메뉴 건너뛰기




Volumn 92, Issue , 2016, Pages 13-24

Hypoxia and GABA shunt activation in the pathogenesis of Alzheimer's disease

Author keywords

Alzheimer's disease; Dementia; Energy metabolism; GABA shunt; GHB; Hypoxia

Indexed keywords

2,4 DIHYDROXYBUTYRATE; 4 AMINOBUTYRIC ACID; 4 HYDROXYBUTYRIC ACID; BUTYRIC ACID; GLUTAMIC ACID; GLUTAMINE; SUCCINATE SEMIALDEHYDE DEHYDROGENASE; UNCLASSIFIED DRUG; 2,4-DIHYDROXYBUTYRATE; BUTANEDIOL; BUTYRIC ACID DERIVATIVE; OXYBATE SODIUM;

EID: 84954126760     PISSN: 01970186     EISSN: 18729754     Source Type: Journal    
DOI: 10.1016/j.neuint.2015.11.005     Document Type: Review
Times cited : (40)

References (216)
  • 2
    • 0346993682 scopus 로고    scopus 로고
    • Mutational spectrum of the succinate semialdehyde dehydrogenase (ALDH5A1) gene and functional analysis of 27 novel disease-causing mutations in patients with SSADH deficiency
    • S. Akaboshi, B.M. Hogema, A. Novelletto, P. Malaspina, G.S. Salomons, G.D. Maropoulos, and et al. Mutational spectrum of the succinate semialdehyde dehydrogenase (ALDH5A1) gene and functional analysis of 27 novel disease-causing mutations in patients with SSADH deficiency Hum. Mutat. 22 2003 442 450
    • (2003) Hum. Mutat. , vol.22 , pp. 442-450
    • Akaboshi, S.1    Hogema, B.M.2    Novelletto, A.3    Malaspina, P.4    Salomons, G.S.5    Maropoulos, G.D.6
  • 3
    • 43549107641 scopus 로고
    • Succinic semialdehyde dehydrogenase: Purification and properties of the enzyme from monkey brain
    • R.W. Albers, and G.J. Koval Succinic semialdehyde dehydrogenase: purification and properties of the enzyme from monkey brain Biochim. Biophys. Acta 52 1961 29 35
    • (1961) Biochim. Biophys. Acta , vol.52 , pp. 29-35
    • Albers, R.W.1    Koval, G.J.2
  • 4
    • 84910647222 scopus 로고    scopus 로고
    • Metabolism of gamma hydroxybutyrate in human hepatoma HepG2 cells by the aldo-keto reductase AKR1A1
    • S. Alzeer, and E.M. Ellis Metabolism of gamma hydroxybutyrate in human hepatoma HepG2 cells by the aldo-keto reductase AKR1A1 Biochem. Pharmacol. 92 2014 499 505
    • (2014) Biochem. Pharmacol. , vol.92 , pp. 499-505
    • Alzeer, S.1    Ellis, E.M.2
  • 6
    • 1842739274 scopus 로고    scopus 로고
    • Amyloid β peptide 1-42 highly correlates with capillary cerebral amyloid angiopathy and Alzheimer disease pathology
    • J. Attems, F. Lintner, and K.A. Jellinger Amyloid β peptide 1-42 highly correlates with capillary cerebral amyloid angiopathy and Alzheimer disease pathology Acta Neuropathol. 107 2004 283 291
    • (2004) Acta Neuropathol. , vol.107 , pp. 283-291
    • Attems, J.1    Lintner, F.2    Jellinger, K.A.3
  • 8
    • 33745893228 scopus 로고    scopus 로고
    • The glutamate/GABA-glutamine cycle: Aspects of transport, neurotransmitter homeostasis and ammonia transfer
    • L.K. Bak, A. Schousboe, and H.S. Waagepetersen The glutamate/GABA-glutamine cycle: aspects of transport, neurotransmitter homeostasis and ammonia transfer J. Neurochem. 98 2006 641 653
    • (2006) J. Neurochem. , vol.98 , pp. 641-653
    • Bak, L.K.1    Schousboe, A.2    Waagepetersen, H.S.3
  • 9
    • 70449435661 scopus 로고    scopus 로고
