메뉴 건너뛰기




Volumn 18, Issue 17, 2013, Pages 2298-2313

Molecular controls of the oxygenation and redox reactions of hemoglobin

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD SUBSTITUTE; HEMOGLOBIN; HEMOPROTEIN;

EID: 84876907799     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.4947     Document Type: Review
Times cited : (55)

References (127)
  • 1
    • 79551477079 scopus 로고    scopus 로고
    • Haptoglobin: Old protein with new functions
    • Alayash AI. Haptoglobin: old protein with new functions. Clin Chim Acta 412: 493-498, 2011.
    • (2011) Clin Chim Acta , vol.412 , pp. 493-498
    • Alayash, A.I.1
  • 2
    • 0033022393 scopus 로고    scopus 로고
    • Hemoglobin-based blood substitutes: Oxygen carriers, pressor agents, or oxidants?
    • DOI 10.1038/9849
    • Alayash AI. Hemoglobin-based blood substitutes: oxygen carriers, pressor agents, or oxidants? Nat Biotechnol 17: 545-549, 1999. (Pubitemid 29262916)
    • (1999) Nature Biotechnology , vol.17 , Issue.6 , pp. 545-549
    • Alayash, A.I.1
  • 3
    • 1242353138 scopus 로고    scopus 로고
    • Oxygen therapeutics: Can we tame haemoglobin?
    • Alayash AI. Oxygen therapeutics: can we tame haemoglobin? Nat Rev Drug Discov 3: 152-159, 2004. (Pubitemid 38239776)
    • (2004) Nature Reviews Drug Discovery , vol.3 , Issue.2 , pp. 152-159
    • Alayash, A.I.1
  • 4
    • 77953353898 scopus 로고    scopus 로고
    • Setbacks in blood substitutes research and development: A biochemical perspective
    • Alayash AI. Setbacks in blood substitutes research and development: a biochemical perspective. Clin Lab Med 30: 381-389, 2010.
    • (2010) Clin Lab Med , vol.30 , pp. 381-389
    • Alayash, A.I.1
  • 6
    • 0033593463 scopus 로고    scopus 로고
    • Reactions of sperm whale myoglobin with hydrogen peroxide: Effects of distal pocket mutations on the formation and stability of ferryl intermediate
    • Alayash AI, Ryan BA, Eich RF, Olson JS, and Cashon RE. Reactions of sperm whale myoglobin with hydrogen peroxide: effects of distal pocket mutations on the formation and stability of ferryl intermediate. J Biol Chem 274: 2029-2037, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 2029-2037
    • Alayash, A.I.1    Ryan, B.A.2    Eich, R.F.3    Olson, J.S.4    Cashon, R.E.5
  • 9
    • 0000462106 scopus 로고
    • The origin and functions of haemoglobin in plants
    • Appleby CA. The origin and functions of haemoglobin in plants. Sci Prog 76: 365-398, 1992.
    • (1992) Sci Prog , vol.76 , pp. 365-398
    • Appleby, C.A.1
  • 10
    • 65249151456 scopus 로고    scopus 로고
    • Structural analysis of fish versus mammalian hemoglobins: Effect of the heme pocket environment on autooxidation and hemin loss
    • Aranda R IV, Cai H, Worley CE, Levin EJ, Li R, Olson JS, Phillips GN, Jr., and Richards MP. Structural analysis of fish versus mammalian hemoglobins: effect of the heme pocket environment on autooxidation and hemin loss. Proteins 75: 217-230, 2009.
    • (2009) Proteins , vol.75 , pp. 217-230
    • Aranda, I.V.R.1    Cai, H.2    Worley, C.E.3    Levin, E.J.4    Li, R.5    Olson, J.S.6    Phillips Jr., G.N.7    Richards, M.P.8
  • 11
    • 0017705575 scopus 로고
    • Structure of human deoxyhemoglobin specifically modified with pyridoxal compounds
    • DOI 10.1016/0022-2836(77)90107-3
    • Arnone A, Benesch RE, and Benesch R. Structure of human deoxy hemoglobin specifically modified with pyridoxal compounds. J Mol Biol 115: 627-642, 1977. (Pubitemid 8206042)
    • (1977) Journal of Molecular Biology , vol.115 , Issue.4 , pp. 627-642
    • Arnone, A.1    Benesch, R.E.2    Benesch, R.3
  • 12
    • 84859712543 scopus 로고    scopus 로고
    • Hemoglobin-driven pathophysiology is an in vivo consequence of the red blood cell storage lesion that can be attenuated in guinea pigs by haptoglobin therapy
    • Baek JH, D'Agnillo F, Vallelian F, Pereira CP, Williams MC, Jia Y, Schaer DJ, and Buehler PW. Hemoglobin-driven pathophysiology is an in vivo consequence of the red blood cell storage lesion that can be attenuated in guinea pigs by haptoglobin therapy. J Clin Invest 122: 1444-1458, 2012.
    • (2012) J Clin Invest , vol.122 , pp. 1444-1458
    • Baek, J.H.1    D'Agnillo, F.2    Vallelian, F.3    Pereira, C.P.4    Williams, M.C.5    Jia, Y.6    Schaer, D.J.7    Buehler, P.W.8
  • 13
    • 0027033841 scopus 로고
    • Endothelial cell heme oxygenase and ferritin induction by heme proteins: A possible mechanism limiting shock damage
    • Balla J, Jacob HS, Balla G, Nath K, and Vercellotti GM. Endothelial cell heme oxygenase and ferritin induction by heme proteins: a possible mechanism limiting shock damage. Trans Assoc Am Physicians 105: 1-6, 1992.
