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Volumn 117, Issue 6, 2011, Pages 1055-1065

Chronic alcoholism in rats induces a compensatory response, preserving brain thiamine diphosphate, but the brain 2-oxo acid dehydrogenases are inactivated despite unchanged coenzyme levels

Author keywords

2 oxoacid dehydrogenases; alcoholism; brain; mitochondria; thiamine diphosphate; thiamine diphosphokinase

Indexed keywords

2 OXOACID DEHYDROGENASE; COCARBOXYLASE; OXOGLUTARATE DEHYDROGENASE; PYRUVATE DEHYDROGENASE; REACTIVE OXYGEN METABOLITE; THIAMINE; THIAMINE PHOSPHATE; THIOL DERIVATIVE;

EID: 79957999673     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2011.07283.x     Document Type: Article
Times cited : (21)

References (60)
  • 1
    • 37849043898 scopus 로고    scopus 로고
    • Reversible inhibition of alpha-ketoglutarate dehydrogenase by hydrogen peroxide: Glutathionylation and protection of lipoic acid
    • Applegate M. A., Humphries K. M., and, Szweda L. I., (2008) Reversible inhibition of alpha-ketoglutarate dehydrogenase by hydrogen peroxide: glutathionylation and protection of lipoic acid. Biochemistry 47, 473-478.
    • (2008) Biochemistry , vol.47 , pp. 473-478
    • Applegate, M.A.1    Humphries, K.M.2    Szweda, L.I.3
  • 3
    • 0013963011 scopus 로고
    • 14C-thiazole-labeled thiamine by the rat induced by a high fat diet or thyroxine
    • 14C-thiazole-labeled thiamine by the rat induced by a high fat diet or thyroxine. J. Nutr. 90, 161-166.
    • (1966) J. Nutr. , vol.90 , pp. 161-166
    • Balaghi, M.1    Pearson, W.N.2
  • 5
    • 0026005270 scopus 로고
    • Determination of thiamine and its phosphate esters in cultured neurons and astrocytes using an ion-pair reversed-phase high-performance liquid chromatographic method
    • Bettendorff L., Peeters M., Jouan C., Wins P., and, Schoffeniels E., (1991) Determination of thiamine and its phosphate esters in cultured neurons and astrocytes using an ion-pair reversed-phase high-performance liquid chromatographic method. Anal. Biochem. 198, 52-59.
    • (1991) Anal. Biochem. , vol.198 , pp. 52-59
    • Bettendorff, L.1    Peeters, M.2    Jouan, C.3    Wins, P.4    Schoffeniels, E.5
  • 6
    • 0034681508 scopus 로고    scopus 로고
    • Increased catalytic performance of the 2-oxoacid dehydrogenase complexes in the presence of thioredoxin, a thiol-disulfide oxidoreductase
    • Bunik V. I., (2000) Increased catalytic performance of the 2-oxoacid dehydrogenase complexes in the presence of thioredoxin, a thiol-disulfide oxidoreductase. J. Mol. Catalysis B: Enzymatic 8, 165-174.
    • (2000) J. Mol. Catalysis B: Enzymatic , vol.8 , pp. 165-174
    • Bunik, V.I.1
  • 7
    • 0037352050 scopus 로고    scopus 로고
    • 2-Oxo acid dehydrogenase complexes in redox regulation: Role of the lipoate residues and thioredoxin
    • DOI 10.1046/j.1432-1033.2003.03470.x
    • Bunik V. I., (2003) 2-Oxo acid dehydrogenase complexes in redox regulation. Role of the lipoate residues and thioredoxin. Eur. J. Biochem. 270, 1036-1042. (Pubitemid 36384437)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.6 , pp. 1036-1042
    • Bunik, V.I.1
  • 8
    • 70249150389 scopus 로고    scopus 로고
    • Metabolic control exerted by the 2-oxoglutarate dehydrogenase reaction: A cross-Kingdom comparison of the crossroad between energy production and nitrogen assimilation
    • Bunik V. I., and, Fernie A., (2009) Metabolic control exerted by the 2-oxoglutarate dehydrogenase reaction: a cross-Kingdom comparison of the crossroad between energy production and nitrogen assimilation. Biochem. J. 422, 405-421.
