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Volumn 24, Issue , 2004, Pages 105-131

New insights into erythropoiesis: The roles of folate, vitamin B 12, and iron

Author keywords

Apoptosis; Erythrocytes; Heme; Iron deficiency anemia; Megaloblastic anemia

Indexed keywords

CYANOCOBALAMIN; DNA; FOLIC ACID; GLOBIN; HEME; IRON; PROTEIN; PURINE; THYMIDINE PHOSPHATE;

EID: 3142674792     PISSN: 01999885     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.nutr.24.012003.132306     Document Type: Review
Times cited : (348)

References (124)
  • 1
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • Abboud S, Haile DJ. 2000. A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J. Biol. Chem. 275:19906-12
    • (2000) J. Biol. Chem. , vol.275 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 3
    • 0142222530 scopus 로고    scopus 로고
    • The ceruloplasmin homolog hephaestin and the control of intestinal iron absorption
    • Anderson GJ, Frazer DM, McKie AT, Vulpe CD. 2002. The ceruloplasmin homolog hephaestin and the control of intestinal iron absorption. Blood Cells Mol. Dis. 29:367-75
    • (2002) Blood Cells Mol. Dis. , vol.29 , pp. 367-375
    • Anderson, G.J.1    Frazer, D.M.2    McKie, A.T.3    Vulpe, C.D.4
  • 4
    • 0002415480 scopus 로고    scopus 로고
    • Megaloblastic anemias
    • ed. R Hoffman, EJ Benz, SJ Shattil, B Furie, HJ Cohen, LE Silberstein, P McGlave, New York: Churchill Livingstone
    • Antony AC. 2000. Megaloblastic anemias. In Hematology, Basic Principles and Practice, ed. R Hoffman, EJ Benz, SJ Shattil, B Furie, HJ Cohen, LE Silberstein, P McGlave, pp. 446-85. New York: Churchill Livingstone
    • (2000) Hematology, Basic Principles and Practice , pp. 446-485
    • Antony, A.C.1
  • 5
    • 0026082926 scopus 로고
    • Megaloblastic hematopoiesis in vitro: Interaction of anti-folate receptor antibodies with hematopoietic progenitors leads to a cell proliferative response independent of megaloblastic changes
    • Antony AC, Briddell RA, Brandt JE, Straneva JE, Verma RS, et al. 1991. Megaloblastic hematopoiesis in vitro: Interaction of anti-folate receptor antibodies with hematopoietic progenitors leads to a cell proliferative response independent of megaloblastic changes. J. Clin. Invest. 87:313-25
    • (1991) J. Clin. Invest. , vol.87 , pp. 313-325
    • Antony, A.C.1    Briddell, R.A.2    Brandt, J.E.3    Straneva, J.E.4    Verma, R.S.5
  • 7
    • 0037101879 scopus 로고    scopus 로고
    • Ferritin, iron homeostasis, and oxidative damage
    • Arosio P, Levi S. 2002. Ferritin, iron homeostasis, and oxidative damage. Free Radic. Biol. Med. 33:457-63
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 457-463
    • Arosio, P.1    Levi, S.2
  • 9
    • 0020445220 scopus 로고
    • Selective expansion of mitochondrial nucleoside triphosphate pools in antimetabolite-treated HeLa cells
    • Bestwick RK, Moffett GL, Mathews CK. 1982. Selective expansion of mitochondrial nucleoside triphosphate pools in antimetabolite-treated HeLa cells. J. Biol. Chem. 257:9300-4
    • (1982) J. Biol. Chem. , vol.257 , pp. 9300-9304
    • Bestwick, R.K.1    Moffett, G.L.2    Mathews, C.K.3
  • 12
    • 0030979178 scopus 로고    scopus 로고
    • Folate deficiency causes uracil misincorporation into human DNA and chromosome breakage: Implications for cancer and neuronal damage
    • Blount BC, Mack MM, Wehr CM, MacGregor JT, Hiatt RA, et al. 1997. Folate deficiency causes uracil misincorporation into human DNA and chromosome breakage: implications for cancer and neuronal damage. Proc. Natl. Acad. Sci. USA 94:3290-95
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3290-3295
    • Blount, B.C.1    Mack, M.M.2    Wehr, C.M.3    MacGregor, J.T.4    Hiatt, R.A.5
  • 15
    • 0034531651 scopus 로고    scopus 로고
    • Iron regulatory proteins in pathobiology
    • Cairo G, Pietrangelo A. 2000. Iron regulatory proteins in pathobiology. Biochem. J. 352:241-50
    • (2000) Biochem. J. , vol.352 , pp. 241-250
    • Cairo, G.1    Pietrangelo, A.2
  • 16
    • 0033564656 scopus 로고    scopus 로고
    • Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron
    • Canonne-Hergaux F, Gruenheid S, Ponka P, Gros P. 1999. Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron. Blood 93:4406-17
    • (1999) Blood , vol.93 , pp. 4406-4417
    • Canonne-Hergaux, F.1    Gruenheid, S.2    Ponka, P.3    Gros, P.4
  • 17
    • 0035895096 scopus 로고    scopus 로고
    • Characterization of the iron transporter DMT1 (NRAMP2/DCT1) in red blood cells of normal and anemic mk/mk mice
    • Canonne-Hergaux F, Zhang AS, Ponka P, Gros P. 2001. Characterization of the iron transporter DMT1 (NRAMP2/DCT1) in red blood cells of normal and anemic mk/mk mice. Blood 98:3823-30
    • (2001) Blood , vol.98 , pp. 3823-3830
    • Canonne-Hergaux, F.1    Zhang, A.S.2    Ponka, P.3    Gros, P.4
  • 18
    • 0035480007 scopus 로고    scopus 로고
    • Hematopoietic development: A balancing act
    • Cantor AB, Orkin SH. 2001. Hematopoietic development: a balancing act. Curr. Opin. Genet. Dev. 11:513-19
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 513-519
    • Cantor, A.B.1    Orkin, S.H.2
  • 19
    • 0030771355 scopus 로고    scopus 로고
    • Cobalamin, the stomach, and aging
    • Carmel R. 1997. Cobalamin, the stomach, and aging. Am. J. Clin. Nutr. 66:750-59
    • (1997) Am. J. Clin. Nutr. , vol.66 , pp. 750-759
    • Carmel, R.1
  • 20
    • 0037372442 scopus 로고    scopus 로고
    • Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia
    • Cazzola M, Invernizzi R, Bergamaschi G, Levi S, Corsi B, et al. 2003. Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia. Blood 101:1996-2000
