메뉴 건너뛰기




Volumn 101, Issue 11, 2003, Pages 4408-4415

Vasoactivity of S-nitrosohemoglobin: Role of oxygen, heme, and NO oxidation states

Author keywords

[No Author keywords available]

Indexed keywords

HEME; HEMOGLOBIN DERIVATIVE; NITRIC OXIDE; OXYGEN; S NITROSOGLUTATHIONE; S NITROSOHEMOGLOBIN; UNCLASSIFIED DRUG; GLUTATHIONE; HEMOGLOBIN; METHEMOGLOBIN; S-NITROSOHEMOGLOBIN; SUPEROXIDE DISMUTASE;

EID: 0037804794     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2002-12-3825     Document Type: Article
Times cited : (53)

References (57)
  • 1
    • 0014675819 scopus 로고
    • Intracellular organic phosphates as regulators of oxygen release by haemoglobin
    • Benesch R, Benesch RE. Intracellular organic phosphates as regulators of oxygen release by haemoglobin. Nature. 1969;221:618-622.
    • (1969) Nature , vol.221 , pp. 618-622
    • Benesch, R.1    Benesch, R.E.2
  • 3
    • 0032495529 scopus 로고    scopus 로고
    • Reactions between nitric oxide and haemoglobin under physiological conditions
    • Gow AJ, Stamler JS. Reactions between nitric oxide and haemoglobin under physiological conditions. Nature. 1998;391:169-173.
    • (1998) Nature , vol.391 , pp. 169-173
    • Gow, A.J.1    Stamler, J.S.2
  • 4
    • 0029875840 scopus 로고    scopus 로고
    • S-nitrosohaemoglobin: A dynamic activity of blood involved in vascular control
    • Jia L, Bonaventura C, Bonaventura J, Stamler JS. S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature. 1996; 380:221-226.
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 5
    • 18444369943 scopus 로고    scopus 로고
    • Nitric oxide in the human respiratory cycle
    • McMahon TJ, Moon RE, Luschinger BP, et al. Nitric oxide in the human respiratory cycle. Nat Med. 2002;8:711-717.
    • (2002) Nat Med , vol.8 , pp. 711-717
    • McMahon, T.J.1    Moon, R.E.2    Luschinger, B.P.3
  • 6
    • 0032570313 scopus 로고    scopus 로고
    • Cell-free and erythrocytic S-nitrosohemoglobin inhibits human platelet aggregation
    • Pawloski JR, Swaminathan RV, Stamler JS. Cell-free and erythrocytic S-nitrosohemoglobin inhibits human platelet aggregation. Circulation. 1998;97:263-267.
    • (1998) Circulation , vol.97 , pp. 263-267
    • Pawloski, J.R.1    Swaminathan, R.V.2    Stamler, J.S.3
  • 7
    • 0030791742 scopus 로고    scopus 로고
    • Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient
    • Stamler JS, Jia L, Eu JP, et al. Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient. Science. 1997;276:2034-2037.
    • (1997) Science , vol.276 , pp. 2034-2037
    • Stamler, J.S.1    Jia, L.2    Eu, J.P.3
  • 8
    • 0019726454 scopus 로고
    • Oxidation of nitrogen oxides by bound dioxygen in hemoproteins
    • Doyle MP, Hoekstra JW. Oxidation of nitrogen oxides by bound dioxygen in hemoproteins. J Inorg Biochem. 1981;14:351-358.
    • (1981) J Inorg Biochem , vol.14 , pp. 351-358
    • Doyle, M.P.1    Hoekstra, J.W.2
  • 9
    • 15844372775 scopus 로고    scopus 로고
    • Mechanism of NO-induced oxidation of myoglobin and hemoglobin
    • Eich RF, LiT, Lemon DD, et al. Mechanism of NO-induced oxidation of myoglobin and hemoglobin. Biochemistry. 1996;35:6976-6983.
