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Volumn 108, Issue 7, 2006, Pages 2428-2434

In vivo tumor growth is inhibited by cytosolic iron deprivation caused by the expression of mitochondrial ferritin

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; FERRITIN; FRATAXIN; HEME OXYGENASE 1; IRON; RNA;

EID: 33749334487     PISSN: 00064971     EISSN: 00064971     Source Type: Journal    
DOI: 10.1182/blood-2006-04-018341     Document Type: Article
Times cited : (46)

References (56)
  • 1
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison PM, Arosio P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta. 1996;1275:161-203.
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 2
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • Torti FM, Torti SV. Regulation of ferritin genes and protein. Blood. 2002;99:3505-3516.
    • (2002) Blood , vol.99 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 3
    • 0024121621 scopus 로고
    • Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs
    • Leibold EA, Munro HN. Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs. Proc Natl Acad Sci U S A. 1988;85:2171-2175.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 2171-2175
    • Leibold, E.A.1    Munro, H.N.2
  • 4
    • 0033826764 scopus 로고    scopus 로고
    • Iron regulatory proteins and the molecular control of mammalian iron metabolism
    • Eisenstein RS. Iron regulatory proteins and the molecular control of mammalian iron metabolism. Annu Rev Nutr. 2000;20:627-662.
    • (2000) Annu Rev Nutr , vol.20 , pp. 627-662
    • Eisenstein, R.S.1
  • 5
    • 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. Post-transcriptional control via iron-responsive elements: the impact of aberrations in hereditary disease. Mutat Res. 1999;437:219-230.
    • (1999) Mutat Res , vol.437 , pp. 219-230
    • Mikulits, W.1    Schranzhofer, M.2    Beug, H.3    Mullner, E.W.4
  • 7
    • 0035816608 scopus 로고    scopus 로고
    • A human mitochondrial ferritin encoded by an intronless gene
    • Levi S, Corsi B, Bosisio M, et al. A human mitochondrial ferritin encoded by an intronless gene. J Biol Chem. 2001;276:24437-24440.
    • (2001) J Biol Chem , vol.276 , pp. 24437-24440
    • Levi, S.1    Corsi, B.2    Bosisio, M.3
  • 8
    • 0037151089 scopus 로고    scopus 로고
    • Human mitochondrial ferritin expressed in HeLa cells incorporates iron and affects cellular iron metabolism
    • Corsi B, Cozzi A, Arosio P, et al. Human mitochondrial ferritin expressed in HeLa cells incorporates iron and affects cellular iron metabolism. J Biol Chem. 2002;277:22430-22437.
    • (2002) J Biol Chem , vol.277 , pp. 22430-22437
    • Corsi, B.1    Cozzi, A.2    Arosio, P.3
  • 9
    • 0242422377 scopus 로고    scopus 로고
    • Mitochondrial ferritin: A new player in iron metabolism
    • Drysdale J, Arosio P, Invernizzi R, et al. Mitochondrial ferritin: a new player in iron metabolism. Blood Cells Mol Dis. 2002;29:376-383.
    • (2002) Blood Cells Mol Dis , vol.29 , pp. 376-383
    • Drysdale, J.1    Arosio, P.2    Invernizzi, R.3
  • 10
    • 14944358625 scopus 로고    scopus 로고
    • Overexpression of mitochondrial ferritin causes cytosolic iron depletion and changes cellular iron homeostasis
    • Nie G, Sheftel AD, Kim SF, Ponka P. Overexpression of mitochondrial ferritin causes cytosolic iron depletion and changes cellular iron homeostasis. Blood. 2005;105:2161-2167.
    • (2005) Blood , vol.105 , pp. 2161-2167
    • Nie, G.1    Sheftel, A.D.2    Kim, S.F.3    Ponka, P.4
  • 11
    • 2942542658 scopus 로고    scopus 로고
    • Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala
    • Langlois dB, Santambrogio P, Granier T, et al. Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala. J Mol Biol. 2004;340:277-293.
    • (2004) J Mol Biol , vol.340 , pp. 277-293
    • Langlois, D.B.1    Santambrogio, P.2    Granier, T.3
  • 12
    • 0037372442 scopus 로고    scopus 로고
    • Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia
    • Cazzola M, Invernizzi R, Bergamaschi G, et al. Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia. Blood. 2003;101:1996-2000.