    • Transgenic expression of Glud1 (glutamate dehydrogenase 1) in neurons: In vivo model of enhanced glutamate release, altered synaptic plasticity, and selective neuronal vulnerability
    • X. Bao, R. Pal, K.N. Hascup, Y. Wang, W.T. Wang, W. Xu, and et al. Transgenic expression of Glud1 (glutamate dehydrogenase 1) in neurons: in vivo model of enhanced glutamate release, altered synaptic plasticity, and selective neuronal vulnerability J. Neurosci. 29 2009 13929 13944
    • (2009) J. Neurosci. , vol.29 , pp. 13929-13944
    • Bao, X.1    Pal, R.2    Hascup, K.N.3    Wang, Y.4    Wang, W.T.5    Xu, W.6
  • 10
    • 0033198703 scopus 로고    scopus 로고
    • Characterization of the human aldehyde reductase gene and promoter
    • O.A. Barski, K.H. Gabbay, and K.M. Bohren Characterization of the human aldehyde reductase gene and promoter Genomics 60 1999 188 198
    • (1999) Genomics , vol.60 , pp. 188-198
    • Barski, O.A.1    Gabbay, K.H.2    Bohren, K.M.3
  • 11
    • 84892367470 scopus 로고    scopus 로고
    • GHB receptor targets in the CNS: Focus on high-affinity binding sites
    • T. Bay, L.F. Eghorn, A.B. Klein, and P. Wellendorph GHB receptor targets in the CNS: focus on high-affinity binding sites Biochem. Pharmacol. 87 2014 220 228
    • (2014) Biochem. Pharmacol. , vol.87 , pp. 220-228
    • Bay, T.1    Eghorn, L.F.2    Klein, A.B.3    Wellendorph, P.4
  • 12
    • 0037636431 scopus 로고    scopus 로고
    • Mitochondrial succinic-semialdehyde dehydrogenase of the gamma-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants
    • N. Bouche, A. Fait, D. Bouchez, S.G. Moller, and H. Fromm Mitochondrial succinic-semialdehyde dehydrogenase of the gamma-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants Proc. Natl. Acad. Sci. U. S. A. 100 2003 6843 6848
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 6843-6848
    • Bouche, N.1    Fait, A.2    Bouchez, D.3    Moller, S.G.4    Fromm, H.5
  • 13
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • H. Braak, and E. Braak Neuropathological stageing of Alzheimer-related changes Acta Neuropathol. 82 1991 239 259
    • (1991) Acta Neuropathol. , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 14
    • 33749150163 scopus 로고    scopus 로고
    • Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry
    • H. Braak, I. Alafuzoff, T. Arzberger, H. Kretzschmar, and K. Del Tredici Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry Acta Neuropathol. 112 2006 389 404
    • (2006) Acta Neuropathol. , vol.112 , pp. 389-404
    • Braak, H.1    Alafuzoff, I.2    Arzberger, T.3    Kretzschmar, H.4    Del Tredici, K.5
  • 16
    • 0001117141 scopus 로고
    • Urinary organic acids in succinic semialdehyde dehydrogenase deficiency: Evidence of alpha-oxidation of 4-hydroxybutyric acid, interaction of succinic semialdehyde with pyruvate dehydrogenase and possible secondary inhibition of mitochondrial beta-oxidation
    • G.K. Brown, C.H. Cromby, N.J. Manning, and R.J. Pollitt Urinary organic acids in succinic semialdehyde dehydrogenase deficiency: evidence of alpha-oxidation of 4-hydroxybutyric acid, interaction of succinic semialdehyde with pyruvate dehydrogenase and possible secondary inhibition of mitochondrial beta-oxidation J. Inherit. Metab. Dis. 10 1987 367 375
