메뉴 건너뛰기




Volumn 11, Issue 12, 2010, Pages 1595-1604

Interaction of carbon monoxide with transition metals: Evolutionary insights into drug target discovery

Author keywords

Carbon monoxide; Carbon monoxide releasing molecules; Hemoglobin; Mitochondria; Transition metals

Indexed keywords

CARBON MONOXIDE; CARBON MONOXIDE RELEASING MOLECULE; CARBOXYHEMOGLOBIN; CYTOCHROME C OXIDASE; DRUG VEHICLE; HEME; HEMOGLOBIN; TRANSITION ELEMENT; UNCLASSIFIED DRUG; BIOLOGICAL MARKER; HEME OXYGENASE; IRON; ORGANOMETALLIC COMPOUND;

EID: 79952278599     PISSN: 13894501     EISSN: 18735592     Source Type: Journal    
DOI: 10.2174/1389450111009011595     Document Type: Review
Times cited : (46)

References (106)
  • 1
    • 0040141555 scopus 로고    scopus 로고
    • Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1
    • Liu Y, Ortiz de Montellano PR. Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1. J Biol Chem 2000; 275: 5297-307.
    • (2000) J Biol Chem , vol.275 , pp. 5297-5307
    • Liu, Y.1    Ortiz de Montellano, P.R.2
  • 3
    • 0035983247 scopus 로고    scopus 로고
    • Heme Oxygenase-1. The "emerging molecule" has arrived
    • Morse D, Choi AMK. Heme Oxygenase-1. The "emerging molecule" has arrived. Am J Respir Cell Mol Biol 2002; 27: 8-16.
    • (2002) Am J Respir Cell Mol Biol , vol.27 , pp. 8-16
    • Morse, D.1    Choi, A.M.K.2
  • 4
    • 41149177025 scopus 로고    scopus 로고
    • Pharmacological and clinical aspects of heme oxygenase
    • Abraham NG, Kappas A. Pharmacological and clinical aspects of heme oxygenase. Pharmacol Rev 2008; 60: 79-127.
    • (2008) Pharmacol Rev , vol.60 , pp. 79-127
    • Abraham, N.G.1    Kappas, A.2
  • 5
    • 0031577783 scopus 로고    scopus 로고
    • Involvement of the heme oxygenase-carbon monoxide pathway in keratinocyte proliferation
    • Clark JE, Green CJ, Motterlini R. Involvement of the heme oxygenase-carbon monoxide pathway in keratinocyte proliferation. Biochem Biophys Res Commun 1997; 241: 215-20.
    • (1997) Biochem Biophys Res Commun , vol.241 , pp. 215-220
    • Clark, J.E.1    Green, C.J.2    Motterlini, R.3
  • 6
    • 28744436501 scopus 로고    scopus 로고
    • Heme oxygenase 1 (HO-1) regulates osteoclastogenesis and bone resorption
    • Zwerina J, Tzima S, Hayer S, et al. Heme oxygenase 1 (HO-1) regulates osteoclastogenesis and bone resorption. FASEB J 2005; 19: 2011-3.
    • (2005) FASEB J , vol.19 , pp. 2011-2013
    • Zwerina, J.1    Tzima, S.2    Hayer, S.3
  • 7
    • 0031722008 scopus 로고    scopus 로고
    • Heme oxygenase-1 induction in skeletal muscle cells: Hemin and sodium nitroprusside are regulators in vitro
    • Vesely MJJ, Exon DJ, Clark JE, Foresti R, Green CJ, Motterlini R. Heme oxygenase-1 induction in skeletal muscle cells: hemin and sodium nitroprusside are regulators in vitro. Am J Physiol 1998; 275: C1087-94.
    • (1998) Am J Physiol , vol.275
    • Vesely, M.J.J.1    Exon, D.J.2    Clark, J.E.3    Foresti, R.4    Green, C.J.5    Motterlini, R.6
  • 8
    • 0032821356 scopus 로고    scopus 로고
    • Fibre type specificity of haem oxygenase-1 induction in rat skeletal muscle
    • Vesely MJJ, Sanders R, Green CJ, Motterlini R. Fibre type specificity of haem oxygenase-1 induction in rat skeletal muscle. FEBS Lett 1999; 458: 257-60.
    • (1999) FEBS Lett , vol.458 , pp. 257-260
    • Vesely, M.J.J.1    Sanders, R.2    Green, C.J.3    Motterlini, R.4
  • 9
    • 0036090811 scopus 로고    scopus 로고
    • Biological chemistry of carbon monoxide
    • Piantadosi CA. Biological chemistry of carbon monoxide. Antioxid Redox Signal 2002; 4: 259-70.
    • (2002) Antioxid Redox Signal , vol.4 , pp. 259-270
    • Piantadosi, C.A.1
  • 12
    • 37049243502 scopus 로고
    • A production of amino acids under possible primitive earth conditions
    • Miller SL. A production of amino acids under possible primitive earth conditions. Science 1953; 117: 528-9.
    • (1953) Science , vol.117 , pp. 528-529
    • Miller, S.L.1
  • 14
    • 0018255852 scopus 로고
    • Synthesis of organic compounds from carbon monoxide and water by UV photolysis
    • Bar-Nun A, Hartman H. Synthesis of organic compounds from carbon monoxide and water by UV photolysis. Orig Life 1978; 9: 93-101.
    • (1978) Orig Life , vol.9 , pp. 93-101
    • Bar-Nun, A.1    Hartman, H.2
  • 15
    • 0030620774 scopus 로고    scopus 로고
    • Activated acetic acid by carbon fixation on (Fe, Ni)S under primordial conditions
    • Huber C, Wachtershauser G. Activated acetic acid by carbon fixation on (Fe, Ni)S under primordial conditions. Science 1997; 276: 245-7.