    • (2003) Blood , vol.101 , pp. 1996-2000
    • Cazzola, M.1    Invernizzi, R.2    Bergamaschi, G.3
  • 13
    • 22044434111 scopus 로고    scopus 로고
    • Aberrant mitochondrial iron distribution and maturation arrest characterizes early erythroid precursors in low-risk myelodysplastic syndromes
    • Tehranchi R, Invernizzi R, Grandien A, et al. Aberrant mitochondrial iron distribution and maturation arrest characterizes early erythroid precursors in low-risk myelodysplastic syndromes. Blood. 2005;106:247-253.
    • (2005) Blood , vol.106 , pp. 247-253
    • Tehranchi, R.1    Invernizzi, R.2    Grandien, A.3
  • 16
    • 0036799489 scopus 로고    scopus 로고
    • The genetics of inherited sideroblastic anemias
    • Fleming MD. The genetics of inherited sideroblastic anemias. Semin Hematol. 2002;39:270-281.
    • (2002) Semin Hematol , vol.39 , pp. 270-281
    • Fleming, M.D.1
  • 17
    • 0031028178 scopus 로고    scopus 로고
    • Tissue-specific regulation of iron metabolism and heme synthesis: Distinct control mechanisms in erythroid cells
    • Ponka P. Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells. Blood. 1997;89:1-25.
    • (1997) Blood , vol.89 , pp. 1-25
    • Ponka, P.1
  • 18
    • 14744294785 scopus 로고    scopus 로고
    • Iron-sulfur-protein biogenesis in eukaryotes
    • Lill R, Muhlenhoff U. Iron-sulfur-protein biogenesis in eukaryotes. Trends Biochem Sci. 2005;30:133-141.
    • (2005) Trends Biochem Sci , vol.30 , pp. 133-141
    • Lill, R.1    Muhlenhoff, U.2
  • 19
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • Rouault TA, Tong WH. Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nat Rev Mol Cell Biol. 2005;6:345-351.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.H.2
  • 20
    • 14944387002 scopus 로고    scopus 로고
    • Iron trafficking in the mitochondrion: Novel pathways revealed by disease
    • Napier I, Ponka P, Richardson DR. Iron trafficking in the mitochondrion: novel pathways revealed by disease. Blood. 2005;105:1867-1874.
    • (2005) Blood , vol.105 , pp. 1867-1874
    • Napier, I.1    Ponka, P.2    Richardson, D.R.3
  • 21
    • 0030846021 scopus 로고    scopus 로고
    • Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin
    • Babcock M, de Silva D, Oaks R, et al. Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin. Science. 1997;276:1709-1712.
    • (1997) Science , vol.276 , pp. 1709-1712
    • Babcock, M.1    De Silva, D.2    Oaks, R.3
  • 22
    • 0642287902 scopus 로고    scopus 로고
    • Iron metabolism and mitochondrial abnormalities in Friedreich ataxia
    • Pandolfo M. Iron metabolism and mitochondrial abnormalities in Friedreich ataxia. Blood Cells Mol Dis. 2002;29:536-547.
    • (2002) Blood Cells Mol Dis , vol.29 , pp. 536-547
    • Pandolfo, M.1
  • 23
    • 0032920837 scopus 로고    scopus 로고
    • Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A)
    • Allikmets R, Raskind WH, Hutchinson A, et al. Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A). Hum Mol Genet. 1999;8:743-749.
    • (1999) Hum Mol Genet , vol.8 , pp. 743-749
    • Allikmets, R.1    Raskind, W.H.2    Hutchinson, A.3
  • 24
    • 0032746009 scopus 로고    scopus 로고
    • The essential role of mitochondria in the biogenesis of cellular iron-sulfur proteins
    • Lill R, Diekert K, Kaut A, et al. The essential role of mitochondria in the biogenesis of cellular iron-sulfur proteins. Biol Chem. 1999;380:1157-1166.
    • (1999) Biol Chem , vol.380 , pp. 1157-1166
    • Lill, R.1    Diekert, K.2    Kaut, A.3
  • 25
    • 3142723133 scopus 로고    scopus 로고
    • Nutrient regulation of cell cycle progression
    • Bohnsack BL, Hirschi KK. Nutrient regulation of cell cycle progression. Annu Rev Nutr. 2004;24:433-453.