    • (1987) J. Inherit. Metab. Dis. , vol.10 , pp. 367-375
    • Brown, G.K.1    Cromby, C.H.2    Manning, N.J.3    Pollitt, R.J.4
  • 18
    • 18244390483 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in Alzheimer brain: Mechanistic implications
    • P. Bubber, V. Haroutunian, G. Fisch, J.P. Blass, and G.E. Gibson Mitochondrial abnormalities in Alzheimer brain: mechanistic implications Ann. Neurol. 57 2005 695 703
    • (2005) Ann. Neurol. , vol.57 , pp. 695-703
    • Bubber, P.1    Haroutunian, V.2    Fisch, G.3    Blass, J.P.4    Gibson, G.E.5
  • 20
    • 0043172479 scopus 로고    scopus 로고
    • The glutamatergic system and Alzheimer's disease: Therapeutic implications
    • D.A. Butterfield, and C.B. Pocernich The glutamatergic system and Alzheimer's disease: therapeutic implications CNS Drugs 17 2003 641 652
    • (2003) CNS Drugs , vol.17 , pp. 641-652
    • Butterfield, D.A.1    Pocernich, C.B.2
  • 21
    • 77953257870 scopus 로고    scopus 로고
    • Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease
    • D.A. Butterfield, M.L. Bader Lange, and R. Sultana Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease Biochim. Biophys. Acta 1801 2010 924 929
    • (2010) Biochim. Biophys. Acta , vol.1801 , pp. 924-929
    • Butterfield, D.A.1    Bader Lange, M.L.2    Sultana, R.3
  • 22
    • 0036753272 scopus 로고    scopus 로고
    • Evidence that amyloid β-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death
    • D.A. Butterfield, A. Castegna, C.M. Lauderback, and J. Drake Evidence that amyloid β-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death Neurobiol. Aging 23 2002 655 664
    • (2002) Neurobiol. Aging , vol.23 , pp. 655-664
    • Butterfield, D.A.1    Castegna, A.2    Lauderback, C.M.3    Drake, J.4
  • 23
    • 33644987632 scopus 로고    scopus 로고
    • Elevated protein-bound levels of the lipid peroxidation product, 4-hydroxy-2-nonenal, in brain from persons with mild cognitive impairment
    • D.A. Butterfield, T. Reed, M. Perluigi, C. De Marco, R. Coccia, C. Cini, and et al. Elevated protein-bound levels of the lipid peroxidation product, 4-hydroxy-2-nonenal, in brain from persons with mild cognitive impairment Neurosci. Lett. 397 2006 170 173
    • (2006) Neurosci. Lett. , vol.397 , pp. 170-173
    • Butterfield, D.A.1    Reed, T.2    Perluigi, M.3    De Marco, C.4    Coccia, R.5    Cini, C.6
  • 24
    • 84939981400 scopus 로고    scopus 로고
    • Targeting the prodromal stage of Alzheimer's disease: Bioenergetic and mitochondrial opportunities
    • C.C. Caldwell, J. Yao, and R.D. Brinton Targeting the prodromal stage of Alzheimer's disease: bioenergetic and mitochondrial opportunities Neurotherapeutics 12 2015 66 80
    • (2015) Neurotherapeutics , vol.12 , pp. 66-80
    • Caldwell, C.C.1    Yao, J.2    Brinton, R.D.3
  • 25
    • 0018596221 scopus 로고
    • Purification from human brain and some properties of two NADPH-linked aldehyde reductases which reduce succinic semialdehyde to 4-hydroxybutyrate
