메뉴 건너뛰기




Volumn 16, Issue 4, 1996, Pages 835-842

Carbon monoxide: An endogenous modulator of the nitric oxide-cyclic GMP signaling system

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; CYCLIC GMP; NITRIC OXIDE; NITRIC OXIDE SYNTHASE;

EID: 0029990994     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(00)80103-8     Document Type: Article
Times cited : (231)

References (55)
  • 1
    • 0027470993 scopus 로고
    • Glutamate and quisqualate regulate expression of metabotropic glutamate receptor mRNA in cultured cerebellar granule cells
    • Bessho, Y., Nawa, H., and Nakanishi, S. (1993). Glutamate and quisqualate regulate expression of metabotropic glutamate receptor mRNA in cultured cerebellar granule cells. J. Neurochem. 60, 253-259.
    • (1993) J. Neurochem. , vol.60 , pp. 253-259
    • Bessho, Y.1    Nawa, H.2    Nakanishi, S.3
  • 2
    • 0024378999 scopus 로고
    • Nitric oxide mediates glutamate-linked enhancement of cGMP levels in the cerebellum
    • Bredt, D.S., and Snyder, S.H. (1989). Nitric oxide mediates glutamate-linked enhancement of cGMP levels in the cerebellum. Proc. Natl. Acad. Sci. USA 86, 9030-9033.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9030-9033
    • Bredt, D.S.1    Snyder, S.H.2
  • 3
    • 0027975453 scopus 로고
    • Nitric oxide: A physiologic messenger molecule
    • Bredt, D.S., and Snyder, S.H. (1994). Nitric oxide: a physiologic messenger molecule. Annu. Rev. Biochem. 63, 175-195.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 175-195
    • Bredt, D.S.1    Snyder, S.H.2
  • 4
    • 0025011298 scopus 로고
    • Localization of nitric oxide synthase indicating a neural role for nitric oxide
    • Bredt, D.S., Hwang, P.M., and Snyder, S.H. (1990). Localization of nitric oxide synthase indicating a neural role for nitric oxide. Nature 347, 768-770.
    • (1990) Nature , vol.347 , pp. 768-770
    • Bredt, D.S.1    Hwang, P.M.2    Snyder, S.H.3
  • 5
    • 0023490534 scopus 로고
    • Inhibition of platelet aggregation by carbon monoxide is mediated by activation of guanylate cyclase
    • Brüne, B., and Ullrich, V. (1987). Inhibition of platelet aggregation by carbon monoxide is mediated by activation of guanylate cyclase. Mol. Pharmacol. 32, 497-504.
    • (1987) Mol. Pharmacol. , vol.32 , pp. 497-504
    • Brüne, B.1    Ullrich, V.2
  • 6
    • 0016589435 scopus 로고
    • Conformation, co-operativity and ligand binding in human hemoglobin
    • Cassoly, R., and Gibson, Q.H. (1975). Conformation, co-operativity and ligand binding in human hemoglobin. J. Mol. Biol. 91, 301-313.
    • (1975) J. Mol. Biol. , vol.91 , pp. 301-313
    • Cassoly, R.1    Gibson, Q.H.2
  • 7
    • 0023854047 scopus 로고
    • Evidence suggesting that the two forms of heme oxygenase are products of different genes
    • Cruse, I., and Maines, M.D. (1988). Evidence suggesting that the two forms of heme oxygenase are products of different genes. J. Biol. Chem. 263, 3348-3353.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3348-3353
    • Cruse, I.1    Maines, M.D.2
  • 9
    • 0027054312 scopus 로고
    • In situ hybridization and immunohistochemical localization of heme oxygenase-2 mRNA and protein in normal rat brain: Differential distribution of isozyme 1 and 2 cell
    • Ewing, J.F., and Maines, M.D. (1992). In situ hybridization and immunohistochemical localization of heme oxygenase-2 mRNA and protein in normal rat brain: differential distribution of isozyme 1 and 2 cell. Mol. Cell. Neurosci. 3, 559-570.