    • (2004) Annu Rev Nutr , vol.24 , pp. 433-453
    • Bohnsack, B.L.1    Hirschi, K.K.2
  • 26
    • 0037009846 scopus 로고    scopus 로고
    • The role of iron in cell cycle progression and the proliferation of neoplastic cells
    • Le NT, Richardson DR. The role of iron in cell cycle progression and the proliferation of neoplastic cells. Biochim Biophys Acta. 2002;1603:31-46.
    • (2002) Biochim Biophys Acta , vol.1603 , pp. 31-46
    • Le, N.T.1    Richardson, D.R.2
  • 27
    • 0027521831 scopus 로고
    • Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators
    • Nyholm S, Mann GJ, Johansson AG, et al. Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators. J Biol Chem. 1993;268:26200-26205.
    • (1993) J Biol Chem , vol.268 , pp. 26200-26205
    • Nyholm, S.1    Mann, G.J.2    Johansson, A.G.3
  • 28
    • 0029833706 scopus 로고    scopus 로고
    • The relationship of intracellular iron chelation to the inhibition and regeneration of human ribonucleotide reductase
    • Cooper CE, Lynagh GR, Hoyes KP, et al. The relationship of intracellular iron chelation to the inhibition and regeneration of human ribonucleotide reductase. J Biol Chem. 1996;271:20291-20299.
    • (1996) J Biol Chem , vol.271 , pp. 20291-20299
    • Cooper, C.E.1    Lynagh, G.R.2    Hoyes, K.P.3
  • 29
    • 0018053775 scopus 로고
    • Regulation of ribonucleotide reductase activity and its possible exploitation in chemotherapy
    • Witt L, Yap T, Blakley RL. Regulation of ribonucleotide reductase activity and its possible exploitation in chemotherapy. Adv Enzyme Regul. 1978;17:157-171.
    • (1978) Adv Enzyme Regul , vol.17 , pp. 157-171
    • Witt, L.1    Yap, T.2    Blakley, R.L.3
  • 30
    • 0023092624 scopus 로고
    • Antineuroblastoma activity of desferoxamine in human cell lines
    • Blatt J, Stitely S. Antineuroblastoma activity of desferoxamine in human cell lines. Cancer Res. 1987;47:1749-1750.
    • (1987) Cancer Res , vol.47 , pp. 1749-1750
    • Blatt, J.1    Stitely, S.2
  • 31
    • 0023135326 scopus 로고
    • In vitro and in vivo effects of deferoxamine in neonatal acute leukemia
    • Estrov Z, Tawa A, Wang XH, et al. In vitro and in vivo effects of deferoxamine in neonatal acute leukemia. Blood. 1987;69:757-761.
    • (1987) Blood , vol.69 , pp. 757-761
    • Estrov, Z.1    Tawa, A.2    Wang, X.H.3
  • 32
    • 0024241764 scopus 로고
    • Deferoxamine inhibition of human neuroblastoma viability and proliferation
    • Becton DL, Bryles P. Deferoxamine inhibition of human neuroblastoma viability and proliferation. Cancer Res. 1988;48:7189-7192.
    • (1988) Cancer Res , vol.48 , pp. 7189-7192
    • Becton, D.L.1    Bryles, P.2
  • 33
    • 0028891974 scopus 로고
    • The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents
    • Richardson DR, Tran EH, Ponka P. The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents. Blood. 1995;86:4295-4306.
    • (1995) Blood , vol.86 , pp. 4295-4306
    • Richardson, D.R.1    Tran, E.H.2    Ponka, P.3
  • 34
    • 0024561408 scopus 로고
    • Effects of desferrioxamine on normal and leukemic human hematopoietic cell growth: In vitro and in vivo studies
    • Dezza L, Cazzola M, Danova M, et al. Effects of desferrioxamine on normal and leukemic human hematopoietic cell growth: in vitro and in vivo studies. Leukemia. 1989;3:104-107.
    • (1989) Leukemia , vol.3 , pp. 104-107
    • Dezza, L.1    Cazzola, M.2    Danova, M.3
  • 35
    • 0041308109 scopus 로고    scopus 로고
    • Therapeutic potential of iron chelators in cancer therapy
    • Richardson DR. Therapeutic potential of iron chelators in cancer therapy. Adv Exp Med Biol. 2002;509:231-249.
    • (2002) Adv Exp Med Biol , vol.509 , pp. 231-249
    • Richardson, D.R.1
  • 36
    • 0036275236 scopus 로고    scopus 로고
    • Conditional derepression of ferritin synthesis in cells expressing a constitutive IRP1 mutant
    • Wang J, Pantopoulos K. Conditional derepression of ferritin synthesis in cells expressing a constitutive IRP1 mutant. Mol Cell Biol. 2002;22:4638-4651.
