메뉴 건너뛰기




Volumn 58, Issue 8, 2014, Pages 1721-1738

Iron, oxidative stress, and redox signaling in the cardiovascular system

Author keywords

Cardiovascular; Disease; Iron; Oxidative stress; Redox

Indexed keywords

IRON INTAKE; OXIDIZING AGENT;

EID: 84905386350     PISSN: 16134125     EISSN: 16134133     Source Type: Journal    
DOI: 10.1002/mnfr.201400036     Document Type: Article
Times cited : (66)

References (146)
  • 1
    • 45549086544 scopus 로고    scopus 로고
    • Regional heterogeneity of decreased myocardial norepinephrine and increased lipid peroxidation levels in patients with end-stage failing heart secondary to dilated or ischemic cardiomyopathy
    • Rochette, L., Tatou, E., Vergely, C., Maupoil, V. et al., Regional heterogeneity of decreased myocardial norepinephrine and increased lipid peroxidation levels in patients with end-stage failing heart secondary to dilated or ischemic cardiomyopathy. J. Heart Lung Transplant. 2008, 27, 767-774.
    • (2008) J. Heart Lung Transplant. , vol.27 , pp. 767-774
    • Rochette, L.1    Tatou, E.2    Vergely, C.3    Maupoil, V.4
  • 3
    • 79959452177 scopus 로고    scopus 로고
    • Atrial and vascular oxidative stress in patients with heart failure
    • Rochette, L., Tatou, E., Maupoil, V., Zeller, M. et al., Atrial and vascular oxidative stress in patients with heart failure. Cell. Physiol. Biochem. 2011, 27, 497-502.
    • (2011) Cell. Physiol. Biochem. , vol.27 , pp. 497-502
    • Rochette, L.1    Tatou, E.2    Maupoil, V.3    Zeller, M.4
  • 4
    • 84884950378 scopus 로고    scopus 로고
    • The complex interplay of iron metabolism, reactive oxygen species, and reactive nitrogen species: insights into the potential of various iron therapies to induce oxidative and nitrosative stress
    • Koskenkorva-Frank, T. S., Weiss, G., Koppenol, W. H., Burckhardt, S., The complex interplay of iron metabolism, reactive oxygen species, and reactive nitrogen species: insights into the potential of various iron therapies to induce oxidative and nitrosative stress. Free Radic. Biol. Med. 2013, 65, 1174-1194.
    • (2013) Free Radic. Biol. Med. , vol.65 , pp. 1174-1194
    • Koskenkorva-Frank, T.S.1    Weiss, G.2    Koppenol, W.H.3    Burckhardt, S.4
  • 6
    • 84857373097 scopus 로고    scopus 로고
    • Non-transferrin bound iron: a key role in iron overload and iron toxicity
    • Brissot, P., Ropert, M., Le Lan, C., Loreal, O., Non-transferrin bound iron: a key role in iron overload and iron toxicity. Biochim. Biophys. Acta 2012, 1820, 403-410.
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 403-410
    • Brissot, P.1    Ropert, M.2    Le Lan, C.3    Loreal, O.4
  • 7
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer, F. Q., Buettner, G. R., Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic. Biol. Med. 2001, 30, 1191-1212.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 8
    • 71849114694 scopus 로고    scopus 로고
    • Oxidative stress and human diseases: origin, link, measurement, mechanisms, and biomarkers
    • Giustarini, D., Dalle-Donne, I., Tsikas, D., Rossi, R., Oxidative stress and human diseases: origin, link, measurement, mechanisms, and biomarkers. Crit. Rev. Clin. Lab. Sci. 2009, 46, 241-281.
    • (2009) Crit. Rev. Clin. Lab. Sci. , vol.46 , pp. 241-281
    • Giustarini, D.1    Dalle-Donne, I.2    Tsikas, D.3    Rossi, R.4
  • 9
    • 0029194750 scopus 로고
    • The definition and measurement of antioxidants in biological systems
    • Halliwell, B., Gutteridge, J. M., The definition and measurement of antioxidants in biological systems. Free Radic. Biol. Med. 1995, 18, 125-126.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 125-126
    • Halliwell, B.1    Gutteridge, J.M.2
  • 10
    • 0344925526 scopus 로고    scopus 로고
    • Identification and quantification of free radicals during myocardial ischemia and reperfusion using electron paramagnetic resonance spectroscopy
    • Vergely, C., Maupoil, V., Clermont, G., Bril, A. et al., Identification and quantification of free radicals during myocardial ischemia and reperfusion using electron paramagnetic resonance spectroscopy. Arch. Biochem. Biophys. 2003, 420, 209-216.
    • (2003) Arch. Biochem. Biophys. , vol.420 , pp. 209-216
    • Vergely, C.1    Maupoil, V.2    Clermont, G.3    Bril, A.4
  • 11
    • 83455185433 scopus 로고    scopus 로고
    • Reactive oxygen species and endothelial function-role of nitric oxide synthase uncoupling and Nox family nicotinamide adenine dinucleotide phosphate oxidases
    • Montezano, A. C., Touyz, R. M., Reactive oxygen species and endothelial function-role of nitric oxide synthase uncoupling and Nox family nicotinamide adenine dinucleotide phosphate oxidases. Basic Clin. Pharmacol. Toxicol. 2012, 110, 87-94.
    • (2012) Basic Clin. Pharmacol. Toxicol. , vol.110 , pp. 87-94
    • Montezano, A.C.1    Touyz, R.M.2
  • 12
    • 33745234267 scopus 로고    scopus 로고
    • NADPH oxidases are in part responsible for increased cardiovascular superoxide production during aging
    • Oudot, A., Martin, C., Busseuil, D., Vergely, C. et al., NADPH oxidases are in part responsible for increased cardiovascular superoxide production during aging. Free Radic. Biol. Med. 2006, 40, 2214-2222.
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 2214-2222
    • Oudot, A.1    Martin, C.2    Busseuil, D.3    Vergely, C.4
  • 13
    • 58149229573 scopus 로고    scopus 로고
    • Effects of angiotensin-1 converting enzyme inhibition on oxidative stress and bradykinin receptor expression during doxorubicin-induced cardiomyopathy in rats
    • Richard, C., Lauzier, B., Delemasure, S., Talbot, S. et al., Effects of angiotensin-1 converting enzyme inhibition on oxidative stress and bradykinin receptor expression during doxorubicin-induced cardiomyopathy in rats. J. Cardiovasc. Pharmacol. 2008, 52, 278-285.
    • (2008) J. Cardiovasc. Pharmacol. , vol.52 , pp. 278-285
    • Richard, C.1    Lauzier, B.2    Delemasure, S.3    Talbot, S.4
  • 14
    • 33746611555 scopus 로고    scopus 로고
    • Modulation of vascular smooth muscle signaling by reactive oxygen species
    • Lyle, A. N., Griendling, K. K., Modulation of vascular smooth muscle signaling by reactive oxygen species. Physiology 2006, 21, 269-280.
    • (2006) Physiology , vol.21 , pp. 269-280
    • Lyle, A.N.1    Griendling, K.K.2
  • 16
    • 79955047965 scopus 로고    scopus 로고
    • Nitric oxide signalling in the regulation of cardiovascular and platelet function
    • Gkaliagkousi, E., Ferro, A., Nitric oxide signalling in the regulation of cardiovascular and platelet function. Front. Biosci. 2011, 16, 1873-1897.
    • (2011) Front. Biosci. , vol.16 , pp. 1873-1897
    • Gkaliagkousi, E.1    Ferro, A.2
  • 17
    • 84887987937 scopus 로고    scopus 로고
    • Arginine and nitric oxide synthase: regulatory mechanisms and cardiovascular aspects
    • Lorin, J., Zeller, M., Guilland, J. C., Cottin, Y. et al., Arginine and nitric oxide synthase: regulatory mechanisms and cardiovascular aspects. Mol. Nutr. Food Res. 2013.
    • (2013) Mol. Nutr. Food Res.