    • (1992) Trans Assoc Am Physicians , vol.105 , pp. 1-6
    • Balla, J.1    Jacob, H.S.2    Balla, G.3    Nath, K.4    Vercellotti, G.M.5
  • 15
    • 0018720275 scopus 로고
    • The binding of chloride ions to ligated and unligated human hemoglobin and its influence on the Bohr effect
    • DOI 10.1111/j.1432-1033.1979.tb13266.x
    • Beek GGMV, Zuiderweg ERP, and Bruin SHD. The binding of chloride ions to ligated and unligated human hemoglobin and its influence on the Bohr effect. Eur J Biochem99: 379-383, 1979. (Pubitemid 10235508)
    • (1979) European Journal of Biochemistry , vol.99 , Issue.2 , pp. 379-383
    • Van Beek, G.G.M.1    Zuiderweg, E.R.P.2    De Bruin, S.H.3
  • 16
    • 7944224443 scopus 로고    scopus 로고
    • New insights into the proton-dependent oxygen affinity of Root effect haemoglobins
    • DOI 10.1111/j.1365-201X.2004.01359.x
    • Bonaventura C, Crumbliss AL, and Weber RE. New insights into the proton-dependent shifts in oxygen affinity of Root effect hemoglobins. Acta Physiol Scand 182: 245-258, 2004. (Pubitemid 39468677)
    • (2004) Acta Physiologica Scandinavica , vol.182 , Issue.3 , pp. 245-258
    • Bonaventura, C.1    Crumbliss, A.L.2    Weber, R.E.3
  • 17
    • 0037054861 scopus 로고    scopus 로고
    • Responses of normal and sickle cell hemoglobin to S-nitroscysteine: Implications for therapeutic applications of NO in treatment of sickle cell disease
    • DOI 10.1016/S0301-4622(02)00092-3, PII S0301462202000923
    • Bonaventura C, Godette G, Ferruzzi G, Tesh S, Stevens RD, and Henkens R. Responses of normal and sickle cell hemoglobin to S-nitroscysteine: implications for therapeutic applications of NO in treatment of sickle cell disease. Biophys Chem 98: 165-181, 2002. (Pubitemid 34785989)
    • (2002) Biophysical Chemistry , vol.98 , Issue.1-2 , pp. 165-181
    • Bonaventura, C.1    Godette, G.2    Ferruzzi, G.3    Tesh, S.4    Stevens, R.D.5    Henkens, R.6
  • 18
    • 34547951699 scopus 로고    scopus 로고
    • Allosteric effects on oxidative and nitrosative reactions of cell-free hemoglobins
    • DOI 10.1080/15216540601188546, PII 778369630, IUBMB Life Dedicated to Maurizio Brunori in the Occasion of his 70th Birthday
    • Bonaventura C, Henkens R, Alayash, AI, and Crumbliss AL. Allosteric effects on oxidative and nitrosative reactions of cell-free hemoglobins. IUBMB Life 59: 498-505, 2007. (Pubitemid 47265859)
    • (2007) IUBMB Life , vol.59 , Issue.8-9 , pp. 498-505
    • Bonaventura, C.1    Henkens, R.2    Alayash, A.I.3    Crumbliss, A.L.4
  • 20
    • 79960556322 scopus 로고    scopus 로고
    • Steric factors moderate conformational fluidity and contribute to the high proton sensitivity of Root effect hemoglobins
    • Bonaventura C, Henkens R, Friedman J, Siburt CJ, Kraiter D, and Crumbliss AL. Steric factors moderate conformational fluidity and contribute to the high proton sensitivity of Root effect hemoglobins. Biochim Biophys Acta 1814: 1261-1268, 2011.
    • (2011) Biochim Biophys Acta , vol.1814 , pp. 1261-1268
    • Bonaventura, C.1    Henkens, R.2    Friedman, J.3    Siburt, C.J.4    Kraiter, D.5    Crumbliss, A.L.6
  • 22
    • 0016766957 scopus 로고
    • Hemoglobin Deer Lodge (b2His/Arg) consequences of altering the 2, 3-diphosphoglycerate binding site
    • Bonaventura J, Bonaventura C, Sullivan B, and Godette G. Hemoglobin Deer Lodge (b2His/Arg) consequences of altering the 2, 3-diphosphoglycerate binding site. J Biol Chem 250: 9250-9255, 1975.
    • (1975) J Biol Chem , vol.250 , pp. 9250-9255
    • Bonaventura, J.1    Bonaventura, C.2    Sullivan, B.3    Godette, G.4
  • 25
    • 0019289058 scopus 로고
    • Superoxide radical and superoxide dismutases: Threat and defense
    • Brawn K and Fridovich I. Superoxide radical and superoxide dismutases: Threat and defense. Acta Physiol Scand Suppl 492: 9-18, 1980. (Pubitemid 11152694)
    • (1980) Acta Physiologica Scandinavica , vol.110 , Issue.SUPPL. 492 , pp. 9-18
    • Brawn, K.1    Fridovich, I.2
  • 26
    • 0035146934 scopus 로고    scopus 로고
    • Nitric oxide, cytochrome-c oxidase and myoglobin
    • DOI 10.1016/S0968-0004(00)01698-4, PII S0968000400016984
    • Brunori M. Nitric oxide, cytochrome-c oxidase and myoglobin. Trends Biochem Sci 26: 21-23, 2001. (Pubitemid 32124705)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.1 , pp. 21-23
    • Brunori, M.1
  • 27
    • 0014409259 scopus 로고
    • Studies on the oxidation-reduction potentials of heme proteins: VII. Oxidation-reduction equilibrium of hemoglobin bound to haptoglobin
    • Brunori M, Alfsen A, Saggese U, Antonini E, and Wyman J. Studies on the oxidation-reduction potentials of heme proteins: VII. Oxidation-reduction equilibrium of hemoglobin bound to haptoglobin. J Biol Chem 243: 2950-2954, 1968.
