메뉴 건너뛰기




Volumn 61, Issue 18, 2013, Pages 1884-1893

Heme levels are increased in human failing hearts

Author keywords

ALAS2; heart failure; heme; iron; mitochondria

Indexed keywords

5 AMINOLEVULINATE SYNTHASE; ERYTHROPOIETIN; HEME; MICRORNA; PROTEIN ALAS2; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 84876958386     PISSN: 07351097     EISSN: 15583597     Source Type: Journal    
DOI: 10.1016/j.jacc.2013.02.012     Document Type: Article
Times cited : (65)

References (54)
  • 1
    • 77649126524 scopus 로고    scopus 로고
    • Heart disease and stroke statistics-2010 update: A report from the American Heart Association
    • D. Lloyd-Jones, R.J. Adams, T.M. Brown, M. Carnethon Heart disease and stroke statistics-2010 update: a report from the American Heart Association Circulation 121 2010 e46 e215
    • (2010) Circulation , vol.121
    • Lloyd-Jones, D.1    Adams, R.J.2    Brown, T.M.3    Carnethon, M.4
  • 2
    • 39749168495 scopus 로고    scopus 로고
    • Tackling heart failure in the twenty-first century
    • J.O. Mudd, D.A. Kass Tackling heart failure in the twenty-first century Nature 451 2008 919 928
    • (2008) Nature , vol.451 , pp. 919-928
    • Mudd, J.O.1    Kass, D.A.2
  • 3
    • 84855598935 scopus 로고    scopus 로고
    • Impaired mitochondrial biogenesis precedes heart failure in right ventricular hypertrophy in congenital heart disease
    • G. Karamanlidis, V. Bautista-Hernandez, F. Fynn-Thompson Impaired mitochondrial biogenesis precedes heart failure in right ventricular hypertrophy in congenital heart disease Circ Heart Fail 4 2011 707 713
    • (2011) Circ Heart Fail , vol.4 , pp. 707-713
    • Karamanlidis, G.1    Bautista-Hernandez, V.2    Fynn-Thompson, F.3
  • 4
    • 84873413349 scopus 로고    scopus 로고
    • Mitochondria as therapeutic target in heart failure
    • M. Bayeva, M. Gheorghiade, H. Ardehali Mitochondria as therapeutic target in heart failure J Am Coll Cardiol 61 2013 599 610
    • (2013) J Am Coll Cardiol , vol.61 , pp. 599-610
    • Bayeva, M.1    Gheorghiade, M.2    Ardehali, H.3
  • 5
    • 58149293410 scopus 로고    scopus 로고
    • PGC-1alpha and ERRalpha target gene downregulation is a signature of the failing human heart
    • S. Sihag, S. Cresci, A.Y. Li, C.C. Sucharov PGC-1alpha and ERRalpha target gene downregulation is a signature of the failing human heart J Mol Cell Cardiol 46 2009 201 212
    • (2009) J Mol Cell Cardiol , vol.46 , pp. 201-212
    • Sihag, S.1    Cresci, S.2    Li, A.Y.3    Sucharov, C.C.4
  • 7
    • 52949153528 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial DNA damage in heart failure
    • H. Tsutsui, S. Kinugawa, S. Matsushima Oxidative stress and mitochondrial DNA damage in heart failure Circ J 72 Suppl A 2008 A31 A37
    • (2008) Circ J , vol.72 , Issue.SUPPL. A
    • Tsutsui, H.1    Kinugawa, S.2    Matsushima, S.3
  • 8
    • 84864296714 scopus 로고    scopus 로고
    • The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism
    • R. Lill, B. Hoffmann, S. Molik, A.J. Pierik The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism Biochim Biophys Acta 1823 2012 1491 1508
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 1491-1508
    • Lill, R.1    Hoffmann, B.2    Molik, S.3    Pierik, A.J.4
  • 9
    • 79955663429 scopus 로고    scopus 로고
    • Control of intracellular heme levels: Heme transporters and heme oxygenases
    • A.A. Khan, J.G. Quigley Control of intracellular heme levels: heme transporters and heme oxygenases Biochim Biophys Acta 1813 2011 668 682