    • C.D. Cash, M. Maitre, and P. Mandel Purification from human brain and some properties of two NADPH-linked aldehyde reductases which reduce succinic semialdehyde to 4-hydroxybutyrate J. Neurochem. 33 1979 1169 1175
    • (1979) J. Neurochem. , vol.33 , pp. 1169-1175
    • Cash, C.D.1    Maitre, M.2    Mandel, P.3
  • 26
    • 0028895777 scopus 로고
    • Molecular cloning of the mature NAD+-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression
    • K.L. Chambliss, D.L. Caudle, D.D. Hinson, C.R. Moomaw, C.A. Slaughter, C. Jakobs, and et al. Molecular cloning of the mature NAD+-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression J. Biol. Chem. 270 1995 461 467
    • (1995) J. Biol. Chem. , vol.270 , pp. 461-467
    • Chambliss, K.L.1    Caudle, D.L.2    Hinson, D.D.3    Moomaw, C.R.4    Slaughter, C.A.5    Jakobs, C.6
  • 27
    • 0032525344 scopus 로고    scopus 로고
    • Downregulation of oxidative phosphorylation in Alzheimer disease: Loss of cytochrome oxidase subunit mRNA in the hippocampus and entorhinal cortex
    • K. Chandrasekaran, K. Hatanpää, D.R. Brady, J. Stoll, and S.I. Rapoport Downregulation of oxidative phosphorylation in Alzheimer disease: loss of cytochrome oxidase subunit mRNA in the hippocampus and entorhinal cortex Brain Res. 796 1998 13 19
    • (1998) Brain Res. , vol.796 , pp. 13-19
    • Chandrasekaran, K.1    Hatanpää, K.2    Brady, D.R.3    Stoll, J.4    Rapoport, S.I.5
  • 28
    • 84867577236 scopus 로고    scopus 로고
    • Cerebral microbleeds and cognition in cerebrovascular disease: An update
    • A. Charidimou, and D.J. Werring Cerebral microbleeds and cognition in cerebrovascular disease: an update J. Neurol. Sci. 322 2012 50 55
    • (2012) J. Neurol. Sci. , vol.322 , pp. 50-55
    • Charidimou, A.1    Werring, D.J.2
  • 29
    • 79954601665 scopus 로고    scopus 로고
    • Analysis of the GAD1 promoter: Trans-acting factors and DNA methylation converge on the 5' untranslated region
    • Y. Chen, E. Dong, and D.R. Grayson Analysis of the GAD1 promoter: trans-acting factors and DNA methylation converge on the 5' untranslated region Neuropharmacology 60 2011 1075 1087
    • (2011) Neuropharmacology , vol.60 , pp. 1075-1087
    • Chen, Y.1    Dong, E.2    Grayson, D.R.3
  • 30
    • 84879605512 scopus 로고    scopus 로고
    • Which way does the citric acid cycle turn during hypoxia? the critical role of α-ketoglutarate dehydrogenase complex
    • C. Chinopoulos Which way does the citric acid cycle turn during hypoxia? the critical role of α-ketoglutarate dehydrogenase complex J. Neurosci. Res. 91 2013 1030 1043
    • (2013) J. Neurosci. Res. , vol.91 , pp. 1030-1043
    • Chinopoulos, C.1
  • 31
    • 0027514002 scopus 로고
    • Kinetics and mechanism of an NADPH-dependent succinic semialdehyde reductase from bovine brain
    • S.W. Cho, M.S. Song, G.Y. Kim, W.D. Kang, E.Y. Choi, and S.Y. Choi Kinetics and mechanism of an NADPH-dependent succinic semialdehyde reductase from bovine brain Eur. J. Biochem. 211 1993 757 762
    • (1993) Eur. J. Biochem. , vol.211 , pp. 757-762
    • Cho, S.W.1    Song, M.S.2    Kim, G.Y.3    Kang, W.D.4    Choi, E.Y.5    Choi, S.Y.6
  • 32