    • (2009) Biochem. J. , vol.422 , pp. 405-421
    • Bunik, V.I.1    Fernie, A.2
  • 9
    • 0036408866 scopus 로고    scopus 로고
    • Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species
    • DOI 10.1046/j.1432-1033.2002.03204.x
    • Bunik V. I., and, Sievers C., (2002) Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species. Eur. J. Biochem. 269, 5004-5015. (Pubitemid 35279014)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.20 , pp. 5004-5015
    • Bunik, V.I.1    Sievers, C.2
  • 11
    • 0024502089 scopus 로고
    • Effect of pyrithiamine treatment and subsequent thiamine rehabilitation on regional cerebral amino acids and thiamine-dependent enzymes
    • DOI 10.1111/j.1471-4159.1989.tb01850.x
    • Butterworth R. F., and, Heroux M., (1989) Effect of pyrithiamine treatment and subsequent thiamine rehabilitation on regional cerebral amino acid and thiamine-dependent enzymes. J. Neurochem. 52, 1079-1084. (Pubitemid 19085929)
    • (1989) Journal of Neurochemistry , vol.52 , Issue.4 , pp. 1079-1084
    • Butterworth, R.F.1    Heroux, M.2
  • 12
    • 33947579265 scopus 로고    scopus 로고
    • Thiamine deficiency (Wernicke's) encephalopathy: Pathophysiological mechanisms and development of positron emission tomography (PET) ligands
    • in (Bisswanger H. and Schellenberger A., eds), pp. A.U.C. Intemann, Prien
    • Butterworth R. F., and, Leong D. K., (1996) Thiamine deficiency (Wernicke's) encephalopathy: pathophysiological mechanisms and development of positron emission tomography (PET) ligands, in Biochemistry and Physiology of Thiamine Diphosphate Enzymes (Bisswanger H., and, Schellenberger A., eds), pp. 409-416. A.U.C. Intemann, Prien.
    • (1996) Biochemistry and Physiology of Thiamine Diphosphate Enzymes , pp. 409-416
    • Butterworth, R.F.1    Leong, D.K.2
  • 13
    • 0027131501 scopus 로고
    • Thiamine-dependent enzyme changes in the brains of alcoholics: Relationship to the Wernicke-Korsakoff Syndrome
    • Butterworth R. F., Kril J. J., and, Harper C. G., (1993) Thiamine-dependent enzyme changes in the brains of alcoholics: relationship to the Wernicke-Korsakoff syndrome. Alcohol. Clin. Exp. Res. 17, 1084-1088. (Pubitemid 24000530)
    • (1993) Alcoholism: Clinical and Experimental Research , vol.17 , Issue.5 , pp. 1084-1088
    • Butterworth, R.F.1    Kril, J.J.2    Harper, C.G.3
  • 14
    • 63149150728 scopus 로고    scopus 로고
    • Contribution of NADH increases to ethanol's inhibition of retinol oxidation by human ADH isoforms
    • Chase J. R., Poolman M. G., and, Fell D. A., (2009) Contribution of NADH increases to ethanol's inhibition of retinol oxidation by human ADH isoforms. Alcohol. Clin. Exp. Res. 33, 571-580.
    • (2009) Alcohol. Clin. Exp. Res. , vol.33 , pp. 571-580
    • Chase, J.R.1    Poolman, M.G.2    Fell, D.A.3
  • 15
    • 0026213194 scopus 로고
    • Fermentation micromethod for the quantitative determination of thiamine diphosphate in biological fluids
    • Chernikevich I.P., Gritsenko E.A., Makarchikov A.F., and, Voskoboev A.I., (1991) Fermentation micromethod for the quantitative determination of thiamine diphosphate in biological fluids. Prikl. Biokhim. Mikrobiol. 27b, 762-771.
    • (1991) Prikl. Biokhim. Mikrobiol. , vol.27 B , pp. 762-771
    • Chernikevich, I.P.1    Gritsenko, E.A.2    Makarchikov, A.F.3    Voskoboev, A.I.4
  • 16
    • 0010381114 scopus 로고
    • Thiamine kinase and thiamine pyrophosphate phosphatase in nervous tissue
    • Cooper J. R., and, Kalyanpur S. G., (1963) Thiamine kinase and thiamine pyrophosphate phosphatase in nervous tissue. Pharmacologist 5, 273.
