메뉴 건너뛰기




Volumn 850, Issue 1-2, 1999, Pages 1-13

Enhanced neuronal expression of the oxidoreductase - Biliverdin reductase - After permanent focal cerebral ischemia

Author keywords

Antioxidant; Bilirubin; Biliverdin reductase; Cerebral ischemia; Heme oxidation

Indexed keywords

BILIVERDIN REDUCTASE; IRON; MESSENGER RNA; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 0032753427     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-8993(99)01726-6     Document Type: Article
Times cited : (33)

References (65)
  • 1
    • 0030885241 scopus 로고    scopus 로고
    • Dendritic changes of the pyramidal neurons in layer V of sensory-motor cortex of the rat brain during the postresuscitation period
    • Akulinin V.A., Stepanov S.S., Semchenko V.V., Belichenko P.V. Dendritic changes of the pyramidal neurons in layer V of sensory-motor cortex of the rat brain during the postresuscitation period. Resuscitation. 35:1997;157-164.
    • (1997) Resuscitation , vol.35 , pp. 157-164
    • Akulinin, V.A.1    Stepanov, S.S.2    Semchenko, V.V.3    Belichenko, P.V.4
  • 3
    • 0029588565 scopus 로고
    • Ferritin as a source of iron and protection from iron-induced toxicities
    • Aust S.D. Ferritin as a source of iron and protection from iron-induced toxicities. Toxicol. Lett. 82/83:1995;941-944.
    • (1995) Toxicol. Lett. , vol.8283 , pp. 941-944
    • Aust, S.D.1
  • 4
    • 0030876019 scopus 로고    scopus 로고
    • Hypoxia-ischemia, but not hypoxia alone, induces the expression of heme oxygenase-1 (HSP32) in newborn rat brain
    • Bergeron M., Ferriero D.M., Vreman H.J., Stevenson D.K., Sharp F.R. Hypoxia-ischemia, but not hypoxia alone, induces the expression of heme oxygenase-1 (HSP32) in newborn rat brain. J. Cereb. Blood Flow Metab. 17:1997;647-658.
    • (1997) J. Cereb. Blood Flow Metab. , vol.17 , pp. 647-658
    • Bergeron, M.1    Ferriero, D.M.2    Vreman, H.J.3    Stevenson, D.K.4    Sharp, F.R.5
  • 7
    • 0031396912 scopus 로고    scopus 로고
    • Histochemical localization of heme oxygenase-2 protein and mRNA expression in rat brain
    • Ewing J.E., Maines M.D. Histochemical localization of heme oxygenase-2 protein and mRNA expression in rat brain. Brain Res. Protoc. 1:1997;165-174.
    • (1997) Brain Res. Protoc. , vol.1 , pp. 165-174
    • Ewing, J.E.1    Maines, M.D.2
  • 8
    • 0028812175 scopus 로고
    • Immunohistochemical localization of biliverdin reductase in rat brain: Age related expression of protein and transcript
    • Ewing J.F., Maines M.D. Immunohistochemical localization of biliverdin reductase in rat brain: age related expression of protein and transcript. Brain Res. 672:1995;29-41.
    • (1995) Brain Res. , vol.672 , pp. 29-41
    • Ewing, J.F.1    Maines, M.D.2
  • 9
    • 0027176344 scopus 로고
    • Biliverdin reductase is heat resistant and coexpressed with constitutive and heat shock forms of heme oxygenase in brain
    • Ewing J.F., Weber C.M., Maines M.D. Biliverdin reductase is heat resistant and coexpressed with constitutive and heat shock forms of heme oxygenase in brain. J. Neurochem. 61:1993;1015-1023.