    • (1992) Mol. Cell. Neurosci. , vol.3 , pp. 559-570
    • Ewing, J.F.1    Maines, M.D.2
  • 10
    • 0342363569 scopus 로고
    • Protohemin
    • K.M. Smith, ed. (Amsterdam: Elsevier Scientific Publishing Company)
    • Falk, J.E. (1975). Protohemin. In Prophyrins and Metalloporphyrins, K.M. Smith, ed. (Amsterdam: Elsevier Scientific Publishing Company), pp. 808.
    • (1975) Prophyrins and Metalloporphyrins , pp. 808
    • Falk, J.E.1
  • 11
    • 0020620370 scopus 로고
    • Turnover rates of amino acid neurotransmitters in regions of rat cerebellum
    • Freeman, M.E., Lane, J.D., and Smith, J.E. (1983). Turnover rates of amino acid neurotransmitters in regions of rat cerebellum. J. Neurochem. 40, 1441-1447.
    • (1983) J. Neurochem. , vol.40 , pp. 1441-1447
    • Freeman, M.E.1    Lane, J.D.2    Smith, J.E.3
  • 12
    • 0026034934 scopus 로고
    • Endothelium-dependent and -independent vasodilation involving cyclic GMP: Relaxation induced by nitric oxide, carbon monoxide and light
    • Furchgott, R.F., and Jothianandan, D. (1991). Endothelium-dependent and -independent vasodilation involving cyclic GMP: relaxation induced by nitric oxide, carbon monoxide and light. Blood Ves. 28, 52-61.
    • (1991) Blood Ves. , vol.28 , pp. 52-61
    • Furchgott, R.F.1    Jothianandan, D.2
  • 13
    • 0025790193 scopus 로고
    • Biosynthesis of δ-aminolevulinic acid and the regulation of heme formation by immature erythoid cells in man
    • Gardner, L.C., Smith, S.J., and Cox, T.M. (1991). Biosynthesis of δ-aminolevulinic acid and the regulation of heme formation by immature erythoid cells in man. J. Biol. Chem. 266, 22010-22018.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22010-22018
    • Gardner, L.C.1    Smith, S.J.2    Cox, T.M.3
  • 14
    • 0026077959 scopus 로고
    • Glutamate, nitric oxide and cell-cell signaling in the nervous system
    • Garthwaite, J. (1991). Glutamate, nitric oxide and cell-cell signaling in the nervous system. Trends Neurol. Sci. 14, 60-67.
    • (1991) Trends Neurol. Sci. , vol.14 , pp. 60-67
    • Garthwaite, J.1
  • 15
    • 0024296032 scopus 로고
    • Endothelium-derived relaxing factor release on activation of NMDA receptors suggests role as intercellular messenger in the brain
    • Garthwaite, J., Charles, S.L., and Chess-Williams, R. (1988). Endothelium-derived relaxing factor release on activation of NMDA receptors suggests role as intercellular messenger in the brain. Nature 336, 385-388.
    • (1988) Nature , vol.336 , pp. 385-388
    • Garthwaite, J.1    Charles, S.L.2    Chess-Williams, R.3
  • 16
    • 0027374973 scopus 로고
    • Inducible nitric oxide synthase from a rat alveolar macrophage cell line inhibited by nitric oxide
    • Griscavage, J.M., Rogers, N.E., Sherman, M.P., and Ignarro, L.J. (1993). Inducible nitric oxide synthase from a rat alveolar macrophage cell line inhibited by nitric oxide. J. Immunol. 151, 6329-6337.
    • (1993) J. Immunol. , vol.151 , pp. 6329-6337
    • Griscavage, J.M.1    Rogers, N.E.2    Sherman, M.P.3    Ignarro, L.J.4
  • 17
    • 0027990370 scopus 로고
    • Nitric oxide inhibits neuronal nitric oxide synthase by interacting with the heme prosthetic group
    • Griscavage, J.M., Fukuto, J.M., Komori, Y., and Ignarro, L.J. (1994). Nitric oxide inhibits neuronal nitric oxide synthase by interacting with the heme prosthetic group. J. Biol. Chem. 269, 21644-21649.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21644-21649
    • Griscavage, J.M.1    Fukuto, J.M.2    Komori, Y.3    Ignarro, L.J.4
  • 19
    • 0021275463 scopus 로고
    • Regulation of soluble guanylate cyclase activity by porphyrins and metalloporphyrins
    • Ignarro, L.J., Ballot, B., and Wood, K.S. (1984). Regulation of soluble guanylate cyclase activity by porphyrins and metalloporphyrins. J. Biol. Chem. 259, 6201-6207.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6201-6207
    • Ignarro, L.J.1    Ballot, B.2    Wood, K.S.3
  • 20
    • 0029590042 scopus 로고
    • Direct demonstration of a physiological role for carbon monoxide in olfactory receptor neurons
    • Ingi, T., and Ronnett, G.V. (1995). Direct demonstration of a physiological role for carbon monoxide in olfactory receptor neurons. J. Neurosci. 15, 8214-8222.