    • (1996) Biochemistry , vol.35 , pp. 6976-6983
    • Eich, R.F.1    Li, T.2    Lemon, D.D.3
  • 13
    • 0036908599 scopus 로고    scopus 로고
    • Cell-free hemoglobin limits nitric oxide bioavailability in sickle-cell disease
    • Reiter CD, Wang X, Tanus-Santos JE, et al. Cell-free hemoglobin limits nitric oxide bioavailability in sickle-cell disease. Nat Med. 2002;8:1383-1389.
    • (2002) Nat Med , vol.8 , pp. 1383-1389
    • Reiter, C.D.1    Wang, X.2    Tanus-Santos, J.E.3
  • 14
    • 0035949654 scopus 로고    scopus 로고
    • Modulation of nitric oxide bioavailability by erythrocytes
    • Huang KT, Han TH, Hyduke DR, et al. Modulation of nitric oxide bioavailability by erythrocytes. Proc Natl Acad Sci U S A. 2001;98:11771-11776.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11771-11776
    • Huang, K.T.1    Han, T.H.2    Hyduke, D.R.3
  • 15
    • 0037135629 scopus 로고    scopus 로고
    • Nitric oxide uptake by erythrocytes is primarily limited by extracellular diffusion not membrane resistance
    • Liu X, Samouilov A, Lancaster JR Jr, Zweier JL. Nitric oxide uptake by erythrocytes is primarily limited by extracellular diffusion not membrane resistance. J Biol Chem. 2002;277:26194-26199.
    • (2002) J Biol Chem , vol.277 , pp. 26194-26199
    • Liu, X.1    Samouilov, A.2    Lancaster J.R., Jr.3    Zweier, J.L.4
  • 16
    • 0034730133 scopus 로고    scopus 로고
    • Relative role of heme nitrosylation and beta-cysteine 93 nitrosation in the transport and metabolism of nitric oxide by hemoglobin in the human circulation
    • Gladwin MT, Ognibene FP, Pannell LK, et al. Relative role of heme nitrosylation and beta-cysteine 93 nitrosation in the transport and metabolism of nitric oxide by hemoglobin in the human circulation. Proc Natl Acad Sci U S A. 2000; 97:9943-9948.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 9943-9948
    • Gladwin, M.T.1    Ognibene, F.P.2    Pannell, L.K.3
  • 17
    • 0034595830 scopus 로고    scopus 로고
    • Functional coupling of oxygen binding and vasoactivity in S-nitrosohemoglobin
    • McMahon TJ, Exton SA, Bonaventura J, Singel DJ, Solomon SJ. Functional coupling of oxygen binding and vasoactivity in S-nitrosohemoglobin. J Biol Chem. 2000;275:16738-16745.
    • (2000) J Biol Chem , vol.275 , pp. 16738-16745
    • McMahon, T.J.1    Exton, S.A.2    Bonaventura, J.3    Singel, D.J.4    Solomon, S.J.5
  • 18
    • 0035252076 scopus 로고    scopus 로고
    • Export by red blood cells of nitric oxide bioactivity
    • Pawloski JR, Hess DT, Stamler JS. Export by red blood cells of nitric oxide bioactivity. Nature. 2001;409:622-626.
    • (2001) Nature , vol.409 , pp. 622-626
    • Pawloski, J.R.1    Hess, D.T.2    Stamler, J.S.3
  • 19
    • 0035252081 scopus 로고    scopus 로고
    • Vascular biology: Targeted delivery of nitric oxide
    • Gross SS. Vascular biology: targeted delivery of nitric oxide. Nature. 2001;409:577-578.
    • (2001) Nature , vol.409 , pp. 577-578
    • Gross, S.S.1
  • 20
    • 0033609913 scopus 로고    scopus 로고
    • Effects of S-nitrosation on oxygen binding by normal and sickle cell hemoglobin
    • Bonaventura C, Ferruzzi G, Tesh S, Stevens RD. Effects of S-nitrosation on oxygen binding by normal and sickle cell hemoglobin. J Biol Chem. 1999;274:24742-24748.