    • 30944439522 scopus 로고    scopus 로고
    • Unravelling the brain targets of γ-hydroxybutyric acid
    • V. Crunelli, Z. Emri, and N. Leresche Unravelling the brain targets of γ-hydroxybutyric acid Curr. Opin. Pharmacol. 6 2006 44 52
    • (2006) Curr. Opin. Pharmacol. , vol.6 , pp. 44-52
    • Crunelli, V.1    Emri, Z.2    Leresche, N.3
  • 34
  • 35
    • 84865405744 scopus 로고    scopus 로고
    • Alzheimer's disease, β-amyloid, glutamate, NMDA receptors and memantine - Searching for the connections
    • W. Danysz, and C.G. Parsons Alzheimer's disease, β-amyloid, glutamate, NMDA receptors and memantine - searching for the connections Br. J. Pharmacol. 167 2012 324 352
    • (2012) Br. J. Pharmacol. , vol.167 , pp. 324-352
    • Danysz, W.1    Parsons, C.G.2
  • 36
    • 33645855881 scopus 로고    scopus 로고
    • Acute regulation of steady-state GABA levels following GABA-transaminase inhibition in rat cerebral cortex
    • R.A. de Graaf, A.B. Patel, D.L. Rothman, and K.L. Behar Acute regulation of steady-state GABA levels following GABA-transaminase inhibition in rat cerebral cortex Neurochem. Int. 48 2006 508 514
    • (2006) Neurochem. Int. , vol.48 , pp. 508-514
    • De Graaf, R.A.1    Patel, A.B.2    Rothman, D.L.3    Behar, K.L.4
  • 37
    • 84895822736 scopus 로고    scopus 로고
    • Biomarker-based prediction of progression in MCI: Comparison of AD signature and hippocampal volume with spinal fluid amyloid-β and tau
    • B.C. Dickerson, D.A. Wolk, and Alzheimer's Disease Neuroimaging Initiative Biomarker-based prediction of progression in MCI: comparison of AD signature and hippocampal volume with spinal fluid amyloid-β and tau Front. Aging Neurosci. 5 2013 55
    • (2013) Front. Aging Neurosci. , vol.5 , pp. 55
    • Dickerson, B.C.1    Wolk, D.A.2    Disease Neuroimaging Initiative, A.3
  • 38
    • 0018192666 scopus 로고
    • Metabolism of γ-hydroxy-[1-14C] butyrate by rat brain: Relationship to the Krebs cycle and metabolic compartmentation of amino acids
    • J.D. Doherty, and R.H. Roth Metabolism of γ-hydroxy-[1-14C] butyrate by rat brain: relationship to the Krebs cycle and metabolic compartmentation of amino acids J. Neurochem. 30 1978 1305 1309
    • (1978) J. Neurochem. , vol.30 , pp. 1305-1309
    • Doherty, J.D.1    Roth, R.H.2
  • 40
    • 69249212441 scopus 로고    scopus 로고
    • Mitochondrial dihydrolipoyl succinyltransferase deficiency accelerates amyloid pathology and memory deficit in a transgenic mouse model of amyloid deposition
    • M. Dumont, D.J. Ho, N.Y. Calingasan, H. Xu, G. Gibson, and M.F. Beal Mitochondrial dihydrolipoyl succinyltransferase deficiency accelerates amyloid pathology and memory deficit in a transgenic mouse model of amyloid deposition Free Radic. Biol. Med. 47 2009 1019 1027
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 1019-1027
    • Dumont, M.1    Ho, D.J.2    Calingasan, N.Y.3    Xu, H.4    Gibson, G.5    Beal, M.F.6
  • 42
    • 0028324791 scopus 로고
    • Comparative localization of two forms of glutamic acid decarboxylase and their mRNAs in rat brain supports the concept of functional differences between the forms