    • (2003) Blood , vol.101 , pp. 1996-2000
    • Cazzola, M.1    Invernizzi, R.2    Bergamaschi, G.3    Levi, S.4    Corsi, B.5
  • 22
    • 0032401601 scopus 로고    scopus 로고
    • Heme-regulated eIF-2alpha kinase purifies as a hemoprotein. Eur
    • Chefalo PJ, Oh J, Rafie-Kolpin M, Kan B, Chen JJ. 1998. Heme-regulated eIF-2alpha kinase purifies as a hemoprotein. Eur. J. Biochem. 258:820-30
    • (1998) J. Biochem. , vol.258 , pp. 820-830
    • Chefalo, P.J.1    Oh, J.2    Rafie-Kolpin, M.3    Kan, B.4    Chen, J.J.5
  • 23
    • 0028935374 scopus 로고
    • Regulation of protein synthesis by heme-regulated eIF-2 alpha kinase
    • Chen JJ, London IM. 1995. Regulation of protein synthesis by heme-regulated eIF-2 alpha kinase. Trends Biochem. Sci. 20:105-8
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 105-108
    • Chen, J.J.1    London, I.M.2
  • 24
    • 0030911173 scopus 로고    scopus 로고
    • Erythropoietic protoporphyria
    • Cox TM. 1997. Erythropoietic protoporphyria. J. Inherit. Metab. Dis. 20:258-69
    • (1997) J. Inherit. Metab. Dis. , vol.20 , pp. 258-269
    • Cox, T.M.1
  • 25
    • 0034329215 scopus 로고    scopus 로고
    • Regulation of hemoglobin synthesis and proliferation of differentiating erythroid cells by heme-regulated eIF-2alpha kinase
    • Crosby JS, Chefalo PJ, Yeh I, Ying S, London IM, et al. 2000. Regulation of hemoglobin synthesis and proliferation of differentiating erythroid cells by heme-regulated eIF-2alpha kinase. Blood 96:3241-48
    • (2000) Blood , vol.96 , pp. 3241-3248
    • Crosby, J.S.1    Chefalo, P.J.2    Yeh, I.3    Ying, S.4    London, I.M.5
  • 26
    • 0028356915 scopus 로고
    • Erythroid expression of the heme- Regulated eIF-2 alpha kinase
    • Crosby JS, Lee K, London M, Chen JJ. 1994. Erythroid expression of the heme- regulated eIF-2 alpha kinase. Mol. Cell Biol. 14:3906-14
    • (1994) Mol. Cell Biol. , vol.14 , pp. 3906-3914
    • Crosby, J.S.1    Lee, K.2    London, M.3    Chen, J.J.4
  • 27
    • 0017337754 scopus 로고
    • Increase in globin chains and globin mRNA in erythroleukemia cells in response to hemin
    • Dabney BJ, Beaudet AL. 1977. Increase in globin chains and globin mRNA in erythroleukemia cells in response to hemin. Arch. Biochem. Biophys. 179:106-12
    • (1977) Arch. Biochem. Biophys. , vol.179 , pp. 106-112
    • Dabney, B.J.1    Beaudet, A.L.2
  • 28
    • 0026064347 scopus 로고
    • Repair of uracil residues closely spaced on the opposite strands of plasmid DNA results in double-strand break and deletion formation
    • Dianov GL, Timchenko TV, Sinitsina OI, Kuzminov AV, Medvedev OA, Salganik RI. 1991. Repair of uracil residues closely spaced on the opposite strands of plasmid DNA results in double-strand break and deletion formation. Mol. Gen. Genet. 225:448-52
    • (1991) Mol. Gen. Genet. , vol.225 , pp. 448-452
    • Dianov, G.L.1    Timchenko, T.V.2    Sinitsina, O.I.3    Kuzminov, A.V.4    Medvedev, O.A.5    Salganik, R.I.6
  • 29
    • 0034677467 scopus 로고    scopus 로고
    • Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
    • Donovan A, Brownlie A, Zhou Y, Shepard J, Pratt SJ, et al. 2000. Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter. Nature 403:776-81
    • (2000) Nature , vol.403 , pp. 776-781
    • Donovan, A.1    Brownlie, A.2    Zhou, Y.3    Shepard, J.4    Pratt, S.J.5
  • 31
    • 0033670837 scopus 로고    scopus 로고
    • Increased uracil misincorporation in lymphocytes from folate-deficient rats
    • Duthie SJ, Grant G, Narayanan S. 2000. Increased uracil misincorporation in lymphocytes from folate-deficient rats. Br. J. Cancer 83:1532-37
    • (2000) Br. J. Cancer , vol.83 , pp. 1532-1537
    • Duthie, S.J.1    Grant, G.2    Narayanan, S.3
  • 33
    • 0029977783 scopus 로고    scopus 로고
    • The molecular basis of the sideroblastic anemias
    • Fitzsimons EJ, May A. 1996. The molecular basis of the sideroblastic anemias. Curr. Opin. Hematol. 3:167-72
    • (1996) Curr. Opin. Hematol. , vol.3 , pp. 167-172
    • Fitzsimons, E.J.1    May, A.2
  • 34
    • 0030763856 scopus 로고    scopus 로고
    • Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
    • Fleming MD, Trenor CC 3rd, Su MA, Foernzler D, Beier DR, et al. 1997. Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene. Nat. Genet. 16:383-86
    • (1997) Nat. Genet. , vol.16 , pp. 383-386
    • Fleming, M.D.1    Trenor III, C.C.2    Su, M.A.3    Foernzler, D.4    Beier, D.R.5
  • 35
    • 0035902586 scopus 로고    scopus 로고
    • Hepcidin: A putative iron-regulatory hormone relevant to hereditary hemochromatosis and the anemia of chronic disease
    • Fleming RE, Sly WS. 2001. Hepcidin: a putative iron-regulatory hormone relevant to hereditary hemochromatosis and the anemia of chronic disease. Proc. Natl. Acad. Sci. USA 98:8160-62
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8160-8162
    • Fleming, R.E.1    Sly, W.S.2
  • 37
    • 0036831170 scopus 로고    scopus 로고
    • The role of hepcidin in iron sequestration during infections and in the pathogenesis of anemia of chronic disease
    • Ganz T. 2002. The role of hepcidin in iron sequestration during infections and in the pathogenesis of anemia of chronic disease. Isr. Med. Assoc. J. 4:1043-45
    • (2002) Isr. Med. Assoc. J. , vol.4 , pp. 1043-1045
    • Ganz, T.1
  • 39
  • 40
    • 0035071706 scopus 로고    scopus 로고
    • Case study: Folate bioavailability
    • Gregory JF 3rd. 2001. Case study: folate bioavailability. J. Nutr. 131(Suppl. 4):1376S-82S
    • (2001) J. Nutr. , vol.131 , Issue.4 SUPPL.