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 668-682
    • Khan, A.A.1    Quigley, J.G.2
  • 12
    • 56749085451 scopus 로고    scopus 로고
    • Body iron metabolism and pathophysiology of iron overload
    • Y. Kohgo, K. Ikuta, T. Ohtake, Y. Torimoto Body iron metabolism and pathophysiology of iron overload Int J Hematol 88 2008 7 15
    • (2008) Int J Hematol , vol.88 , pp. 7-15
    • Kohgo, Y.1    Ikuta, K.2    Ohtake, T.3    Torimoto, Y.4
  • 13
    • 46749083764 scopus 로고    scopus 로고
    • Detection of mitochondrial dysfunction by EPR technique in mouse model of dilated cardiomyopathy
    • M. Elas, J. Bielanska, K. Pustelny Detection of mitochondrial dysfunction by EPR technique in mouse model of dilated cardiomyopathy Free Radic Biol Med 45 2008 321 328
    • (2008) Free Radic Biol Med , vol.45 , pp. 321-328
    • Elas, M.1    Bielanska, J.2    Pustelny, K.3
  • 14
    • 84858199608 scopus 로고    scopus 로고
    • Disruption of ATP-binding cassette B8 in mice leads to cardiomyopathy through a decrease in mitochondrial iron export
    • Y. Ichikawa, M. Bayeva, M. Ghanefar Disruption of ATP-binding cassette B8 in mice leads to cardiomyopathy through a decrease in mitochondrial iron export Proc Natl Acad Sci U S A 109 2012 4152 4157
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 4152-4157
    • Ichikawa, Y.1    Bayeva, M.2    Ghanefar, M.3
  • 15
    • 33845337036 scopus 로고    scopus 로고
    • Iron and iron-responsive proteins in the cardiomyopathy of Friedreich's ataxia
    • S. Michael, S.V. Petrocine, J. Qian Iron and iron-responsive proteins in the cardiomyopathy of Friedreich's ataxia Cerebellum 5 2006 257 267
    • (2006) Cerebellum , vol.5 , pp. 257-267
    • Michael, S.1    Petrocine, S.V.2    Qian, J.3
  • 16
    • 79955468608 scopus 로고    scopus 로고
    • The heart in Friedreich's ataxia: Basic findings and clinical implications
    • R.M. Payne The heart in Friedreich's ataxia: basic findings and clinical implications Prog Pediatr Cardiol 31 2011 103 109
    • (2011) Prog Pediatr Cardiol , vol.31 , pp. 103-109
    • Payne, R.M.1
  • 17
    • 33644748145 scopus 로고    scopus 로고
    • Mitoferrin is essential for erythroid iron assimilation
    • G.C. Shaw, J.J. Cope, L. Li, K. Corson Mitoferrin is essential for erythroid iron assimilation Nature 440 2006 96 100
    • (2006) Nature , vol.440 , pp. 96-100
    • Shaw, G.C.1    Cope, J.J.2    Li, L.3    Corson, K.4
  • 18
    • 59449083869 scopus 로고    scopus 로고
    • Regulation of mitochondrial iron import through differential turnover of mitoferrin 1 and mitoferrin 2
    • P.N. Paradkar, K.B. Zumbrennen, B.H. Paw, D.M. Ward Regulation of mitochondrial iron import through differential turnover of mitoferrin 1 and mitoferrin 2 Mol Cell Biol 29 2009 1007 1016
    • (2009) Mol Cell Biol , vol.29 , pp. 1007-1016
    • Paradkar, P.N.1    Zumbrennen, K.B.2    Paw, B.H.3    Ward, D.M.4
  • 19
    • 79952162002 scopus 로고    scopus 로고
    • Regulation of cellular iron metabolism
    • J. Wang, K. Pantopoulos Regulation of cellular iron metabolism Biochem J 434 2011 365 381
    • (2011) Biochem J , vol.434 , pp. 365-381
    • Wang, J.1    Pantopoulos, K.2
  • 20
    • 34948858043 scopus 로고    scopus 로고
    • Heme as a magnificent molecule with multiple missions: Heme determines its own fate and governs cellular homeostasis
    • K. Furuyama, K. Kaneko, P.D. Vargas Heme as a magnificent molecule with multiple missions: heme determines its own fate and governs cellular homeostasis Tohoku J Exp Med 213 2007 1 16
    • (2007) Tohoku J Exp Med , vol.213 , pp. 1-16