    • (1997) Science , vol.276 , pp. 245-247
    • Huber, C.1    Wachtershauser, G.2
  • 17
    • 0028925554 scopus 로고
    • Carbon monoxide-dependent growth of Rhodospirillum rubrum
    • Kerby RL, Ludden PW, Roberts GP. Carbon monoxide-dependent growth of Rhodospirillum rubrum. J Bacteriol 1995; 177: 2241-4.
    • (1995) J Bacteriol , vol.177 , pp. 2241-2244
    • Kerby, R.L.1    Ludden, P.W.2    Roberts, G.P.3
  • 18
    • 0028963922 scopus 로고
    • Carbon monoxideinduced activation of gene expression in Rhodospirillum rubrum requires the product of cooA, a member of the cyclic AMP receptor protein family of transcriptional regulators
    • Shelver D, Kerby RL, He YP, Roberts GP. Carbon monoxideinduced activation of gene expression in Rhodospirillum rubrum requires the product of cooA, a member of the cyclic AMP receptor protein family of transcriptional regulators. J Bacteriol 1995; 177: 2157-63.
    • (1995) J Bacteriol , vol.177 , pp. 2157-2163
    • Shelver, D.1    Kerby, R.L.2    He, Y.P.3    Roberts, G.P.4
  • 19
    • 0024347769 scopus 로고
    • Regulation of carbon monoxide dehydrogenase and hydrogenase in Rhodospirillum rubrum: Effects of CO and oxygen on synthesis and activity
    • Bonam D, Lehman L, Roberts GP, Ludden PW. Regulation of carbon monoxide dehydrogenase and hydrogenase in Rhodospirillum rubrum: effects of CO and oxygen on synthesis and activity. J Bacteriol 1989; 171: 3102-7.
    • (1989) J Bacteriol , vol.171 , pp. 3102-3107
    • Bonam, D.1    Lehman, L.2    Roberts, G.P.3    Ludden, P.W.4
  • 21
    • 0344066227 scopus 로고    scopus 로고
    • Biochemical and biophysical properties of the CO-sensing transcriptional activator CooA
    • Aono S. Biochemical and biophysical properties of the CO-sensing transcriptional activator CooA. Acc Chem Res 2003; 36: 825-31.
    • (2003) Acc Chem Res , vol.36 , pp. 825-831
    • Aono, S.1
  • 23
    • 0037131241 scopus 로고    scopus 로고
    • A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase
    • Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science 2002; 298: 567-72.
    • (2002) Science , vol.298 , pp. 567-572
    • Doukov, T.I.1    Iverson, T.M.2    Seravalli, J.3    Ragsdale, S.W.4    Drennan, C.L.5
  • 24
    • 69449098185 scopus 로고    scopus 로고
    • Heme oxygenase-1/carbon monoxide: From metabolism to molecular therapy
    • Ryter SW, Choi AM. Heme oxygenase-1/carbon monoxide: from metabolism to molecular therapy. Am J Respir Cell Mol Biol 2009; 41: 251-60.
    • (2009) Am J Respir Cell Mol Biol , vol.41 , pp. 251-260
    • Ryter, S.W.1    Choi, A.M.2
  • 25
    • 43349092136 scopus 로고    scopus 로고
    • Use of carbon monoxide as a therapeutic agent: Promises and challenges
    • Foresti R, Bani-Hani MG, Motterlini R. Use of carbon monoxide as a therapeutic agent: promises and challenges. Intensive Care Med 2008; 34: 649-58.
    • (2008) Intensive Care Med , vol.34 , pp. 649-658
    • Foresti, R.1    Bani-Hani, M.G.2    Motterlini, R.3
  • 27
    • 48549090696 scopus 로고    scopus 로고
    • Carbon monoxide, reactive oxygen signaling, and oxidative stress
    • Piantadosi CA. Carbon monoxide, reactive oxygen signaling, and oxidative stress. Free Radic Biol Med 2008; 45: 562-9.
    • (2008) Free Radic Biol Med , vol.45 , pp. 562-569
    • Piantadosi, C.A.1
  • 28
    • 0022033461 scopus 로고
    • Carboxyhemoglobin levels in banked blood
    • Poulton TJ. Carboxyhemoglobin levels in banked blood. Chest 1985; 87: 408-9.
    • (1985) Chest , vol.87 , pp. 408-409
    • Poulton, T.J.1
  • 32
    • 49249103763 scopus 로고    scopus 로고
    • The diversity of carbon monoxide intoxication: Medical courses can differ extremely-A case report
    • Grieb G, Groger A, Bozkurt A, Stoffels I, Piatkowski A, Pallua N. The diversity of carbon monoxide intoxication: medical courses can differ extremely-A case report. Inhal Toxicol 2008; 20: 911-5.
    • (2008) Inhal Toxicol , vol.20 , pp. 911-915
    • Grieb, G.1    Groger, A.2    Bozkurt, A.3    Stoffels, I.4    Piatkowski, A.5    Pallua, N.6
  • 33
    • 33846079683 scopus 로고    scopus 로고
    • Hemorrhagic shock resuscitation with carbon monoxide saturated blood
    • Cabrales P, Tsai AG, Intaglietta M. Hemorrhagic shock resuscitation with carbon monoxide saturated blood. Resuscitation 2007; 72: 306-18.
    • (2007) Resuscitation , vol.72 , pp. 306-318
    • Cabrales, P.1    Tsai, A.G.2    Intaglietta, M.3
  • 34
    • 67649305095 scopus 로고    scopus 로고
    • Hemoglobin vesicles and red blood cells as carriers of carbon monoxide prior to oxygen for resuscitation after hemorrhagic shock in a rat model
    • Sakai H, Horinouchi H, Tsuchida E, Kobayashi K. Hemoglobin vesicles and red blood cells as carriers of carbon monoxide prior to oxygen for resuscitation after hemorrhagic shock in a rat model. Shock 2009; 31: 507-14.