    • M. Esclapez, N.J. Tillakaratne, D.L. Kaufman, A.J. Tobin, and C.R. Houser Comparative localization of two forms of glutamic acid decarboxylase and their mRNAs in rat brain supports the concept of functional differences between the forms J. Neurosci. 14 1994 1834 1855
    • (1994) J. Neurosci. , vol.14 , pp. 1834-1855
    • Esclapez, M.1    Tillakaratne, N.J.2    Kaufman, D.L.3    Tobin, A.J.4    Houser, C.R.5
  • 44
  • 45
    • 84871140204 scopus 로고    scopus 로고
    • Role of glutamate metabolism in bacterial responses towards acid and other stresses
    • C. Feehily, and K.A. Karatzas Role of glutamate metabolism in bacterial responses towards acid and other stresses J. Appl. Microbiol. 114 2013 11 24
    • (2013) J. Appl. Microbiol. , vol.114 , pp. 11-24
    • Feehily, C.1    Karatzas, K.A.2
  • 47
    • 23244435445 scopus 로고    scopus 로고
    • The α-ketoglutarate-dehydrogenase complex: A mediator between mitochondria and oxidative stress in neurodegeneration
    • G.E. Gibson, J.P. Blass, M.F. Beal, and V. Bunik The α-ketoglutarate-dehydrogenase complex: a mediator between mitochondria and oxidative stress in neurodegeneration Mol. Neurobiol. 31 2005 43 63
    • (2005) Mol. Neurobiol. , vol.31 , pp. 43-63
    • Gibson, G.E.1    Blass, J.P.2    Beal, M.F.3    Bunik, V.4
  • 48
    • 0024473121 scopus 로고
    • Metabolism of [U-14C]-4-hydroxybutyric acid to intermediates of the tricarboxylic acid cycle in extracts of rat liver and kidney mitochondria
    • K.M. Gibson, and W.L. Nyhan Metabolism of [U-14C]-4-hydroxybutyric acid to intermediates of the tricarboxylic acid cycle in extracts of rat liver and kidney mitochondria Eur. J. Drug Metab. Pharmacokinet. 14 1989 61 70
    • (1989) Eur. J. Drug Metab. Pharmacokinet. , vol.14 , pp. 61-70
    • Gibson, K.M.1    Nyhan, W.L.2
  • 49
    • 0025864422 scopus 로고
    • Comparative effect of transient global ischemia on extracellular levels of glutamate, glycine, and gamma-aminobutyric acid in vulnerable and nonvulnerable brain regions in the rat
    • M.Y. Globus, R. Busto, E. Martinez, I. Valdes, W.D. Dietrich, and M.D. Ginsberg Comparative effect of transient global ischemia on extracellular levels of glutamate, glycine, and gamma-aminobutyric acid in vulnerable and nonvulnerable brain regions in the rat J. Neurochem. 57 1991 470 478
    • (1991) J. Neurochem. , vol.57 , pp. 470-478
    • Globus, M.Y.1    Busto, R.2    Martinez, E.3    Valdes, I.4    Dietrich, W.D.5    Ginsberg, M.D.6
  • 50
    • 84911163843 scopus 로고    scopus 로고
    • Metabolomic screening of regional brain alterations in the APP/PS1 transgenic model of Alzheimer's disease by direct infusion mass spectrometry
    • R. Gonzalez-Dominguez, T. Garcia-Barrera, J. Vitorica, and J.L. Gomez-Ariza Metabolomic screening of regional brain alterations in the APP/PS1 transgenic model of Alzheimer's disease by direct infusion mass spectrometry J. Pharm. Biomed. Anal. 102 2015 425 435
    • (2015) J. Pharm. Biomed. Anal. , vol.102 , pp. 425-435
    • Gonzalez-Dominguez, R.1    Garcia-Barrera, T.2    Vitorica, J.3    Gomez-Ariza, J.L.4
  • 51
    • 4444323611 scopus 로고    scopus 로고