    • Furuyama, K.1    Kaneko, K.2    Vargas, P.D.3
  • 21
    • 84859802748 scopus 로고    scopus 로고
    • Heme oxygenase-1 in inflammation and cardiovascular disease
    • M.L. Wu, Y.C. Ho, C.Y. Lin, S.F. Yet Heme oxygenase-1 in inflammation and cardiovascular disease Am J Cardiovasc Dis 1 2011 150 158
    • (2011) Am J Cardiovasc Dis , vol.1 , pp. 150-158
    • Wu, M.L.1    Ho, Y.C.2    Lin, C.Y.3    Yet, S.F.4
  • 22
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • T.A. Rouault, W.H. Tong Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis Nat Rev Mol Cell Biol 6 2005 345 351
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.H.2
  • 23
    • 43749114744 scopus 로고    scopus 로고
    • Cellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis
    • A. Hausmann, B. Samans, R. Lill, U. Muhlenhoff Cellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis J Biol Chem 283 2008 8318 8330
    • (2008) J Biol Chem , vol.283 , pp. 8318-8330
    • Hausmann, A.1    Samans, B.2    Lill, R.3    Muhlenhoff, U.4
  • 24
    • 14944387002 scopus 로고    scopus 로고
    • Iron trafficking in the mitochondrion: Novel pathways revealed by disease
    • I. Napier, P. Ponka, D.R. Richardson Iron trafficking in the mitochondrion: novel pathways revealed by disease Blood 105 2005 1867 1874
    • (2005) Blood , vol.105 , pp. 1867-1874
    • Napier, I.1    Ponka, P.2    Richardson, D.R.3
  • 25
    • 0021719812 scopus 로고
    • Heme regulation of HeLa cell transferrin receptor number
    • J.H. Ward, I. Jordan, J.P. Kushner, J. Kaplan Heme regulation of HeLa cell transferrin receptor number J Biol Chem 259 1984 13235 13240
    • (1984) J Biol Chem , vol.259 , pp. 13235-13240
    • Ward, J.H.1    Jordan, I.2    Kushner, J.P.3    Kaplan, J.4
  • 26
    • 59049093631 scopus 로고    scopus 로고
    • Blockade of the erbB2 receptor induces cardiomyocyte death through mitochondrial and reactive oxygen species-dependent pathways
    • L.I. Gordon, M.A. Burke, A.T. Singh Blockade of the erbB2 receptor induces cardiomyocyte death through mitochondrial and reactive oxygen species-dependent pathways J Biol Chem 284 2009 2080 2087
    • (2009) J Biol Chem , vol.284 , pp. 2080-2087
    • Gordon, L.I.1    Burke, M.A.2    Singh, A.T.3
  • 27
    • 0035896205 scopus 로고    scopus 로고
    • Mitochondrial DNA damage and dysfunction associated with oxidative stress in failing hearts after myocardial infarction
    • T. Ide, H. Tsutsui, S. Hayashidani Mitochondrial DNA damage and dysfunction associated with oxidative stress in failing hearts after myocardial infarction Circ Res 88 2001 529 535
    • (2001) Circ Res , vol.88 , pp. 529-535
    • Ide, T.1    Tsutsui, H.2    Hayashidani, S.3
  • 28
    • 0029361568 scopus 로고
    • Impaired mitochondrial function in idiopathic dilated cardiomyopathy: Biochemical and molecular analysis
    • J. Marin-Garcia, M.J. Goldenthal, M.E. Pierpont, R. Ananthakrishnan Impaired mitochondrial function in idiopathic dilated cardiomyopathy: biochemical and molecular analysis J Card Fail 1 1995 285 291
    • (1995) J Card Fail , vol.1 , pp. 285-291
    • Marin-Garcia, J.1    Goldenthal, M.J.2    Pierpont, M.E.3    Ananthakrishnan, R.4
  • 29
    • 0033973712 scopus 로고    scopus 로고
    • The heme synthesis and degradation pathways: Role in oxidant sensitivity Heme oxygenase has both pro- and antioxidant properties
    • S.W. Ryter, R.M. Tyrrell The heme synthesis and degradation pathways: role in oxidant sensitivity Heme oxygenase has both pro- and antioxidant properties Free Radic Biol Med 28 2000 289 309