    • (1968) J Biol Chem , vol.243 , pp. 2950-2954
    • Brunori, M.1    Alfsen, A.2    Saggese, U.3    Antonini, E.4    Wyman, J.5
  • 29
    • 52249096215 scopus 로고    scopus 로고
    • All hemoglobin-based oxygen carriers are not created equally
    • Buehler PW and Alayash AI. All hemoglobin-based oxygen carriers are not created equally. Biochim Biophys Acta 1784: 1378-1381, 2008.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1378-1381
    • Buehler, P.W.1    Alayash, A.I.2
  • 30
    • 34548842263 scopus 로고    scopus 로고
    • Effects of endogenous ascorbate on oxidation, oxygenation, and toxicokinetics of cell-free modified hemoglobin after exchange transfusion in rat and guinea pig
    • DOI 10.1124/jpet.107.126409
    • Buehler PW, D'Agnillo F, Hoffman V, and Alayash AI. Effects of endogenous ascorbate on oxidation, oxygenation, and toxicokinetics of cell-free modified hemoglobin after exchange transfusion in rat and guinea pig. J Pharmacol Exp Ther 323: 49-60, 2007. (Pubitemid 47443285)
    • (2007) Journal of Pharmacology and Experimental Therapeutics , vol.323 , Issue.1 , pp. 49-60
    • Buehler, P.W.1    D'Agnillo, F.2    Hoffman, V.3    Alayash, A.I.4
  • 34
    • 0006354220 scopus 로고
    • Kinetics of oxygen and carbon monoxide binding to synthetic analogs of the myoglobin and hemoglobin active sites
    • Chang CK and Traylor TG. Kinetics of oxygen and carbon monoxide binding to synthetic analogs of the myoglobin and hemoglobin active sites. Proc Natl Acad Sci USA 72: 1166-1170, 1975.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 1166-1170
    • Chang, C.K.1    Traylor, T.G.2
  • 35
    • 0025026028 scopus 로고
    • Glutaraldehyde effect on hemoglobin: Evidence for an ion environment modification based on electron paramagnetic resonance and mossbauer spectroscopies
    • Chevalier A, Guillochon D, Nedjar N, Piot J, and Daniel MWV. Glutaraldehyde effect on hemoglobin: evidence for an ion environment modification based on electron paramagnetic resonance and Mossbauer spectroscopies. Biochem Cell Biol 68: 813-818, 1990. (Pubitemid 20292774)
    • (1990) Biochemistry and Cell Biology , vol.68 , Issue.4 , pp. 813-818
    • Chevalier, A.1    Guillochon, D.2    Nedjar, N.3    Piot, J.M.4    Vijayalakshmi, M.W.5    Thomas, D.6
  • 37
    • 82855184916 scopus 로고    scopus 로고
    • Hemoglobins S and C interfere with actin remodeling in Plasmodium falciparum-infected erythrocytes
    • Cyrklaff M, Sanchez CP, Kilian N, Bisseye C, Simpore J, Frischknecht F, and Lanzer M. Hemoglobins S and C interfere with actin remodeling in Plasmodium falciparum-infected erythrocytes. Science 334: 1283-1286, 2011.
    • (2011) Science , vol.334 , pp. 1283-1286
    • Cyrklaff, M.1    Sanchez, C.P.2    Kilian, N.3    Bisseye, C.4    Simpore, J.5    Frischknecht, F.6    Lanzer, M.7
  • 38
    • 17144408393 scopus 로고    scopus 로고
    • Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family
    • DOI 10.1080/15216540500059640
    • de Sanctis D, Pesce A, Nardini M, Bolognesi M, Bocedi A, and Ascenzi P. Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family. IUBMB Life 56: 643-651, 2004. (Pubitemid 40515808)
    • (2004) IUBMB Life , vol.56 , Issue.11-12 , pp. 643-651
    • De Sanctis, D.1    Pesce, A.2    Nardini, M.3    Bolognesi, M.4    Bocedi, A.5    Ascenzi, P.6
  • 39
    • 0022313068 scopus 로고
    • Autocatalytic oxidation of hemoglobin induced by nitrite: Activation and chemical inhibition
    • Doyle MP, Herman JG, and Dykstra RL. Autocatalytic oxidation of hemoglobin induced by nitrite: activation and chemical inhibition. J Free Radic Biol Med 1: 145-153, 1985.
    • (1985) J Free Radic Biol Med , vol.1 , pp. 145-153
    • Doyle, M.P.1    Herman, J.G.2    Dykstra, R.L.3
  • 41
    • 0031888099 scopus 로고    scopus 로고
    • Hemoglobin autooxidation/oxidation mechanisms and methemoglobin prevention or reduction processes in the bloodstream: Literature review and outline of autooxidation reaction
    • Faivre B, Menu P, Labrude P, and Vigneron C. Hemoglobin autooxidation/oxidation mechanisms and methemoglobin prevention or reduction processes in the bloodstream. Literature review and outline of autooxidation reaction. Artif Cells Blood Substit Immobil Biotechnol 26: 17-26, 1998. (Pubitemid 28122168)
    • (1998) Artificial Cells, Blood Substitutes, and Immobilization Biotechnology , vol.26 , Issue.1 , pp. 17-26
    • Faivre, B.1    Menu, P.2    Labrude, P.3    Vigneron, C.4
  • 42
    • 0029063668 scopus 로고
    • A Spectroelectrochemical method for differentiation of steric and electronic effects in hemoglobins and myoglobins
    • Faulkner KM, Bonaventura C, and Crumbliss AL. A Spectroelectrochemical method for differentiation of steric and electronic effects in hemoglobins and myoglobins. J Biol Chem 270: 13604-13612, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 13604-13612
    • Faulkner, K.M.1    Bonaventura, C.2    Crumbliss, A.L.3
  • 43
    • 0000938221 scopus 로고
    • A spectroelectrochemical method for evaluating factors which regulate the redox potential of hemoglobins
    • Faulkner KM, Bonaventura C, and Crumbliss AL. A spectroelectrochemical method for evaluating factors which regulate the redox potential of hemoglobins. Inorg Chim Acta 226: 187-194, 1994.