    • (1999) J Biol Chem , vol.274 , pp. 24742-24748
    • Bonaventura, C.1    Ferruzzi, G.2    Tesh, S.3    Stevens, R.D.4
  • 21
    • 0035040873 scopus 로고    scopus 로고
    • Effects of S-nitrosation of hemoglobin on hypoxic pulmonary vasoconstriction and nitric oxide flux
    • Deem S, Gladwin MT, Berg JT, Kerr ME, Swenson ER. Effects of S-nitrosation of hemoglobin on hypoxic pulmonary vasoconstriction and nitric oxide flux. Am J Respir Crit Care Med. 2001;163: 1164-1170.
    • (2001) Am J Respir Crit Care Med , vol.163 , pp. 1164-1170
    • Deem, S.1    Gladwin, M.T.2    Berg, J.T.3    Kerr, M.E.4    Swenson, E.R.5
  • 22
    • 0033016469 scopus 로고    scopus 로고
    • Biochemical characterization of human S-nitrosohemoglobin: Effects on oxygen binding and transnitrosation
    • Patel RP, Hogg N, Spencer NY, Kalyanaraman B, Matalon S, Darley-Usmar VM. Biochemical characterization of human S-nitrosohemoglobin: effects on oxygen binding and transnitrosation. J Biol Chem. 1999;274:15487-15492.
    • (1999) J Biol Chem , vol.274 , pp. 15487-15492
    • Patel, R.P.1    Hogg, N.2    Spencer, N.Y.3    Kalyanaraman, B.4    Matalon, S.5    Darley-Usmar, V.M.6
  • 24
    • 0032848295 scopus 로고    scopus 로고
    • Biochemical characterization of S-nitrosohemoglobin: Mechanisms underlying synthesis, NO release, and biological activity
    • Wolzt M, MacAllister RJ, Davis D, et al. Biochemical characterization of S-nitrosohemoglobin: mechanisms underlying synthesis, NO release, and biological activity. J Biol Chem. 1999;274: 28983-28990.
    • (1999) J Biol Chem , vol.274 , pp. 28983-28990
    • Wolzt, M.1    MacAllister, R.J.2    Davis, D.3
  • 25
    • 0037019986 scopus 로고    scopus 로고
    • Effects of S-nitrosation and cross-linking of hemoglobin on hypoxic pulmonary vasoconstriction in isolated rat lungs
    • Deem S, Kim JU, Manjula BN, et al. Effects of S-nitrosation and cross-linking of hemoglobin on hypoxic pulmonary vasoconstriction in isolated rat lungs. Circ Res. 2002;91:626-632.
    • (2002) Circ Res , vol.91 , pp. 626-632
    • Deem, S.1    Kim, J.U.2    Manjula, B.N.3
  • 26
    • 0034633659 scopus 로고    scopus 로고
    • Role of circulating nitrite and S-nitrosohemoglobin in the regulation of regional blood flow in humans
    • Gladwin MT, Shelhamer JH, Schechter AN, et al. Role of circulating nitrite and S-nitrosohemoglobin in the regulation of regional blood flow in humans. Proc Natl Aced Sci U S A. 2000;97:11482-11487.
    • (2000) Proc Natl Aced Sci U S A , vol.97 , pp. 11482-11487
    • Gladwin, M.T.1    Shelhamer, J.H.2    Schechter, A.N.3
  • 27
    • 0037008720 scopus 로고    scopus 로고
    • S-nitrosohemoglobin is unstable in the reductive red cell environment and lacks O2/NO-linked allosteric function
    • Gladwin MT, Wang X, Reiter CD, et al. S-nitrosohemoglobin is unstable in the reductive red cell environment and lacks O2/NO-linked allosteric function. J Biol Chem. 2002;277:27818-27828.