    • (1993) J. Neurochem. , vol.61 , pp. 1015-1023
    • Ewing, J.F.1    Weber, C.M.2    Maines, M.D.3
  • 10
    • 0026641481 scopus 로고
    • Expression and characterization of a cDNA for rat kidney biliverdin reductase: Evidence suggesting the liver and kidney enzymes are the same transcript product
    • Fakhrai H., Maines M.D. Expression and characterization of a cDNA for rat kidney biliverdin reductase: evidence suggesting the liver and kidney enzymes are the same transcript product. J. Biol. Chem. 267:1992;4023-4029.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4023-4029
    • Fakhrai, H.1    Maines, M.D.2
  • 11
    • 0031832025 scopus 로고    scopus 로고
    • Cerebellar stimulation reduces inducible nitric oxide synthase expression and protects brain from ischemia
    • Galea E., Golanov E.V., Feinstein D.L., Kobylarz K.A., Glickstein S.B., Reis D.J. Cerebellar stimulation reduces inducible nitric oxide synthase expression and protects brain from ischemia. Am. J. Physiol. 274:1998;H2035-H2045.
    • (1998) Am. J. Physiol. , vol.274
    • Galea, E.1    Golanov, E.V.2    Feinstein, D.L.3    Kobylarz, K.A.4    Glickstein, S.B.5    Reis, D.J.6
  • 12
    • 0029971924 scopus 로고    scopus 로고
    • Permanent focal and transient global cerebral ischemia increase glial and neuronal expression of heme oxygenase-1, but not heme oxygenase-2, protein in rat brain
    • Geddes J.W., Pettigrew L.C., Holtz M.L., Craddock S.D., Maines M.D. Permanent focal and transient global cerebral ischemia increase glial and neuronal expression of heme oxygenase-1, but not heme oxygenase-2, protein in rat brain. Neurosci. Lett. 210:1996;205-208.
    • (1996) Neurosci. Lett. , vol.210 , pp. 205-208
    • Geddes, J.W.1    Pettigrew, L.C.2    Holtz, M.L.3    Craddock, S.D.4    Maines, M.D.5
  • 13
    • 0030036986 scopus 로고    scopus 로고
    • Intracellular accumulation of unconjugated bilirubin inhibits phytohemagglutinin-induced proliferation and interleukin-2 production of human lymphocytes
    • Haga Y., Tempero M.A., Kay D., Zetterman R.K. Intracellular accumulation of unconjugated bilirubin inhibits phytohemagglutinin-induced proliferation and interleukin-2 production of human lymphocytes. Dig. Dis. Sci. 41:1996;1468-1474.
    • (1996) Dig. Dis. Sci. , vol.41 , pp. 1468-1474
    • Haga, Y.1    Tempero, M.A.2    Kay, D.3    Zetterman, R.K.4
  • 14
    • 0029895670 scopus 로고    scopus 로고
    • Unconjugated bilirubin inhibits in vitro major histocompatibility complex-unrestricted cytotoxicity in human lymphocytes
    • Haga Y., Tempero M.A., Zetterman R.K. Unconjugated bilirubin inhibits in vitro major histocompatibility complex-unrestricted cytotoxicity in human lymphocytes. Biochim. Biophys. Acta. 1316:1996;29-34.
    • (1996) Biochim. Biophys. Acta , vol.1316 , pp. 29-34
    • Haga, Y.1    Tempero, M.A.2    Zetterman, R.K.3
  • 15
    • 0029954653 scopus 로고    scopus 로고
    • Bilirubin has widespread inhibitory effects on protein phosphorylation
    • Hansen T.W., Mathiesen S.B., Walaas S.I. Bilirubin has widespread inhibitory effects on protein phosphorylation. Pediatr. Res. 39:1996;1072-1077.
    • (1996) Pediatr. Res. , vol.39 , pp. 1072-1077
    • Hansen, T.W.1    Mathiesen, S.B.2    Walaas, S.I.3
  • 16
    • 0032551702 scopus 로고    scopus 로고
    • Inductions of hepatocyte growth factor and its activator in rat brain with permanent middle cerebral artery occlusion
    • Hayashi T., Abe K., Sakurai M., Itoyama Y. Inductions of hepatocyte growth factor and its activator in rat brain with permanent middle cerebral artery occlusion. Brain Res. 799:1998;311-316.
    • (1998) Brain Res. , vol.799 , pp. 311-316
    • Hayashi, T.1    Abe, K.2    Sakurai, M.3    Itoyama, Y.4
  • 17
    • 0032033868 scopus 로고    scopus 로고
    • Growth factors and gangliosides as neuroprotective agents in excitotoxicity and ischemia
    • Hicks D., Heidinger V., Mohand-Said S., Sahel J., Dreyfus H. Growth factors and gangliosides as neuroprotective agents in excitotoxicity and ischemia. Gen. Pharmacol. 30:1998;265-273.