    • (2000) Free Radic Biol Med , vol.28 , pp. 289-309
    • Ryter, S.W.1    Tyrrell, R.M.2
  • 30
    • 78650842623 scopus 로고    scopus 로고
    • Egr-1 regulates the transcriptional repression of mouse delta-aminolevulinic acid synthase 1 by heme
    • S. Gotoh, T. Nakamura, T. Kataoka, S. Taketani Egr-1 regulates the transcriptional repression of mouse delta-aminolevulinic acid synthase 1 by heme Gene 472 2011 28 36
    • (2011) Gene , vol.472 , pp. 28-36
    • Gotoh, S.1    Nakamura, T.2    Kataoka, T.3    Taketani, S.4
  • 31
    • 0034681996 scopus 로고    scopus 로고
    • Transcriptional regulation of the murine erythroid-specific 5-aminolevulinate synthase gene
    • M.F. Kramer, P. Gunaratne, G.C. Ferreira Transcriptional regulation of the murine erythroid-specific 5-aminolevulinate synthase gene Gene 247 2000 153 166
    • (2000) Gene , vol.247 , pp. 153-166
    • Kramer, M.F.1    Gunaratne, P.2    Ferreira, G.C.3
  • 32
    • 79951635887 scopus 로고    scopus 로고
    • Hypoxic induction of human erythroid-specific delta-aminolevulinate synthase mediated by hypoxia-inducible factor 1
    • F.L. Zhang, G.M. Shen, X.L. Liu Hypoxic induction of human erythroid-specific delta-aminolevulinate synthase mediated by hypoxia-inducible factor 1 Biochemistry 50 2011 1194 1202
    • (2011) Biochemistry , vol.50 , pp. 1194-1202
    • Zhang, F.L.1    Shen, G.M.2    Liu, X.L.3
  • 33
    • 0032832182 scopus 로고    scopus 로고
    • Regulation of erythroid 5-aminolevulinate synthase expression during erythropoiesis
    • T.J. Sadlon, T. Dell'Oso, K.H. Surinya, B.K. May Regulation of erythroid 5-aminolevulinate synthase expression during erythropoiesis Int J Biochem Cell Biol 31 1999 1153 1167
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 1153-1167
    • Sadlon, T.J.1    Dell'Oso, T.2    Surinya, K.H.3    May, B.K.4
  • 34
    • 84885617020 scopus 로고    scopus 로고
    • Suppression of erythropoiesis in patients with chronic heart failure and anaemia of unknown origin: Evidence of an immune basis
    • [E-pub ahead of print]
    • D.O. Okonko, S.B. Marley, S.D. Anker Suppression of erythropoiesis in patients with chronic heart failure and anaemia of unknown origin: evidence of an immune basis Int J Cardiol 2011 [E-pub ahead of print]; http://dx.doi.org/10. 1016/j.ijcard.2011.11.081
    • (2011) Int J Cardiol
    • Okonko, D.O.1    Marley, S.B.2    Anker, S.D.3
  • 35
    • 24644520622 scopus 로고    scopus 로고
    • Expression of the erythropoietin receptor in human heart
    • R. Depping, K. Kawakami, H. Ocker Expression of the erythropoietin receptor in human heart J Thorac Cardiovasc Surg 130 2005 877 878
    • (2005) J Thorac Cardiovasc Surg , vol.130 , pp. 877-878
    • Depping, R.1    Kawakami, K.2    Ocker, H.3
  • 36
    • 0027327484 scopus 로고
    • JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin
    • B.A. Witthuhn, F.W. Quelle, O. Silvennoinen JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin Cell 74 1993 227 236
    • (1993) Cell , vol.74 , pp. 227-236
    • Witthuhn, B.A.1    Quelle, F.W.2    Silvennoinen, O.3
  • 38
    • 19444386445 scopus 로고    scopus 로고
    • Free heme toxicity and its detoxification systems in humans
    • S. Kumar, U. Bandyopadhyay Free heme toxicity and its detoxification systems in humans Toxicol Lett 157 2005 175 188
    • (2005) Toxicol Lett , vol.157 , pp. 175-188
    • Kumar, S.1    Bandyopadhyay, U.2
  • 39
    • 38349169664 scopus 로고    scopus 로고
    • Mechanisms of post-transcriptional regulation by microRNAs: Are the answers in sight?