    • (2002) J Biol Chem , vol.277 , pp. 27818-27828
    • Gladwin, M.T.1    Wang, X.2    Reiter, C.D.3
  • 28
    • 0036677518 scopus 로고    scopus 로고
    • Nitric oxide is consumed, rather than conserved, by reaction with oxyhemoglobin under physiological conditions
    • Joshi MS, Ferguson TB Jr, Han TH, et al. Nitric oxide is consumed, rather than conserved, by reaction with oxyhemoglobin under physiological conditions. Proc Natl Acad Sci U S A. 2002;99: 10341-10346.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10341-10346
    • Joshi, M.S.1    Ferguson T.B., Jr.2    Han, T.H.3
  • 29
    • 0036591864 scopus 로고    scopus 로고
    • Mixing artifacts from the bolus addition of nitric oxide to oxymyoglobin: Implications for S-nitrosothiol formation
    • Zhang Y, Hogg N. Mixing artifacts from the bolus addition of nitric oxide to oxymyoglobin: implications for S-nitrosothiol formation. Free Radic Biol Med. 2002;32:1212-1219.
    • (2002) Free Radic Biol Med , vol.32 , pp. 1212-1219
    • Zhang, Y.1    Hogg, N.2
  • 32
    • 0034709457 scopus 로고    scopus 로고
    • S-nitrosothiol formation in blood of lipopolysaccharide-treated rats
    • Jourd'heuil D, Gray L, Grisham MB. S-nitrosothiol formation in blood of lipopolysaccharide-treated rats. Biochem Biophys Res Commun. 2000;273: 22-26.
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 22-26
    • Jourd'heuil, D.1    Gray, L.2    Grisham, M.B.3
  • 33
    • 0034656839 scopus 로고    scopus 로고
    • Biochemical aspects of the reaction of hemoglobin and NO: Implications for Hb-based blood substitutes
    • Patel RP. Biochemical aspects of the reaction of hemoglobin and NO: implications for Hb-based blood substitutes. Free Radic Biol Med. 2000;28: 1518-1525.
    • (2000) Free Radic Biol Med , vol.28 , pp. 1518-1525
    • Patel, R.P.1
  • 34
    • 0025145949 scopus 로고
    • Oxidative reactions of hemoglobin
    • Winterbourn CC. Oxidative reactions of hemoglobin. Methods Enzymol. 1990;186:265-272.
    • (1990) Methods Enzymol , vol.186 , pp. 265-272
    • Winterbourn, C.C.1
  • 35
    • 0034800326 scopus 로고    scopus 로고
    • Endothelial dysfunction is induced by proinflammatory oxidant hypochlorous acid
    • Zhang C, Patel R, Eiserich JP, et al. Endothelial dysfunction is induced by proinflammatory oxidant hypochlorous acid. Am J Physiol Heart Circ Physiol. 2001;281:H1469-H1475.
    • (2001) Am J Physiol Heart Circ Physiol , vol.281
    • Zhang, C.1    Patel, R.2    Eiserich, J.P.3
  • 36
    • 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, Chaudhuri G. Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide. Proc Natl Acad Sci U S A. 1987;84: 9265-9269.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 9265-9269
    • Ignarro, L.J.1    Buga, G.M.2    Wood, K.S.3    Byrns, R.E.4    Chaudhuri, G.5
  • 37
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
    • Palmer RM, Ferrige AG, Moncada S. Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor. Nature. 1987; 327:524-526.
    • (1987) Nature , vol.327 , pp. 524-526
    • Palmer, R.M.1    Ferrige, A.G.2    Moncada, S.3
  • 38
    • 0029758908 scopus 로고    scopus 로고
    • Circulating plasma xanthine oxidase contributes to vascular dysfunction in hypercholesterolemic rabbits
    • White CR, Darley-Usmar V, Berrington WR, et al. Circulating plasma xanthine oxidase contributes to vascular dysfunction in hypercholesterolemic rabbits. Proc Natl Acad Sci U S A. 1996;93:8745-8749.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 8745-8749
    • White, C.R.1    Darley-Usmar, V.2    Berrington, W.R.3
  • 39
    • 0028987969 scopus 로고
    • NO+, NO, and NO- donation by S-nitrosothiols: Implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation
    • Arnelle DR, Stamler JS. NO+, NO, and NO- donation by S-nitrosothiols: implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation. Arch Biochem Biophys. 1995;318:279-285.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 279-285
    • Arnelle, D.R.1    Stamler, J.S.2
  • 40
    • 0032554614 scopus 로고    scopus 로고
    • Reaction between S-nitrosothiols and thiols: Generation of nitroxyl (HNO) and subsequent chemistry
    • Wong PS, Hyun J, Fukuto JM, et al. Reaction between S-nitrosothiols and thiols: generation of nitroxyl (HNO) and subsequent chemistry. Biochemistry. 1998;37:5362-5371.