    • (1963) Pharmacologist , vol.5 , pp. 273
    • Cooper, J.R.1    Kalyanpur, S.G.2
  • 17
    • 0015374472 scopus 로고
    • The partial purification and characterization of thiamine pyrophosphatase from rabbit brain
    • Cooper J. R., and, Kini M. M., (1972) The partial purification and characterization of thiamine pyrophosphatase from rabbit brain. J. Neurochem. 19, 1809-1811.
    • (1972) J. Neurochem. , vol.19 , pp. 1809-1811
    • Cooper, J.R.1    Kini, M.M.2
  • 18
    • 0017401380 scopus 로고
    • Subcellular distribution of thiamine pyrophosphokinase and thiamine pyrophosphatase activities in rat isolated enterocytes
    • Cusaro G., Rindi G., and, Sciorelli G., (1977) Subcellular distribution of thiamine-pyrophosphokinase and thiamine-pyrophosphatase activities in rat isolated enterocytes. Int. J. Vitamin. Nutr. Res. 47, 99-106. (Pubitemid 8124811)
    • (1977) International Journal for Vitamin and Nutrition Research , vol.47 , Issue.2 , pp. 99-106
    • Cusaro, G.1    Rindi, G.2    Sciorelli, G.3
  • 19
    • 84961030199 scopus 로고
    • Contents in rat tissue of thiamine and its phosphates during dietary thiamine deficiency
    • De Caro L., Rindi G., and, De Giuseppe L., (1961) Contents in rat tissue of thiamine and its phosphates during dietary thiamine deficiency. Int. Z. Vitaminforsch. 31, 333-340.
    • (1961) Int. Z. Vitaminforsch. , vol.31 , pp. 333-340
    • De Caro, L.1    Rindi, G.2    De Giuseppe, L.3
  • 20
    • 0014915089 scopus 로고
    • Subcellular distribution of thiamine pyrophosphokinase activity in rat liver and erythrocytes
    • Deus B., and, Blum H., (1970) Subcellular distribution of thiamine pyrophosphokinase activity in rat liver and erythrocytes. Biochim. Biophys. Acta 219, 489-92.
    • (1970) Biochim. Biophys. Acta , vol.219 , pp. 489-492
    • Deus, B.1    Blum, H.2
  • 21
    • 0023406340 scopus 로고
    • Effect of age on behavioral and enzymatic changes during thiamine deficiency
    • Freeman G. B., Nielsen P. E., and, Gibson G. E., (1987) Effect of age on behavioral and enzymatic changes during thiamine deficiency. Neurobiol. Aging 8, 429-434.
    • (1987) Neurobiol. Aging , vol.8 , pp. 429-434
    • Freeman, G.B.1    Nielsen, P.E.2    Gibson, G.E.3
  • 22
    • 77954296914 scopus 로고    scopus 로고
    • Effect of fasting on the urinary excretion of water-soluble vitamins in humans and rats
    • Fukuwatari T., Yoshida E., Takahashi K., and, Shibata K., (2010) Effect of fasting on the urinary excretion of water-soluble vitamins in humans and rats. J. Nutr. Sci. Vitaminol. 56, 19-26.