    • (1994) Inorg Chim Acta , vol.226 , pp. 187-194
    • Faulkner, K.M.1    Bonaventura, C.2    Crumbliss, A.L.3
  • 45
    • 0036794855 scopus 로고    scopus 로고
    • Bacterial hemoglobins and flavohemoglobins for alleviation of nitrosative stress in Escherichia coli
    • DOI 10.1128/AEM.68.10.4835-4840.2002
    • Frey AD, Farrés J, Bollinger CJT, and Kallio PT. Bacterial hemoglobins and flavohemoglobins for alleviation of nitrosative stress in Escherichia coli. Appl Environ Microbiol 68: 4835-4840, 2002. (Pubitemid 35154789)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.10 , pp. 4835-4840
    • Frey, A.D.1    Farres, J.2    Bollinger, C.J.T.3    Kallio, P.T.4
  • 46
    • 0018263443 scopus 로고
    • The biology of oxygen radicals
    • Fridovich I. The biology of oxygen radicals. Science 201: 875-880, 1978.
    • (1978) Science , vol.201 , pp. 875-880
    • Fridovich, I.1
  • 47
    • 0019195506 scopus 로고
    • The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine
    • DOI 10.1038/288373a0
    • Furchgott RF and Zawadzki JV. The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine. Nature 288: 373-376, 1980. (Pubitemid 11169009)
    • (1980) Nature , vol.288 , Issue.5789 , pp. 373-376
    • Furchgott, R.F.1    Zawadzki, J.V.2
  • 48
    • 33947092689 scopus 로고
    • Model compounds for R-state and T-state hemoglobins
    • Geibel J, Cannon J, Campbell D, and Traylor TG. Model compounds for R-state and T-state hemoglobins. J Am Chem Soc 100: 3575-3585, 1978.
    • (1978) J Am Chem Soc , vol.100 , pp. 3575-3585
    • Geibel, J.1    Cannon, J.2    Campbell, D.3    Traylor, T.G.4
  • 49
    • 0034730133 scopus 로고    scopus 로고
    • Relative role of heme nitrosylation and b-cysteine 93 nitrosation in the transport and metabolism of nitric oxide by hemoglobin in the human circulation
    • Gladwin MT, Ognibene FP, Pannell LK, Nichols FS, Pease-Fye ME, Shelhamer JH, and Schechter AN. Relative role of heme nitrosylation and b-cysteine 93 nitrosation in the transport and metabolism of nitric oxide by hemoglobin in the human circulation. Proc Natl Acad Sci USA 97: 9943-9947, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9943-9947
    • Gladwin, M.T.1    Ognibene, F.P.2    Pannell, L.K.3    Nichols, F.S.4    Pease-Fye, M.E.5    Shelhamer, J.H.6    Schechter, A.N.7
  • 53
    • 0032516492 scopus 로고    scopus 로고
    • Mechanisms of autoxidation of the oxygen sensor FixL and Aplysia myoglobin: Implications for oxygen-binding heme proteins
    • DOI 10.1021/bi980529x
    • Gonzalez G, Gilles-Gonzalez M A, Rybak-Akimova E V, Buchalova M, and Busch DH. Mechanism of autoxidation of the oxygen sensor FixL and aplysia myoglobin: implications for oxygen-binding heme proteins. Biochemistry 37: 10188-10194, 1998. (Pubitemid 28366374)
    • (1998) Biochemistry , vol.37 , Issue.28 , pp. 10188-10194
    • Gonzalez, G.1    Gilles-Gonzalez, M.A.2    Rybak-Akimova, E.V.3    Buchalova, M.4    Busch, D.H.5
  • 54
    • 41249092640 scopus 로고    scopus 로고
    • Nitrite reductase activity of hemoglobin S (sickle) provides insight into contributions of heme redox potential versus ligand affinity
    • Grubina R, Basu S, Tiso M, Kim-Shapiro DB, and Gladwin MT. Nitrite reductase activity of hemoglobin S (sickle) provides insight into contributions of heme redox potential versus ligand affinity. J Biol Chem 283: 3628-3638, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 3628-3638
    • Grubina, R.1    Basu, S.2    Tiso, M.3    Kim-Shapiro, D.B.4    Gladwin, M.T.5
  • 55
    • 13344264987 scopus 로고
    • Iron and free radical reactions: Two aspects of antioxidant protection
    • Halliwell B and Gutteridge JMC. Iron and free radical reactions: two aspects of antioxidant protection. Trends Biochem Sci 11: 372-375, 1986.
    • (1986) Trends Biochem Sci , vol.11 , pp. 372-375
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 56
    • 0022394280 scopus 로고
    • The importance of free radicals and catalytic metal ions in human diseases
    • DOI 10.1016/0098-2997(85)90001-9
    • Halliwell B and Gutteridge JMC. The importance of free radicals and catalytic metal ions in human diseases. Mol Aspects Med 8: 89-193, 1985. (Pubitemid 16224567)
    • (1985) Molecular Aspects of Medicine , vol.8 , Issue.2 , pp. 89-193
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 59
    • 78851468762 scopus 로고    scopus 로고
    • Reconstructing sickle cell disease: A data-based analysis of the hyperhemolysis paradigm for pulmonary hypertension from the perspective of evidence-based medicine
    • Hebbel RP. Reconstructing sickle cell disease: a data-based analysis of the "hyperhemolysis paradigm" for pulmonary hypertension from the perspective of evidence-based medicine. Am J Hematol 86: 123-154, 2011.
    • (2011) Am J Hematol , vol.86 , pp. 123-154
    • Hebbel, R.P.1
  • 60
    • 17744364065 scopus 로고    scopus 로고
    • 2 and by NO/methemoglobin
    • DOI 10.1016/j.abb.2005.02.013
    • Herlod S and Rock G. Mechanistic studies of S nitrosothiol formation by NO$/O2 and by NO$/methemoglobin. Arch Biochem Biophys 436: 386-396, 2005. (Pubitemid 40576278)
    • (2005) Archives of Biochemistry and Biophysics , vol.436 , Issue.2 , pp. 386-396
    • Herold, S.1    Rock, G.2
  • 61
    • 0003043542 scopus 로고
    • The possible effects of the aggregation of the molecules of hæmoglobin on its dissociation curves
    • Hill AV. The possible effects of the aggregation of the molecules of hæmoglobin on its dissociation curves. J Physiol 40: iv-vii, 1910.