    • (1998) Biochemistry , vol.37 , pp. 5362-5371
    • Wong, P.S.1    Hyun, J.2    Fukuto, J.M.3
  • 41
    • 0036174890 scopus 로고    scopus 로고
    • The biochemistry and physiology of S-nitrosothiols
    • Hogg N. The biochemistry and physiology of S-nitrosothiols. Annu Rev Pharmacol Toxicol. 2002; 42:585-600.
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 585-600
    • Hogg, N.1
  • 42
    • 0028858786 scopus 로고
    • NO nitrosonium ions, nitroxide ions, nitrosothiols and iron-nitrosyls in biology: A chemist's perspective
    • Butler AR, Flitney FW, Williams DL. NO, nitrosonium ions, nitroxide ions, nitrosothiols and iron-nitrosyls in biology: a chemist's perspective. Trends Pharmacol Sci. 1995;16:18-22.
    • (1995) Trends Pharmacol Sci , vol.16 , pp. 18-22
    • Butler, A.R.1    Flitney, F.W.2    Williams, D.L.3
  • 43
    • 0037177797 scopus 로고    scopus 로고
    • Heme redox properties of S-nitrosated hemoglobin A0 and hemoglobin S: Implications for interactions of nitric oxide with normal and sickle red blood cells
    • Bonaventura C, Taboy CH, Low PS, Stevens RD, Lafon C, Crumbliss AL. Heme redox properties of S-nitrosated hemoglobin A0 and hemoglobin S: implications for interactions of nitric oxide with normal and sickle red blood cells. J Biol Chem. 2002;277:14557-14563.
    • (2002) J Biol Chem , vol.277 , pp. 14557-14563
    • Bonaventura, C.1    Taboy, C.H.2    Low, P.S.3    Stevens, R.D.4    Lafon, C.5    Crumbliss, A.L.6
  • 44
    • 0033605140 scopus 로고    scopus 로고
    • Internal electron transfer between hemes and Cu(II) bound at cysteine beta93 promotes methemoglobin reduction by carbon monoxide
    • Bonaventura C, Godette G, Tesh S, et al. Internal electron transfer between hemes and Cu(II) bound at cysteine beta93 promotes methemoglobin reduction by carbon monoxide. J Biol Chem. 1999;274:5499-5507.
    • (1999) J Biol Chem , vol.274 , pp. 5499-5507
    • Bonaventura, C.1    Godette, G.2    Tesh, S.3
  • 45
    • 0034804272 scopus 로고    scopus 로고
    • Release of nitric oxide from S-nitrosohemoglobin: Electron transfer as a response to deoxygenation
    • Pezacki JP, Ship NJ, Kluger R. Release of nitric oxide from S-nitrosohemoglobin: electron transfer as a response to deoxygenation. J Am Chem Soc. 2001;123:4615-4616.
    • (2001) J Am Chem Soc , vol.123 , pp. 4615-4616
    • Pezacki, J.P.1    Ship, N.J.2    Kluger, R.3
  • 46
    • 0031574042 scopus 로고    scopus 로고
    • A method to study kinetics of transnitrosation with nitrosoglutathione: Reactions with hemoglobin and other thiols
    • Rossi R, Lusini L, Giannerini F, Giustarini D, Lungarella G, Di Simplicio P. A method to study kinetics of transnitrosation with nitrosoglutathione: reactions with hemoglobin and other thiols. Anal Biochem. 1997;254:215-220.