    • (2010) J. Nutr. Sci. Vitaminol. , vol.56 , pp. 19-26
    • Fukuwatari, T.1    Yoshida, E.2    Takahashi, K.3    Shibata, K.4
  • 23
    • 0024552754 scopus 로고
    • Regionally selective alterations in enzymatic activities and metabolic fluxes during thiamin deficiency
    • DOI 10.1007/BF00969752
    • Gibson G. E., Nielsen P., Mykytyn V., Carlson K., and, Blass J. P., (1989) Regionally selective alterations in enzymatic activities and metabolic fluxes during thiamine deficiency. Neurochem. Res. 14, 17-24. (Pubitemid 19075269)
    • (1989) Neurochemical Research , vol.14 , Issue.1 , pp. 17-24
    • Gibson, G.1    Nielsen, P.2    Mykytyn, V.3    Carlson, K.4    Blass, J.5
  • 24
    • 23244435445 scopus 로고    scopus 로고
    • The α-ketoglutarate-dehydrogenase complex: A mediator between mitochondria and oxidative stress in neurodegeneration
    • Gibson G. E., Blass J. P., Beal M. F., and, Bunik V., (2005) The α-ketoglutarate-dehydrogenase complex: a mediator between mitochondria and oxidative stress in neurodegeneration. Mol. Neurobiol. 31, 43-63. (Pubitemid 41271193)
    • (2005) Molecular Neurobiology , vol.31 , Issue.1-3 , pp. 43-63
    • Gibson, G.E.1    Blass, J.P.2    Beal, M.F.3    Bunik, V.4
  • 25
    • 35448999182 scopus 로고    scopus 로고
    • 2+ mobilization and increases GFAP content in rat hippocampal astrocytes
    • DOI 10.1016/j.brainres.2007.08.040, PII S0006899307018756
    • 2 +mobilization and increases GFAP content in rat hippocampal astrocytes. Brain Res. 1178, 28-37. (Pubitemid 47625358)
    • (2007) Brain Research , vol.1178 , Issue.1 , pp. 28-37
    • Gonzalez, A.1    Pariente, J.A.2    Salido, G.M.3
  • 26
    • 0016693716 scopus 로고
    • Properties of thiamine di- and triphosphatases in rat brain microsomes: Effects of chlorpromazine
    • Iwata H., Baba A., Matsuda T., and, Terashita Z., (1975a) Properties of thiamine di- and triphosphatases in rat brain microsomes: effects of chlorpromazine. J. Neurochem. 24, 1209-1213.
    • (1975) J. Neurochem. , vol.24 , pp. 1209-1213
    • Iwata, H.1    Baba, A.2    Matsuda, T.3    Terashita, Z.4
  • 27
    • 0016756176 scopus 로고
    • Effect of various nucleotides and drugs on microsomal thiamine diphosphatase activity in rat brain
    • Iwata H., Matsuda T., and, Baba A., (1975b) Effect of various nucleotides and drugs on microsomal thiamine diphosphatase activity in rat brain. J. Nutr. Sci. Vitaminol. 21, 323-329.
    • (1975) J. Nutr. Sci. Vitaminol. , vol.21 , pp. 323-329
    • Iwata, H.1    Matsuda, T.2    Baba, A.3
  • 28
    • 0014252638 scopus 로고
    • Studies on the physiological functions of thiamine (III) phosphorylation of thiamine in brain
    • Johnson L. R., and, Gubler C. J., (1968) Studies on the physiological functions of thiamine (III) phosphorylation of thiamine in brain. Biochem. Biophys. Acta 156, 85-96.
    • (1968) Biochem. Biophys. Acta , vol.156 , pp. 85-96
    • Johnson, L.R.1    Gubler, C.J.2
  • 29
    • 63149092201 scopus 로고    scopus 로고
    • Synthetic regulators of the 2-oxoglutarate oxidative decarboxylation alleviate the glutamate excitotoxicity in cerebellar granule neurons
    • Kabysheva M. S., Storozhevykh T. P., Pinelis V. G., Pinelis V. G., and, Bunik V. I., (2009) Synthetic regulators of the 2-oxoglutarate oxidative decarboxylation alleviate the glutamate excitotoxicity in cerebellar granule neurons. Biochem. Pharmacol. 77, 1531-1540.
    • (2009) Biochem. Pharmacol. , vol.77 , pp. 1531-1540
    • Kabysheva, M.S.1    Storozhevykh, T.P.2    Pinelis, V.G.3    Pinelis, V.G.4    Bunik, V.I.5
  • 30
    • 78651119314 scopus 로고
    • Biochemical changes in rat tissues after prolonged alcohol consumption
    • Kissling K. H., and, Tilander K., (1961) Biochemical changes in rat tissues after prolonged alcohol consumption. Q. J. Stud. Alcohol. 22, 535-543.