    • (1995) J. Neurosci. , vol.15 , pp. 8214-8222
    • Ingi, T.1    Ronnett, G.V.2
  • 21
    • 0028691715 scopus 로고
    • Inhibition of nitric oxide-dependent vasodilation by halogenated anesthetics
    • Jing, M., Hart, J.L., Bina, S., and Muldoon, S.M. (1994). Inhibition of nitric oxide-dependent vasodilation by halogenated anesthetics. Adv. Pharmacol. 31, 459-469.
    • (1994) Adv. Pharmacol. , vol.31 , pp. 459-469
    • Jing, M.1    Hart, J.L.2    Bina, S.3    Muldoon, S.M.4
  • 22
    • 0028938533 scopus 로고
    • Vascular effects of halothane and isoflurane: CGMP dependent and independent actions
    • Jing, M., Hart, J.L., Masaki, E., Van Dyke, R.A., Bina, S., and Muldoon, S.M. (1995). Vascular effects of halothane and isoflurane: cGMP dependent and independent actions. Life Sci. 56, 19-29.
    • (1995) Life Sci. , vol.56 , pp. 19-29
    • Jing, M.1    Hart, J.L.2    Masaki, E.3    Van Dyke, R.A.4    Bina, S.5    Muldoon, S.M.6
  • 24
    • 0026565555 scopus 로고
    • Glutamate receptor agonists stimulate nitric oxide synthase in primary cultures of cerebellar granule cells
    • Kiedrowski, L., Costa, E., and Wroblewski, J.T. (1992). Glutamate receptor agonists stimulate nitric oxide synthase in primary cultures of cerebellar granule cells. J. Neurochem. 58, 335-341.
    • (1992) J. Neurochem. , vol.58 , pp. 335-341
    • Kiedrowski, L.1    Costa, E.2    Wroblewski, J.T.3
  • 25
    • 0028237924 scopus 로고
    • Identification and partial purification of an endogenous inhibitor of soluble guanylyl cyclase from bovine lung
    • Kim, T.D., and Burstyn, J.N. (1994). Identification and partial purification of an endogenous inhibitor of soluble guanylyl cyclase from bovine lung. J. Biol. Chem. 269, 15540-15545.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15540-15545
    • Kim, T.D.1    Burstyn, J.N.2
  • 26
    • 0021905801 scopus 로고
    • Survival, morphology and adhesion properties of cerebellar interneurons cultured in chemically defined and serum-supplemented medium
    • Kingsbury, A.E., Gallo, V., Woodhams, P.L., and Balazs, R. (1985). Survival, morphology and adhesion properties of cerebellar interneurons cultured in chemically defined and serum-supplemented medium. Dev. Brain Res. 17, 17-25.
    • (1985) Dev. Brain Res. , vol.17 , pp. 17-25
    • Kingsbury, A.E.1    Gallo, V.2    Woodhams, P.L.3    Balazs, R.4
  • 27
    • 0027321686 scopus 로고
    • Effects of temperature, oxygen, heme ligands and sulfhydryl alkylation on the reactions of nitroprusside and nitroglycerin with hemoglobin
    • Kruszyna, H., Kruszyna, R., Rochelle, L.G., Smith, R.P., and Wilcox, D.E. (1993). Effects of temperature, oxygen, heme ligands and sulfhydryl alkylation on the reactions of nitroprusside and nitroglycerin with hemoglobin. Biochem. Pharmacol. 46, 95-102.
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 95-102
    • Kruszyna, H.1    Kruszyna, R.2    Rochelle, L.G.3    Smith, R.P.4    Wilcox, D.E.5
  • 30
    • 0013943591 scopus 로고
    • Endogenous production of carbon-14 labeled carbon monoxide: An in vivo technique for the study of heme catabolism
    • Landaw, S.A., and Winchell, H.S. (1966). Endogenous production of carbon-14 labeled carbon monoxide: an in vivo technique for the study of heme catabolism. J. Nucl. Med. 7, 696-707.
