopus 로고
    • Microsatellite polymorphism in the heme oxygenase-1 gene promoter is associated with susceptibility to emphysema
    • Yamada, N., Yamaya, M., Okinaga, S., Nakayama, K., Sekizawa, K., Shibahara, S. & Sasaki, H. (2000) Microsatellite polymorphism in the heme oxygenase-1 gene promoter is associated with susceptibility to emphysema. Am. J. Hum. Genet., 66, 187-195.
    • (2000) Am. J. Hum. Genet , vol.66 , pp. 187-195
    • Yamada, N.1    Yamaya, M.2    Okinaga, S.3    Nakayama, K.4    Sekizawa, K.5    Shibahara, S.6    Sasaki, H.7
  • 107
    • 0020482065 scopus 로고
    • Evidence for the transcriptional inhibition by heme of the synthesis of delta-aminolevulinate synthase in rat liver
    • Yamamoto, M., Hayashi, N. & Kikuchi, G. (1982) Evidence for the transcriptional inhibition by heme of the synthesis of delta-aminolevulinate synthase in rat liver. Biochem. Biophys. Res. Commun., 105, 985-990.
    • (1982) Biochem. Biophys. Res. Commun , vol.105 , pp. 985-990
    • Yamamoto, M.1    Hayashi, N.2    Kikuchi, G.3
  • 108
    • 0020601625 scopus 로고
    • Translational inhibition by heme of the synthesis of hepatic delta-aminolevulinate synthase in a cell-free system
    • Yamamoto, M., Hayashi, N. & Kikuchi, G. (1983) Translational inhibition by heme of the synthesis of hepatic delta-aminolevulinate synthase in a cell-free system. Biochem. Biophys. Res. Commun., 115, 225-231.
    • (1983) Biochem. Biophys. Res. Commun , vol.115 , pp. 225-231
    • Yamamoto, M.1    Hayashi, N.2    Kikuchi, G.3
  • 110
    • 0018826065 scopus 로고
    • Translocation of delta-aminolevulinate synthase from the cytosol to the mitochondria and its regulation by hemin in the rat liver
    • Yamauchi, K., Hayashi, N. & Kikuchi, G. (1980) Translocation of delta-aminolevulinate synthase from the cytosol to the mitochondria and its regulation by hemin in the rat liver. J. Biol. Chem., 255, 1746-1751.
    • (1980) J. Biol. Chem , vol.255 , pp. 1746-1751
    • Yamauchi, K.1    Hayashi, N.2    Kikuchi, G.3
  • 111
    • 33646808650 scopus 로고    scopus 로고
    • Airway remodeling in asthma and its influence on clinical pathophysiology
    • Yamauchi, K. (2006) Airway remodeling in asthma and its influence on clinical pathophysiology. Tohoku J. Exp. Med., 209, 75-87.
    • (2006) Tohoku J. Exp. Med , vol.209 , pp. 75-87
    • Yamauchi, K.1
  • 112
    • 34547121697 scopus 로고    scopus 로고
    • Evidence that the heme regulatory motifs in heme oxygenase-2 serve as a thiol/disulfide redox switch regulating heme binding
    • Yi, L. & Ragsdale, S.W. (2007) Evidence that the heme regulatory motifs in heme oxygenase-2 serve as a thiol/disulfide redox switch regulating heme binding. J. Biol. Chem., 282, 21056-21067.
    • (2007) J. Biol. Chem , vol.282 , pp. 21056-21067
    • Yi, L.1    Ragsdale, S.W.2
  • 113
  • 114
    • 0031556535 scopus 로고    scopus 로고
    • Reactive oxygen species-induced DNA damage and its modification: A chemical investigation
    • Yu, T.W. & Anderson, D. (1997) Reactive oxygen species-induced DNA damage and its modification: a chemical investigation. Mutat. Res., 379, 201-210.
    • (1997) Mutat. Res , vol.379 , pp. 201-210
    • Yu, T.W.1    Anderson, D.2
  • 115
    • 33745594047 scopus 로고    scopus 로고
    • Hypoxia reduces the expression of heme oxygenase-2 in various types of human cell lines. A possible strategy for the maintenance of intracellular heme level
    • Zhang, Y., Furuyama, K., Kaneko, K., Ding, Y., Ogawa, K., Yoshizawa, M., Kawamura, M., Takeda, K., Yoshida, T. & Shibahara, S. (2006) Hypoxia reduces the expression of heme oxygenase-2 in various types of human cell lines. A possible strategy for the maintenance of intracellular heme level. FEBS J., 273, 3136-3147.
    • (2006) FEBS J , vol.273 , pp. 3136-3147
    • Zhang, Y.1    Furuyama, K.2    Kaneko, K.3    Ding, Y.4    Ogawa, K.5    Yoshizawa, M.6    Kawamura, M.7    Takeda, K.8    Yoshida, T.9    Shibahara, S.10
  • 116
    • 0027048349 scopus 로고
    • Binding of cytosolic aconitase to the iron responsive element of porcine mitochondrial aconitase mRNA
    • Zheng, L., Kennedy, M.C., Blondin, G.A., Beinert, H. & Zalkin, H. (1992) Binding of cytosolic aconitase to the iron responsive element of porcine mitochondrial aconitase mRNA. Arch. Biochem. Biophys., 299, 356-360.
    • (1992) Arch. Biochem. Biophys , vol.299 , pp. 356-360
    • Zheng, L.1    Kennedy, M.C.2    Blondin, G.A.3    Beinert, H.4    Zalkin, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.