    • (1961) Q. J. Stud. Alcohol. , vol.22 , pp. 535-543
    • Kissling, K.H.1    Tilander, K.2
  • 31
    • 0025639118 scopus 로고
    • Effects of acute and chronic ethanol administration on thiamine metabolizing enzymes in some brain areas and in other organs of the rat
    • Laforenza U., Patrini C., Gastaldi G., and, Rindi G., (1990) Effects of acute and chronic ethanol administration on thiamine metabolizing enzymes in some brain areas and in other organs of the rat. Alcohol Alcohol. 25, 591-603.
    • (1990) Alcohol Alcohol. , vol.25 , pp. 591-603
    • Laforenza, U.1    Patrini, C.2    Gastaldi, G.3    Rindi, G.4
  • 32
    • 0029116717 scopus 로고
    • Reduced activities of thiamine-dependent enzymes in brains of alcoholics in the absence of Wernicke's encephalopathy
    • Lavoie J., and, Butterworth R. F., (1995) Reduced activities of thiamine-dependent enzymes in brains of alcoholics in the absence of Wernicke's encephalopathy. Alcohol. Clin. Exp. Res. 19, 1073-1077.
    • (1995) Alcohol. Clin. Exp. Res. , vol.19 , pp. 1073-1077
    • Lavoie, J.1    Butterworth, R.F.2
  • 34
    • 66349101019 scopus 로고    scopus 로고
    • Execution of superoxide-induced cell death by the proapoptotic Bcl-2-related proteins Bid and Bak
    • Madesh M., Zong W. X., Hawkins B. J., et al. (2009) Execution of superoxide-induced cell death by the proapoptotic Bcl-2-related proteins Bid and Bak. Mol. Cell. Biol. 29, 3099-3112.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3099-3112
    • Madesh, M.1    Zong, W.X.2    Hawkins, B.J.3
  • 36
    • 61549133968 scopus 로고    scopus 로고
    • Biomarkers in alcohol misuse: Their role in the prevention and detection of thiamine deficiency
    • Mancinelli R., and, Ceccanti M., (2009) Biomarkers in alcohol misuse: their role in the prevention and detection of thiamine deficiency. Alcohol Alcohol. 44, 177-182.
    • (2009) Alcohol Alcohol. , vol.44 , pp. 177-182
    • Mancinelli, R.1    Ceccanti, M.2
  • 37
    • 33746067845 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and Alzheimer's disease: New developments
    • Mancuso M., Siciliano G., Filosto M., and, Murri l., (2006) Mitochondrial dysfunction and Alzheimer's disease: new developments. J. Alzheimer Disease 9, 111-117. (Pubitemid 44078639)
    • (2006) Journal of Alzheimer's Disease , vol.9 , Issue.2 , pp. 111-117
    • Mancuso, M.1    Siciliano, G.2    Filosto, M.3    Murri, L.4
  • 38
    • 0017795323 scopus 로고
    • Characterization of thiamine diphosphatase in rat small intestine
    • Matsuda T., Maeda S., Baba A., and, Iwata H., (1978) Characterization of thiamine diphosphatase in rat small intestine. J. Nutr. Sci. Vitaminol. 24, 123-132.
    • (1978) J. Nutr. Sci. Vitaminol. , vol.24 , pp. 123-132
    • Matsuda, T.1    Maeda, S.2    Baba, A.3    Iwata, H.4
  • 39
    • 57049143140 scopus 로고    scopus 로고
    • Mitochondria in neuroplasticity and neurological disorders
    • Mattson M. P., Gleichmann M., and, Cheng A., (2008) Mitochondria in neuroplasticity and neurological disorders. Neuron 60, 748-766.
    • (2008) Neuron , vol.60 , pp. 748-766
    • Mattson, M.P.1    Gleichmann, M.2    Cheng, A.3
  • 40
    • 51649099329 scopus 로고    scopus 로고
    • Region-selective alterations of glucose oxidation and amino acid synthesis in the thiamine-deficient rat brain: A re-evaluation using 1H/13C nuclear magnetic resonance spectroscopy
    • Navarro D., Zwingmann C., and, Butterworth R. F., (2008) Region-selective alterations of glucose oxidation and amino acid synthesis in the thiamine-deficient rat brain: a re-evaluation using 1H/13C nuclear magnetic resonance spectroscopy. J. Neurochem. 106 (2), 603-612.