    • (1998) Gen. Pharmacol. , vol.30 , pp. 265-273
    • Hicks, D.1    Heidinger, V.2    Mohand-Said, S.3    Sahel, J.4    Dreyfus, H.5
  • 18
    • 0031663391 scopus 로고    scopus 로고
    • NMDA receptors in the inferior colliculus are critically involved in audiogenic seizures in the adult rats with neonatal hypothyroidism
    • Higashiyma A., Ishida N., Nishimura T., Yasuda S., Kuroda Y., McEwen B.S., Kato N. NMDA receptors in the inferior colliculus are critically involved in audiogenic seizures in the adult rats with neonatal hypothyroidism. Exp. Neurol. 153:1998;94-101.
    • (1998) Exp. Neurol. , vol.153 , pp. 94-101
    • Higashiyma, A.1    Ishida, N.2    Nishimura, T.3    Yasuda, S.4    Kuroda, Y.5    McEwen, B.S.6    Kato, N.7
  • 19
    • 0021329973 scopus 로고
    • The regional distribution and cellular localization of iron in the rat brain
    • Hill J.M., Switzer R.C. The regional distribution and cellular localization of iron in the rat brain. Neuroscience. 11:1984;595-603.
    • (1984) Neuroscience , vol.11 , pp. 595-603
    • Hill, J.M.1    Switzer, R.C.2
  • 20
    • 0027476419 scopus 로고
    • Stress-induced inhibition of protein synthesis initiation: Modulation of initiation factor 2 and guanidine nucleotide exchange factor activities following transient cerebral ischemia in the rat
    • Hu B.R., Wieloch T. Stress-induced inhibition of protein synthesis initiation: modulation of initiation factor 2 and guanidine nucleotide exchange factor activities following transient cerebral ischemia in the rat. J. Neurosci. 13:1993;1830-1838.
    • (1993) J. Neurosci. , vol.13 , pp. 1830-1838
    • Hu, B.R.1    Wieloch, T.2
  • 21
    • 0024348120 scopus 로고
    • Detection of ten variants of biliverdin reductase in rat liver by two-dimensional gel electrophoresis
    • Huang T.J., Trakshel G.M., Maines M.D. Detection of ten variants of biliverdin reductase in rat liver by two-dimensional gel electrophoresis. J. Biol. Chem. 264:1989;7844-7849.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7844-7849
    • Huang, T.J.1    Trakshel, G.M.2    Maines, M.D.3
  • 23
    • 0031687793 scopus 로고    scopus 로고
    • Understanding cell death in Parkinson's disease
    • Suppl. 1
    • Jenner P., Olanow C.W. Understanding cell death in Parkinson's disease. Ann. Neurol. 44(3):1998;72-84. Suppl. 1.
    • (1998) Ann. Neurol. , vol.44 , Issue.3 , pp. 72-84
    • Jenner, P.1    Olanow, C.W.2
  • 24
    • 0029863341 scopus 로고    scopus 로고
    • Reduced nicotinamide adenine dinucleotide-selective stimulation of inositol 1,4,5-triphosphate receptors mediates hypoxic mobilization of calcium
    • Kaplin A.I., Snyder S.H., Linden D.J. Reduced nicotinamide adenine dinucleotide-selective stimulation of inositol 1,4,5-triphosphate receptors mediates hypoxic mobilization of calcium. J. Neurosci. 16:1996;2002-2011.
    • (1996) J. Neurosci. , vol.16 , pp. 2002-2011
    • Kaplin, A.I.1    Snyder, S.H.2    Linden, D.J.3
  • 26
    • 0027492357 scopus 로고
    • Induction of 70-kDa heat shock protein and hsp70 mRNA following transient focal cerebral ischemia in the rat
    • Kinouchi H., Sharp F.R., Hill M.P., Koistinaho J., Sagar S.M., Chan P.H. Induction of 70-kDa heat shock protein and hsp70 mRNA following transient focal cerebral ischemia in the rat. J. Cereb. Blood Flow Metab. 13:1993;105-115.