    • Lorin, J.1    Zeller, M.2    Guilland, J.C.3    Cottin, Y.4
  • 18
    • 84878232006 scopus 로고    scopus 로고
    • Redox signaling in cardiovascular health and disease
    • Madamanchi, N. R., Runge, M. S., Redox signaling in cardiovascular health and disease. Free Radic. Biol. Med. 2013, 61C, 473-501.
    • (2013) Free Radic. Biol. Med. , vol.61 C , pp. 473-501
    • Madamanchi, N.R.1    Runge, M.S.2
  • 19
    • 0034682916 scopus 로고    scopus 로고
    • Lipid peroxidation, antioxidants and cardiovascular disease: how should we move forward
    • Halliwell, B., Lipid peroxidation, antioxidants and cardiovascular disease: how should we move forward? Cardiovasc. Res. 2000, 47, 410-418.
    • (2000) Cardiovasc. Res. , vol.47 , pp. 410-418
    • Halliwell, B.1
  • 20
    • 74349096419 scopus 로고    scopus 로고
    • Antioxidant properties of an endogenous thiol: alpha-lipoic acid, useful in the prevention of cardiovascular diseases
    • Ghibu, S., Richard, C., Vergely, C., Zeller, M. et al., Antioxidant properties of an endogenous thiol: alpha-lipoic acid, useful in the prevention of cardiovascular diseases. J. Cardiovasc. Pharmacol. 2009, 54, 391-398.
    • (2009) J. Cardiovasc. Pharmacol. , vol.54 , pp. 391-398
    • Ghibu, S.1    Richard, C.2    Vergely, C.3    Zeller, M.4
  • 21
    • 84872146192 scopus 로고    scopus 로고
    • Direct and indirect antioxidant properties of alpha-lipoic acid and therapeutic potential
    • Rochette, L., Ghibu, S., Richard, C., Zeller, M. et al., Direct and indirect antioxidant properties of alpha-lipoic acid and therapeutic potential. Mol. Nutr. Food. Res. 2013, 57, 114-125.
    • (2013) Mol. Nutr. Food. Res. , vol.57 , pp. 114-125
    • Rochette, L.1    Ghibu, S.2    Richard, C.3    Zeller, M.4
  • 22
    • 84878525986 scopus 로고    scopus 로고
    • Oxidative stress in vascular disease and its pharmacological prevention
    • Li, H., Horke, S., Forstermann, U., Oxidative stress in vascular disease and its pharmacological prevention. Trends Pharmacol. Sci. 2013, 34, 313-319.
    • (2013) Trends Pharmacol. Sci. , vol.34 , pp. 313-319
    • Li, H.1    Horke, S.2    Forstermann, U.3
  • 23
    • 80054072517 scopus 로고    scopus 로고
    • Formation and signaling actions of electrophilic lipids
    • Schopfer, F. J., Cipollina, C., Freeman, B. A., Formation and signaling actions of electrophilic lipids. Chem. Rev. 2011, 111, 5997-6021.
    • (2011) Chem. Rev. , vol.111 , pp. 5997-6021
    • Schopfer, F.J.1    Cipollina, C.2    Freeman, B.A.3
  • 24
    • 0035909483 scopus 로고    scopus 로고
    • Mutagenicity of the malondialdehyde oligomerization products 2-(3'-oxo-1'-propenyl)-malondialdehyde and 2,4-dihydroxymethylene-3-(2,2-dimethoxyethyl)glutaraldehyde in Salmonella
    • Riggins, J. N., Marnett, L. J., Mutagenicity of the malondialdehyde oligomerization products 2-(3'-oxo-1'-propenyl)-malondialdehyde and 2, 4-dihydroxymethylene-3-(2, 2-dimethoxyethyl)glutaraldehyde in Salmonella. Mutat. Res. 2001, 497, 153-157.
    • (2001) Mutat. Res. , vol.497 , pp. 153-157
    • Riggins, J.N.1    Marnett, L.J.2
  • 25
    • 79952442409 scopus 로고    scopus 로고
    • Free radicals and antioxidants-quo vadis?
    • Halliwell, B., Free radicals and antioxidants-quo vadis? Trends Pharmacol. Sci. 2011, 32, 125-130.
    • (2011) Trends Pharmacol. Sci. , vol.32 , pp. 125-130
    • Halliwell, B.1
  • 26
    • 0027292789 scopus 로고
    • Interaction of vitamin C and vitamin E during free radical stress in plasma: an ESR study
    • Sharma, M. K., Buettner, G. R., Interaction of vitamin C and vitamin E during free radical stress in plasma: an ESR study. Free Radic. Biol. Med. 1993, 14, 649-653.
    • (1993) Free Radic. Biol. Med. , vol.14 , pp. 649-653
    • Sharma, M.K.1    Buettner, G.R.2
  • 27
    • 84872679855 scopus 로고    scopus 로고
    • Transition metals and mitochondrial metabolism in the heart
    • Rines, A. K., Ardehali, H., Transition metals and mitochondrial metabolism in the heart. J. Mol. Cell. Cardiol. 2013, 55, 50-57.
    • (2013) J. Mol. Cell. Cardiol. , vol.55 , pp. 50-57
    • Rines, A.K.1    Ardehali, H.2
  • 28
    • 84871061522 scopus 로고    scopus 로고
    • Lysosomal iron, iron chelation, and cell death
    • Terman, A., Kurz, T., Lysosomal iron, iron chelation, and cell death. Antioxid. Redox. Signal. 2013, 18, 888-898.
    • (2013) Antioxid. Redox. Signal. , vol.18 , pp. 888-898
    • Terman, A.1    Kurz, T.2
  • 29
    • 24044481966 scopus 로고    scopus 로고
    • Copper, oxidative stress, and human health
    • Uriu-Adams, J. Y., Keen, C. L., Copper, oxidative stress, and human health. Mol. Aspects Med. 2005, 26, 268-298.
    • (2005) Mol. Aspects Med. , vol.26 , pp. 268-298
    • Uriu-Adams, J.Y.1    Keen, C.L.2
  • 30
    • 54149096363 scopus 로고    scopus 로고
    • Manganese superoxide dismutase and aldehyde dehydrogenase deficiency increase mitochondrial oxidative stress and aggravate age-dependent vascular dysfunction
    • Wenzel, P., Schuhmacher, S., Kienhofer, J., Muller, J. et al., Manganese superoxide dismutase and aldehyde dehydrogenase deficiency increase mitochondrial oxidative stress and aggravate age-dependent vascular dysfunction. Cardiovasc. Res. 2008, 80, 280-289.
    • (2008) Cardiovasc. Res. , vol.80 , pp. 280-289
    • Wenzel, P.1    Schuhmacher, S.2    Kienhofer, J.3    Muller, J.4
  • 32
    • 84870715491 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin reductase in relation to reversible S-nitrosylation
    • Sengupta, R., Holmgren, A., Thioredoxin and thioredoxin reductase in relation to reversible S-nitrosylation. Antioxid. Redox. Signal. 2013, 18, 259-269.
    • (2013) Antioxid. Redox. Signal. , vol.18 , pp. 259-269
    • Sengupta, R.1    Holmgren, A.2
  • 33
    • 84856556021 scopus 로고    scopus 로고
    • There is no evidence that mitochondria are the main source of reactive oxygen species in mammalian cells
    • Brown, G. C., Borutaite, V., There is no evidence that mitochondria are the main source of reactive oxygen species in mammalian cells. Mitochondrion 2012, 12, 1-4.
    • (2012) Mitochondrion , vol.12 , pp. 1-4
    • Brown, G.C.1    Borutaite, V.2
  • 34
    • 80054978144 scopus 로고    scopus 로고
    • Mitochondrial approaches to protect against cardiac ischemia and reperfusion injury
    • Camara, A. K., Bienengraeber, M., Stowe, D. F., Mitochondrial approaches to protect against cardiac ischemia and reperfusion injury. Front. Physiol. 2011, 2, 13.
    • (2011) Front. Physiol. , vol.2 , pp. 13
    • Camara, A.K.1    Bienengraeber, M.2    Stowe, D.F.3
  • 35
    • 84863738048 scopus 로고    scopus 로고
    • Molecular mechanisms of superoxide production by the mitochondrial respiratory chain
    • Drose, S., Brandt, U., Molecular mechanisms of superoxide production by the mitochondrial respiratory chain. Adv. Exp. Med. Biol. 2012, 748, 145-169.