    • (2008) J. Neurochem. , vol.106 , Issue.2 , pp. 603-612
    • Navarro, D.1    Zwingmann, C.2    Butterworth, R.F.3
  • 41
    • 0345146921 scopus 로고    scopus 로고
    • Reversible inactivation of α-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status
    • DOI 10.1021/bi027370f
    • Nulton-Persson A. C., Starke D. W., Mieyal J. J., and, Szweda L. I., (2003) Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status. Biochemistry 42, 4235-4242. (Pubitemid 36418317)
    • (2003) Biochemistry , vol.42 , Issue.14 , pp. 4235-4242
    • Nulton-Persson, A.C.1    Starke, D.W.2    Mieyal, J.J.3    Szweda, L.I.4
  • 42
    • 8944231558 scopus 로고
    • Thiamine
    • in (Ostrovskii Yu. M., ed.), pp. Nauka i tekhnika, Minsk [Russian]
    • Ostrovskii Yu. M., (1979) Thiamine, in Experimental Vitaminology (Ostrovskii Yu. M., ed.), pp. 176-223. Nauka i tekhnika, Minsk [Russian].
    • (1979) Experimental Vitaminology , pp. 176-223
    • Ostrovskii, Yu.M.1
  • 43
    • 0022815539 scopus 로고
    • Thiamine phosphates and regulation of the pyruvate dehydrogenase complex activity in rat liver mitochondria
    • [article in Russian]
    • Parkhomenko Iu. M., Protasova Z. S., and, Khalmuradov A. G., (1986) Thiamine phosphates and regulation of the pyruvate dehydrogenase complex activity in rat liver mitochondria. Ukr. Biochem. J. 58, 35-41 [article in Russian].
    • (1986) Ukr. Biochem. J , vol.58 , pp. 35-41
    • Parkhomenko, Iu.M.1    Protasova, Z.S.2    Khalmuradov, A.G.3
  • 44
    • 0016704839 scopus 로고
    • Partial purification and properties of thiamine pyrophosphokinase from pig brain
    • Peterson J. W., Gubler C. J., and, Kuby S. A., (1975) Partial purification and properties of thiamine pyrophosphokinase from pig brain. Biochim. Biophys. Acta 397, 377-394.
    • (1975) Biochim. Biophys. Acta , vol.397 , pp. 377-394
    • Peterson, J.W.1    Gubler, C.J.2    Kuby, S.A.3
  • 45
    • 42149194307 scopus 로고    scopus 로고
    • Properties of thiamin transport in isolated perfused hearts of chronically alcoholic guinea pigs
    • DOI 10.1139/Y08-013
    • Petrovic M. M., Scepanovic L., Rosic G., and, Mitrovic D. M., (2008) Properties of thiamine transport in isolated perfused hearts of chronically alcoholic guinea pigs. J. Physiol. Pharmacol. 86, 160-165. (Pubitemid 351536446)
    • (2008) Canadian Journal of Physiology and Pharmacology , vol.86 , Issue.4 , pp. 160-165
    • Petrovic, M.M.1    Scepanovic, L.2    Rosic, G.3    Mitrovic, D.M.4
  • 48
    • 0037351228 scopus 로고    scopus 로고
    • Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1
    • DOI 10.1046/j.1432-1033.2003.03468.x
    • Roche T. E., Hiromasa Y., Turkan A., Gong X., Peng T., Yan X., Kasten S. A., Bao H., and, Donget J., (2003) Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1. Eur. J. Biochem. 270, 1050-1056. (Pubitemid 36384439)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.6 , pp. 1050-1056
    • Roche, T.E.1    Hiromasa, Y.2    Turkan, A.3    Gong, X.4    Peng, T.5    Yan, X.6    Kasten, S.A.7    Bao, H.8    Dong, J.9
  • 50
    • 0014428865 scopus 로고
    • Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent
    • Sedlak J., and, Lindsay R. H., (1968) Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent. Anal. Biochem. 25, 192-205.