    • Gregory III, J.F.1
  • 41
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled metal-ion transporter
    • Gunshin H, Mackenzie B, Berger UV, Gunshin Y, Romero MF, et al. 1997. Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature 388:482-88
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.1    Mackenzie, B.2    Berger, U.V.3    Gunshin, Y.4    Romero, M.F.5
  • 42
    • 0024776421 scopus 로고
    • The intestinal absorption of dietary folates in health and disease
    • Halsted CH. 1989. The intestinal absorption of dietary folates in health and disease. J. Am. Coll. Nutr. 8:650-58
    • (1989) J. Am. Coll. Nutr. , vol.8 , pp. 650-658
    • Halsted, C.H.1
  • 43
    • 17944362905 scopus 로고    scopus 로고
    • Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency
    • Han AP, Yu C, Lu L, Fujiwara Y, Browne C, et al. 2001. Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency. EMBO J. 20:6909-18
    • (2001) EMBO J. , vol.20 , pp. 6909-6918
    • Han, A.P.1    Yu, C.2    Lu, L.3    Fujiwara, Y.4    Browne, C.5
  • 44
    • 0013918995 scopus 로고
    • Cytogenetic observations in vitamin B12 and folate deficiency
    • Heath CW. 1966. Cytogenetic observations in vitamin B12 and folate deficiency. Blood 27:800-15
    • (1966) Blood , vol.27 , pp. 800-815
    • Heath, C.W.1
  • 45
    • 0036400025 scopus 로고    scopus 로고
    • Ceruloplasmin metabolism and function
    • Hellman NE, Gitlin JD. 2002. Ceruloplasmin metabolism and function. Annu. Rev. Nutr. 22:439-58
    • (2002) Annu. Rev. Nutr. , vol.22 , pp. 439-458
    • Hellman, N.E.1    Gitlin, J.D.2
  • 46
    • 0000236060 scopus 로고
    • Interrelations of vitamin B12 and folic acid metabolism: Folic acid clearance studies
    • Herbert V, Zalusky R. 1962. Interrelations of vitamin B12 and folic acid metabolism: folic acid clearance studies. J. Clin. Invest. 41:1263-76
    • (1962) J. Clin. Invest. , vol.41 , pp. 1263-1276
    • Herbert, V.1    Zalusky, R.2
  • 47
    • 0017681998 scopus 로고
    • Storage iron regulation
    • Hershko C. 1977. Storage iron regulation. Prog. Hematol. 10:105-48
    • (1977) Prog. Hematol. , vol.10 , pp. 105-148
    • Hershko, C.1
  • 49
    • 0024314404 scopus 로고
    • Effects of nitrous oxide inactivation of vitamin B12 and of methionine on folate coenzyme metabolism in rat liver, kidney, brain, small intestine and bone marrow
    • Horne DW. 1989. Effects of nitrous oxide inactivation of vitamin B12 and of methionine on folate coenzyme metabolism in rat liver, kidney, brain, small intestine and bone marrow. Biofactors 2:65-68
    • (1989) Biofactors , vol.2 , pp. 65-68
    • Horne, D.W.1
  • 51
    • 0019938320 scopus 로고
    • Characteristic abnormality of deoxyribonucleoside triphosphate metabolism in megaloblastic anemia
    • Iwata N, Omine M, Yamauchi H, Maekawa T. 1982. Characteristic abnormality of deoxyribonucleoside triphosphate metabolism in megaloblastic anemia. Blood 60:918-23
    • (1982) Blood , vol.60 , pp. 918-923
    • Iwata, N.1    Omine, M.2    Yamauchi, H.3    Maekawa, T.4
  • 52
    • 0033551352 scopus 로고    scopus 로고
    • The effect of folic acid fortification on plasma folate and total homocysteine concentrations
    • Jacques PF, Selhub J, Bostom AG, Wilson PWF, Rosenberg IH. 1999. The effect of folic acid fortification on plasma folate and total homocysteine concentrations. N. Engl. J. Med. 340:1449-54
    • (1999) N. Engl. J. Med. , vol.340 , pp. 1449-1454
    • Jacques, P.F.1    Selhub, J.2    Bostom, A.G.3    Wilson, P.W.F.4    Rosenberg, I.H.5
  • 53
    • 0027074765 scopus 로고
    • Alterations in nucleotide pools in rats fed diets deficient in choline, methionine and/or folic acid
    • James SJ, Cross DR, Miller BJ. 1992. Alterations in nucleotide pools in rats fed diets deficient in choline, methionine and/or folic acid. Carcinogenesis 13:2471-74
    • (1992) Carcinogenesis , vol.13 , pp. 2471-2474
    • James, S.J.1    Cross, D.R.2    Miller, B.J.3
  • 54
    • 0027360191 scopus 로고
    • Survival or death of individual proerythroblasts results from differing erythropoietin sensitivities: A mechanism for controlled rates of erythrocyte production
    • Kelley LL, Koury MJ, Bondurant MC, Koury ST, Sawyer ST, Wickrema A. 1993. Survival or death of individual proerythroblasts results from differing erythropoietin sensitivities: a mechanism for controlled rates of erythrocyte production. Blood 82:2340-52
    • (1993) Blood , vol.82 , pp. 2340-2352
    • Kelley, L.L.1    Koury, M.J.2    Bondurant, M.C.3    Koury, S.T.4    Sawyer, S.T.5    Wickrema, A.6
  • 55
    • 0025343574 scopus 로고
    • Erythropoietin retards DNA breakdown and prevents programmed death in erythroid progenitor cells
    • Koury MJ, Bondurant MC. 1990. Erythropoietin retards DNA breakdown and prevents programmed death in erythroid progenitor cells. Science 248:378-81