    • (1993) J. Cereb. Blood Flow Metab. , vol.13 , pp. 105-115
    • Kinouchi, H.1    Sharp, F.R.2    Hill, M.P.3    Koistinaho, J.4    Sagar, S.M.5    Chan, P.H.6
  • 27
    • 0025008802 scopus 로고
    • Astrocytic acidosis in hyperglycemic and complete ischemia
    • Kraig R.P., Chesler M. Astrocytic acidosis in hyperglycemic and complete ischemia. J. Cereb. Blood Flow Metab. 10:1990;104-114.
    • (1990) J. Cereb. Blood Flow Metab. , vol.10 , pp. 104-114
    • Kraig, R.P.1    Chesler, M.2
  • 29
    • 0030934491 scopus 로고    scopus 로고
    • A putative role for platelet-derived growth factor in angiogenesis and neuroprotection after ischemic stroke in humans
    • Krupinsky J., Issa R., Bujny T., Slevin M., Kumar P., Kumar S., Kaluza J. A putative role for platelet-derived growth factor in angiogenesis and neuroprotection after ischemic stroke in humans. Stroke. 28:1997;654-673.
    • (1997) Stroke , vol.28 , pp. 654-673
    • Krupinsky, J.1    Issa, R.2    Bujny, T.3    Slevin, M.4    Kumar, P.5    Kumar, S.6    Kaluza, J.7
  • 30
    • 0019887888 scopus 로고
    • Purification and characterization of biliverdin reductase from the rat liver
    • Kutty R.K., Maines M.D. Purification and characterization of biliverdin reductase from the rat liver. J. Biol. Chem. 256:1981;3956-3962.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3956-3962
    • Kutty, R.K.1    Maines, M.D.2
  • 31
    • 0026035905 scopus 로고
    • Bilirubin inhibits the activation of superoxide-producing NADPH oxidase in a neutrophil cell-free system
    • Kwak J.Y., Takeshiege K., Cheung B.S., Minakami S. Bilirubin inhibits the activation of superoxide-producing NADPH oxidase in a neutrophil cell-free system. Biochim. Biophys. Acta. 1076:1991;369-373.
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 369-373
    • Kwak, J.Y.1    Takeshiege, K.2    Cheung, B.S.3    Minakami, S.4
  • 32
    • 0031903967 scopus 로고    scopus 로고
    • Expression of nerve growth factor and trkA after transient focal cerebral ischemia in rats
    • Lee T.-H., Kato H., Chen S.-T., Kogure K., Itoyama Y. Expression of nerve growth factor and trkA after transient focal cerebral ischemia in rats. Stroke. 29:1998;1687-1697.
    • (1998) Stroke , vol.29 , pp. 1687-1697
    • Lee, T.-H.1    Kato, H.2    Chen, S.-T.3    Kogure, K.4    Itoyama, Y.5
  • 33
    • 0030698867 scopus 로고    scopus 로고
    • The role of dendritic dysfunction in neurodegeneration
    • Lin R.C., Matesic D.F., Connor J.A. The role of dendritic dysfunction in neurodegeneration. Ann. N. Y. Acad. Sci. 825:1997;134-145.
    • (1997) Ann. N. Y. Acad. Sci. , vol.825 , pp. 134-145
    • Lin, R.C.1    Matesic, D.F.2    Connor, J.A.3
  • 34
    • 0032579756 scopus 로고    scopus 로고
    • Differential regulation of ciliary neurotrophic factor (CNTF) and CNTF receptor α (CNTFRα) expression following focal cerebral ischemia
    • Lin T.-N., Wang P.-Y., Chi S.-I., Kuo J.-S. Differential regulation of ciliary neurotrophic factor (CNTF) and CNTF receptor α (CNTFRα) expression following focal cerebral ischemia. Mol. Brain Res. 55:1998;71-80.