    • (1910) J Physiol , vol.40
    • Hill, A.V.1
  • 64
    • 0023505509 scopus 로고
    • Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide
    • Ignarro LJ, Buga GM, Wood KS, Byrns RE, and Chaudhuri G. Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide. Proc Natl Acad Sci USA 84: 9265-9269, 1987.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 9265-9269
    • Ignarro, L.J.1    Buga, G.M.2    Wood, K.S.3    Byrns, R.E.4    Chaudhuri, G.5
  • 65
    • 0035746036 scopus 로고    scopus 로고
    • Comparative analysis of the autoxidation of haemoglobin
    • Jensen FB. Comparative analysis of the autoxidation of haemoglobin. J Exp Biol 204: 2029-2033 2001.
    • (2001) J Exp Biol , vol.204 , pp. 2029-2033
    • Jensen, F.B.1
  • 66
    • 0029875840 scopus 로고    scopus 로고
    • S-nitrosohaemoglobin: A dynamic activity of blood involved in vascular control
    • DOI 10.1038/380221a0
    • Jia L, Bonaventura C, Bonaventura J, and Stamler JS. SNitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature 380: 221-226, 1996. (Pubitemid 26090643)
    • (1996) Nature , vol.380 , Issue.6571 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 67
    • 67650865895 scopus 로고    scopus 로고
    • Intrinsic non-symbiotic and truncated haemoglobins and heterologous Vitreoscilla haemoglobin expression in plants
    • Jokipii-Lukkari S, Frey AD, Kallio PT, and Häggman H. Intrinsic non-symbiotic and truncated haemoglobins and heterologous Vitreoscilla haemoglobin expression in plants. J Exp Bot 60: 409-422, 2009.
    • (2009) J Exp Bot , vol.60 , pp. 409-422
    • Jokipii-Lukkari, S.1    Frey, A.D.2    Kallio, P.T.3    Häggman, H.4
  • 69
    • 0025026382 scopus 로고
    • Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands
    • Kraus DW and Wittenberg JB. Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands. J Biol Chem 265: 16043-16053, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 16043-16053
    • Kraus, D.W.1    Wittenberg, J.B.2
  • 70
    • 0027992219 scopus 로고
    • Simulation of diffusion and reaction of endogenously produced nitric oxide
    • Lancaster JR. Simulation of diffusion and reaction of endogenously produced nitric oxide. Proc Natl Acad Sci USA 91: 8137-8141, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8137-8141
    • Lancaster, J.R.1
  • 71
    • 75149137411 scopus 로고    scopus 로고
    • Bacterial nitric oxide detoxification prevents host cell S-nitrosothiol formation: A novel mechanism of bacterial pathogenesis
    • Laver JR, Stevanin TM, Messenger SL, Dehn LA, Lee ME, Moir JWB, Poole RK, and Read RC. Bacterial nitric oxide detoxification prevents host cell S-nitrosothiol formation: a novel mechanism of bacterial pathogenesis. FASEB J 24: 286-295, 2010.
    • (2010) FASEB J , vol.24 , pp. 286-295
    • Laver, J.R.1    Stevanin, T.M.2    Messenger, S.L.3    Dehn, L.A.4    Lee, M.E.5    Jwb, M.6    Poole, R.K.7    Read, R.C.8
  • 73
    • 0024468312 scopus 로고
    • The effects of E7 and E11 mutations on the kinetics of ligand binding to R state human hemoglobin
    • Mathews AJ, Rohlfs RJ, Olson JS, Tame J, Renaud JP, and Nagai K. The effects of E7 and E11 mutations on the kinetics of ligand binding to R state human hemoglobin. J Biol Chem 264: 16573-16583, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 16573-16583
    • Mathews, A.J.1    Rohlfs, R.J.2    Olson, J.S.3    Tame, J.4    Renaud, J.P.5    Nagai, K.6
  • 74
    • 78650038011 scopus 로고    scopus 로고
    • Peroxynitrite stress is exacerbated by flavohaemoglobin-derived oxidative stress in Salmonella Typhimurium and is relieved by nitric oxide
    • McLean S, Bowman LAH, and Poole RK. Peroxynitrite stress is exacerbated by flavohaemoglobin-derived oxidative stress in Salmonella Typhimurium and is relieved by nitric oxide. Microbiology 156: 3556-3565, 2010.
    • (2010) Microbiology , vol.156 , pp. 3556-3565
    • McLean, S.1    Bowman, L.A.H.2    Poole, R.K.3
  • 75
    • 0017121129 scopus 로고
    • Characterization of enzyme-like activity of human hemoglobin. Properties of the hemoglobin-P-450 reductase-coupled aniline hydroxylase system
    • Mieyal JJ, Ackerman RS, Blumer JL, and Freeman LS. Characterization of enzyme-like activity of human hemoglobin. Properties of the hemoglobin-P-450 reductase-coupled aniline hydroxylase system. J Biol Chem 251: 3436-3441, 1976.
    • (1976) J Biol Chem , vol.251 , pp. 3436-3441
    • Mieyal, J.J.1    Ackerman, R.S.2    Blumer, J.L.3    Freeman, L.S.4
  • 77
    • 0015502066 scopus 로고
    • The Generation of superoxide radical during the autoxidation of hemoglobin
    • Misra HP and Fridovich I. The Generation of superoxide radical during the autoxidation of hemoglobin. J Biol Chem 247: 6960-6962, 1972.
    • (1972) J Biol Chem , vol.247 , pp. 6960-6962
    • Misra, H.P.1    Fridovich, I.2
  • 78
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J, and J-P Changeux. On the nature of allosteric transitions: a plausible model. J Mol Biol 12: 88-118, 1965.