    • (2009) Shock , vol.31 , pp. 507-514
    • Sakai, H.1    Horinouchi, H.2    Tsuchida, E.3    Kobayashi, K.4
  • 35
    • 0029792561 scopus 로고    scopus 로고
    • Isolation and oxygenation reactions of nitrosylmyoglobins
    • Arnold EV, Bohle DS. Isolation and oxygenation reactions of nitrosylmyoglobins. Methods Enzymol 1996; 269: 41-55.
    • (1996) Methods Enzymol , vol.269 , pp. 41-55
    • Arnold, E.V.1    Bohle, D.S.2
  • 38
    • 33847261166 scopus 로고    scopus 로고
    • Ligand dynamics in an electron transfer protein. Picosecond geminate recombination of carbon monoxide to heme in mutant forms of cytochrome c
    • Silkstone G, Jasaitis A, Wilson MT, Vos MH. Ligand dynamics in an electron transfer protein. Picosecond geminate recombination of carbon monoxide to heme in mutant forms of cytochrome c. J Biol Chem 2007; 282: 1638-49.
    • (2007) J Biol Chem , vol.282 , pp. 1638-1649
    • Silkstone, G.1    Jasaitis, A.2    Wilson, M.T.3    Vos, M.H.4
  • 39
    • 61749099621 scopus 로고    scopus 로고
    • Interaction of carbon monoxide with the apoptosis-inducing cytochrome c-cardiolipin complex
    • Kapetanaki SM, Silkstone G, Husu I, Liebl U, Wilson MT, Vos MH. Interaction of carbon monoxide with the apoptosis-inducing cytochrome c-cardiolipin complex. Biochemistry 2009; 48: 1613-9.
    • (2009) Biochemistry , vol.48 , pp. 1613-1619
    • Kapetanaki, S.M.1    Silkstone, G.2    Husu, I.3    Liebl, U.4    Wilson, M.T.5    Vos, M.H.6
  • 40
    • 0037428458 scopus 로고    scopus 로고
    • Carbon monoxide inhibition of apoptosis during ischemia-reperfusion lung injury is dependent on the p38 mitogen-activated protein kinase pathway and involves caspase 3
    • Zhang X, Shan P, Otterbein LE, et al. Carbon monoxide inhibition of apoptosis during ischemia-reperfusion lung injury is dependent on the p38 mitogen-activated protein kinase pathway and involves caspase 3. J Biol Chem 2003; 278: 1248-58.
    • (2003) J Biol Chem , vol.278 , pp. 1248-1258
    • Zhang, X.1    Shan, P.2    Otterbein, L.E.3
  • 41
    • 0041733077 scopus 로고    scopus 로고
    • Cardioprotective actions by a water-soluble carbon monoxide-releasing molecule
    • Clark JE, Naughton P, Shurey S, et al. Cardioprotective actions by a water-soluble carbon monoxide-releasing molecule. Circ Res 2003; 93: e2-8.
    • (2003) Circ Res , vol.93
    • Clark, J.E.1    Naughton, P.2    Shurey, S.3
  • 43
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin MT, Beal MF. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 2006; 443: 787-95.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 45
    • 21844468521 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain and NAD(P)H oxidase are targets for the antiproliferative effect of carbon monoxide in human airway smooth muscle
    • Taille C, El-Benna J, Lanone S, Boczkowski J, Motterlini R. Mitochondrial respiratory chain and NAD(P)H oxidase are targets for the antiproliferative effect of carbon monoxide in human airway smooth muscle. J Biol Chem 2005; 280: 25350-60.
    • (2005) J Biol Chem , vol.280 , pp. 25350-25360
    • Taille, C.1    El-Benna, J.2    Lanone, S.3    Boczkowski, J.4    Motterlini, R.5
  • 46
    • 54049113885 scopus 로고    scopus 로고
    • Carbon monoxide inhibits L-type Ca2+ channels via redox modulation of key cysteine residues by mitochondrial reactive oxygen species
    • Scragg JL, Dallas ML, Wilkinson JA, Varadi G, Peers C. Carbon monoxide inhibits L-type Ca2+ channels via redox modulation of key cysteine residues by mitochondrial reactive oxygen species. J Biol Chem 2008; 283: 24412-9.
    • (2008) J Biol Chem , vol.283 , pp. 24412-24419
    • Scragg, J.L.1    Dallas, M.L.2    Wilkinson, J.A.3    Varadi, G.4    Peers, C.5
  • 48
    • 33847291917 scopus 로고    scopus 로고
    • Carbon monoxide protects against hyperoxia-induced endothelial cell apoptosis by inhibiting reactive oxygen species formation
    • Wang X, Wang Y, Kim HP, Nakahira K, Ryter SW, Choi AM. Carbon monoxide protects against hyperoxia-induced endothelial cell apoptosis by inhibiting reactive oxygen species formation. J Biol Chem 2007; 282: 1718-26.
    • (2007) J Biol Chem , vol.282 , pp. 1718-1726
    • Wang, X.1    Wang, Y.2    Kim, H.P.3    Nakahira, K.4    Ryter, S.W.5    Choi, A.M.6
  • 49
    • 18744380991 scopus 로고    scopus 로고
    • Carbon monoxide prevents multiple organ injury in a model of hemorrhagic shock and resuscitation
    • Zuckerbraun BS, McCloskey CA, Gallo D, et al. Carbon monoxide prevents multiple organ injury in a model of hemorrhagic shock and resuscitation. Shock 2005; 23: 527-32.
    • (2005) Shock , vol.23 , pp. 527-532
    • Zuckerbraun, B.S.1    McCloskey, C.A.2    Gallo, D.3
  • 50
    • 33846237222 scopus 로고    scopus 로고
    • Carbon monoxide inhalation rescues mice from fulminant hepatitis through improving hepatic energy metabolism
    • Tsui TY, Obed A, Siu YT, et al. Carbon monoxide inhalation rescues mice from fulminant hepatitis through improving hepatic energy metabolism. Shock 2007; 27: 165-71.