    • (2002) Mol Cell Biol , vol.22 , pp. 4638-4651
    • Wang, J.1    Pantopoulos, K.2
  • 37
    • 0017289492 scopus 로고
    • Sequential induction of heme pathway enzymes during erythroid differentiation of mouse Friend leukemia virus-infected cells
    • Sassa S. Sequential induction of heme pathway enzymes during erythroid differentiation of mouse Friend leukemia virus-infected cells. J Exp Med. 1976;143:305-315.
    • (1976) J Exp Med , vol.143 , pp. 305-315
    • Sassa, S.1
  • 38
    • 0023899855 scopus 로고
    • Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples
    • Fish WW. Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples. Methods Enzymol. 1988;158:357-364.
    • (1988) Methods Enzymol , vol.158 , pp. 357-364
    • Fish, W.W.1
  • 39
    • 0024516594 scopus 로고
    • Oxidation-reduction and the molecular mechanism of a regulatory RNA-protein interaction
    • Hentze MW, Rouault TA, Harford JB, Klausner RD. Oxidation-reduction and the molecular mechanism of a regulatory RNA-protein interaction. Science. 1989;244:357-359.
    • (1989) Science , vol.244 , pp. 357-359
    • Hentze, M.W.1    Rouault, T.A.2    Harford, J.B.3    Klausner, R.D.4
  • 40
    • 0038825777 scopus 로고    scopus 로고
    • Profiling of pathway-specific changes in gene expression following growth of human cancer cell lines transplanted into mice
    • Creighton C, Kuick R, Misek DE, et al. Profiling of pathway-specific changes in gene expression following growth of human cancer cell lines transplanted into mice. Genome Biol. 2003;4:R46.
    • (2003) Genome Biol , vol.4
    • Creighton, C.1    Kuick, R.2    Misek, D.E.3
  • 41
    • 23944500052 scopus 로고    scopus 로고
    • Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis
    • Wingert RA, Galloway JL, Barut B, et al. Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis. Nature. 2005;436:1035-1039.
    • (2005) Nature , vol.436 , pp. 1035-1039
    • Wingert, R.A.1    Galloway, J.L.2    Barut, B.3
  • 42
    • 13344270899 scopus 로고    scopus 로고
    • Friedreich's ataxia: Autosomal recessive disease caused by an intronic GAA triplet repeat expansion
    • Campuzano V, Montermini L, Molto MD, et al. Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion. Science. 1996;271:1423-1427.
    • (1996) Science , vol.271 , pp. 1423-1427
    • Campuzano, V.1    Montermini, L.2    Molto, M.D.3
  • 43
    • 0342700237 scopus 로고    scopus 로고
    • Recent advances in the molecular pathogenesis of Friedreich ataxia
    • Puccio H, Koenig M. Recent advances in the molecular pathogenesis of Friedreich ataxia. Hum Mol Genet. 2000;9:887-892.
    • (2000) Hum Mol Genet , vol.9 , pp. 887-892
    • Puccio, H.1    Koenig, M.2
  • 44
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
    • Puccio H, Simon D, Cossee M, et al. Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat Genet. 2001;27:181-186.
    • (2001) Nat Genet , vol.27 , pp. 181-186
    • Puccio, H.1    Simon, D.2    Cossee, M.3
  • 45
    • 0030813487 scopus 로고    scopus 로고
    • Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin
    • Koutnikova H, Campuzano V, Foury F, et al. Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin. Nat Genet. 1997;16:345-351.
    • (1997) Nat Genet , vol.16 , pp. 345-351
    • Koutnikova, H.1    Campuzano, V.2    Foury, F.3
  • 46
    • 0000989147 scopus 로고    scopus 로고
    • Aconitase as iron-sulfur protein, enzyme, and iron-regulatory protein
    • Beinert H, Kennedy MC, Stout CD. Aconitase as iron-sulfur protein, enzyme, and iron-regulatory protein. Chem Rev. 1996;96:2335-2374.