    • (1990) Science , vol.248 , pp. 378-381
    • Koury, M.J.1    Bondurant, M.C.2
  • 56
    • 0027049472 scopus 로고
    • The molecular mechanism of erythropoietin action
    • Koury MJ, Bondurant MC. 1992. The molecular mechanism of erythropoietin action. Eur. J. Biochem. 210:649-63
    • (1992) Eur. J. Biochem. , vol.210 , pp. 649-663
    • Koury, M.J.1    Bondurant, M.C.2
  • 57
    • 0028221050 scopus 로고
    • Apoptosis mediates and thymidine prevents erythroblast destruction in folate deficiency anemia
    • Koury MJ, Horne DW 1994. Apoptosis mediates and thymidine prevents erythroblast destruction in folate deficiency anemia. Proc. Natl. Acad. Sci. USA 91:4067-71
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4067-4071
    • Koury, M.J.1    Horne, D.W.2
  • 58
    • 0030998489 scopus 로고    scopus 로고
    • Apoptosis of late stage erythroblasts in megaloblastic anemia: Association with DNA damage and macrocyte production
    • Koury MJ, Horne DW, Brown ZA, Pietenpol J, Blount BC, et al. 1997. Apoptosis of late stage erythroblasts in megaloblastic anemia: association with DNA damage and macrocyte production. Blood 89: 4617-23
    • (1997) Blood , vol.89 , pp. 4617-4623
    • Koury, M.J.1    Horne, D.W.2    Brown, Z.A.3    Pietenpol, J.4    Blount, B.C.5
  • 59
    • 0034329261 scopus 로고    scopus 로고
    • Apoptosis in megaloblastic anemia occurs during DNA synthesis by a p53- Independent, nucleoside-reversible mechanism
    • Koury MJ, Price JO, Hicks GG. 2000. Apoptosis in megaloblastic anemia occurs during DNA synthesis by a p53- independent, nucleoside-reversible mechanism. Blood 96:3249-55
    • (2000) Blood , vol.96 , pp. 3249-3255
    • Koury, M.J.1    Price, J.O.2    Hicks, G.G.3
  • 61
    • 0023868741 scopus 로고
    • Localization of erythropoietin synthesizing cells in murine kidneys by in situ hybridization
    • Koury ST, Bondurant MC, Koury MJ. 1988. Localization of erythropoietin synthesizing cells in murine kidneys by in situ hybridization. Blood 71:524-27
    • (1988) Blood , vol.71 , pp. 524-527
    • Koury, S.T.1    Bondurant, M.C.2    Koury, M.J.3
  • 62
    • 0024322837 scopus 로고
    • Quantitation of erythropoietin-producing cells in kidneys of mice by in situ hybridization: Correlation with hematocrit, renal erythropoietin mRNA and serum erythropoietin concentration
    • Koury ST, Koury MJ, Bondurant MC, Caro J, Graber SE. 1989. Quantitation of erythropoietin-producing cells in kidneys of mice by in situ hybridization: correlation with hematocrit, renal erythropoietin mRNA and serum erythropoietin concentration. Blood 74:645-51
    • (1989) Blood , vol.74 , pp. 645-651
    • Koury, S.T.1    Koury, M.J.2    Bondurant, M.C.3    Caro, J.4    Graber, S.E.5
  • 63
    • 0026019106 scopus 로고
    • Erythropoietin
    • Krantz SB. 1991. Erythropoietin. Blood 77:419-34
    • (1991) Blood , vol.77 , pp. 419-434
    • Krantz, S.B.1
  • 64
    • 0023837516 scopus 로고
    • Peritubular cells are the site of erythropoietin synthesis in the murine hypoxic kidney
    • Lacombe C, DaSilva J-L, Bruneval P, Fournier JG, Wendling F, et al. 1988. Peritubular cells are the site of erythropoietin synthesis in the murine hypoxic kidney. J. Clin. Invest. 81:620-23
    • (1988) J. Clin. Invest. , vol.81 , pp. 620-623
    • Lacombe, C.1    DaSilva, J.-L.2    Bruneval, P.3    Fournier, J.G.4    Wendling, F.5
  • 65
    • 0035138456 scopus 로고    scopus 로고
    • Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice
    • LaVaute T, Smith S, Cooperman S, Iwai K, Land W, et al. 2001. Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice. Nat. Genet. 27:209-14
    • (2001) Nat. Genet. , vol.27 , pp. 209-214
    • Lavaute, T.1    Smith, S.2    Cooperman, S.3    Iwai, K.4    Land, W.5
  • 66
    • 0032104739 scopus 로고    scopus 로고
    • The human Nramp2 gene: Characterization of the gene structure, alternative splicing, promoter region and polymorphisms
    • Lee PL, Gelbart T, West C, Halloran C, Beutler E. 1998. The human Nramp2 gene: characterization of the gene structure, alternative splicing, promoter region and polymorphisms. Blood Cells Mol. Dis. 24:199-215
    • (1998) Blood Cells Mol. Dis. , vol.24 , pp. 199-215
    • Lee, P.L.1    Gelbart, T.2    West, C.3    Halloran, C.4    Beutler, E.5
  • 67
    • 0032959574 scopus 로고    scopus 로고
    • Transferrin receptor is necessary for development of erythrocytes and the nervous system
    • Levy JE, Jin O, Fujiwara Y, Kuo F, Andrews NC. 1999. Transferrin receptor is necessary for development of erythrocytes and the nervous system. Nat. Genet. 21:396-99
    • (1999) Nat. Genet. , vol.21 , pp. 396-399
    • Levy, J.E.1    Jin, O.2    Fujiwara, Y.3    Kuo, F.4    Andrews, N.C.5
  • 68