    • Succinic semialdehyde dehydrogenase deficiency (SSADH) (4-hydroxybutyric aciduria, gamma-hydroxybutyric aciduria)
    • N. Gordon Succinic semialdehyde dehydrogenase deficiency (SSADH) (4-hydroxybutyric aciduria, gamma-hydroxybutyric aciduria) Eur. J. Paediatr. Neurol. 8 2004 261 265
    • (2004) Eur. J. Paediatr. Neurol. , vol.8 , pp. 261-265
    • Gordon, N.1
  • 52
    • 0025788909 scopus 로고
    • Vigabatrin. A review of its pharmacodynamic and pharmacokinetic properties, and therapeutic potential in epilepsy and disorders of motor control
    • S.M. Grant, and R.C. Heel Vigabatrin. A review of its pharmacodynamic and pharmacokinetic properties, and therapeutic potential in epilepsy and disorders of motor control Drugs 41 1991 889 926
    • (1991) Drugs , vol.41 , pp. 889-926
    • Grant, S.M.1    Heel, R.C.2
  • 53
    • 0028233223 scopus 로고
    • Age-related reference values for urinary organic acids in a healthy Turkish pediatric population
    • F. Guneral, and C. Bachmann Age-related reference values for urinary organic acids in a healthy Turkish pediatric population Clin. Chem. 40 1994 862 866
    • (1994) Clin. Chem. , vol.40 , pp. 862-866
    • Guneral, F.1    Bachmann, C.2
  • 56
    • 3142743789 scopus 로고    scopus 로고
    • Value of CSF beta-amyloid1-42 and tau as predictors of Alzheimer's disease in patients with mild cognitive impairment
    • H. Hampel, S.J. Teipel, T. Fuchsberger, N. Andreasen, J. Wiltfang, M. Otto, and et al. Value of CSF beta-amyloid1-42 and tau as predictors of Alzheimer's disease in patients with mild cognitive impairment Mol. Psychiatry 9 2004 705 710
    • (2004) Mol. Psychiatry , vol.9 , pp. 705-710
    • Hampel, H.1    Teipel, S.J.2    Fuchsberger, T.3    Andreasen, N.4    Wiltfang, J.5    Otto, M.6
  • 58
    • 0031659606 scopus 로고    scopus 로고
    • Quantification of the GABA shunt and the importance of the GABA shunt versus the 2-oxoglutarate dehydrogenase pathway in GABAergic neurons
    • B. Hassel, C.U. Johannessen, U. Sonnewald, and F. Fonnum Quantification of the GABA shunt and the importance of the GABA shunt versus the 2-oxoglutarate dehydrogenase pathway in GABAergic neurons J. Neurochem. 71 1998 1511 1518
    • (1998) J. Neurochem. , vol.71 , pp. 1511-1518
    • Hassel, B.1    Johannessen, C.U.2    Sonnewald, U.3    Fonnum, F.4
  • 59
    • 0021171529 scopus 로고
    • Interactions between 4-aminobutyrate aminotransferase and succinic semialdehyde dehydrogenase, two mitochondrial enzymes
    • W.G. Hearl, and J.E. Churchich Interactions between 4-aminobutyrate aminotransferase and succinic semialdehyde dehydrogenase, two mitochondrial enzymes J. Biol. Chem. 259 1984 11459 11463
    • (1984) J. Biol. Chem. , vol.259 , pp. 11459-11463
    • Hearl, W.G.1    Churchich, J.E.2
  • 61
    • 77952212178 scopus 로고    scopus 로고
    • Glutaminase 2, a novel p53 target gene regulating energy metabolism and antioxidant function
    • W. Hu, C. Zhang, R. Wu, Y. Sun, A. Levine, and Z. Feng Glutaminase 2, a novel p53 target gene regulating energy metabolism and antioxidant function Proc. Natl. Acad. Sci. U. S. A. 107 2010 7455 7460
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 7455-7460