    • W. Filipowicz, S.N. Bhattacharyya, N. Sonenberg Mechanisms of post-transcriptional regulation by microRNAs: are the answers in sight? Nat Rev Genet 9 2008 102 114
    • (2008) Nat Rev Genet , vol.9 , pp. 102-114
    • Filipowicz, W.1    Bhattacharyya, S.N.2    Sonenberg, N.3
  • 40
    • 79960601913 scopus 로고    scopus 로고
    • Myocardial and systemic iron depletion in heart failure implications for anemia accompanying heart failure
    • M.T. Maeder, O. Khammy, C. dos Remedios, D.M. Kaye Myocardial and systemic iron depletion in heart failure implications for anemia accompanying heart failure J Am Coll Cardiol 58 2011 474 480
    • (2011) J Am Coll Cardiol , vol.58 , pp. 474-480
    • Maeder, M.T.1    Khammy, O.2    Dos Remedios, C.3    Kaye, D.M.4
  • 41
    • 82755179957 scopus 로고    scopus 로고
    • Heme oxygenase-1 induction protects the heart and modulates cellular and extracellular remodelling after myocardial infarction in rats
    • P. Lakkisto, J.M. Siren, V. Kyto Heme oxygenase-1 induction protects the heart and modulates cellular and extracellular remodelling after myocardial infarction in rats Exp Biol Med (Maywood) 236 2011 1437 1448
    • (2011) Exp Biol Med (Maywood) , vol.236 , pp. 1437-1448
    • Lakkisto, P.1    Siren, J.M.2    Kyto, V.3
  • 42
    • 80051962945 scopus 로고    scopus 로고
    • A central role of heme oxygenase-1 in cardiovascular protection
    • M.L. Wu, Y.C. Ho, S.F. Yet A central role of heme oxygenase-1 in cardiovascular protection Antioxid Redox Signal 15 2011 1835 1846
    • (2011) Antioxid Redox Signal , vol.15 , pp. 1835-1846
    • Wu, M.L.1    Ho, Y.C.2    Yet, S.F.3
  • 43
  • 44
    • 72449156527 scopus 로고    scopus 로고
    • Ferric carboxymaltose in patients with heart failure and iron deficiency
    • S.D. Anker, J. Comin Colet, G. Filippatos Ferric carboxymaltose in patients with heart failure and iron deficiency N Engl J Med 361 2009 2436 2448
    • (2009) N Engl J Med , vol.361 , pp. 2436-2448
    • Anker, S.D.1    Comin Colet, J.2    Filippatos, G.3
  • 45
    • 38449083833 scopus 로고    scopus 로고
    • Ito Haeme-regulated degradation of delta-aminolevulinate synthase 1 in rat liver mitochondria
    • K. Yoshino, H. Munakata, O. Kuge, Ito Haeme-regulated degradation of delta-aminolevulinate synthase 1 in rat liver mitochondria J Biochem 142 2007 453 458
    • (2007) J Biochem , vol.142 , pp. 453-458
    • Yoshino, K.1    Munakata, H.2    Kuge, O.3
  • 46
    • 55649122540 scopus 로고    scopus 로고
    • Differential regulation of human ALAS1 mRNA and protein levels by heme and cobalt protoporphyrin
    • J. Zheng, Y. Shan, R.W. Lambrecht Differential regulation of human ALAS1 mRNA and protein levels by heme and cobalt protoporphyrin Mol Cell Biochem 319 2008 153 161
    • (2008) Mol Cell Biochem , vol.319 , pp. 153-161
    • Zheng, J.1    Shan, Y.2    Lambrecht, R.W.3
  • 48
    • 0344413737 scopus 로고    scopus 로고
    • The major splice variant of human 5-aminolevulinate synthase-2 contributes significantly to erythroid heme biosynthesis