    • (2007) Shock , vol.27 , pp. 165-171
    • Tsui, T.Y.1    Obed, A.2    Siu, Y.T.3
  • 51
    • 9444268085 scopus 로고    scopus 로고
    • Carbon monoxide improves cardiac energetics and safeguards the heart during reperfusion after cardiopulmonary bypass in pigs
    • Lavitrano M, Smolenski RT, Musumeci A, et al. Carbon monoxide improves cardiac energetics and safeguards the heart during reperfusion after cardiopulmonary bypass in pigs. FASEB J 2004; 18: 1093-5.
    • (2004) FASEB J , vol.18 , pp. 1093-1095
    • Lavitrano, M.1    Smolenski, R.T.2    Musumeci, A.3
  • 52
    • 33846993042 scopus 로고    scopus 로고
    • A new activating role for CO in cardiac mitochondrial biogenesis
    • Suliman HB, Carraway MS, Tatro LG, Piantadosi CA. A new activating role for CO in cardiac mitochondrial biogenesis. J Cell Sci 2006; 120: 299-308.
    • (2006) J Cell Sci , vol.120 , pp. 299-308
    • Suliman, H.B.1    Carraway, M.S.2    Tatro, L.G.3    Piantadosi, C.A.4
  • 53
    • 65649135789 scopus 로고    scopus 로고
    • Carbon monoixde rescues mice from lethal sepsis by supporting mitochondrial energetic metabolism and activating mitochondrial biogenesis
    • Lancel S, Hassoun SM, Favory R, Decoster B, Motterlini R, Neviere R. Carbon monoixde rescues mice from lethal sepsis by supporting mitochondrial energetic metabolism and activating mitochondrial biogenesis. J Pharmacol Exp Ther 2009; 1329: 641-8.
    • (2009) J Pharmacol Exp Ther , vol.1329 , pp. 641-648
    • Lancel, S.1    Hassoun, S.M.2    Favory, R.3    Decoster, B.4    Motterlini, R.5    Neviere, R.6
  • 54
    • 58149328569 scopus 로고    scopus 로고
    • Heme oxygenase-1 regulates cardiac mitochondrial biogenesis via Nrf2-mediated transcriptional control of nuclear respiratory factor-1
    • Piantadosi CA, Carraway MS, Babiker A, Suliman HB. Heme oxygenase-1 regulates cardiac mitochondrial biogenesis via Nrf2-mediated transcriptional control of nuclear respiratory factor-1. Circ Res 2008; 103: 1232-40.
    • (2008) Circ Res , vol.103 , pp. 1232-1240
    • Piantadosi, C.A.1    Carraway, M.S.2    Babiker, A.3    Suliman, H.B.4
  • 55
    • 67650067091 scopus 로고    scopus 로고
    • Carbon monoxide, skeletal muscle oxidative stress, and mitochondrial biogenesis in humans
    • Rhodes MA, Carraway MS, Piantadosi CA, et al. Carbon monoxide, skeletal muscle oxidative stress, and mitochondrial biogenesis in humans. Am J Physiol Heart Circ Physiol 2009; 297: H392-9.
    • (2009) Am J Physiol Heart Circ Physiol , vol.297
    • Rhodes, M.A.1    Carraway, M.S.2    Piantadosi, C.A.3
  • 56
    • 19644368345 scopus 로고    scopus 로고
    • Nitric oxide: Orchestrating hypoxia regulation through mitochondrial respiration and the endoplasmic reticulum stress response
    • Xu W, Charles IG, Moncada S. Nitric oxide: orchestrating hypoxia regulation through mitochondrial respiration and the endoplasmic reticulum stress response. Cell Res 2005; 15: 63-5.
    • (2005) Cell Res , vol.15 , pp. 63-65
    • Xu, W.1    Charles, I.G.2    Moncada, S.3
  • 57
    • 49449115443 scopus 로고    scopus 로고
    • CO-MP4, a polyethylene glycol-conjugated haemoglobin derivative and carbon monoxide carrier that reduces myocardial infarct size in rats
    • Vandegriff KD, Young MA, Lohman J, et al. CO-MP4, a polyethylene glycol-conjugated haemoglobin derivative and carbon monoxide carrier that reduces myocardial infarct size in rats. Br J Pharmacol 2008; 154: 1649-61.
    • (2008) Br J Pharmacol , vol.154 , pp. 1649-1661
    • Vandegriff, K.D.1    Young, M.A.2    Lohman, J.3
  • 58
    • 0005310902 scopus 로고
    • 100 Years of metal carbonyls. A serendipitous chemical discovery of major scientific and industrial impact
    • Herrmann WA. 100 Years of metal carbonyls. A serendipitous chemical discovery of major scientific and industrial impact. J Organomet Chem 1990; 383: 21-44.
    • (1990) J Organomet Chem , vol.383 , pp. 21-44
    • Herrmann, W.A.1
  • 59
    • 0001366582 scopus 로고
    • Photochemistry of metal-metal bonded complexes. II. The photochemistry of rhenium and manganese carbonyl complexes containing a metal-metal bond
    • Wrighton MS, Ginley DS. Photochemistry of metal-metal bonded complexes. II. The photochemistry of rhenium and manganese carbonyl complexes containing a metal-metal bond. J Am Chem Soc 1975; 97: 2065-72.
    • (1975) J Am Chem Soc , vol.97 , pp. 2065-2072
    • Wrighton, M.S.1    Ginley, D.S.2
  • 60
    • 0037622140 scopus 로고    scopus 로고
    • Carbon monoxide-releasing molecules: Characterization of biochemical and vascular activities
    • Motterlini R, Clark JE, Foresti R, Sarathchandra P, Mann BE, Green CJ. Carbon monoxide-releasing molecules: characterization of biochemical and vascular activities. Circ Res 2002; 90: E17-24.