    • (2012) Adv. Exp. Med. Biol. , vol.748 , pp. 145-169
    • Drose, S.1    Brandt, U.2
  • 36
  • 37
    • 84881555646 scopus 로고    scopus 로고
    • Mitochondrial permeability transition and cell death: the role of cyclophilin d
    • Javadov, S., Kuznetsov, A., Mitochondrial permeability transition and cell death: the role of cyclophilin d. Front. Physiol. 2013, 4, 76.
    • (2013) Front. Physiol. , vol.4 , pp. 76
    • Javadov, S.1    Kuznetsov, A.2
  • 38
    • 0035923615 scopus 로고    scopus 로고
    • Identification of a neuronal nitric oxide synthase in isolated cardiac mitochondria using electrochemical detection
    • Kanai, A. J., Pearce, L. L., Clemens, P. R., Birder, L. A. et al., Identification of a neuronal nitric oxide synthase in isolated cardiac mitochondria using electrochemical detection. Proc. Natl. Acad. Sci. USA 2001, 98, 14126-14131.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14126-14131
    • Kanai, A.J.1    Pearce, L.L.2    Clemens, P.R.3    Birder, L.A.4
  • 39
    • 0037163081 scopus 로고    scopus 로고
    • Recycling of RNA binding iron regulatory protein 1 into an aconitase after nitric oxide removal depends on mitochondrial ATP
    • Bouton, C., Chauveau, M. J., Lazereg, S., Drapier, J. C., Recycling of RNA binding iron regulatory protein 1 into an aconitase after nitric oxide removal depends on mitochondrial ATP. J. Biol. Chem. 2002, 277, 31220-31227.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31220-31227
    • Bouton, C.1    Chauveau, M.J.2    Lazereg, S.3    Drapier, J.C.4
  • 40
    • 84870545221 scopus 로고    scopus 로고
    • Strategic localization of heart mitochondrial NOS: a review of the evidence
    • Zaobornyj, T., Ghafourifar, P., Strategic localization of heart mitochondrial NOS: a review of the evidence. Am. J. Physiol. Heart Circ. Physiol. 2012, 303, H1283-H1293.
    • (2012) Am. J. Physiol. Heart Circ. Physiol. , vol.303
    • Zaobornyj, T.1    Ghafourifar, P.2
  • 41
    • 14744278436 scopus 로고    scopus 로고
    • Anemia of chronic disease
    • Weiss, G., Goodnough, L. T., Anemia of chronic disease. N. Engl. J. Med. 2005, 352, 1011-1023.
    • (2005) N. Engl. J. Med. , vol.352 , pp. 1011-1023
    • Weiss, G.1    Goodnough, L.T.2
  • 42
    • 77956806828 scopus 로고    scopus 로고
    • The efficacy and safety of current intravenous iron preparations for the management of iron-deficiency anaemia: a review
    • Qunibi, W. Y., The efficacy and safety of current intravenous iron preparations for the management of iron-deficiency anaemia: a review. Arzneimittelforschung 2010, 60, 399-412.
    • (2010) Arzneimittelforschung , vol.60 , pp. 399-412
    • Qunibi, W.Y.1
  • 43
    • 0036431480 scopus 로고    scopus 로고
    • Clinical implications of changes in the modern diet: iron intake, absorption and status
    • Heath, A. L., Fairweather-Tait, S. J., Clinical implications of changes in the modern diet: iron intake, absorption and status. Best Pract. Res. Clin. Haematol. 2002, 15, 225-241.
    • (2002) Best Pract. Res. Clin. Haematol. , vol.15 , pp. 225-241
    • Heath, A.L.1    Fairweather-Tait, S.J.2
  • 44
    • 84882957091 scopus 로고    scopus 로고
    • Combined treatment of mulberry leaf and fruit extract ameliorates obesity-related inflammation and oxidative stress in high fat diet-induced obese mice
    • Lim, H. H., Yang, S. J., Kim, Y., Lee, M. et al., Combined treatment of mulberry leaf and fruit extract ameliorates obesity-related inflammation and oxidative stress in high fat diet-induced obese mice. J. Med. Food 2013, 16, 673-680.
    • (2013) J. Med. Food , vol.16 , pp. 673-680
    • Lim, H.H.1    Yang, S.J.2    Kim, Y.3    Lee, M.4
  • 45
    • 79953781994 scopus 로고    scopus 로고
    • Intestinal iron absorption: regulation by dietary & systemic factors
    • Sharp, P. A., Intestinal iron absorption: regulation by dietary & systemic factors. Int. J. Vitam. Nutr. Res. 2010, 80, 231-242.
    • (2010) Int. J. Vitam. Nutr. Res. , vol.80 , pp. 231-242
    • Sharp, P.A.1
  • 47
    • 79952101502 scopus 로고    scopus 로고
    • Novel development of 5-aminolevurinic acid (ALA) in cancer diagnoses and therapy
    • Ishizuka, M., Abe, F., Sano, Y., Takahashi, K. et al., Novel development of 5-aminolevurinic acid (ALA) in cancer diagnoses and therapy. Int. Immunopharmacol. 2011, 11, 358-365.
    • (2011) Int. Immunopharmacol. , vol.11 , pp. 358-365
    • Ishizuka, M.1    Abe, F.2    Sano, Y.3    Takahashi, K.4
  • 49
    • 0014670945 scopus 로고
    • Microsomal heme oxygenase. Characterization of the enzyme
    • Tenhunen, R., Marver, H. S., Schmid, R., Microsomal heme oxygenase. Characterization of the enzyme. J. Biol. Chem. 1969, 244, 6388-6394.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6388-6394
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 50
    • 84872804281 scopus 로고    scopus 로고
    • Carbon monoxide: mechanisms of action and potential clinical implications
    • Rochette, L., Cottin, Y., Zeller, M., Vergely, C., Carbon monoxide: mechanisms of action and potential clinical implications. Pharmacol. Ther. 2013, 137, 133-152.
    • (2013) Pharmacol. Ther. , vol.137 , pp. 133-152
    • Rochette, L.1    Cottin, Y.2    Zeller, M.3    Vergely, C.4
  • 51
    • 37249039500 scopus 로고    scopus 로고
    • Subcellular location of heme oxygenase 1 and 2 and divalent metal transporter 1 in relation to endocytotic markers during heme iron absorption
    • West, A. R., Oates, P. S., Subcellular location of heme oxygenase 1 and 2 and divalent metal transporter 1 in relation to endocytotic markers during heme iron absorption. J. Gastroenterol. Hepatol. 2008, 23, 150-158.
    • (2008) J. Gastroenterol. Hepatol. , vol.23 , pp. 150-158
    • West, A.R.1    Oates, P.S.2
  • 52
    • 84867406948 scopus 로고    scopus 로고
    • Role of cysteine residues in heme binding to human heme oxygenase-2 elucidated by two-dimensional NMR spectroscopy
    • Varfaj, F., Lampe, J. N., Ortiz de Montellano, P. R., Role of cysteine residues in heme binding to human heme oxygenase-2 elucidated by two-dimensional NMR spectroscopy. J. Biol. Chem. 2012, 287, 35181-35191.
    • (2012) J. Biol. Chem. , vol.287 , pp. 35181-35191
    • Varfaj, F.1    Lampe, J.N.2    Ortiz de Montellano, P.R.3
  • 53
    • 3042799349 scopus 로고    scopus 로고
    • Characterization of rat heme oxygenase-3 gene. Implication of processed pseudogenes derived from heme oxygenase-2 gene
    • Hayashi, S., Omata, Y., Sakamoto, H., Higashimoto, Y. et al., Characterization of rat heme oxygenase-3 gene. Implication of processed pseudogenes derived from heme oxygenase-2 gene. Gene 2004, 336, 241-250.