    • (1996) Chem Rev , vol.96 , pp. 2335-2374
    • Beinert, H.1    Kennedy, M.C.2    Stout, C.D.3
  • 48
    • 0014988440 scopus 로고
    • Microspectrophotometric and electron microscopic studies of bone marrow in hereditary sideroblastic anaemia
    • Wickramasinghe SN, Fulker MJ, Losowsky MS, Hall R. Microspectrophotometric and electron microscopic studies of bone marrow in hereditary sideroblastic anaemia. Acta Haematol. 1971;45:236-244.
    • (1971) Acta Haematol , vol.45 , pp. 236-244
    • Wickramasinghe, S.N.1    Fulker, M.J.2    Losowsky, M.S.3    Hall, R.4
  • 49
    • 0036269005 scopus 로고    scopus 로고
    • Iron chelators as therapeutic agents for the treatment of cancer
    • Richardson DR. Iron chelators as therapeutic agents for the treatment of cancer. Crit Rev Oncol Hematol. 2002;42:267-281.
    • (2002) Crit Rev Oncol Hematol , vol.42 , pp. 267-281
    • Richardson, D.R.1
  • 50
    • 4444248453 scopus 로고    scopus 로고
    • Novel di-2-pyridyl-derived iron chelators with marked and selective antitumor activity: In vitro and in vivo assessment
    • Yuan J, Lovejoy DB, Richardson DR. Novel di-2-pyridyl-derived iron chelators with marked and selective antitumor activity: in vitro and in vivo assessment. Blood. 2004;104:1450-1458.
    • (2004) Blood , vol.104 , pp. 1450-1458
    • Yuan, J.1    Lovejoy, D.B.2    Richardson, D.R.3
  • 51
    • 0037067692 scopus 로고    scopus 로고
    • Activation of caspase pathways during iron chelator-mediated apoptosis
    • Greene BT, Thorburn J, Willingham MC, et al. Activation of caspase pathways during iron chelator-mediated apoptosis. J Biol Chem. 2002;277:25568-25575.
    • (2002) J Biol Chem , vol.277 , pp. 25568-25575
    • Greene, B.T.1    Thorburn, J.2    Willingham, M.C.3
  • 52
    • 0035353194 scopus 로고    scopus 로고
    • Repression of ferritin expression increases the labile iron pool, oxidative stress, and short-term growth of human erythroleukemia cells
    • Kakhlon O, Gruenbaum Y, Cabantchik ZI. Repression of ferritin expression increases the labile iron pool, oxidative stress, and short-term growth of human erythroleukemia cells. Blood. 2001;97:2863-2871.
    • (2001) Blood , vol.97 , pp. 2863-2871
    • Kakhlon, O.1    Gruenbaum, Y.2    Cabantchik, Z.I.3
  • 53
    • 0034682761 scopus 로고    scopus 로고
    • Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: In vivo role of ferritin ferroxidase activity
    • Cozzi A, Corsi B, Levi S, et al. Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: in vivo role of ferritin ferroxidase activity. J Biol Chem. 2000;275:25122-25129.
    • (2000) J Biol Chem , vol.275 , pp. 25122-25129
    • Cozzi, A.1    Corsi, B.2    Levi, S.3
  • 54
    • 0033571363 scopus 로고    scopus 로고
    • H-ferritin subunit overexpression in erythroid cells reduces the oxidative stress response and induces multidrug resistance properties
    • Epsztejn S, Glickstein H, Picard V, et al. H-ferritin subunit overexpression in erythroid cells reduces the oxidative stress response and induces multidrug resistance properties. Blood. 1999;94:3593-3603.
    • (1999) Blood , vol.94 , pp. 3593-3603
    • Epsztejn, S.1    Glickstein, H.2    Picard, V.3
  • 55
    • 29844457587 scopus 로고    scopus 로고
    • The evolution of iron chelators for the treatment of iron overload disease and cancer
    • Kalinowski DS, Richardson DR. The evolution of iron chelators for the treatment of iron overload disease and cancer. Pharmacol Rev. 2005;57:547-583.
    • (2005) Pharmacol Rev , vol.57 , pp. 547-583
    • Kalinowski, D.S.1    Richardson, D.R.2
  • 56
    • 27744528421 scopus 로고    scopus 로고
    • Molecular mechanisms of iron uptake by cells and the use of iron chelators for the treatment of cancer
    • Richardson DR. Molecular mechanisms of iron uptake by cells and the use of iron chelators for the treatment of cancer. Curr Med Chem. 2005;12:2711-2729.
    • (2005) Curr Med Chem , vol.12 , pp. 2711-2729
    • Richardson, D.R.1


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