    • (2002) Circ Res , vol.90 , pp. 17-24
    • Motterlini, R.1    Clark, J.E.2    Foresti, R.3    Sarathchandra, P.4    Mann, B.E.5    Green, C.J.6
  • 61
    • 27744492554 scopus 로고    scopus 로고
    • Therapeutic applications of carbon monoxide-releasing molecules (CO-RMs)
    • Motterlini R, Mann BE, Foresti R. Therapeutic applications of carbon monoxide-releasing molecules (CO-RMs). Expert Opin Investig Drugs 2005; 14: 1305-18.
    • (2005) Expert Opin Investig Drugs , vol.14 , pp. 1305-1318
    • Motterlini, R.1    Mann, B.E.2    Foresti, R.3
  • 62
    • 24144476659 scopus 로고    scopus 로고
    • Therapy from a silent killer
    • Mann BE, Motterlini R. Therapy from a silent killer. Chem Ind 2005; 16: 16-8.
    • (2005) Chem Ind , vol.16 , pp. 16-18
    • Mann, B.E.1    Motterlini, R.2
  • 63
    • 34247365619 scopus 로고    scopus 로고
    • Chemistry and biological activities of CO-releasing molecules (CORMs) and transition metal complexes
    • Alberto R, Motterlini R. Chemistry and biological activities of CO-releasing molecules (CORMs) and transition metal complexes. Dalton Trans 2007; 1651-60.
    • (2007) Dalton Trans , pp. 1651-1660
    • Alberto, R.1    Motterlini, R.2
  • 64
    • 36749043642 scopus 로고    scopus 로고
    • Carbon monoxide-releasing molecules (CO-RMs): Vasodilatory, anti-ischemic and anti-inflammatory activities
    • Motterlini R. Carbon monoxide-releasing molecules (CO-RMs): vasodilatory, anti-ischemic and anti-inflammatory activities. Biochem Soc Trans 2007; 35: 1142-6.
    • (2007) Biochem Soc Trans , vol.35 , pp. 1142-1146
    • Motterlini, R.1
  • 67
    • 30344442146 scopus 로고    scopus 로고
    • ee-Pyrone iron(0) carbonyl complexes as effective CO-releasing molecules (CO-RMs)
    • Fairlamb IJS, Duhme-Klair AK, Lynam JM, et al. ee-Pyrone iron(0) carbonyl complexes as effective CO-releasing molecules (CO-RMs). Bioorg Med Chem Lett 2006; 16: 995-8.
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 995-998
    • Fairlamb, I.J.S.1    Duhme-Klair, A.K.2    Lynam, J.M.3
  • 68
    • 33745285383 scopus 로고    scopus 로고
    • Bioactive properties of iron-containing carbon monoxide-releasing molecules (CO-RMs)
    • Sawle P, Hammad J, Fairlamb IJ, et al. Bioactive properties of iron-containing carbon monoxide-releasing molecules (CO-RMs). J Pharmacol Exp Ther 2006; 318: 403-10.
    • (2006) J Pharmacol Exp Ther , vol.318 , pp. 403-410
    • Sawle, P.1    Hammad, J.2    Fairlamb, I.J.3
  • 69
    • 35548990674 scopus 로고    scopus 로고
    • [([-C(5)H(4)R)Fe(CO)(2)X], X = Cl, Br, I, NO(3), CO(2)Me and [(C-C(5)H(4)R)Fe(CO)(3)](+), R = (CH(2)(n)CO(2)Me (n = 0-2), and CO(2)CH(2)CH(2)OH: A new group of CO-releasing molecules
    • Scapens D, Adams H, Johnson TR, et al. [([-C(5)H(4)R)Fe(CO)(2)X], X = Cl, Br, I, NO(3), CO(2)Me and [(C-C(5)H(4)R)Fe(CO)(3)](+), R = (CH(2)(n)CO(2)Me (n = 0-2), and CO(2)CH(2)CH(2)OH: a new group of CO-releasing molecules. Dalton Trans 2007; 4962-73.
    • (2007) Dalton Trans , pp. 4962-4973
    • Scapens, D.1    Adams, H.2    Johnson, T.R.3
  • 70
    • 67249154377 scopus 로고    scopus 로고
    • mu(2)-Alkyne dicobalt(0)hexacarbonyl complexes as carbon monoxide-releasing molecules (CO-RMs): Probing the release mechanism
    • Atkin AJ, Williams S, Sawle P, Motterlini R, Lynam JM, Fairlamb IJ. mu(2)-Alkyne dicobalt(0)hexacarbonyl complexes as carbon monoxide-releasing molecules (CO-RMs): probing the release mechanism. Dalton Trans 2009; 3653-6.
    • (2009) Dalton Trans , pp. 3653-3656
    • Atkin, A.J.1    Williams, S.2    Sawle, P.3    Motterlini, R.4    Lynam, J.M.5    Fairlamb, I.J.6
  • 71
    • 13244291654 scopus 로고    scopus 로고
    • CORM-A1: A new pharmacologically active carbon monoxide-releasing molecule
    • Motterlini R, Sawle P, Bains S, et al. CORM-A1: a new pharmacologically active carbon monoxide-releasing molecule. FASEB J 2005; 19: 284-6.
    • (2005) FASEB J , vol.19 , pp. 284-286
    • Motterlini, R.1    Sawle, P.2    Bains, S.3
  • 72
    • 3042826932 scopus 로고    scopus 로고
    • Vasoactive properties of CORM-3, a novel water-soluble carbon monoxide-releasing molecule
    • Foresti R, Hammad J, Clark JE, et al. Vasoactive properties of CORM-3, a novel water-soluble carbon monoxide-releasing molecule. Br J Pharmacol 2004; 142: 453-60.