    • (2004) Gene , vol.336 , pp. 241-250
    • Hayashi, S.1    Omata, Y.2    Sakamoto, H.3    Higashimoto, Y.4
  • 54
    • 28844494034 scopus 로고    scopus 로고
    • Redox biology of blood revisited: the role of red blood cells in maintaining circulatory reductive capacity
    • Buehler, P. W., Alayash, A. I., Redox biology of blood revisited: the role of red blood cells in maintaining circulatory reductive capacity. Antioxid. Redox. Signal. 2005, 7, 1755-1760.
    • (2005) Antioxid. Redox. Signal. , vol.7 , pp. 1755-1760
    • Buehler, P.W.1    Alayash, A.I.2
  • 55
    • 80051605134 scopus 로고    scopus 로고
    • Ultrastructural aspects of iron storage, transport and metabolism
    • Iancu, T. C., Ultrastructural aspects of iron storage, transport and metabolism. J. Neural. Transm. 2011, 118, 329-335.
    • (2011) J. Neural. Transm. , vol.118 , pp. 329-335
    • Iancu, T.C.1
  • 58
    • 77955610477 scopus 로고    scopus 로고
    • Iron-sensing proteins that regulate hepcidin and enteric iron absorption
    • Knutson, M. D., Iron-sensing proteins that regulate hepcidin and enteric iron absorption. Annu. Rev. Nutr. 2010, 30, 149-171.
    • (2010) Annu. Rev. Nutr. , vol.30 , pp. 149-171
    • Knutson, M.D.1
  • 59
    • 0035793856 scopus 로고    scopus 로고
    • An iron-regulated ferric reductase associated with the absorption of dietary iron
    • McKie, A. T., Barrow, D., Latunde-Dada, G. O., Rolfs, A. et al., An iron-regulated ferric reductase associated with the absorption of dietary iron. Science 2001, 291, 1755-1759.
    • (2001) Science , vol.291 , pp. 1755-1759
    • McKie, A.T.1    Barrow, D.2    Latunde-Dada, G.O.3    Rolfs, A.4
  • 62
    • 84864319642 scopus 로고    scopus 로고
    • Mammalian iron metabolism and its control by iron regulatory proteins
    • Anderson, C. P., Shen, M., Eisenstein, R. S., Leibold, E. A., Mammalian iron metabolism and its control by iron regulatory proteins. Biochim. Biophys. Acta 2012, 1823, 1468-1483.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 1468-1483
    • Anderson, C.P.1    Shen, M.2    Eisenstein, R.S.3    Leibold, E.A.4
  • 63
    • 34249686049 scopus 로고    scopus 로고
    • Ferritin and ferritin isoforms I: structure-function relationships, synthesis, degradation and secretion
    • Koorts, A. M., Viljoen, M., Ferritin and ferritin isoforms I: structure-function relationships, synthesis, degradation and secretion. Arch. Physiol. Biochem. 2007, 113, 30-54.
    • (2007) Arch. Physiol. Biochem. , vol.113 , pp. 30-54
    • Koorts, A.M.1    Viljoen, M.2
  • 64
    • 77953807901 scopus 로고    scopus 로고
    • Oxido-reduction is not the only mechanism allowing ions to traverse the ferritin protein shell
    • Watt, R. K., Hilton, R. J., Graff, D. M., Oxido-reduction is not the only mechanism allowing ions to traverse the ferritin protein shell. Biochim. Biophys. Acta 2010, 1800, 745-759.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 745-759
    • Watt, R.K.1    Hilton, R.J.2    Graff, D.M.3
  • 65
    • 41349120026 scopus 로고    scopus 로고
    • Intracellular iron transport and storage: from molecular mechanisms to health implications
    • MacKenzie, E. L., Iwasaki, K., Tsuji, Y., Intracellular iron transport and storage: from molecular mechanisms to health implications. Antioxid. Redox. Signal 2008, 10, 997-1030.
    • (2008) Antioxid. Redox. Signal , vol.10 , pp. 997-1030
    • MacKenzie, E.L.1    Iwasaki, K.2    Tsuji, Y.3
  • 66
    • 38349111676 scopus 로고    scopus 로고
    • Role of the hypoxia inducible factors HIF in iron metabolism
    • Peyssonnaux, C., Nizet, V., Johnson, R. S., Role of the hypoxia inducible factors HIF in iron metabolism. Cell Cycle 2008, 7, 28-32.
    • (2008) Cell Cycle , vol.7 , pp. 28-32
    • Peyssonnaux, C.1    Nizet, V.2    Johnson, R.S.3
  • 67
    • 34548594676 scopus 로고    scopus 로고
    • Hepcidin and its role in regulating systemic iron metabolism
    • Ganz, T., Hepcidin and its role in regulating systemic iron metabolism. Hematology Am. Soc. Hematol. Educ. Program 2006, 507, 29-35.
    • (2006) Hematology Am. Soc. Hematol. Educ. Program , vol.507 , pp. 29-35
    • Ganz, T.1
  • 68
    • 84885768132 scopus 로고    scopus 로고
    • Systemic iron homeostasis
    • Ganz, T., Systemic iron homeostasis. Physiol. Rev. 2013, 93, 1721-1741.
    • (2013) Physiol. Rev. , vol.93 , pp. 1721-1741
    • Ganz, T.1
  • 69
    • 84860574815 scopus 로고    scopus 로고
    • Iron sensing and signalling
    • Evstatiev, R., Gasche, C., Iron sensing and signalling. Gut 2012, 61, 933-952.
    • (2012) Gut , vol.61 , pp. 933-952
    • Evstatiev, R.1    Gasche, C.2
  • 71
    • 84861355868 scopus 로고    scopus 로고
    • Hepcidin and iron homeostasis
    • Ganz, T., Nemeth, E., Hepcidin and iron homeostasis. Biochim. Biophys. Acta 2012, 1823, 1434-1443.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 1434-1443
    • Ganz, T.1    Nemeth, E.2
  • 72
    • 84864309529 scopus 로고    scopus 로고
    • Structure, function, and assembly of heme centers in mitochondrial respiratory complexes
    • Kim, H. J., Khalimonchuk, O., Smith, P. M., Winge, D. R., Structure, function, and assembly of heme centers in mitochondrial respiratory complexes. Biochim. Biophys Acta 2012, 1823, 1604-1616.
    • (2012) Biochim. Biophys Acta , vol.1823 , pp. 1604-1616
    • Kim, H.J.1    Khalimonchuk, O.2    Smith, P.M.3    Winge, D.R.4
  • 73
    • 84864296714 scopus 로고    scopus 로고
    • The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism
    • Lill, R., Hoffmann, B., Molik, S., Pierik, A. J. et al., The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism. Biochim. Biophys. Acta 2012, 1823, 1491-1508.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 1491-1508
    • Lill, R.1    Hoffmann, B.2    Molik, S.3    Pierik, A.J.4
  • 74
    • 33746868343 scopus 로고    scopus 로고
    • Mechanisms of iron-sulfur protein maturation in mitochondria, cytosol and nucleus of eukaryotes
    • Lill, R., Dutkiewicz, R., Elsasser, H. P., Hausmann, A. et al., Mechanisms of iron-sulfur protein maturation in mitochondria, cytosol and nucleus of eukaryotes. Biochim. Biophys. Acta 2006, 1763, 652-667.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 652-667
    • Lill, R.1    Dutkiewicz, R.2    Elsasser, H.P.3    Hausmann, A.4
  • 75
    • 84878905186 scopus 로고    scopus 로고
    • Mitochondrial complex I
    • Hirst, J., Mitochondrial complex I. Annu. Rev. Biochem. 2013, 82, 551-575.
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 551-575
    • Hirst, J.1
  • 76
    • 84884673676 scopus 로고    scopus 로고
    • Unanswered questions about the structure of cytochrome bc1 complexes
    • Berry, E. A., De Bari, H., Huang, L. S., Unanswered questions about the structure of cytochrome bc1 complexes. Biochim. Biophys. Acta 2013, 1827, 1258-1277.