    • (1966) J. Nucl. Med. , vol.7 , pp. 696-707
    • Landaw, S.A.1    Winchell, H.S.2
  • 31
    • 0028884298 scopus 로고
    • Regulation of cyclic nucleotide-gated channels and membrane excitability in olfactory receptor cells by carbon monoxide
    • Leinders-Zufall, T., Shepherd, G.M., and Zufall, F. (1995). Regulation of cyclic nucleotide-gated channels and membrane excitability in olfactory receptor cells by carbon monoxide. J. Neurophysiol. 74, 1498-1508.
    • (1995) J. Neurophysiol. , vol.74 , pp. 1498-1508
    • Leinders-Zufall, T.1    Shepherd, G.M.2    Zufall, F.3
  • 32
    • 0024402675 scopus 로고
    • Heme catabolism in cultured hepatocytes: Evidence that heme oxygenase is the predominant pathway and that a proportion of synthesized heme is converted rapidly to biliverdin
    • Lincoln, B.C., Aw, T.Y., and Bonkovsky, H.L. (1989). Heme catabolism in cultured hepatocytes: evidence that heme oxygenase is the predominant pathway and that a proportion of synthesized heme is converted rapidly to biliverdin. Biochim. Biophys. Acta 992, 49-58.
    • (1989) Biochim. Biophys. Acta , vol.992 , pp. 49-58
    • Lincoln, B.C.1    Aw, T.Y.2    Bonkovsky, H.L.3
  • 33
    • 0028176233 scopus 로고
    • Metalloporphyrins inhibit nitric oxide-dependent cGMP formation in vivo
    • Luo, D., and Vincent, S.R. (1994). Metalloporphyrins inhibit nitric oxide-dependent cGMP formation in vivo. Eur. J. Pharmacol. 267, 263-267.
    • (1994) Eur. J. Pharmacol. , vol.267 , pp. 263-267
    • Luo, D.1    Vincent, S.R.2
  • 34
    • 0019883606 scopus 로고
    • Zinc-protoporphyrin is a selective inhibitor of heme oxygenase activity in the neonatal rat
    • Maines, M.D. (1981). Zinc-protoporphyrin is a selective inhibitor of heme oxygenase activity in the neonatal rat. Biochim. Biophys. Acta 673, 339-350.
    • (1981) Biochim. Biophys. Acta , vol.673 , pp. 339-350
    • Maines, M.D.1
  • 35
    • 0023731036 scopus 로고
    • Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
    • Maines, M.D. (1988). Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications. FASEB J. 2, 2557-2568.
    • (1988) FASEB J. , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 36
    • 0026744212 scopus 로고
    • Localization of adenylyl and guanylyl cyclase in rat brain by in situ hybridization: Comparison with calmodulin mRNA distribution
    • Matsuoka, I., Giuili, G., Poyard, M., Stengel, D., Parma, J., Cuellaen, G., and Hanoune, J. (1992). Localization of adenylyl and guanylyl cyclase in rat brain by in situ hybridization: comparison with calmodulin mRNA distribution. J. Neurosci. 12, 3350-3360.
    • (1992) J. Neurosci. , vol.12 , pp. 3350-3360
    • Matsuoka, I.1    Giuili, G.2    Poyard, M.3    Stengel, D.4    Parma, J.5    Cuellaen, G.6    Hanoune, J.7
  • 37
    • 0026471538 scopus 로고
    • Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme which binds carbon monoxide
    • McMillan, K., Bredt, D.S., Hirsch, D.J., Snyder, S.H., Clark, J.E., and Masters, B.S.S. (1992). Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme which binds carbon monoxide. Proc. Natl. Acad. Sci. USA 89, 11141-11145.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11141-11145
    • McMillan, K.1    Bredt, D.S.2    Hirsch, D.J.3    Snyder, S.H.4    Clark, J.E.5    Masters, B.S.S.6
  • 38
    • 0028067882 scopus 로고
    • Inhibition of hippocampal heme oxygenase, nitric oxide synthase, and long-term potentiation by metalloporphyrins
    • Meffert, M.K., Haley, J.E., Schuman, E.M., Schulman, H., and Madison, D.V. (1994). Inhibition of hippocampal heme oxygenase, nitric oxide synthase, and long-term potentiation by metalloporphyrins. Neuron 13, 1225-1233.