    • (2004) Br J Pharmacol , vol.142 , pp. 453-460
    • Foresti, R.1    Hammad, J.2    Clark, J.E.3
  • 73
    • 23044459608 scopus 로고    scopus 로고
    • Carbon monoxide-releasing molecules (CO-RMs) attenuate the inflammatory response elicited by lipopolysaccharide in RAW264.7 murine macrophages
    • Sawle P, Foresti R, Mann BE, Johnson TR, Green CJ, Motterlini R. Carbon monoxide-releasing molecules (CO-RMs) attenuate the inflammatory response elicited by lipopolysaccharide in RAW264.7 murine macrophages. Br J Pharmacol 2005; 145: 800-10.
    • (2005) Br J Pharmacol , vol.145 , pp. 800-810
    • Sawle, P.1    Foresti, R.2    Mann, B.E.3    Johnson, T.R.4    Green, C.J.5    Motterlini, R.6
  • 74
    • 33747609353 scopus 로고    scopus 로고
    • Modulation of thrombin-induced neuroinflammation in BV-2 microglia by a carbon monoxide-releasing molecule (CORM-3)
    • Bani-Hani MG, Greenstein D, Mann BE, Green CJ, Motterlini R. Modulation of thrombin-induced neuroinflammation in BV-2 microglia by a carbon monoxide-releasing molecule (CORM-3). J Pharmacol Exp Ther 2006; 318: 1315-22.
    • (2006) J Pharmacol Exp Ther , vol.318 , pp. 1315-1322
    • Bani-Hani, M.G.1    Greenstein, D.2    Mann, B.E.3    Green, C.J.4    Motterlini, R.5
  • 75
    • 1942437473 scopus 로고    scopus 로고
    • Administration of a CO-releasing molecule at the time of reperfusion reduces infarct size in vivo
    • Guo Y, Stein AB, Wu WJ, Tan W, Zhu X, Li QH et al. Administration of a CO-releasing molecule at the time of reperfusion reduces infarct size in vivo. Am J Physiol Heart Circ Physiol 2004; 286: H1649-53.
    • (2004) Am J Physiol Heart Circ Physiol , vol.286
    • Guo, Y.1    Stein, A.B.2    Wu, W.J.3    Tan, W.4    Zhu, X.5    Li, Q.H.6
  • 76
    • 33845603148 scopus 로고    scopus 로고
    • Positive inotropic effects of carbon monoxide-releasing molecules (CO-RMs) in the isolated perfused rat heart
    • Musameh MD, Fuller BJ, Mann BE, Green CJ, Motterlini R. Positive inotropic effects of carbon monoxide-releasing molecules (CO-RMs) in the isolated perfused rat heart. Br J Pharmacol 2006; 149: 1104-12.
    • (2006) Br J Pharmacol , vol.149 , pp. 1104-1112
    • Musameh, M.D.1    Fuller, B.J.2    Mann, B.E.3    Green, C.J.4    Motterlini, R.5
  • 77
    • 77649293826 scopus 로고    scopus 로고
    • CO Liberated from a Carbon Monoxide-Releasing Molecule Exerts a Positive Inotropic Effect in Doxorubicin-Induced Cardiomyopathy
    • Musameh MD, Green CJ, Mann BE, Motterlini R, Fuller BJ. CO Liberated from a Carbon Monoxide-Releasing Molecule Exerts a Positive Inotropic Effect in Doxorubicin-Induced Cardiomyopathy. J Cardiovasc Pharmacol 2010; 55: 168-75.
    • (2010) J Cardiovasc Pharmacol , vol.55 , pp. 168-175
    • Musameh, M.D.1    Green, C.J.2    Mann, B.E.3    Motterlini, R.4    Fuller, B.J.5
  • 78
    • 33644638482 scopus 로고    scopus 로고
    • Treatment with carbon monoxide-releasing molecules (CORMs) during cold storage improves renal function at reperfusion
    • Sandouka A, Fuller BJ, Mann BE, Green CJ, Foresti R, Motterlini R. Treatment with carbon monoxide-releasing molecules (CORMs) during cold storage improves renal function at reperfusion. Kidney Int 2006; 69: 239-47.
    • (2006) Kidney Int , vol.69 , pp. 239-247
    • Sandouka, A.1    Fuller, B.J.2    Mann, B.E.3    Green, C.J.4    Foresti, R.5    Motterlini, R.6
  • 79
    • 36048947996 scopus 로고    scopus 로고
    • Improved myocardial function after cold storage with preservation solution supplemented with a carbon monoxide-releasing molecule (CORM-3)
    • Musameh MD, Green CJ, Mann BE, Fuller BJ, Motterlini R. Improved myocardial function after cold storage with preservation solution supplemented with a carbon monoxide-releasing molecule (CORM-3). J Heart Lung Transplant 2007; 26: 1192-8.
    • (2007) J Heart Lung Transplant , vol.26 , pp. 1192-1198
    • Musameh, M.D.1    Green, C.J.2    Mann, B.E.3    Fuller, B.J.4    Motterlini, R.5
  • 80
    • 67349176092 scopus 로고    scopus 로고
    • Protective effects of a carbon monoxide-releasing molecule (CORM-3) during hepatic cold preservation
    • Pizarro MD, Rodriguez JV, Mamprin ME, et al. Protective effects of a carbon monoxide-releasing molecule (CORM-3) during hepatic cold preservation. Cryobiology 2009; 58: 248-55.
    • (2009) Cryobiology , vol.58 , pp. 248-255
    • Pizarro, M.D.1    Rodriguez, J.V.2    Mamprin, M.E.3
  • 81
    • 50249111616 scopus 로고    scopus 로고
    • Treatment with a CO-releasing molecule (CORM-3) reduces joint inflammation and erosion in murine collagen-induced arthritis
    • Ferrandiz ML, Maicas N, Garcia-Arnandis I, et al. Treatment with a CO-releasing molecule (CORM-3) reduces joint inflammation and erosion in murine collagen-induced arthritis. Ann Rheum Dis 2008; 67: 1211-7.