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 1258-1277
    • Berry, E.A.1    De Bari, H.2    Huang, L.S.3
  • 77
    • 34547130863 scopus 로고    scopus 로고
    • The role of mitochondria in protection of the heart by preconditioning
    • Halestrap, A. P., Clarke, S. J., Khaliulin, I., The role of mitochondria in protection of the heart by preconditioning. Biochim. Biophys. Acta 2007, 1767, 1007-1031.
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1007-1031
    • Halestrap, A.P.1    Clarke, S.J.2    Khaliulin, I.3
  • 78
    • 33845337036 scopus 로고    scopus 로고
    • Iron and iron-responsive proteins in the cardiomyopathy of Friedreich's ataxia
    • Michael, S., Petrocine, S. V., Qian, J., Lamarche, J. B. et al., Iron and iron-responsive proteins in the cardiomyopathy of Friedreich's ataxia. Cerebellum 2006, 5, 257-267.
    • (2006) Cerebellum , vol.5 , pp. 257-267
    • Michael, S.1    Petrocine, S.V.2    Qian, J.3    Lamarche, J.B.4
  • 79
    • 46749083764 scopus 로고    scopus 로고
    • Detection of mitochondrial dysfunction by EPR technique in mouse model of dilated cardiomyopathy
    • Elas, M., Bielanska, J., Pustelny, K., Plonka, P. M. et al., Detection of mitochondrial dysfunction by EPR technique in mouse model of dilated cardiomyopathy. Free Radic. Biol. Med. 2008, 45, 321-328.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 321-328
    • Elas, M.1    Bielanska, J.2    Pustelny, K.3    Plonka, P.M.4
  • 80
    • 84873672891 scopus 로고    scopus 로고
    • Iron speciation in the cytosol: an overview
    • Hider, R. C., Kong, X., Iron speciation in the cytosol: an overview. Dalton Trans. 2013, 42, 3220-3229.
    • (2013) Dalton Trans. , vol.42 , pp. 3220-3229
    • Hider, R.C.1    Kong, X.2
  • 81
    • 55349132417 scopus 로고    scopus 로고
    • Cardiomyocyte death and renewal in the normal and diseased heart
    • Buja, L. M., Vela, D., Cardiomyocyte death and renewal in the normal and diseased heart. Cardiovasc. Pathol. 2008, 17, 349-374.
    • (2008) Cardiovasc. Pathol. , vol.17 , pp. 349-374
    • Buja, L.M.1    Vela, D.2
  • 82
    • 0028044205 scopus 로고
    • Changes in the microvascular network during cardiac growth, development, and aging
    • Rakusan, K., Cicutti, N., Flanagan, M. F., Changes in the microvascular network during cardiac growth, development, and aging. Cell. Mol. Biol. Res. 1994, 40, 117-122.
    • (1994) Cell. Mol. Biol. Res. , vol.40 , pp. 117-122
    • Rakusan, K.1    Cicutti, N.2    Flanagan, M.F.3
  • 83
    • 80053547300 scopus 로고    scopus 로고
    • Role of cardiac stem cells in cardiac pathophysiology: a paradigm shift in human myocardial biology
    • Leri, A., Kajstura, J., Anversa, P., Role of cardiac stem cells in cardiac pathophysiology: a paradigm shift in human myocardial biology. Circ. Res. 2011, 109, 941-961.
    • (2011) Circ. Res. , vol.109 , pp. 941-961
    • Leri, A.1    Kajstura, J.2    Anversa, P.3
  • 84
    • 0018915753 scopus 로고
    • Enzymatic defenses of the mouse heart against reactive oxygen metabolites: alterations produced by doxorubicin
    • Doroshow, J. H., Locker, G. Y., Myers, C. E., Enzymatic defenses of the mouse heart against reactive oxygen metabolites: alterations produced by doxorubicin. J. Clin. Invest. 1980, 65, 128-135.
    • (1980) J. Clin. Invest. , vol.65 , pp. 128-135
    • Doroshow, J.H.1    Locker, G.Y.2    Myers, C.E.3
  • 85
    • 79961017532 scopus 로고    scopus 로고
    • Biochemical study of oxidative stress markers in the liver, kidney and heart of high fat diet induced obesity in rats
    • Noeman, S. A., Hamooda, H. E., Baalash, A. A., Biochemical study of oxidative stress markers in the liver, kidney and heart of high fat diet induced obesity in rats. Diabetol. Metab. Syndr. 2011, 3, 17.
    • (2011) Diabetol. Metab. Syndr. , vol.3 , pp. 17
    • Noeman, S.A.1    Hamooda, H.E.2    Baalash, A.A.3
  • 87
    • 0344548127 scopus 로고    scopus 로고
    • Selective effects of oxygen free radicals on excitation-contraction coupling in ventricular muscle. Implications for the mechanism of stunned myocardium
    • Gao, W. D., Liu, Y., Marban, E., Selective effects of oxygen free radicals on excitation-contraction coupling in ventricular muscle. Implications for the mechanism of stunned myocardium. Circulation 1996, 94, 2597-2604.
    • (1996) Circulation , vol.94 , pp. 2597-2604
    • Gao, W.D.1    Liu, Y.2    Marban, E.3
  • 88
    • 84872680832 scopus 로고    scopus 로고
    • SR and mitochondria: calcium cross-talk between kissing cousins
    • Dorn, G. W., II, Maack, C., SR and mitochondria: calcium cross-talk between kissing cousins. J. Mol. Cell. Cardiol. 2013, 55, 42-49.
    • (2013) J. Mol. Cell. Cardiol. , vol.55 , pp. 42-49
    • Dorn II, G.W.1    Maack, C.2
  • 89
    • 79952021934 scopus 로고    scopus 로고
    • Innate immunity in the adult mammalian heart: for whom the cell tolls
    • discussion 50-31.
    • Mann, D. L., Topkara, V. K., Evans, S., Barger, P. M., Innate immunity in the adult mammalian heart: for whom the cell tolls. Trans. Am. Clin. Climatol. Assoc. 2010, 121, 34-50; discussion 50-31.
    • (2010) Trans. Am. Clin. Climatol. Assoc. , vol.121 , pp. 34-50
    • Mann, D.L.1    Topkara, V.K.2    Evans, S.3    Barger, P.M.4
  • 90
    • 51849148491 scopus 로고    scopus 로고
    • Pathological autoantibodies in cardiomyopathy
    • Jahns, R., Boivin, V., Schwarzbach, V., Ertl, G. et al., Pathological autoantibodies in cardiomyopathy. Autoimmunity 2008, 41, 454-461.
    • (2008) Autoimmunity , vol.41 , pp. 454-461
    • Jahns, R.1    Boivin, V.2    Schwarzbach, V.3    Ertl, G.4
  • 91
    • 79953303630 scopus 로고    scopus 로고
    • Role of toll-like receptors in cardiovascular diseases
    • Vallejo, J. G., Role of toll-like receptors in cardiovascular diseases. Clin. Sci. 2011, 121, 1-10.
    • (2011) Clin. Sci. , vol.121 , pp. 1-10
    • Vallejo, J.G.1
  • 92
    • 47249145558 scopus 로고    scopus 로고
    • Bacillus Calmette-Guerin and TLR4 agonist prevent cardiovascular hypertrophy and fibrosis by regulating immune microenvironment
    • Liu, Y. Y., Cai, W. F., Yang, H. Z., Cui, B. et al., Bacillus Calmette-Guerin and TLR4 agonist prevent cardiovascular hypertrophy and fibrosis by regulating immune microenvironment. J. Immunol. 2008, 180, 7349-7357.
    • (2008) J. Immunol. , vol.180 , pp. 7349-7357
    • Liu, Y.Y.1    Cai, W.F.2    Yang, H.Z.3    Cui, B.4
  • 93
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D., Walter, P., Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell. Biol. 2007, 8, 519-529.
    • (2007) Nat. Rev. Mol. Cell. Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 94
    • 84878225746 scopus 로고    scopus 로고
    • Functional and morphological impact of ER stress on mitochondria
    • Vannuvel, K., Renard, P., Raes, M., Arnould, T., Functional and morphological impact of ER stress on mitochondria. J. Cell. Physiol. 2013, 228, 1802-1818.