    • 0034604603 scopus 로고    scopus 로고
    • Identification of an erythroid active element in the transferrin receptor gene
    • Lok CN, Ponka P. 2000. Identification of an erythroid active element in the transferrin receptor gene. J. Biol. Chem. 275:24185-90
    • (2000) J. Biol. Chem. , vol.275 , pp. 24185-24190
    • Lok, C.N.1    Ponka, P.2
  • 69
    • 0000775172 scopus 로고
    • The regulation of initiation of protein synthesis in eukaryotic cells by eIF-2α kinase
    • ed. PD Boyer, EG Krebs, New York: Academic
    • London M, Levin DH, Matts RL, Thomas SB, Petryshyn R, Chen J-J. 1987. The regulation of initiation of protein synthesis in eukaryotic cells by eIF-2α kinase. In The Enzymes, ed. PD Boyer, EG Krebs, Vol. 18, Part B, pp. 360-80. New York: Academic
    • (1987) The Enzymes , vol.18 , Issue.PART B , pp. 360-380
    • London, M.1    Levin, D.H.2    Matts, R.L.3    Thomas, S.B.4    Petryshyn, R.5    Chen, J.-J.6
  • 70
    • 0030942667 scopus 로고    scopus 로고
    • "Spontaneous" genetic damage in man: Evaluation of interindividual variability, relationship among markers of damage, and influence of nutritional status
    • MacGregor JT, Wehr CM, Hiatt RA, Peters B, Tucker JD, et al. 1997. "Spontaneous" genetic damage in man: evaluation of interindividual variability, relationship among markers of damage, and influence of nutritional status. Mutat. Res. 377:125-35
    • (1997) Mutat. Res. , vol.377 , pp. 125-135
    • MacGregor, J.T.1    Wehr, C.M.2    Hiatt, R.A.3    Peters, B.4    Tucker, J.D.5
  • 71
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • Maines MD. 1997. The heme oxygenase system: a regulator of second messenger gases. Annu. Rev. Pharmacol. Toxicol. 37:517-54
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 72
  • 73
    • 0035793856 scopus 로고    scopus 로고
    • An iron- Regulated ferric reductase associated with the absorption of dietary iron
    • McKie AT, Barrow D, Latunde-Dada GO, Rolfs A, Sager G, et al. 2001. An iron- regulated ferric reductase associated with the absorption of dietary iron. Science 291:1755-59
    • (2001) Science , vol.291 , pp. 1755-1759
    • McKie, A.T.1    Barrow, D.2    Latunde-Dada, G.O.3    Rolfs, A.4    Sager, G.5
  • 74
    • 0033861745 scopus 로고    scopus 로고
    • A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation
    • McKie AT, Marciani P, Rolfs A, Brennan K, Wehr K, et al. 2000. A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation. Mol. Cell 5:299-309
    • (2000) Mol. Cell , vol.5 , pp. 299-309
    • McKie, A.T.1    Marciani, P.2    Rolfs, A.3    Brennan, K.4    Wehr, K.5
  • 75
    • 0013962898 scopus 로고
    • Cytogenetic and cytochemical studies on marrow cells in B12 and folate deficiency
    • Menzies RC, Crossen PE, Fitzgerald PH, Gunz FW. 1966. Cytogenetic and cytochemical studies on marrow cells in B12 and folate deficiency. Blood 28:581-94
    • (1966) Blood , vol.28 , pp. 581-594
    • Menzies, R.C.1    Crossen, P.E.2    Fitzgerald, P.H.3    Gunz, F.W.4
  • 76
    • 0032736896 scopus 로고    scopus 로고
    • Post-transcriptional control via iron-responsive elements: The impact of aberrations in hereditary disease
    • Mikulits W, Schranzhofer M, Beug H, Mullner EW. 1999. Post-transcriptional control via iron-responsive elements: the impact of aberrations in hereditary disease. Mutat. Res. 437:219-30
    • (1999) Mutat. Res. , vol.437 , pp. 219-230
    • Mikulits, W.1    Schranzhofer, M.2    Beug, H.3    Mullner, E.W.4
  • 77
    • 0042866137 scopus 로고    scopus 로고
    • Physiology and molecular biology of dietary iron absorption
    • Miret S, Simpson RJ, McKie AT. 2003. Physiology and molecular biology of dietary iron absorption. Annu. Rev. Nutr. 23:283-301
    • (2003) Annu. Rev. Nutr. , vol.23 , pp. 283-301
    • Miret, S.1    Simpson, R.J.2    McKie, A.T.3
  • 78
    • 0032570583 scopus 로고    scopus 로고
    • 12 receptor and target of teratogenic antibodies is a megalin-binding peripheral membrane protein with homology to developmental proteins
    • 12 receptor and target of teratogenic antibodies is a megalin-binding peripheral membrane protein with homology to developmental proteins. J. Biol. Chem. 273:5235-42
    • (1998) J. Biol. Chem. , vol.273 , pp. 5235-5242
    • Moestrup, S.K.1    Kozyraki, R.2    Kristiansen, M.3    Kaysen, J.H.4    Rasmussen, H.H.5
  • 79
    • 17944380796 scopus 로고    scopus 로고
    • Autosomal- Dominant hemochromatosis is associated with a mutation in the ferroportin (SLC11A3) gene
    • Montosi G, Donovan A, Totaro A, Garuti C, Pignatti E, et al. 2001. Autosomal- dominant hemochromatosis is associated with a mutation in the ferroportin (SLC11A3) gene. J. Clin. Invest. 108:619-23
    • (2001) J. Clin. Invest. , vol.108 , pp. 619-623
    • Montosi, G.1    Donovan, A.2    Totaro, A.3    Garuti, C.4    Pignatti, E.5