    • (2008) Ann Rheum Dis , vol.67 , pp. 1211-1217
    • Ferrandiz, M.L.1    Maicas, N.2    Garcia-Arnandis, I.3
  • 82
    • 63249116346 scopus 로고    scopus 로고
    • Carbon monoxidereleasing antibacterial molecules target respiration and global transcriptional regulators
    • Davidge KS, Sanguinetti G, Yee CH, et al. Carbon monoxidereleasing antibacterial molecules target respiration and global transcriptional regulators. J Biol Chem 2009; 284: 4516-24.
    • (2009) J Biol Chem , vol.284 , pp. 4516-4524
    • Davidge, K.S.1    Sanguinetti, G.2    Yee, C.H.3
  • 83
    • 65349103539 scopus 로고    scopus 로고
    • A carbon monoxidereleasing molecule (CORM-3) exerts bactericidal activity against Pseudomonas aeruginosa and improves survival in an animal model of bacteraemia
    • Desmard M, Davidge KS, Bouvet O, et al. A carbon monoxidereleasing molecule (CORM-3) exerts bactericidal activity against Pseudomonas aeruginosa and improves survival in an animal model of bacteraemia. FASEB J 2009; 23: 1023-31.
    • (2009) FASEB J , vol.23 , pp. 1023-1031
    • Desmard, M.1    Davidge, K.S.2    Bouvet, O.3
  • 84
    • 61649124114 scopus 로고    scopus 로고
    • Water-soluble CO-releasing molecules (CO-RMs) reduce the development of postoperative ileus via modulation of MAPK/HO-1 signaling and reduction of oxidative stress
    • De Backer O, Elinck E, Blanckaert B, Leybaert L, Motterlini R, Lefebvre RA. Water-soluble CO-releasing molecules (CO-RMs) reduce the development of postoperative ileus via modulation of MAPK/HO-1 signaling and reduction of oxidative stress. Gut 2009; 58: 347-56.
    • (2009) Gut , vol.58 , pp. 347-356
    • de Backer, O.1    Elinck, E.2    Blanckaert, B.3    Leybaert, L.4    Motterlini, R.5    Lefebvre, R.A.6
  • 85
    • 70949103175 scopus 로고    scopus 로고
    • Carbon Monoxide Rapidly Impairs Alveolar Fluid Clearance by Inhibiting Epithelial Sodium Channels
    • Althaus M, Fronius M, Buchackert Y, et al. Carbon Monoxide Rapidly Impairs Alveolar Fluid Clearance by Inhibiting Epithelial Sodium Channels. Am J Respir Cell Mol Biol 2009; 41: 639-50.
    • (2009) Am J Respir Cell Mol Biol , vol.41 , pp. 639-650
    • Althaus, M.1    Fronius, M.2    Buchackert, Y.3
  • 86
    • 33745449736 scopus 로고    scopus 로고
    • Carbon monoxide released by CORM-3 inhibits human platelets by a mechanism independent of soluble guanylate cyclase
    • Chlopicki S, Olszanecki R, Marcinkiewicz E, Lomnicka M, Motterlini R. Carbon monoxide released by CORM-3 inhibits human platelets by a mechanism independent of soluble guanylate cyclase. Cardiovasc Res 2006; 71: 393-401.
    • (2006) Cardiovasc Res , vol.71 , pp. 393-401
    • Chlopicki, S.1    Olszanecki, R.2    Marcinkiewicz, E.3    Lomnicka, M.4    Motterlini, R.5
  • 87
    • 61449255986 scopus 로고    scopus 로고
    • Carbon monoxide inhibits TLR-induced dendritic cell immunogenicity
    • Remy S, Blancou P, Tesson L, et al. Carbon monoxide inhibits TLR-induced dendritic cell immunogenicity. J Immunol 2009; 182: 1877-84.
    • (2009) J Immunol , vol.182 , pp. 1877-1884
    • Remy, S.1    Blancou, P.2    Tesson, L.3
  • 88
    • 67649947461 scopus 로고    scopus 로고
    • Carbon monoxide rescues heme oxygenase-1-deficient mice from arterial thrombosis in allogeneic aortic transplantation
    • Chen B, Guo L, Fan C, Bolisetty S, et al. Carbon monoxide rescues heme oxygenase-1-deficient mice from arterial thrombosis in allogeneic aortic transplantation. Am J Pathol 2009; 175: 422-9.
    • (2009) Am J Pathol , vol.175 , pp. 422-429
    • Chen, B.1    Guo, L.2    Fan, C.3    Bolisetty, S.4
  • 89
    • 77951878150 scopus 로고    scopus 로고
    • Cardioprotective and antiapoptotic effects of heme oxygenase-1 in the failing heart
    • Wang G, Hamid T, Keith RJ, et al. Cardioprotective and antiapoptotic effects of heme oxygenase-1 in the failing heart. Circulation 2010; 121: 1912-25.
    • (2010) Circulation , vol.121 , pp. 1912-1925
    • Wang, G.1    Hamid, T.2    Keith, R.J.3
  • 90
    • 33748526198 scopus 로고    scopus 로고
    • UV-Visible and electrochemical monitoring of carbon monoxide release by donor complexes to myoglobin solutions and to electrodes modified with films containing hemin
    • Obirai JC, Hamadi S, Ithurbide A, et al. UV-Visible and electrochemical monitoring of carbon monoxide release by donor complexes to myoglobin solutions and to electrodes modified with films containing hemin. Electroanalyis 2006; 1689-95.
    • (2006) Electroanalyis , pp. 1689-1695
    • Obirai, J.C.1    Hamadi, S.2    Ithurbide, A.3
  • 91
    • 67649237642 scopus 로고    scopus 로고
    • Diversity and design of metal-based carbon monoxidereleasing molecules (CO-RMs) in aqueous systems: Revealing the essential trends
    • Zhang WQ, Atkin AJ, Thatcher RJ, Whitwood AC, Fairlamb IJ, Lynam JM. Diversity and design of metal-based carbon monoxidereleasing molecules (CO-RMs) in aqueous systems: revealing the essential trends. Dalton Trans 2009; 4351-8.