    • (2013) J. Cell. Physiol. , vol.228 , pp. 1802-1818
    • Vannuvel, K.1    Renard, P.2    Raes, M.3    Arnould, T.4
  • 95
    • 84872375449 scopus 로고    scopus 로고
    • Endoplasmic reticulum and the unfolded protein response: dynamics and metabolic integration
    • Bravo, R., Parra, V., Gatica, D., Rodriguez, A. E. et al., Endoplasmic reticulum and the unfolded protein response: dynamics and metabolic integration. Int. Rev. Cell. Mol. Biol. 2013, 301, 215-290.
    • (2013) Int. Rev. Cell. Mol. Biol. , vol.301 , pp. 215-290
    • Bravo, R.1    Parra, V.2    Gatica, D.3    Rodriguez, A.E.4
  • 96
    • 84859799949 scopus 로고    scopus 로고
    • Stress management at the ER: regulators of ER stress-induced apoptosis
    • Gorman, A. M., Healy, S. J., Jager, R., Samali, A., Stress management at the ER: regulators of ER stress-induced apoptosis. Pharmacol. Ther. 2012, 134, 306-316.
    • (2012) Pharmacol. Ther. , vol.134 , pp. 306-316
    • Gorman, A.M.1    Healy, S.J.2    Jager, R.3    Samali, A.4
  • 98
    • 84870239310 scopus 로고    scopus 로고
    • Immunogenic cell death and DAMPs in cancer therapy
    • Krysko, D. V., Garg, A. D., Kaczmarek, A., Krysko, O. et al., Immunogenic cell death and DAMPs in cancer therapy. Nat. Rev. Cancer 2012, 12, 860-875.
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 860-875
    • Krysko, D.V.1    Garg, A.D.2    Kaczmarek, A.3    Krysko, O.4
  • 100
    • 77953725586 scopus 로고    scopus 로고
    • Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM)
    • Simmen, T., Lynes, E. M., Gesson, K., Thomas, G., Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM). Biochim. Biophys. Acta 2010, 1798, 1465-1473.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1465-1473
    • Simmen, T.1    Lynes, E.M.2    Gesson, K.3    Thomas, G.4
  • 101
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology
    • Bedard, K., Krause, K. H., The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 2007, 87, 245-313.
    • (2007) Physiol. Rev. , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 102
    • 84875087381 scopus 로고    scopus 로고
    • NADPH oxidase biology and the regulation of tyrosine kinase receptor signaling and cancer drug cytotoxicity
    • Paletta-Silva, R., Rocco-Machado, N., Meyer-Fernandes, J. R., NADPH oxidase biology and the regulation of tyrosine kinase receptor signaling and cancer drug cytotoxicity. Int. J. Mol. Sci. 2013, 14, 3683-3704.
    • (2013) Int. J. Mol. Sci. , vol.14 , pp. 3683-3704
    • Paletta-Silva, R.1    Rocco-Machado, N.2    Meyer-Fernandes, J.R.3
  • 104
    • 70350689746 scopus 로고    scopus 로고
    • Biochemical and cellular toxicology of peroxynitrite: implications in cell death and autoimmune phenomenon
    • Ahmad, R., Rasheed, Z., Ahsan, H., Biochemical and cellular toxicology of peroxynitrite: implications in cell death and autoimmune phenomenon. Immunopharmacol. Immunotoxicol. 2009, 31, 388-396.
    • (2009) Immunopharmacol. Immunotoxicol. , vol.31 , pp. 388-396
    • Ahmad, R.1    Rasheed, Z.2    Ahsan, H.3
  • 106
    • 84866932320 scopus 로고    scopus 로고
    • ER stress-induced inflammation: does it aid or impede disease progression?
    • Garg, A. D., Kaczmarek, A., Krysko, O., Vandenabeele, P. et al., ER stress-induced inflammation: does it aid or impede disease progression? Trends Mol. Med. 2012, 18, 589-598.
    • (2012) Trends Mol. Med. , vol.18 , pp. 589-598
    • Garg, A.D.1    Kaczmarek, A.2    Krysko, O.3    Vandenabeele, P.4
  • 107
    • 84857116578 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
    • Ray, P. D., Huang, B. W., Tsuji, Y., Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling. Cell. Signal. 2012, 24, 981-990.
    • (2012) Cell. Signal. , vol.24 , pp. 981-990
    • Ray, P.D.1    Huang, B.W.2    Tsuji, Y.3
  • 108
    • 33847050801 scopus 로고    scopus 로고
    • Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway
    • Kensler, T. W., Wakabayashi, N., Biswal, S., Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway. Annu. Rev. Pharmacol. Toxicol. 2007, 47, 89-116.
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 89-116
    • Kensler, T.W.1    Wakabayashi, N.2    Biswal, S.3
  • 109
    • 3543008924 scopus 로고    scopus 로고
    • Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2
    • Kobayashi, A., Kang, M. I., Okawa, H., Ohtsuji, M. et al., Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2. Mol. Cell. Biol. 2004, 24, 7130-7139.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7130-7139
    • Kobayashi, A.1    Kang, M.I.2    Okawa, H.3    Ohtsuji, M.4
  • 110
    • 81855204961 scopus 로고    scopus 로고
    • Oxidative stress in health and disease: the therapeutic potential of Nrf2 activation
    • Hybertson, B. M., Gao, B., Bose, S. K., McCord, J. M., Oxidative stress in health and disease: the therapeutic potential of Nrf2 activation. Mol. Aspects Med. 2011, 32, 234-246.
    • (2011) Mol. Aspects Med. , vol.32 , pp. 234-246
    • Hybertson, B.M.1    Gao, B.2    Bose, S.K.3    McCord, J.M.4
  • 111
    • 70249138697 scopus 로고    scopus 로고
    • Characterization of the cancer chemopreventive NRF2-dependent gene battery in human keratinocytes: demonstration that the KEAP1-NRF2 pathway, and not the BACH1-NRF2 pathway, controls cytoprotection against electrophiles as well as redox-cycling compounds
    • MacLeod, A. K., McMahon, M., Plummer, S. M., Higgins, L. G. et al., Characterization of the cancer chemopreventive NRF2-dependent gene battery in human keratinocytes: demonstration that the KEAP1-NRF2 pathway, and not the BACH1-NRF2 pathway, controls cytoprotection against electrophiles as well as redox-cycling compounds. Carcinogenesis 2009, 30, 1571-1580.
    • (2009) Carcinogenesis , vol.30 , pp. 1571-1580
    • MacLeod, A.K.1    McMahon, M.2    Plummer, S.M.3    Higgins, L.G.4
  • 112
    • 38949110010 scopus 로고    scopus 로고
    • Negative feedback regulation of lipopolysaccharide-induced inducible nitric oxide synthase gene expression by heme oxygenase-1 induction in macrophages
    • Ashino, T., Yamanaka, R., Yamamoto, M., Shimokawa, H. et al., Negative feedback regulation of lipopolysaccharide-induced inducible nitric oxide synthase gene expression by heme oxygenase-1 induction in macrophages. Mol. Immunol. 2008, 45, 2106-2115.
    • (2008) Mol. Immunol. , vol.45 , pp. 2106-2115
    • Ashino, T.1    Yamanaka, R.2    Yamamoto, M.3    Shimokawa, H.4
  • 113
    • 84875729120 scopus 로고    scopus 로고
    • Inflammation and oxidative stress in angiogenesis and vascular disease
    • Kim, Y. W., West, X. Z., Byzova, T. V., Inflammation and oxidative stress in angiogenesis and vascular disease. J. Mol. Med. 2013, 91, 323-328.
    • (2013) J. Mol. Med. , vol.91 , pp. 323-328
    • Kim, Y.W.1    West, X.Z.2    Byzova, T.V.3
  • 114
    • 68949196898 scopus 로고    scopus 로고
    • Redox regulation of nuclear post-translational modifications during NF-kappaB activation
    • Gloire, G., Piette, J., Redox regulation of nuclear post-translational modifications during NF-kappaB activation. Antioxid. Redox. Signal. 2009, 11, 2209-2222.