    • (1998) Mol. Brain Res. , vol.55 , pp. 71-80
    • Lin, T.-N.1    Wang, P.-Y.2    Chi, S.-I.3    Kuo, J.-S.4
  • 35
    • 0031946532 scopus 로고    scopus 로고
    • Inhibition of poly(ADP-ribose) polymerase: Reduction of ischemic injury and attenuation of N-methyl-D-aspartate-induced neurotransmitter dysregulation
    • Lo E.H., Bosque-Hamilton P., Meng W. Inhibition of poly(ADP-ribose) polymerase: reduction of ischemic injury and attenuation of N-methyl-D-aspartate-induced neurotransmitter dysregulation. Stroke. 29:1998;830-836.
    • (1998) Stroke , vol.29 , pp. 830-836
    • Lo, E.H.1    Bosque-Hamilton, P.2    Meng, W.3
  • 36
    • 0033515795 scopus 로고    scopus 로고
    • Group I metabotropic receptors down-regulate nitric oxide induced caspase-3 activity in rat hippocampal neurons
    • Maiese K., Vincent A.M. Group I metabotropic receptors down-regulate nitric oxide induced caspase-3 activity in rat hippocampal neurons. Neurosci. Lett. 264:1999;17-20.
    • (1999) Neurosci. Lett. , vol.264 , pp. 17-20
    • Maiese, K.1    Vincent, A.M.2
  • 38
    • 0029671237 scopus 로고    scopus 로고
    • Human biliverdin IX alpha reductase is a zinc-metalloprotein. Characterization of purified and Escherichia coli expressed enzymes
    • Maines M.D., Polevoda B.V., Huang T.J., McCoubrey W.K. Jr. Human biliverdin IX alpha reductase is a zinc-metalloprotein. Characterization of purified and Escherichia coli expressed enzymes. Eur. J. Biochem. 235:1996;372-381.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 372-381
    • Maines, M.D.1    Polevoda, B.V.2    Huang, T.J.3    McCoubrey W.K., Jr.4
  • 39
    • 0027199553 scopus 로고
    • Purification and characterization of human biliverdin reductase
    • Maines M.D., Trakshel G.K. Purification and characterization of human biliverdin reductase. Arch. Biochem. Biophys. 300:1993;320-326.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 320-326
    • Maines, M.D.1    Trakshel, G.K.2
  • 40
    • 8544246393 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3
    • McCoubrey W.K. Jr., Huang T.J., Maines M.D. Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3. Eur. J. Biochem. 247:1997;725-732.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 725-732
    • McCoubrey W.K., Jr.1    Huang, T.J.2    Maines, M.D.3
  • 41
    • 0025281223 scopus 로고
    • Is bilirubin good for you?
    • McDonagh A.F. Is bilirubin good for you? Clin. Perinat. 17:1990;359-369.
    • (1990) Clin. Perinat. , vol.17 , pp. 359-369
    • McDonagh, A.F.1
  • 42
    • 0032897558 scopus 로고    scopus 로고
    • Antioxidant and cytotoxic effects of bilirubin on neonatal erythrocytes
    • Mireles L.C., Lum M.L., Dennery P.A. Antioxidant and cytotoxic effects of bilirubin on neonatal erythrocytes. Pediatr. Res. 45:1999;355-362.
    • (1999) Pediatr. Res. , vol.45 , pp. 355-362
    • Mireles, L.C.1    Lum, M.L.2    Dennery, P.A.3
  • 43
    • 0027452195 scopus 로고
    • A beneficial role of bile pigments as an endogenous tissue protector: Anti-complement effects of biliverdin and conjugated bilirubin
    • Nakagami T., Toyomura K., Kinoshita T., Morisawa S. A beneficial role of bile pigments as an endogenous tissue protector: anti-complement effects of biliverdin and conjugated bilirubin. Biochim. Biophys. Acta. 1158:1993;189-193.
    • (1993) Biochim. Biophys. Acta , vol.1158 , pp. 189-193
    • Nakagami, T.1    Toyomura, K.2    Kinoshita, T.3    Morisawa, S.4
  • 44
    • 0026778021 scopus 로고
    • Antiviral activity of a bile pigment, biliverdin, against human herpes virus 6 (HH6) in vitro
    • Nakagami T., Taji S., Takahashi M., Yamanishi K. Antiviral activity of a bile pigment, biliverdin, against human herpes virus 6 (HH6) in vitro. Microbiol. Immunol. 36:1992;381-390.