    • (1968) Anal. Biochem. , vol.25 , pp. 192-205
    • Sedlak, J.1    Lindsay, R.H.2
  • 53
    • 34250790605 scopus 로고    scopus 로고
    • Responses of the mitochondrial alpha-ketoglutarate dehydrogenase complex to thiamine deficiency may contribute to regional selective vulnerability
    • DOI 10.1016/j.neuint.2007.03.010, PII S019701860700071X
    • Shi Q., Karuppagounder S. S., Xu H., and, Gibson G. E., (2007) Responses of the mitochondrial α-ketoglutarate dehydrogenase complex to thiamine deficiency may contribute to regional selective vulnerability. Neurochem. Int. 50, 921-931. (Pubitemid 46962817)
    • (2007) Neurochemistry International , vol.50 , Issue.7-8 , pp. 921-931
    • Shi, Q.1    Karuppagounder, S.S.2    Xu, H.3    Pechman, D.4    Chen, H.5    Gibson, G.E.6
  • 54
    • 77953817833 scopus 로고    scopus 로고
    • Effect of chronic alcohol feeding on physiological and molecular parameters of renal thiamine transport
    • Subramanian V. S., Subramanya S. B., Tsukamoto H., and, Said H. M., (2010) Effect of chronic alcohol feeding on physiological and molecular parameters of renal thiamine transport. Am. J. Physiol. Renal. Physiol. 299, 28-34.
    • (2010) Am. J. Physiol. Renal. Physiol. , vol.299 , pp. 28-34
    • Subramanian, V.S.1    Subramanya, S.B.2    Tsukamoto, H.3    Said, H.M.4
  • 56
    • 83455181308 scopus 로고    scopus 로고
    • Synaptic mitochondria in synaptic transmission and organization of vesicle pools in health and disease
    • Vos M., Lauwers E., and, Verstreken P., (2010) Synaptic mitochondria in synaptic transmission and organization of vesicle pools in health and disease. Front. Synaptic Neurosci. 2, 139.
    • (2010) Front. Synaptic Neurosci. , vol.2 , pp. 139
    • Vos, M.1    Lauwers, E.2    Verstreken, P.3
  • 57
    • 0042368567 scopus 로고
    • Some properties of the purified thiamine pyrophosphokinase from pig brain
    • Wakabayashi Y., (1978) Some properties of the purified thiamine pyrophosphokinase from pig brain. Vitamins 5-6, 229-236.
    • (1978) Vitamins , vol.56 , pp. 229-236
    • Wakabayashi, Y.1
  • 58
    • 0014409304 scopus 로고
    • Allosteric properties of nucleoside diphosphatase and its identity with thiamine pyrophosphatase
    • Yamazaki M., and, Hayaishi O., (1968) Allosteric properties of nucleoside diphosphatase and its identity with thiamine pyrophosphatase. J. Biol. Chem. 243, 2934-2942.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2934-2942
    • Yamazaki, M.1    Hayaishi, O.2
  • 59
    • 65249177776 scopus 로고    scopus 로고
    • Suppressive effects of hydroxytyrosol on oxidative stress and nuclear factor-kappa B activation in THP-1 cells
    • Zhang X., Cao J., Jiang L., and, Zhong L., (2009) Suppressive effects of hydroxytyrosol on oxidative stress and nuclear factor-kappa B activation in THP-1 cells. Biol. Pharm. Bull. 32, 578-582.
    • (2009) Biol. Pharm. Bull. , vol.32 , pp. 578-582
    • Zhang, X.1    Cao, J.2    Jiang, L.3    Zhong, L.4
  • 60
    • 58149469744 scopus 로고    scopus 로고
    • α-Ketoglutarate dehydrogenase contributes to production of reactive oxygen species in glutamate-stimulated hippocampal neurons in situ
    • Zündorf G., Kahlert S., Bunik V. I., and, Reiser G., (2009) α-Ketoglutarate dehydrogenase contributes to production of reactive oxygen species in glutamate-stimulated hippocampal neurons in situ. Neuroscience 158, 610-616.
    • (2009) Neuroscience , vol.158 , pp. 610-616
    • Zündorf, G.1    Kahlert, S.2    Bunik, V.I.3    Reiser, G.4


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