    • (2009) Antioxid. Redox. Signal. , vol.11 , pp. 2209-2222
    • Gloire, G.1    Piette, J.2
  • 115
    • 79959732295 scopus 로고    scopus 로고
    • Nrf2 is essential for cholesterol crystal-induced inflammasome activation and exacerbation of atherosclerosis
    • Freigang, S., Ampenberger, F., Spohn, G., Heer, S. et al., Nrf2 is essential for cholesterol crystal-induced inflammasome activation and exacerbation of atherosclerosis. Eur. J. Immunol. 2011, 41, 2040-2051.
    • (2011) Eur. J. Immunol. , vol.41 , pp. 2040-2051
    • Freigang, S.1    Ampenberger, F.2    Spohn, G.3    Heer, S.4
  • 116
    • 84894236540 scopus 로고    scopus 로고
    • Dietary iron intake and body iron stores are associated with risk of coronary heart disease in a meta-analysis of prospective cohort studies
    • Hunnicutt, J., He, K., Xun, P., Dietary iron intake and body iron stores are associated with risk of coronary heart disease in a meta-analysis of prospective cohort studies. J. Nutr. 2014, 144, 359-366.
    • (2014) J. Nutr. , vol.144 , pp. 359-366
    • Hunnicutt, J.1    He, K.2    Xun, P.3
  • 117
    • 0025159057 scopus 로고
    • Adaptation in iron metabolism
    • Cook, J. D., Adaptation in iron metabolism. Am. J. Clin. Nutr. 1990, 51, 301-308.
    • (1990) Am. J. Clin. Nutr. , vol.51 , pp. 301-308
    • Cook, J.D.1
  • 118
    • 22144487720 scopus 로고    scopus 로고
    • Hereditary hemochromatosis and risk of ischemic heart disease: a prospective study and a case-control study
    • Ellervik, C., Tybjaerg-Hansen, A., Grande, P., Appleyard, M. et al., Hereditary hemochromatosis and risk of ischemic heart disease: a prospective study and a case-control study. Circulation 2005, 112, 185-193.
    • (2005) Circulation , vol.112 , pp. 185-193
    • Ellervik, C.1    Tybjaerg-Hansen, A.2    Grande, P.3    Appleyard, M.4
  • 119
    • 80053272245 scopus 로고    scopus 로고
    • Plasma ferritin levels, genetic variations in HFE gene, and coronary heart disease in Chinese: a case-control study
    • Shi, Y., Zhou, L., Huang, L. H., Lian, Y. T. et al., Plasma ferritin levels, genetic variations in HFE gene, and coronary heart disease in Chinese: a case-control study. Atherosclerosis 2011, 218, 386-390.
    • (2011) Atherosclerosis , vol.218 , pp. 386-390
    • Shi, Y.1    Zhou, L.2    Huang, L.H.3    Lian, Y.T.4
  • 120
    • 84893972482 scopus 로고    scopus 로고
    • Hereditary hemochromatosis, iron, hepcidin, and coronary heart disease
    • Mascitelli, L., Goldstein, M. R., Hereditary hemochromatosis, iron, hepcidin, and coronary heart disease. Med. Hypotheses 2014, 82, 402-403.
    • (2014) Med. Hypotheses , vol.82 , pp. 402-403
    • Mascitelli, L.1    Goldstein, M.R.2
  • 121
    • 77957664307 scopus 로고    scopus 로고
    • HFE gene mutations increase the risk of coronary heart disease in women
    • Pardo Silva, M. C., Njajou, O. T., Alizadeh, B. Z., Hofman, A. et al., HFE gene mutations increase the risk of coronary heart disease in women. Eur. J. Epidemiol. 2010, 25, 643-649.
    • (2010) Eur. J. Epidemiol. , vol.25 , pp. 643-649
    • Pardo Silva, M.C.1    Njajou, O.T.2    Alizadeh, B.Z.3    Hofman, A.4
  • 122
    • 79953706285 scopus 로고    scopus 로고
    • Explaining sex difference in coronary heart disease: is it time to shift from the oestrogen hypothesis to the iron hypothesis
    • Mascitelli, L., Goldstein, M. R., Pezzetta, F., Explaining sex difference in coronary heart disease: is it time to shift from the oestrogen hypothesis to the iron hypothesis? J. Cardiovasc. Med. 2011, 12, 64-65.
    • (2011) J. Cardiovasc. Med. , vol.12 , pp. 64-65
    • Mascitelli, L.1    Goldstein, M.R.2    Pezzetta, F.3
  • 123
    • 84859717284 scopus 로고    scopus 로고
    • Red meat consumption and mortality: results from 2 prospective cohort studies
    • Pan, A., Sun, Q., Bernstein, A. M., Schulze, M. B. et al., Red meat consumption and mortality: results from 2 prospective cohort studies. Arch. Intern. Med. 2012, 172, 555-563.
    • (2012) Arch. Intern. Med. , vol.172 , pp. 555-563
    • Pan, A.1    Sun, Q.2    Bernstein, A.M.3    Schulze, M.B.4
  • 124
    • 0028353561 scopus 로고
    • Dietary iron intake and risk of coronary disease among men
    • Ascherio, A., Willett, W. C., Rimm, E. B., Giovannucci, E. L. et al., Dietary iron intake and risk of coronary disease among men. Circulation 1994, 89, 969-974.
    • (1994) Circulation , vol.89 , pp. 969-974
    • Ascherio, A.1    Willett, W.C.2    Rimm, E.B.3    Giovannucci, E.L.4
  • 126
    • 84894052945 scopus 로고    scopus 로고
    • Heme iron intake and acute myocardial infarction: a prospective study of men
    • Kaluza, J., Larsson, S. C., Hakansson, N., Wolk, A., Heme iron intake and acute myocardial infarction: a prospective study of men. Int. J. Cardiol. 2014, 172, 155-160.
    • (2014) Int. J. Cardiol. , vol.172 , pp. 155-160
    • Kaluza, J.1    Larsson, S.C.2    Hakansson, N.3    Wolk, A.4
  • 127
    • 36749018108 scopus 로고    scopus 로고
    • Heart failure and malignant ventricular tachyarrhythmias due to hereditary hemochromatosis with iron overload cardiomyopathy
    • Demant, A. W., Schmiedel, A., Buttner, R., Lewalter, T. et al., Heart failure and malignant ventricular tachyarrhythmias due to hereditary hemochromatosis with iron overload cardiomyopathy. Clin. Res. Cardiol. 2007, 96, 900-903.
    • (2007) Clin. Res. Cardiol. , vol.96 , pp. 900-903
    • Demant, A.W.1    Schmiedel, A.2    Buttner, R.3    Lewalter, T.4
  • 128
    • 84857790195 scopus 로고    scopus 로고
    • Incidence of cardiac arrhythmias in asymptomatic hereditary hemochromatosis subjects with C282Y homozygosity
    • Shizukuda, Y., Tripodi, D. J., Zalos, G., Bolan, C. D. et al., Incidence of cardiac arrhythmias in asymptomatic hereditary hemochromatosis subjects with C282Y homozygosity. Am. J. Cardiol. 2012, 109, 856-860.
    • (2012) Am. J. Cardiol. , vol.109 , pp. 856-860
    • Shizukuda, Y.1    Tripodi, D.J.2    Zalos, G.3    Bolan, C.D.4
  • 129
    • 84855933329 scopus 로고    scopus 로고
    • Electrocardiographic consequences of cardiac iron overload in thalassemia major
    • Detterich, J., Noetzli, L., Dorey, F., Bar-Cohen, Y. et al., Electrocardiographic consequences of cardiac iron overload in thalassemia major. Am. J. Hematol. 2012, 87, 139-144.
    • (2012) Am. J. Hematol. , vol.87 , pp. 139-144
    • Detterich, J.1    Noetzli, L.2    Dorey, F.3    Bar-Cohen, Y.4
  • 130
    • 84905377406 scopus 로고    scopus 로고
    • Atrial and ventricular function in thalassemic patients with supra-ventricular arrhythmias
    • Monte, I., Capodanno, D., Nicolosi, E., Licciardi, S. et al., Atrial and ventricular function in thalassemic patients with supra-ventricular arrhythmias. Heart Int. 2009, 4, e3.