    • (1992) Microbiol. Immunol. , vol.36 , pp. 381-390
    • Nakagami, T.1    Taji, S.2    Takahashi, M.3    Yamanishi, K.4
  • 45
    • 0029997537 scopus 로고    scopus 로고
    • Heme oxygenase-1 (HO-1) protein induction in rat brain following focal ischemia
    • Nimura T., Weinstein P.R., Massa S.M., Panter S., Sharp F.R. Heme oxygenase-1 (HO-1) protein induction in rat brain following focal ischemia. Mol. Brain Res. 37:1996;201-208.
    • (1996) Mol. Brain Res. , vol.37 , pp. 201-208
    • Nimura, T.1    Weinstein, P.R.2    Massa, S.M.3    Panter, S.4    Sharp, F.R.5
  • 46
    • 0032972686 scopus 로고    scopus 로고
    • Overexpression of heme oxygenase-1 is neuroprotective in a model of permanent middle cerebral artery occlusion in transgenic mice
    • Panahian N., Yoshiura M., Maines M.D. Overexpression of heme oxygenase-1 is neuroprotective in a model of permanent middle cerebral artery occlusion in transgenic mice. J. Neurochem. 72:1999;1187-1203.
    • (1999) J. Neurochem. , vol.72 , pp. 1187-1203
    • Panahian, N.1    Yoshiura, M.2    Maines, M.D.3
  • 48
    • 0023501904 scopus 로고
    • Histochemical detection of lipid peroxidation in the liver of bromobenzine-poisoned mice
    • Pompella A., Maellaro E., Casini A.F., Comporti M. Histochemical detection of lipid peroxidation in the liver of bromobenzine-poisoned mice. Am. J. Pathol. 129:1987;295-301.
    • (1987) Am. J. Pathol. , vol.129 , pp. 295-301
    • Pompella, A.1    Maellaro, E.2    Casini, A.F.3    Comporti, M.4
  • 49
    • 0031963449 scopus 로고    scopus 로고
    • Function and regulation of transferrin and ferritin
    • Ponka P., Beaumont C., Richardson D.R. Function and regulation of transferrin and ferritin. Semin. Hematol. 35:1998;35-54.
    • (1998) Semin. Hematol. , vol.35 , pp. 35-54
    • Ponka, P.1    Beaumont, C.2    Richardson, D.R.3
  • 50
    • 0029029016 scopus 로고
    • Hypoxia alters iron homeostasis and induces ferritin synthesis in oligodendrocytes
    • Qi Y., Jamindar T.M., Dawson G. Hypoxia alters iron homeostasis and induces ferritin synthesis in oligodendrocytes. J. Neurochem. 64:1995;2458-2464.
    • (1995) J. Neurochem. , vol.64 , pp. 2458-2464
    • Qi, Y.1    Jamindar, T.M.2    Dawson, G.3
  • 51
    • 0029780523 scopus 로고    scopus 로고
    • Nitric oxide synthase inhibition by L-NAME prevents brain acidosis during focal cerebral ischemia in rabbits
    • Regli L., Held M.C., Anderson R.E., Meyer F.B. Nitric oxide synthase inhibition by L-NAME prevents brain acidosis during focal cerebral ischemia in rabbits. J. Cereb. Blood Flow Metab. 16:1996;988-995.
    • (1996) J. Cereb. Blood Flow Metab. , vol.16 , pp. 988-995
    • Regli, L.1    Held, M.C.2    Anderson, R.E.3    Meyer, F.B.4
  • 53
    • 0030988138 scopus 로고    scopus 로고
    • Nitric oxide synthase in models of focal ischemia
    • A.F. Samdani, T.M. Dawson, V.L. Dawson, Nitric oxide synthase in models of focal ischemia, Stroke 28, 1283-1288.
    • Stroke , vol.28 , pp. 1283-1288
    • Samdani, A.F.1    Dawson, T.M.2    Dawson, V.L.3
  • 54
    • 0021920319 scopus 로고
    • Mode of inhibitory action of bilirubin on protein kinase C
    • Sano K., Nakamura H., Matsuo T. Mode of inhibitory action of bilirubin on protein kinase C. Pediatr. Res. 19:1985;587-590.