    • (1994) Neuron , vol.13 , pp. 1225-1233
    • Meffert, M.K.1    Haley, J.E.2    Schuman, E.M.3    Schulman, H.4    Madison, D.V.5
  • 39
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology and pharmacology
    • Moncada, S., Palmer, R.M.J., and Higgs, E.A. (1991). Nitric oxide: physiology, pathophysiology and pharmacology. Pharmacol. Rev. 43, 109-142.
    • (1991) Pharmacol. Rev. , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.J.2    Higgs, E.A.3
  • 40
    • 0028941685 scopus 로고
    • + pump as a site of action for carbon monoxide and glutamate: A mechanism for long-term modulation of cellular activity
    • + pump as a site of action for carbon monoxide and glutamate: a mechanism for long-term modulation of cellular activity. Neuron 14, 781-794.
    • (1995) Neuron , vol.14 , pp. 781-794
    • Nathanson, J.A.1    Scavone, C.2    Scanlon, C.3    McKee, M.4
  • 41
    • 0021993655 scopus 로고
    • Regulation of heme synthesis in erythroid cells: Hemin inhibits transferrin iron utilization but not protoporphyrin synthesis
    • Ponka, P., and Schulman, H.M. (1985). Regulation of heme synthesis in erythroid cells: hemin inhibits transferrin iron utilization but not protoporphyrin synthesis. Blood 65, 850-857.
    • (1985) Blood , vol.65 , pp. 850-857
    • Ponka, P.1    Schulman, H.M.2
  • 42
    • 0028880959 scopus 로고
    • Hippocampal long-term potentiation is normal in heme oxygenase-2 mutant mice
    • Poss, K.D., Thomas, M.J., Ebralidze, A.K., O'Dell, T.J., and Tonegawa, S. (1995). Hippocampal long-term potentiation is normal in heme oxygenase-2 mutant mice. Neuron 15, 867-873.
    • (1995) Neuron , vol.15 , pp. 867-873
    • Poss, K.D.1    Thomas, M.J.2    Ebralidze, A.K.3    O'Dell, T.J.4    Tonegawa, S.5
  • 43
    • 0342798430 scopus 로고
    • Induction of enzymes of the heme biosynthetic pathway in friend leukemia cells in culture
    • K. Nakao, J.W. Fisher, and F. Takaku, eds. (Tokyo: University of Tokyo Press)
    • Sassa, S., Granick, S., Chang, C., and Kappas, A. (1975). Induction of enzymes of the heme biosynthetic pathway in Friend leukemia cells in culture. In Erythropoiesis, K. Nakao, J.W. Fisher, and F. Takaku, eds. (Tokyo: University of Tokyo Press), pp. 383-396.
    • (1975) Erythropoiesis , pp. 383-396
    • Sassa, S.1    Granick, S.2    Chang, C.3    Kappas, A.4
  • 44
    • 0026643197 scopus 로고
    • NO CO and OH endogenous soluble guanylyl cyclase-activating factors
    • Schmidt, H.H.H.W. (1992). NO CO and OH endogenous soluble guanylyl cyclase-activating factors. FEBS Lett. 307, 102-107.
    • (1992) FEBS Lett. , vol.307 , pp. 102-107
    • Schmidt, H.H.H.W.1
  • 45
    • 0025370305 scopus 로고
    • Changes with aging in the levels of amino acids in rat CNS structural elements: IV. Methionine and basic amino acids
    • Schwartz, M.B., Lajtha, A., and Palkovits, M. (1990). Changes with aging in the levels of amino acids in rat CNS structural elements: IV. Methionine and basic amino acids. J. Neurosci. 26, 217-223.
    • (1990) J. Neurosci. , vol.26 , pp. 217-223
    • Schwartz, M.B.1    Lajtha, A.2    Palkovits, M.3
  • 46
    • 0027296209 scopus 로고
    • Reversal of long-term potentiation by inhibitors of heme oxygenase
    • Stevens, C.F., and Wang, Y. (1993). Reversal of long-term potentiation by inhibitors of heme oxygenase. Nature 364, 147-148.