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 79
    • 0014360531 scopus 로고
    • Plasma concentrations of hemopexin, haptoglobin and heme in patients with various hemolytic diseases
    • Muller-Eberhard U, Javid J, Liem HH, Hanstein A, and Hanna M. Plasma concentrations of hemopexin, haptoglobin and heme in patients with various hemolytic diseases. Blood 32: 811-815, 1968.
    • (1968) Blood , vol.32 , pp. 811-815
    • Muller-Eberhard, U.1    Javid, J.2    Liem, H.H.3    Hanstein, A.4    Hanna, M.5
  • 80
    • 0037062603 scopus 로고    scopus 로고
    • Site-specific cross-linking of human and bovine hemoglobins differentially alters oxygen binding and redox side reactions producing rhombic heme and heme degradation
    • DOI 10.1021/bi0121048
    • Nagababu E, Somasundaram R, Rifkind JM, Jia Y, and Alayash AI. Site-specific cross-linking of human and bovine hemoglobins differentially alters oxygen binding and redox side reactions producing rhombic heme and heme degradation. Biochemistry 41: 7407-7415, 2002. (Pubitemid 34602459)
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7407-7415
    • Nagababu, E.1    Ramasamy, S.2    Rifkind, J.M.3    Jia, Y.4    Alayash, A.I.5
  • 81
    • 0344443777 scopus 로고    scopus 로고
    • Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin-mediated nitrite reduction
    • DOI 10.1074/jbc.M307572200
    • Nagababu E, Ramasamy S, Abernethy DR, and Rifkind JM. Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin-mediated nitrite reduction. J Biol Chem 278: 46349-46356, 2003. (Pubitemid 37452205)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 46349-46356
    • Nagababu, E.1    Ramasamy, S.2    Abernethy, D.R.3    Rifkind, J.M.4
  • 82
    • 35348877494 scopus 로고    scopus 로고
    • Intermediates detected by visible spectroscopy during the reaction of nitrite with deoxyhemoglobin: The effect of nitrite concentration and diphosphoglycerate
    • DOI 10.1021/bi700364e
    • Nagababu E, Ramasamy S, and Rifkind JM. Intermediates detected by visible spectroscopy during the reaction of nitrite with deoxyhemoglobin: the effect of nitrite concentration and diphosphoglycerate. Biochemistry 46: 11650-11659, 2007. (Pubitemid 47585511)
    • (2007) Biochemistry , vol.46 , Issue.41 , pp. 11650-11659
    • Nagababu, E.1    Ramasamy, S.2    Rifkind, J.M.3
  • 86
    • 0017239164 scopus 로고
    • Binding of inositol hexaphosphate to human methemoglobin
    • Olson JS. Binding of inositol hexaphosphate to human methemoglobin. J Biol Chem 251: 447-458, 1976.
    • (1976) J Biol Chem , vol.251 , pp. 447-458
    • Olson, J.S.1
  • 88
    • 0023521335 scopus 로고
    • Ligand recombination to the α and β subunits of human hemoglobin
    • Olson JS, Rohlfs RJ, and Gibson QH. Ligand recombination to the a and b subunits of human hemoglobin. J Biol Chem 262: 12930-12938, 1987. (Pubitemid 18001236)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.27 , pp. 12930-12938
    • Olson, J.S.1    Rohlfs, R.J.2    Gibson, Q.H.3
  • 89
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
    • DOI 10.1038/327524a0
    • Palmer RMJ, Ferrige AG, And Moncada S. Nitric oxide release accounts for the biological activity of endotheliumderived relaxing factor. Nature 327: 524-526, 1987. (Pubitemid 17085822)
    • (1987) Nature , vol.327 , Issue.6122 , pp. 524-526
    • Palmer, R.M.J.1    Ferrige, A.G.2    Moncada, S.3
  • 90
    • 0035252076 scopus 로고    scopus 로고
    • Export by red blood cells of nitric oxide bioactivity
    • DOI 10.1038/35054560
    • Pawloski JR, Hess DT, and Stamler JS. Export by red blood cells of nitric oxide bioactivity. Nature 409: 622-626, 2001. (Pubitemid 32154814)
    • (2001) Nature , vol.409 , Issue.6820 , pp. 622-626
    • Pawloski, J.R.1    Hes, D.T.2    Stamler, J.S.3
  • 91
    • 0025289366 scopus 로고
    • Influence of organic phosphates on the root effect of multiple fish haemoglobins
    • Pelster B and Webber RE. Influence of organic phosphates on the root effects of multiple fish hemoglobin. J Exp Biol 149: 425-437, 1990. (Pubitemid 20165294)
    • (1990) Journal of Experimental Biology , vol.149 , pp. 425-437
    • Pelster, B.1    Weber, R.E.2
  • 92
    • 0018168011 scopus 로고
    • Hemoglobin structure and respiratory transport
    • Perutz MF. Hemoglobin structure and respiratory transport. Sci Amer 239: 92-125, 1978.
    • (1978) Sci Amer , vol.239 , pp. 92-125
    • Perutz, M.F.1
  • 95
    • 77955880548 scopus 로고    scopus 로고
    • The redox activity of hemoglobins: From physiologic functions to pathologic mechanisms
    • Reeder BJ. The redox activity of hemoglobins: from physiologic functions to pathologic mechanisms. Antioxid Redox Signal 13: 1087-1123, 2010.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1087-1123
    • Reeder, B.J.1
  • 96
    • 27744458259 scopus 로고    scopus 로고
    • Hemoglobin and myoglobin associated oxidative stress: From molecular mechanisms to disease states
    • DOI 10.2174/092986705774463021
    • Reeder BJ and Wilson MT. Hemoglobin and myoglobin associated oxidative stress: From molecular mechanisms to disease states. Curr Med Chem 12: 2741-2751, 2005. (Pubitemid 41601571)
    • (2005) Current Medicinal Chemistry , vol.12 , Issue.23 , pp. 2741-2751
    • Reeder, B.J.1    Wilson, M.T.2
  • 97
    • 0019223598 scopus 로고
    • Equilibrium binding of alkyl isocyanides to human hemoglobin
    • Reisberg PI and Olson JS. Equilibrium binding of alkyl isocyanides to human hemoglobin. J Biol Chem 255: 4144-4150, 1980. (Pubitemid 10053047)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.9 , pp. 4144-4150
    • Reisberg, P.I.1    Olson, J.S.2
  • 101
    • 0015216974 scopus 로고
    • The binding of hemoglobin to haptoglobin and its relation to subunit dissociation of hemoglobin
    • Ronald N and Quentin G. The binding of hemoglobin to haptoglobin and its relation to subunit dissociation of hemoglobin. J Biol Chem 246: 69-73, 1971.