    • (1985) Pediatr. Res. , vol.19 , pp. 587-590
    • Sano, K.1    Nakamura, H.2    Matsuo, T.3
  • 55
    • 0032918137 scopus 로고    scopus 로고
    • Caspases as treatment targets in stroke and neurodegenerative diseases
    • Schulz J.B., Weller M., Moskowitz M.A. Caspases as treatment targets in stroke and neurodegenerative diseases. Ann. Neurol. 45:1999;421-429.
    • (1999) Ann. Neurol. , vol.45 , pp. 421-429
    • Schulz, J.B.1    Weller, M.2    Moskowitz, M.A.3
  • 56
    • 0028835291 scopus 로고
    • Global incomplete cerebral ischemia produces predominantly cortical neuronal injury
    • Sieber F.E., Palmon S.C., Traystman R.J., Martin L.J. Global incomplete cerebral ischemia produces predominantly cortical neuronal injury. Stroke. 26:1995;2091-2096.
    • (1995) Stroke , vol.26 , pp. 2091-2096
    • Sieber, F.E.1    Palmon, S.C.2    Traystman, R.J.3    Martin, L.J.4
  • 59
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • Smith M.A., Haris P.L.R., Sayre L.M., Perry G. Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. Proc. Natl. Acad. Sci. U. S. A. 94:1997;9866-9868.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9866-9868
    • Smith, M.A.1    Haris, P.L.R.2    Sayre, L.M.3    Perry, G.4
  • 60
    • 0031831270 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman E.R., Berlett B.S. Reactive oxygen-mediated protein oxidation in aging and disease. Drug Metab. Rev. 30:1998;225-243.
    • (1998) Drug Metab. Rev. , vol.30 , pp. 225-243
    • Stadtman, E.R.1    Berlett, B.S.2
  • 61
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • Stocker P., Yamamoto Y., McDonagh A.F., Glazer A.N., Ames B.N. Bilirubin is an antioxidant of possible physiological importance. Science. 235:1987;1043-1047.
    • (1987) Science , vol.235 , pp. 1043-1047
    • Stocker, P.1    Yamamoto, Y.2    McDonagh, A.F.3    Glazer, A.N.4    Ames, B.N.5
  • 63
    • 0031900954 scopus 로고    scopus 로고
    • Induction of heme oxygenase protein protects neurons in cortex and striatum, but not in hippocampus against transient forebrain ischemia
    • Takizawa S., Hirabayashi H., Matsushima K., Tokuoka K., Shinohara Y. Induction of heme oxygenase protein protects neurons in cortex and striatum, but not in hippocampus against transient forebrain ischemia. J. Cereb. Blood Flow Metab. 18:1998;559-569.
    • (1998) J. Cereb. Blood Flow Metab. , vol.18 , pp. 559-569
    • Takizawa, S.1    Hirabayashi, H.2    Matsushima, K.3    Tokuoka, K.4    Shinohara, Y.5
  • 64
    • 0031960759 scopus 로고    scopus 로고
    • Cell cycle-related gene expression in the adult rat brain: Selective induction of cyclin G1 and p21 in neurons following focal cerebral ischemia
    • Van Lookeren Campagne M., Gill R. Cell cycle-related gene expression in the adult rat brain: selective induction of cyclin G1 and p21 in neurons following focal cerebral ischemia. Neuroscience. 84:1998;1097-1112.
    • (1998) Neuroscience , vol.84 , pp. 1097-1112
    • Van Lookeren Campagne, M.1    Gill, R.2
  • 65
    • 0030045835 scopus 로고    scopus 로고
    • Heme oxygenase: A novel target for the modulation of the inflammatory response
    • Willis D., Moore A.R., Frederick R., Willoughby D.A. Heme oxygenase: a novel target for the modulation of the inflammatory response. Nat. Med. 2:1996;87-90.
    • (1996) Nat. Med. , vol.2 , pp. 87-90
    • Willis, D.1    Moore, A.R.2    Frederick, R.3    Willoughby, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.