  • 80
    • 0035902605 scopus 로고    scopus 로고
    • Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 (USF2) knockout mice
    • Nicolas G, Bennoun M, Devaux I, Beaumont C, Grandchamp B, et al. 2001. Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 (USF2) knockout mice. Proc. Natl. Acad. Sci. USA 98:8780-85
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8780-8785
    • Nicolas, G.1    Bennoun, M.2    Devaux, I.3    Beaumont, C.4    Grandchamp, B.5
  • 82
    • 0035896642 scopus 로고    scopus 로고
    • Hepcidin, a urinary antimicrobial peptide synthesized in the liver
    • Park CH, Valore EV, Waring AJ, Ganz T. 2001. Hepcidin, a urinary antimicrobial peptide synthesized in the liver. J. Biol. Chem. 276:7806-10
    • (2001) J. Biol. Chem. , vol.276 , pp. 7806-7810
    • Park, C.H.1    Valore, E.V.2    Waring, A.J.3    Ganz, T.4
  • 83
    • 0032884078 scopus 로고    scopus 로고
    • Mice lacking the folic acid-binding protein Folbp1 are defective in early embryonic development
    • Piedrahita JA, Oetama B, Bennett GD, van Waes J, Kamen BA, et al. 1999. Mice lacking the folic acid-binding protein Folbp1 are defective in early embryonic development. Nat. Genet. 23:228-32
    • (1999) Nat. Genet. , vol.23 , pp. 228-232
    • Piedrahita, J.A.1    Oetama, B.2    Bennett, G.D.3    Van Waes, J.4    Kamen, B.A.5
  • 84
    • 0017102074 scopus 로고
    • The reversal of methotrexate cytotoxicity to mouse bone marrow cells by leucovorin and nucleosides
    • Pinedo HM, Zaharko DS, Bull JM, Chabner BA. 1976. The reversal of methotrexate cytotoxicity to mouse bone marrow cells by leucovorin and nucleosides. Cancer Res. 36:4418-24
    • (1976) Cancer Res. , vol.36 , pp. 4418-4424
    • Pinedo, H.M.1    Zaharko, D.S.2    Bull, J.M.3    Chabner, B.A.4
  • 85
    • 0031028178 scopus 로고    scopus 로고
    • Tissue-specific regulation of iron metabolism and heme synthesis: Distinct control mechanisms in erythroid cells
    • Ponka P. 1997. Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells. Blood 89:1-25
    • (1997) Blood , vol.89 , pp. 1-25
    • Ponka, P.1
  • 86
    • 0033511832 scopus 로고    scopus 로고
    • Cell biology of heme
    • Ponka P. 1999. Cell biology of heme. Am. J. Med. Sci. 318:241-56
    • (1999) Am. J. Med. Sci. , vol.318 , pp. 241-256
    • Ponka, P.1
  • 87
    • 0039327515 scopus 로고    scopus 로고
    • Iron deficiency
    • ed. RE Rakel, ET Bope,. London: Saunders
    • Ponka P. 2001. Iron deficiency. In Conn's Current Therapy, ed. RE Rakel, ET Bope, pp. 369-76. London: Saunders
    • (2001) Conn's Current Therapy , pp. 369-376
    • Ponka, P.1
  • 88
    • 0036800650 scopus 로고    scopus 로고
    • Rare causes of hereditary iron overload
    • Ponka P. 2002. Rare causes of hereditary iron overload. Semin. Hematol. 39:249-62
    • (2002) Semin. Hematol. , vol.39 , pp. 249-262
    • Ponka, P.1
  • 89
    • 0242610777 scopus 로고    scopus 로고
    • Recent advances in cellular iron metabolism
    • Ponka P. 2003. Recent advances in cellular iron metabolism. J. Trace Elem. Exp. Med. 16:201-17
    • (2003) J. Trace Elem. Exp. Med. , vol.16 , pp. 201-217
    • Ponka, P.1
  • 90
    • 0031963449 scopus 로고    scopus 로고
    • Function and regulation of transferrin and ferritin
    • Ponka P, Beaumont C, Richardson DR. 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
  • 91
    • 0032830130 scopus 로고    scopus 로고
    • The transferrin receptor: Role in health and disease
    • Ponka P, Lok CN. 1999. The transferrin receptor: role in health and disease. Int. J. Biochem. Cell Biol. 31:1111-37
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 1111-1137
    • Ponka, P.1    Lok, C.N.2
  • 92
  • 93
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • Poss KD, Tonegawa S. 1997. Heme oxygenase 1 is required for mammalian iron reutilization. Proc. Natl. Acad. Sci. USA 94:10919-24
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 94
    • 0030886054 scopus 로고    scopus 로고
    • Reduced stress defense in heme oxygenase 1- Deficient cells
    • Poss KD, Tonegawa S. 1997. Reduced stress defense in heme oxygenase 1- deficient cells. Proc. Natl. Acad. Sci. USA 94:10925-30
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10925-10930
    • Poss, K.D.1    Tonegawa, S.2
  • 95
    • 0032782065 scopus 로고    scopus 로고
    • Transcobalamin II synthesized in the intestinal villi facilitates transfer of cobalamin to the portal blood
    • Quadros EV, Regec AL, Khan KM, Quadros E, Rothenberg SP. 1999. Transcobalamin II synthesized in the intestinal villi facilitates transfer of cobalamin to the portal blood. Am. J. Physiol. 277:G161-66
    • (1999) Am. J. Physiol. , vol.277
    • Quadros, E.V.1    Regec, A.L.2    Khan, K.M.3    Quadros, E.4    Rothenberg, S.P.5
  • 96