    • (1971) J Biol Chem , vol.246 , pp. 69-73
    • Ronald, N.1    Quentin, G.2
  • 102
    • 0038930935 scopus 로고
    • The respiratory function of the blood of marine fishes
    • Root RW. The respiratory function of the blood of marine fishes. Biol Bull 61: 427-456, 1931.
    • (1931) Biol Bull , vol.61 , pp. 427-456
    • Root, R.W.1
  • 103
    • 0019457407 scopus 로고
    • Asynchronous ligand binding and proton release in a root effect hemoglobin
    • Saffran WA and Gibson QH. Asynchronous ligand binding and proton release in a Root effect hemoglobin. J Biol Chem 256: 4551-4556, 1981. (Pubitemid 11089718)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.9 , pp. 4551-4556
    • Saffran, W.A.1    Gibson, Q.H.2
  • 104
    • 0016744077 scopus 로고
    • Magnitude of subunit inequivalence for oxygen release from hemoglobin: Reinvestigation of the oxygen-pulse experiment
    • Salhany JM, Castillo CL, McDonald MJ, and Gibson QH. Magnitude of subunit inequivalence for oxygen release from hemoglobin: reinvestigation of the oxygen-pulse experiment. Proc Natl Acad Sci USA 10: 3998-4002, 1975.
    • (1975) Proc Natl Acad Sci USA , vol.10 , pp. 3998-4002
    • Salhany, J.M.1    Castillo, C.L.2    McDonald, M.J.3    Gibson, Q.H.4
  • 105
    • 0343504735 scopus 로고
    • Secretion of gasses against high pressures in swim bladders of deep sea fishes
    • Scholander PF and Van Dam L. Secretion of gasses against high pressures in swim bladders of deep sea fishes. Biol Bull 107: 247-249, 1954.
    • (1954) Biol Bull , vol.107 , pp. 247-249
    • Scholander, P.F.1    Van Dam, L.2
  • 107
    • 33344467539 scopus 로고    scopus 로고
    • 2 bonding in myoglobin and hemoglobin: A new molecular paradigm
    • DOI 10.1016/j.pbiomolbio.2005.04.001, PII S0079610705000131
    • Shikama K. Nature of the FeO2 bonding in myoglobin and hemoglobin: a new molecular paradigm. Prog Biophys Mol Biol 91: 83-162, 2006. (Pubitemid 43288988)
    • (2006) Progress in Biophysics and Molecular Biology , vol.91 , Issue.1-2 , pp. 83-162
    • Shikama, K.1
  • 110
    • 33645973287 scopus 로고    scopus 로고
    • Nitric oxide stimulatesthe erythrocyte for ascorbate recycling
    • Spagnuolo MS, Carlucci A, Cigliano L, and Abrescia P. Nitric oxide stimulatesthe erythrocyte for ascorbate recycling. Nitric Oxide 14: 272-277, 2006.
    • (2006) Nitric Oxide , vol.14 , pp. 272-277
    • Spagnuolo, M.S.1    Carlucci, A.2    Cigliano, L.3    Abrescia, P.4
  • 111
    • 0021757969 scopus 로고
    • Influences on carbon monoxide and dioxygen binding to iron(II) porphyrins
    • Suslick KS, Fox MM, and Reinert TR. Influences on carbon monoxide and dioxygen binding to iron(II) porphyrins. J Am Chem Soc 106: 4522-4525, 1984.
    • (1984) J Am Chem Soc , vol.106 , pp. 4522-4525
    • Suslick, K.S.1    Fox, M.M.2    Reinert, T.R.3
  • 112
    • 0023645311 scopus 로고
    • Autoxidation of oxymyoglobin with the distal (E7) glutamine
    • Suzuki T. Autoxidation of oxymyoglobin with the distal (E7) glutamine. Biochim Biophys Acta 914: 170-176, 1987.
    • (1987) Biochim Biophys Acta , vol.914 , pp. 170-176
    • Suzuki, T.1
  • 113
    • 0033029098 scopus 로고    scopus 로고
    • Spectroelectrochemistry of heme proteins: Effects of active-site heterogeneity on Nernst plots
    • DOI 10.1016/S0302-4598(98)00236-0, PII S0302459898002360
    • Taboy CH, Bonaventura C, and Crumbliss AL. Spectroelectrochemistry of heme proteins: effects of active-site heterogeneity on Nernst plots. Bioelectrochem Bioenerg 48: 79-86, 1999. (Pubitemid 29150365)
    • (1999) Bioelectrochemistry and Bioenergetics , vol.48 , Issue.1 , pp. 79-86
    • Taboy, C.H.1    Bonaventura, C.2    Crumbliss, A.L.3
  • 114
    • 0036282180 scopus 로고    scopus 로고
    • Anaerobic oxidations of myoglobin and hemoglobin by spectroelectrochemistry
    • DOI 10.1016/S0076-6879(02)53048-2
    • Taboy CH, Bonaventura C, and Crumbliss AL. Anaerobic oxidations of myoglobin and hemoglobin using spectroelectrochemistry. Methods Enzymol 353: 187-209, 2002. (Pubitemid 34632574)
    • (2002) Methods in Enzymology , vol.353 , pp. 187-209
    • Taboy, C.H.1    Bonaventura, C.2    Crumbliss, A.L.3
  • 115
    • 0034671715 scopus 로고    scopus 로고
    • Concentration-dependent effects of anions on the anaerobic oxidation of hemoglobin and myoglobin
    • DOI 10.1074/jbc.M004547200
    • Taboy CH, Faulkner KM, Kraiter D, Bonaventura C, and Crumbliss AL. Concentration-dependent effects of anions on the anaerobic oxidation of hemoglobin and myoglobin. J Biol Chem 275: 39048-39054, 2000. (Pubitemid 32058918)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.50 , pp. 39048-39054
    • Taboy, C.H.1    Faulkner, K.M.2    Kraiter, D.3    Bonaventura, C.4    Crumbliss, A.L.5
  • 118
    • 33847085494 scopus 로고
    • Isocyanide binding to chelated protoheme. Kinetic criteria for distal steric effects in hemoproteins
    • Traylor TG and Stynes DV. Isocyanide binding to chelated protoheme. Kinetic criteria for distal steric effects in hemoproteins. J Am Chem Soc 102: 5938-5939, 1980.