    • (2009) Heart Int. , vol.4
    • Monte, I.1    Capodanno, D.2    Nicolosi, E.3    Licciardi, S.4
  • 131
    • 0030048681 scopus 로고    scopus 로고
    • Results of long-term iron-chelating therapy
    • Gabutti, V., Piga, A., Results of long-term iron-chelating therapy. Acta Haematol. 1996, 95, 26-36.
    • (1996) Acta Haematol. , vol.95 , pp. 26-36
    • Gabutti, V.1    Piga, A.2
  • 132
    • 33846078725 scopus 로고    scopus 로고
    • Reversal of cardiac complications by deferiprone and deferoxamine combination therapy in a patient affected by a severe type of juvenile hemochromatosis (JH)
    • Fabio, G., Minonzio, F., Delbini, P., Bianchi, A. et al., Reversal of cardiac complications by deferiprone and deferoxamine combination therapy in a patient affected by a severe type of juvenile hemochromatosis (JH). Blood 2007, 109, 362-364.
    • (2007) Blood , vol.109 , pp. 362-364
    • Fabio, G.1    Minonzio, F.2    Delbini, P.3    Bianchi, A.4
  • 134
    • 84891785521 scopus 로고    scopus 로고
    • The role of treatment for anemia as a therapeutic target in the management of chronic heart failure: insights after RED-HF
    • Gaggin, H. K., Dec, G. W., The role of treatment for anemia as a therapeutic target in the management of chronic heart failure: insights after RED-HF. Curr. Treat. Options Cardiovasc. Med. 2014, 16, 279-288.
    • (2014) Curr. Treat. Options Cardiovasc. Med. , vol.16 , pp. 279-288
    • Gaggin, H.K.1    Dec, G.W.2
  • 135
    • 79955783358 scopus 로고    scopus 로고
    • Heart failure-associated anemia: bone marrow dysfunction and response to erythropoietin
    • Ruifrok, W. P., Qian, C., Sillje, H. H., van Goor, H. et al., Heart failure-associated anemia: bone marrow dysfunction and response to erythropoietin. J. Mol. Med. 2011, 89, 377-387.
    • (2011) J. Mol. Med. , vol.89 , pp. 377-387
    • Ruifrok, W.P.1    Qian, C.2    Sillje, H.H.3    van Goor, H.4
  • 136
    • 84899850056 scopus 로고    scopus 로고
    • Clinical outcomes of erythropoietin use in heart failure patients with anemia of chronic kidney disease
    • Jackevicius, C., Fan, C. S., Warner, A., Clinical outcomes of erythropoietin use in heart failure patients with anemia of chronic kidney disease. J. Card. Fail. 2014, 20, 327-333.
    • (2014) J. Card. Fail. , vol.20 , pp. 327-333
    • Jackevicius, C.1    Fan, C.S.2    Warner, A.3
  • 137
    • 17644412023 scopus 로고    scopus 로고
    • Inflammation, atherosclerosis, and coronary artery disease
    • Hansson, G. K., Inflammation, atherosclerosis, and coronary artery disease. N. Engl. J. Med. 2005, 352, 1685-1695.
    • (2005) N. Engl. J. Med. , vol.352 , pp. 1685-1695
    • Hansson, G.K.1
  • 138
    • 33846672638 scopus 로고    scopus 로고
    • Increased superoxide anion production is associated with early atherosclerosis and cardiovascular dysfunctions in a rabbit model
    • Collin, B., Busseuil, D., Zeller, M., Perrin, C. et al., Increased superoxide anion production is associated with early atherosclerosis and cardiovascular dysfunctions in a rabbit model. Mol. Cell Biochem. 2007, 294, 225-235.
    • (2007) Mol. Cell Biochem. , vol.294 , pp. 225-235
    • Collin, B.1    Busseuil, D.2    Zeller, M.3    Perrin, C.4
  • 140
    • 0037443734 scopus 로고    scopus 로고
    • Correlation of iron and zinc levels with lesion depth in newly formed atherosclerotic lesions
    • Minqin, R., Watt, F., Huat, B. T., Halliwell, B., Correlation of iron and zinc levels with lesion depth in newly formed atherosclerotic lesions. Free Radic. Biol. Med. 2003, 34, 746-752.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 746-752
    • Minqin, R.1    Watt, F.2    Huat, B.T.3    Halliwell, B.4
  • 141
    • 0031472394 scopus 로고    scopus 로고
    • Effect of iron overload and iron deficiency on atherosclerosis in the hypercholesterolemic rabbit
    • Dabbagh, A. J., Shwaery, G. T., Keaney, J. F., Jr., Frei, B., Effect of iron overload and iron deficiency on atherosclerosis in the hypercholesterolemic rabbit. Arterioscler. Thromb. Vasc. Biol. 1997, 17, 2638-2645.
    • (1997) Arterioscler. Thromb. Vasc. Biol. , vol.17 , pp. 2638-2645
    • Dabbagh, A.J.1    Shwaery, G.T.2    Keaney Jr, J.F.3    Frei, B.4
  • 142
    • 15944403231 scopus 로고    scopus 로고
    • The iron chelator desferrioxamine inhibits atherosclerotic lesion development and decreases lesion iron concentrations in the cholesterol-fed rabbit
    • Minqin, R., Rajendran, R., Pan, N., Tan, B. K. et al., The iron chelator desferrioxamine inhibits atherosclerotic lesion development and decreases lesion iron concentrations in the cholesterol-fed rabbit. Free Radic. Biol. Med. 2005, 38, 1206-1211.
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1206-1211
    • Minqin, R.1    Rajendran, R.2    Pan, N.3    Tan, B.K.4
  • 143
    • 0035849568 scopus 로고    scopus 로고
    • Iron chelation improves endothelial function in patients with coronary artery disease
    • Duffy, S. J., Biegelsen, E. S., Holbrook, M., Russell, J. D. et al., Iron chelation improves endothelial function in patients with coronary artery disease. Circulation 2001, 103, 2799-2804.
    • (2001) Circulation , vol.103 , pp. 2799-2804
    • Duffy, S.J.1    Biegelsen, E.S.2    Holbrook, M.3    Russell, J.D.4
  • 144
    • 33645885351 scopus 로고    scopus 로고
    • Antioxidants protect from atherosclerosis by a heme oxygenase-1 pathway that is independent of free radical scavenging
    • Wu, B. J., Kathir, K., Witting, P. K., Beck, K. et al., Antioxidants protect from atherosclerosis by a heme oxygenase-1 pathway that is independent of free radical scavenging. J. Exp. Med. 2006, 203, 1117-1127.
    • (2006) J. Exp. Med. , vol.203 , pp. 1117-1127
    • Wu, B.J.1    Kathir, K.2    Witting, P.K.3    Beck, K.4
  • 145
    • 0032442153 scopus 로고    scopus 로고
    • Studies by electron paramagnetic resonance of the importance of iron in the hydroxyl scavenging properties of ascorbic acid in plasma: effects of iron chelators
    • Benderitter, M., Maupoil, V., Vergely, C., Dalloz, F. et al., Studies by electron paramagnetic resonance of the importance of iron in the hydroxyl scavenging properties of ascorbic acid in plasma: effects of iron chelators. Fundam. Clin. Pharmacol. 1998, 12, 510-516.
    • (1998) Fundam. Clin. Pharmacol. , vol.12 , pp. 510-516
    • Benderitter, M.1    Maupoil, V.2    Vergely, C.3    Dalloz, F.4
  • 146
    • 3242753676 scopus 로고    scopus 로고
    • The design and development of deferiprone (L1) and other iron chelators for clinical use: targeting methods and application prospects
    • Kontoghiorghes, G. J., Pattichis, K., Neocleous, K., Kolnagou, A., The design and development of deferiprone (L1) and other iron chelators for clinical use: targeting methods and application prospects. Curr. Med. Chem. 2004, 11, 2161-2183.
    • (2004) Curr. Med. Chem. , vol.11 , pp. 2161-2183
    • Kontoghiorghes, G.J.1    Pattichis, K.2    Neocleous, K.3    Kolnagou, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.