    • T.C. Cox, T.J. Sadlon, Q.P. Schwarz, C.S. Matthews The major splice variant of human 5-aminolevulinate synthase-2 contributes significantly to erythroid heme biosynthesis Int J Biochem Cell Biol 36 2004 281 295
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 281-295
    • Cox, T.C.1    Sadlon, T.J.2    Schwarz, Q.P.3    Matthews, C.S.4
  • 49
    • 60349106841 scopus 로고    scopus 로고
    • Hypoxia induces erythroid-specific 5-aminolevulinate synthase expression in human erythroid cells through transforming growth factor-beta signaling
    • K. Kaneko, K. Furuyama, H. Aburatani, S. Shibahara Hypoxia induces erythroid-specific 5-aminolevulinate synthase expression in human erythroid cells through transforming growth factor-beta signaling FEBS J 276 2009 1370 1382
    • (2009) FEBS J , vol.276 , pp. 1370-1382
    • Kaneko, K.1    Furuyama, K.2    Aburatani, H.3    Shibahara, S.4
  • 50
    • 82955167943 scopus 로고    scopus 로고
    • The role of microRNA-145 in human embryonic stem cell differentiation into vascular cells
    • S. Yamaguchi, K. Yamahara, K. Homma, S. Suzuki The role of microRNA-145 in human embryonic stem cell differentiation into vascular cells Atherosclerosis 219 2011 468 474
    • (2011) Atherosclerosis , vol.219 , pp. 468-474
    • Yamaguchi, S.1    Yamahara, K.2    Homma, K.3    Suzuki, S.4
  • 51
    • 79959691239 scopus 로고    scopus 로고
    • MiR-143 and miR-145: Molecular keys to switch the phenotype of vascular smooth muscle cells
    • A.Y. Rangrez, Z.A. Massy, V. Metzinger-Le Meuth, L. Metzinger miR-143 and miR-145: molecular keys to switch the phenotype of vascular smooth muscle cells Circ Cardiovasc Genet 4 2011 197 205
    • (2011) Circ Cardiovasc Genet , vol.4 , pp. 197-205
    • Rangrez, A.Y.1    Massy, Z.A.2    Metzinger-Le Meuth, V.3    Metzinger, L.4
  • 52
    • 77950818716 scopus 로고    scopus 로고
    • MicroRNA145 targets BNIP3 and suppresses prostate cancer progression
    • X. Chen, J. Gong, H. Zeng, N. Chen MicroRNA145 targets BNIP3 and suppresses prostate cancer progression Cancer Res 70 2010 2728 2738
    • (2010) Cancer Res , vol.70 , pp. 2728-2738
    • Chen, X.1    Gong, J.2    Zeng, H.3    Chen, N.4
  • 53
    • 67649373019 scopus 로고    scopus 로고
    • Mechanism of growth inhibition by MicroRNA 145: The role of the IGF-I receptor signaling pathway
    • G. La Rocca, M. Badin, B. Shi Mechanism of growth inhibition by MicroRNA 145: the role of the IGF-I receptor signaling pathway J Cell Physiol 220 2009 485 491
    • (2009) J Cell Physiol , vol.220 , pp. 485-491
    • La Rocca, G.1    Badin, M.2    Shi, B.3
  • 54
    • 57049156135 scopus 로고    scopus 로고
    • Reverse changes in cardiac substrate oxidation in dogs recovering from heart failure
    • K. Qanud, M. Mamdani, M. Pepe Reverse changes in cardiac substrate oxidation in dogs recovering from heart failure Am J Physiol Heart Circ Physiol 295 2008 H2098 H2105
    • (2008) Am J Physiol Heart Circ Physiol , vol.295
    • Qanud, K.1    Mamdani, M.2    Pepe, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.