    • (1980) J Am Chem Soc , vol.102 , pp. 5938-5939
    • Traylor, T.G.1    Stynes, D.V.2
  • 119
    • 0020014972 scopus 로고
    • Considerations for the design of useful synthetic oxygen carriers
    • Traylor TG and Traylor PS. Considerations for the design of useful synthetic oxygen carriers. Annu Rev Biophys Bioeng 11: 105-127, 1982.
    • (1982) Annu Rev Biophys Bioeng , vol.11 , pp. 105-127
    • Traylor, T.G.1    Traylor, P.S.2
  • 120
    • 84856816307 scopus 로고    scopus 로고
    • A sliding scale rule for selectivity among NO, CO, and O2 by heme protein sensors
    • Tsai AL, Olson JS, Berka V, and Martin E. A "sliding scale rule" for selectivity among NO, CO, and O2 by heme protein sensors. Biochemistry 51: 172-186, 2012.
    • (2012) Biochemistry , vol.51 , pp. 172-186
    • Tsai, A.L.1    Olson, J.S.2    Berka, V.3    Martin, E.4
  • 121
    • 0032502724 scopus 로고    scopus 로고
    • The molecular mechanism of autoxidation for human oxyhemoglobin. Tilting of the distal histidine causes nonequivalent oxidation in the β chain
    • DOI 10.1074/jbc.273.15.8607
    • Tsuruga M, Matsuoka A, Hachimori A, Sugawara Y, and Shikama K. The molecular mechanism of autoxidation for human oxyhemoglobin: tilting of the distal histidine causes nonequivalent oxidation in the b chain. J Biol Chem 273: 8607-8615, 1998. (Pubitemid 28176135)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.15 , pp. 8607-8615
    • Tsuruga, M.1    Matsuoka, A.2    Hachimori, A.3    Sugawara, Y.4    Shikama, K.5
  • 122
    • 0019995366 scopus 로고
    • Mechanism of autooxidation for hemoglobins and myoglobins. Promotion of superoxide production by protons and anions
    • Wallace WJ, Houtchens RA, Maxwell JC, and Caughey WS. Mechanism of autooxidation for hemoglobins and myoglobins. Promotion of superoxide production by protons and anions. J Biol Chem 257: 4966-4977, 1982. (Pubitemid 12063190)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.9 , pp. 4966-4977
    • Wallace, W.J.1    Houtchens, R.A.2    Maxwell, J.C.3    Caughey, W.S.4
  • 123
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: Functions and molecular adaptations
    • Weber RE and Vinogradov SN. Nonvertebrate hemoglobins: functions and molecular adaptations. Physiol Rev 81: 569-628, 2001. (Pubitemid 32267074)
    • (2001) Physiological Reviews , vol.81 , Issue.2 , pp. 569-628
    • Weber, R.E.1    Vinogradov, S.N.2
  • 124
    • 0022272178 scopus 로고
    • Free-radical production and oxidative reactions of hemoglobin
    • Winterbourn CC. Free-radical production and oxidative reactions of hemoglobin. Environ Health Perspec 64: 321-330, 1985. (Pubitemid 16135800)
    • (1985) Environmental Health Perspectives , vol.VOL. 64 , pp. 321-330
    • Winterbourn, C.C.1
  • 125
    • 0037072945 scopus 로고    scopus 로고
    • Global allostery model of hemoglobin: Modulation of O2-Affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors
    • Yonetani T, Park S, Tsuneshige A, Imai K, and Kanaori K. Global allostery model of hemoglobin: modulation of O2-Affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors. J Biol Chem 277: 34508-34520, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 34508-34520
    • Yonetani, T.1    Park, S.2    Tsuneshige, A.3    Imai, K.4    Kanaori, K.5
  • 126
    • 77954746068 scopus 로고    scopus 로고
    • Structure and properties of a bis-histidyl ligated globin from Caenorhabditis elegans
    • Yoon J, Herzik MA Jr., Winter MB, Tran R, Olea C, Jr., and Marletta MA. Structure and properties of a bis-histidyl ligated globin from Caenorhabditis elegans. Biochemistry 49: 5662-5670, 2010.
    • (2010) Biochemistry , vol.49 , pp. 5662-5670
    • Yoon, J.1    Herzik Jr., M.A.2    Winter, M.B.3    Tran, R.4    Olea Jr., C.5    Marletta, M.A.6
  • 127
    • 0026651286 scopus 로고
    • Yeast flavohemoglobin is an ancient protein related to globins and a reductase family
    • Zhu H and Riggs AF. Yeast flavohemoglobin is an ancient protein related to globins and a reductase family. Proc Natl Acad Sci USA 89: 5015-5019, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5015-5019
    • Zhu, H.1    Riggs, A.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.