    • (2009) Dalton Trans , pp. 4351-4358
    • Zhang, W.Q.1    Atkin, A.J.2    Thatcher, R.J.3    Whitwood, A.C.4    Fairlamb, I.J.5    Lynam, J.M.6
  • 92
    • 0025977048 scopus 로고
    • Signal transduction mechanisms involving NO
    • Ignarro LJ. Signal transduction mechanisms involving NO. Biochem Pharmacol 1991; 41: 485-90.
    • (1991) Biochem Pharmacol , vol.41 , pp. 485-490
    • Ignarro, L.J.1
  • 94
    • 0031767014 scopus 로고    scopus 로고
    • Carbon monoxide is a major contributor to the regulation of vascular tone in aortas expressing high levels of haeme oxygenase-1
    • Sammut IA, Foresti R, Clark JE, et al. Carbon monoxide is a major contributor to the regulation of vascular tone in aortas expressing high levels of haeme oxygenase-1. Br J Pharmacol 1998; 125: 1437-44.
    • (1998) Br J Pharmacol , vol.125 , pp. 1437-1444
    • Sammut, I.A.1    Foresti, R.2    Clark, J.E.3
  • 95
    • 0032494085 scopus 로고    scopus 로고
    • Heme oxygenase-1-derived carbon monoxide contributes to the suppression of acute hypertensive responses in vivo
    • Motterlini R, Gonzales A, Foresti R, Clark JE, Green CJ, Winslow RM. Heme oxygenase-1-derived carbon monoxide contributes to the suppression of acute hypertensive responses in vivo. Circ Res 1998; 83: 568-77.
    • (1998) Circ Res , vol.83 , pp. 568-577
    • Motterlini, R.1    Gonzales, A.2    Foresti, R.3    Clark, J.E.4    Green, C.J.5    Winslow, R.M.6
  • 96
    • 0344284580 scopus 로고    scopus 로고
    • Carbon monoxide suppresses arteriosclerotic lesions associated with chronic graft rejection and with balloon injury
    • Otterbein LE, Zuckerbraun BS, Haga M, et al. Carbon monoxide suppresses arteriosclerotic lesions associated with chronic graft rejection and with balloon injury. Nat Med 2003; 9: 183-90.
    • (2003) Nat Med , vol.9 , pp. 183-190
    • Otterbein, L.E.1    Zuckerbraun, B.S.2    Haga, M.3
  • 99
    • 0030610004 scopus 로고    scopus 로고
    • Ca channels by carbon monoxide in vascular smooth muscle cells
    • Ca channels by carbon monoxide in vascular smooth muscle cells. J Biol Chem 1997; 272: 8222-6.
    • (1997) J Biol Chem , vol.272 , pp. 8222-8226
    • Wang, R.1    Wu, L.2
  • 100
    • 26844519194 scopus 로고    scopus 로고
    • Heme is a carbon monoxide receptor for large-conductance Ca2+-activated K+ channels
    • Jaggar JH, Li A, Parfenova H, et al. Heme is a carbon monoxide receptor for large-conductance Ca2+-activated K+ channels. Circ Res 2005; 97: 805-12.
    • (2005) Circ Res , vol.97 , pp. 805-812
    • Jaggar, J.H.1    Li, A.2    Parfenova, H.3
  • 101
    • 10844248490 scopus 로고    scopus 로고
    • Hemoxygenase-2 is an oxygen sensor for a calcium-sensitive potassium channel
    • Williams SE, Wootton P, Mason HS, et al. Hemoxygenase-2 is an oxygen sensor for a calcium-sensitive potassium channel. Science 2004; 306: 2093-7.
    • (2004) Science , vol.306 , pp. 2093-2097
    • Williams, S.E.1    Wootton, P.2    Mason, H.S.3
  • 102
    • 43149105180 scopus 로고    scopus 로고
    • A structural motif in the C-terminal tail of slo1 confers carbon monoxide sensitivity to human BK(Ca) channels
    • Williams SE, Brazier SP, Baban N, et al. A structural motif in the C-terminal tail of slo1 confers carbon monoxide sensitivity to human BK(Ca) channels. Pflugers Arch 2008; 456: 561-72.
    • (2008) Pflugers Arch , vol.456 , pp. 561-572
    • Williams, S.E.1    Brazier, S.P.2    Baban, N.3
  • 103
    • 61849162674 scopus 로고    scopus 로고
    • Targeting proteins with metal complexes
    • (Camb)
    • Meggers E. Targeting proteins with metal complexes. Chem Commun (Camb) 2009; 1001-10.
    • (2009) Chem Commun , pp. 1001-1010
    • Meggers, E.1
  • 104
    • 73249139334 scopus 로고    scopus 로고
    • Inhibition of the [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F by carbon monoxide: An FTIR and EPR spectroscopic study
    • Pandelia ME, Ogata H, Currell LJ, Flores M, Lubitz W. Inhibition of the [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F by carbon monoxide: an FTIR and EPR spectroscopic study. Biochim Biophys Acta 2010; 1797: 304-13.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 304-313
    • Pandelia, M.E.1    Ogata, H.2    Currell, L.J.3    Flores, M.4    Lubitz, W.5
  • 105
    • 0034071424 scopus 로고    scopus 로고
    • Carbon monoxide has antiinflammatory effects involving the mitogen-activated protein kinase pathway
    • Otterbein LE, Bach FH, Alam J, et al. Carbon monoxide has antiinflammatory effects involving the mitogen-activated protein kinase pathway. Nature Med 2000; 6: 422-8.
    • (2000) Nature Med , vol.6 , pp. 422-428
    • Otterbein, L.E.1    Bach, F.H.2    Alam, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.