    • (1997) Anal Biochem , vol.254 , pp. 215-220
    • Rossi, R.1    Lusini, L.2    Giannerini, F.3    Giustarini, D.4    Lungarella, G.5    Di Simplicio, P.6
  • 47
    • 0034711297 scopus 로고    scopus 로고
    • Reaction of S-nitrosoglutathione with the heme group of deoxyhemoglobin
    • Spencer NY, Zeng H, Patel RP, Hogg N. Reaction of S-nitrosoglutathione with the heme group of deoxyhemoglobin. J Biol Chem. 2000;275:36562-36567.
    • (2000) J Biol Chem , vol.275 , pp. 36562-36567
    • Spencer, N.Y.1    Zeng, H.2    Patel, R.P.3    Hogg, N.4
  • 48
    • 0034769184 scopus 로고    scopus 로고
    • Effects of agents that inactivate free radical NO (NO*) on nitroxyl anion-mediated relaxations, and on the detection of NO* released from the nitroxyl anion donor Angeli's salt
    • Ellis A, Lu H, Li CG, Rand MJ. Effects of agents that inactivate free radical NO (NO*) on nitroxyl anion-mediated relaxations, and on the detection of NO* released from the nitroxyl anion donor Angeli's salt. Br J Pharmacol. 2001;134:521-528.
    • (2001) Br J Pharmacol , vol.134 , pp. 521-528
    • Ellis, A.1    Lu, H.2    Li, C.G.3    Rand, M.J.4
  • 49
    • 0035793311 scopus 로고    scopus 로고
    • Role of copper ions and cytochrome P450 in the vasodilator actions of the nitroxyl anion generator, Angeli's salt, on rat aorta
    • Nelli S, McIntosh L, Martin W. Role of copper ions and cytochrome P450 in the vasodilator actions of the nitroxyl anion generator, Angeli's salt, on rat aorta. Eur J Pharmacol. 2001;412:281-289.
    • (2001) Eur J Pharmacol , vol.412 , pp. 281-289
    • Nelli, S.1    McIntosh, L.2    Martin, W.3
  • 50
    • 0035910389 scopus 로고    scopus 로고
    • Unique oxidative mechanisms for the reactive nitrogen oxide species, nitroxyl anion
    • Miranda KM, Espey MG, Yamada K, et al. Unique oxidative mechanisms for the reactive nitrogen oxide species, nitroxyl anion. J Biol Chem. 2001; 276:1720-1727.
    • (2001) J Biol Chem , vol.276 , pp. 1720-1727
    • Miranda, K.M.1    Espey, M.G.2    Yamada, K.3
  • 53
    • 0032513115 scopus 로고    scopus 로고
    • Superoxide-mediated decomposition of biological S-nitrosothiols
    • Aleryani S, Milo E, Rose Y, Kostka P, Superoxide-mediated decomposition of biological S-nitrosothiols. J Biol Chem. 1998;273:6041-6045.
    • (1998) J Biol Chem , vol.273 , pp. 6041-6045
    • Aleryani, S.1    Milo, E.2    Rose, Y.3    Kostka, P.4
  • 56
    • 0034966810 scopus 로고    scopus 로고
    • Preparation and characterization of SNO-PEG-hemoglobin as a candidate for oxygen transporting material
    • Nakai K, Togashi H, Yasukohchi T, et al. Preparation and characterization of SNO-PEG-hemoglobin as a candidate for oxygen transporting material. Int J Artif Organs. 2001;24:322-328.
    • (2001) Int J Artif Organs , vol.24 , pp. 322-328
    • Nakai, K.1    Togashi, H.2    Yasukohchi, T.3
  • 57
    • 0032700169 scopus 로고    scopus 로고
    • In vitro formation of S-nitrosohemoglobin in red cells by inducible nitric oxide synthase
    • Mamone G, Sannolo N, Malorni A, Ferranti P. In vitro formation of S-nitrosohemoglobin in red cells by inducible nitric oxide synthase. FEBS Lett. 1999;462:241-245.
    • (1999) FEBS Lett , vol.462 , pp. 241-245
    • Mamone, G.1    Sannolo, N.2    Malorni, A.3    Ferranti, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.