    • 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 AP, Chen JJ. 2003. Autophosphorylation of threonine 485 in the activation loop is essential for attaining eIF2alpha kinase activity of HRI. Biochemistry 42:6536-44
    • (2003) Biochemistry , vol.42 , pp. 6536-6544
    • Rafie-Kolpin, M.1    Han, A.P.2    Chen, J.J.3
  • 97
    • 0030039395 scopus 로고    scopus 로고
    • Nucleic acid composition of bone marrow mononuclear cells in cobalamin deficiency
    • Ramsahoye BH, Burnett AK, Taylor C. 1996. Nucleic acid composition of bone marrow mononuclear cells in cobalamin deficiency. Blood 87:2065-70
    • (1996) Blood , vol.87 , pp. 2065-2070
    • Ramsahoye, B.H.1    Burnett, A.K.2    Taylor, C.3
  • 98
    • 0033152344 scopus 로고    scopus 로고
    • Expression and functional characterization of the beta-isoform of the folate receptor on CD34(+) cells
    • Reddy JA, Haneline LS, Srour EF, Antony AC, Clapp DW, Low PS. 1999. Expression and functional characterization of the beta-isoform of the folate receptor on CD34(+) cells. Blood 93:3940-48
    • (1999) Blood , vol.93 , pp. 3940-3948
    • Reddy, J.A.1    Haneline, L.S.2    Srour, E.F.3    Antony, A.C.4    Clapp, D.W.5    Low, P.S.6
  • 99
    • 0036139822 scopus 로고    scopus 로고
    • Uracil inhuman DNA from subjects with normal and impaired folate status as determined by high-performance liquid chromatography-tandem mass spectrometry
    • Ren J, Ulvik A, Refsum H, Ueland PM. 2002. Uracil inhuman DNA from subjects with normal and impaired folate status as determined by high-performance liquid chromatography-tandem mass spectrometry. Anal. Chem. 74:295-99
    • (2002) Anal. Chem. , vol.74 , pp. 295-299
    • Ren, J.1    Ulvik, A.2    Refsum, H.3    Ueland, P.M.4
  • 100
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • Richardson DR, 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
  • 102
    • 0015466148 scopus 로고
    • Globin messenger-RNA induction during erythroid differentiation of cultured leukemia cells
    • Ross J, Ikawa Y, Leder P. 1972. Globin messenger-RNA induction during erythroid differentiation of cultured leukemia cells. Proc. Natl. Acad. Sci. USA 69:3620-23
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3620-3623
    • Ross, J.1    Ikawa, Y.2    Leder, P.3
  • 103
    • 0017170804 scopus 로고
    • Induction of globin mRNA accumulation by hemin in cultured erythroleukemic cells
    • Ross J, Sautner D. 1976. Induction of globin mRNA accumulation by hemin in cultured erythroleukemic cells. Cell 8:513-20
    • (1976) Cell , vol.8 , pp. 513-520
    • Ross, J.1    Sautner, D.2
  • 104
    • 0030624029 scopus 로고    scopus 로고
    • Regulation of iron metabolism in eukaryotes
    • Rouault T, Klausner R. 1997. Regulation of iron metabolism in eukaryotes. Curr. Top. Cell Regul. 35:1-19
    • (1997) Curr. Top. Cell Regul. , vol.35 , pp. 1-19
    • Rouault, T.1    Klausner, R.2
  • 105
    • 0029960838 scopus 로고    scopus 로고
    • The role of heme in gene expression
    • Sassa S, Nagai T. 1996. The role of heme in gene expression. Int. J. Hematol. 63:167-78
    • (1996) Int. J. Hematol. , vol.63 , pp. 167-178
    • Sassa, S.1    Nagai, T.2
  • 107
    • 0032836233 scopus 로고    scopus 로고
    • Cellular import of cobalamin (vitamin B-12)
    • Seetharam B, Bose S, Li N. 1999. Cellular import of cobalamin (vitamin B-12). J. Nutr. 129:1761-64
    • (1999) J. Nutr. , vol.129 , pp. 1761-1764
    • Seetharam, B.1    Bose, S.2    Li, N.3
  • 109
    • 0036728509 scopus 로고    scopus 로고
    • Iron and the anemia of chronic disease
    • Spivak JL. 2002. Iron and the anemia of chronic disease. Oncology (Huntingt.) 16(Suppl. 10):25-33
    • (2002) Oncology (Huntingt.) , vol.16 , Issue.10 SUPPL. , pp. 25-33
    • Spivak, J.L.1
  • 110
    • 0030881762 scopus 로고    scopus 로고
    • Vitamin B-12 deficiency in the elderly: Current dilemmas
    • Stabler SP, Lindenbaum J, Allen RH. 1997. Vitamin B-12 deficiency in the elderly: current dilemmas. Am. J. Clin. Nutr. 66:741-49
    • (1997) Am. J. Clin. Nutr. , vol.66 , pp. 741-749
    • Stabler, S.P.1    Lindenbaum, J.2    Allen, R.H.3
  • 111
    • 0025834082 scopus 로고
    • Folate-deficient human lymphoblasts: Changes in deoxynucleotide metabolism and thymidylate cycle activities
    • van der Weyden MB, Hayman RJ, Rose IS, Brumley J. 1991. Folate-deficient human lymphoblasts: changes in deoxynucleotide metabolism and thymidylate cycle activities. Eur. J. Haematol. 47:109-14
    • (1991) Eur. J. Haematol. , vol.47 , pp. 109-114
    • Van Der Weyden, M.B.1    Hayman, R.J.2    Rose, I.S.3    Brumley, J.4
  • 112
    • 0032909207 scopus 로고    scopus 로고
    • Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
    • Vulpe CD, Kuo YM, Murphy TL, Cowley L, Askwith C, et al. 1999. Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse. Nat. Genet. 21:195-99