    • (1993) Nature , vol.364 , pp. 147-148
    • Stevens, C.F.1    Wang, Y.2
  • 47
    • 0028228808 scopus 로고
    • Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states
    • Stone, J.R., and Marietta, M.A. (1994). Soluble guanylate cyclase from bovine lung: activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states. Biochemistry 33, 5636-5640.
    • (1994) Biochemistry , vol.33 , pp. 5636-5640
    • Stone, J.R.1    Marietta, M.A.2
  • 48
    • 0025303671 scopus 로고
    • Developmental expression of heme oxygenase isozymes in rat brain: Two HO-2 mRNAs are detected
    • Sun, Y., Rotenberg, M.O., and Maines, M.D. (1990). Developmental expression of heme oxygenase isozymes in rat brain: two HO-2 mRNAs are detected. J. Biol. Chem. 265, 8212-8217.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8212-8217
    • Sun, Y.1    Rotenberg, M.O.2    Maines, M.D.3
  • 49
    • 0024388901 scopus 로고
    • Macrophage oxidation of L-arginine to nitric oxide, nitrite, and nitrate
    • Tayeh, M.A., and Marietta, M.A. (1989). Macrophage oxidation of L-arginine to nitric oxide, nitrite, and nitrate. J. Biol. Chem. 264, 19654-19658.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19654-19658
    • Tayeh, M.A.1    Marietta, M.A.2
  • 50
    • 0027939785 scopus 로고
    • Nitric oxide released by platelets inhibits neutrophil B2 integrin function following acute carbon monoxide poisoning
    • Thom, S.R., Ohnishi, T., and Ischiropoulos, H. (1994). Nitric oxide released by platelets inhibits neutrophil B2 integrin function following acute carbon monoxide poisoning. Toxicol. Pharmacol. 128, 105-110.
    • (1994) Toxicol. Pharmacol. , vol.128 , pp. 105-110
    • Thom, S.R.1    Ohnishi, T.2    Ischiropoulos, H.3
  • 52
    • 0026410728 scopus 로고
    • In vitro and in vivo characteristics of a heme oxygenase inhibitor: ZnBG
    • Vreman, H.J., Lee, O.H., and Stevenson, D.K. (1991). In vitro and in vivo characteristics of a heme oxygenase inhibitor: ZnBG. Am. J. Med. Sci. 302, 335-341.
    • (1991) Am. J. Med. Sci. , vol.302 , pp. 335-341
    • Vreman, H.J.1    Lee, O.H.2    Stevenson, D.K.3
  • 53
    • 0026735580 scopus 로고
    • Nitric oxide synthase is a cytochrome P-450 type hemoprotein
    • White, K.A., and Marletta, M.A. (1992). Nitric oxide synthase is a cytochrome P-450 type hemoprotein. Biochemistry 31, 6627-6631.
    • (1992) Biochemistry , vol.31 , pp. 6627-6631
    • White, K.A.1    Marletta, M.A.2
  • 54
    • 0027486719 scopus 로고
    • Tissue distribution of succinylacetone in the rat in vivo: A possible basis for neurotoxicity in hereditary infantile tyrosinemia
    • Wyss, P.A., Boyton, S., Chu, J., and Roth, K.S. (1993). Tissue distribution of succinylacetone in the rat in vivo: a possible basis for neurotoxicity in hereditary infantile tyrosinemia. Biochim. Biophys. Acta. 1182, 323-328.
    • (1993) Biochim. Biophys. Acta. , vol.1182 , pp. 323-328
    • Wyss, P.A.1    Boyton, S.2    Chu, J.3    Roth, K.S.4
  • 55
    • 0027267817 scopus 로고
    • Nitric oxide and carbon monoxide produce activity-dependent long-term synaptic enhancement in hippocampus
    • Zhuo, M., Small, S.A., Kandel, E.R., and Hawkins, R.D. (1993). Nitric oxide and carbon monoxide produce activity-dependent long-term synaptic enhancement in hippocampus. Science 260, 1946-1950.
    • (1993) Science , vol.260 , pp. 1946-1950
    • Zhuo, M.1    Small, S.A.2    Kandel, E.R.3    Hawkins, R.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.