    • (1999) Nat. Genet. , vol.21 , pp. 195-199
    • Vulpe, C.D.1    Kuo, Y.M.2    Murphy, T.L.3    Cowley, L.4    Askwith, C.5
  • 113
    • 0028171125 scopus 로고
    • eIF-2 kinases: Regulators of general and gene-specific translation initiation
    • Wek RC. 1994. eIF-2 kinases: regulators of general and gene-specific translation initiation. Trends Biochem. Sci. 19:491-96
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 491-496
    • Wek, R.C.1
  • 114
    • 0032936106 scopus 로고    scopus 로고
    • The wide spectrum and unresolved issues of megaloblastic anemia
    • Wickramasinghe SN. 1999. The wide spectrum and unresolved issues of megaloblastic anemia. Semin. Hematol. 36:3-18
    • (1999) Semin. Hematol. , vol.36 , pp. 3-18
    • Wickramasinghe, S.N.1
  • 115
    • 0014260473 scopus 로고
    • A study of erythropoiesis by combined morphologic, quantitative cytochemical and autoradiographic methods
    • Wickramasinghe SN, Cooper EH, Chalmers DG. 1968. A study of erythropoiesis by combined morphologic, quantitative cytochemical and autoradiographic methods. Blood 31:304-13
    • (1968) Blood , vol.31 , pp. 304-313
    • Wickramasinghe, S.N.1    Cooper, E.H.2    Chalmers, D.G.3
  • 116
    • 0028345658 scopus 로고
    • 12- And folate- deficient patients misincorporate uracil into DNA
    • 12- and folate- deficient patients misincorporate uracil into DNA. Blood 83:1656-61
    • (1994) Blood , vol.83 , pp. 1656-1661
    • Wickramasinghe, S.N.1    Fida, S.2
  • 117
    • 0018912788 scopus 로고
    • Reduced rate of DNA replication fork movement in megaloblastic anemia. J
    • Wickramasinghe RG, Hoffbrand AV. 1980. Reduced rate of DNA replication fork movement in megaloblastic anemia. J. Clin. Invest. 65:26-36
    • (1980) Clin. Invest. , vol.65 , pp. 26-36
    • Wickramasinghe, R.G.1    Hoffbrand, A.V.2
  • 119
    • 0028880455 scopus 로고
    • Generation of committed erythroid BFU-E and CFU-E progenitors does not require erythropoietin or the erythropoietin receptor
    • Wu H, Liu X, Jaenisch R, Lodish HF. 1995. Generation of committed erythroid BFU-E and CFU-E progenitors does not require erythropoietin or the erythropoietin receptor. Cell 83:59-67
    • (1995) Cell , vol.83 , pp. 59-67
    • Wu, H.1    Liu, X.2    Jaenisch, R.3    Lodish, H.F.4
  • 120
    • 0032893958 scopus 로고    scopus 로고
    • Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency
    • Yachie A, Niida Y, Wada T, Igarashi N, Kaneda H, et al. 1999. Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency. J. Clin. Invest. 103:129-35
    • (1999) J. Clin. Invest. , vol.103 , pp. 129-135
    • Yachie, A.1    Niida, Y.2    Wada, T.3    Igarashi, N.4    Kaneda, H.5
  • 121
    • 0014261853 scopus 로고
    • Proliferation of megaloblasts in pernicious anemia as observed from nucleic acid metabolism
    • Yoshida Y, Todo A, Shirakawa S, Wakisaka G, Uchino H. 1968. Proliferation of megaloblasts in pernicious anemia as observed from nucleic acid metabolism. Blood 31:292-303
    • (1968) Blood , vol.31 , pp. 292-303
    • Yoshida, Y.1    Todo, A.2    Shirakawa, S.3    Wakisaka, G.4    Uchino, H.5
  • 122
    • 0023655202 scopus 로고
    • Deoxyribonucleoside triphosphate imbalance. 5-Fluorodeoxyuridine-induced DNA double strand breaks in mouse FM3A cells and the mechanism of cell death
    • Yoshioka A, Tanaka S, Hiraoka O, Koyama Y, Hirota Y, et al. 1987. Deoxyribonucleoside triphosphate imbalance. 5-fluorodeoxyuridine-induced DNA double strand breaks in mouse FM3A cells and the mechanism of cell death. J. Biol. Chem. 262:8235-41
    • (1987) J. Biol. Chem. , vol.262 , pp. 8235-8241
    • Yoshioka, A.1    Tanaka, S.2    Hiraoka, O.3    Koyama, Y.4    Hirota, Y.5
  • 123
    • 0035971190 scopus 로고    scopus 로고
    • Rescue of embryonic lethality in reduced folate carrier-deficient mice by maternal folic acid supplementation reveals early neonatal failure of hematopoietic organs
    • Zhao R, Russell RG, Wang Y, Liu L, Gao F, et al. 2001. Rescue of embryonic lethality in reduced folate carrier-deficient mice by maternal folic acid supplementation reveals early neonatal failure of hematopoietic organs. J. Biol. Chem. 276:10224-28
    • (2001) J. Biol. Chem. , vol.276 , pp. 10224-10228
    • Zhao, R.1    Russell, R.G.2    Wang, Y.3    Liu, L.4    Gao, F.5
  • 124
    • 0014252635 scopus 로고
    • Stimulation of globin-chain initiation by hemin in the reticulocyte cell-free system
    • Zucker WV, Schulman HM. 1968. Stimulation of globin-chain initiation by hemin in the reticulocyte cell-free system. Proc. Natl. Acad. Sci. USA 59:582-89
    • (1968) Proc. Natl. Acad. Sci. USA , vol.59 , pp. 582-589
    • Zucker, W.V.1    Schulman, H.M.2


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