    • Hu, W.1    Zhang, C.2    Wu, R.3    Sun, Y.4    Levine, A.5    Feng, Z.6
  • 62
    • 4644354687 scopus 로고    scopus 로고
    • Changes of pyridoxal kinase expression and activity in the gerbil hippocampus following transient forebrain ischemia
    • I.K. Hwang, K.Y. Yoo, D.S. Kim, W.S. Eum, J.K. Park, J. Park, and et al. Changes of pyridoxal kinase expression and activity in the gerbil hippocampus following transient forebrain ischemia Neuroscience 128 2004 511 518
    • (2004) Neuroscience , vol.128 , pp. 511-518
    • Hwang, I.K.1    Yoo, K.Y.2    Kim, D.S.3    Eum, W.S.4    Park, J.K.5    Park, J.6
  • 63
    • 84890528022 scopus 로고    scopus 로고
    • Biomarker modeling of Alzheimer's disease
    • C.R. Jack Jr., and D.M. Holtzman Biomarker modeling of Alzheimer's disease Neuron 80 2013 1347 1358
    • (2013) Neuron , vol.80 , pp. 1347-1358
    • Jack, C.R.1    Holtzman, D.M.2
  • 64
    • 0033533136 scopus 로고    scopus 로고
    • Role of nitric oxide on GABA, glutamic acid, activities of GABA-T and GAD in rat brain cerebral cortex
    • A.R. Jayakumar, R. Sujatha, V. Paul, C. Asokan, S. Govindasamy, and R. Jayakumar Role of nitric oxide on GABA, glutamic acid, activities of GABA-T and GAD in rat brain cerebral cortex Brain Res. 837 1999 229 235
    • (1999) Brain Res. , vol.837 , pp. 229-235
    • Jayakumar, A.R.1    Sujatha, R.2    Paul, V.3    Asokan, C.4    Govindasamy, S.5    Jayakumar, R.6
  • 65
    • 33749143872 scopus 로고    scopus 로고
    • The possible role of capillary cerebral amyloid angiopathy in Alzheimer lesion development: A regional comparison
    • B. Jeynes, and J. Provias The possible role of capillary cerebral amyloid angiopathy in Alzheimer lesion development: a regional comparison Acta Neuropathol. 112 2006 417 427
    • (2006) Acta Neuropathol. , vol.112 , pp. 417-427
    • Jeynes, B.1    Provias, J.2
  • 66
    • 84905822105 scopus 로고    scopus 로고
    • GABA from reactive astrocytes impairs memory in mouse models of Alzheimer's disease
    • S. Jo, O. Yarishkin, Y.J. Hwang, Y.E. Chun, M. Park, D.H. Woo, and et al. GABA from reactive astrocytes impairs memory in mouse models of Alzheimer's disease Nat. Med. 20 2014 886 896
    • (2014) Nat. Med. , vol.20 , pp. 886-896
    • Jo, S.1    Yarishkin, O.2    Hwang, Y.J.3    Chun, Y.E.4    Park, M.5    Woo, D.H.6
  • 67
    • 84900819324 scopus 로고    scopus 로고
    • Gamma-hydroxybutyrate (GHB) induces cognitive deficits and affects GABAB receptors and IGF-1 receptors in male rats
    • J. Johansson, A. Grönbladh, and M. Hallberg Gamma-hydroxybutyrate (GHB) induces cognitive deficits and affects GABAB receptors and IGF-1 receptors in male rats Behav. Brain Res. 269 2014 164 174
    • (2014) Behav. Brain Res. , vol.269 , pp. 164-174
    • Johansson, J.1    Grönbladh, A.2    Hallberg, M.3
  • 68
    • 0034603512 scopus 로고    scopus 로고
    • The role of cerebral ischemia in Alzheimer's disease
    • R.N. Kalaria The role of cerebral ischemia in Alzheimer's disease Neurobiol. Aging 21 2000 321 330
    • (2000) Neurobiol. Aging , vol.21 , pp. 321-330
    • Kalaria, R.N.1
  • 69
    • 2942541293 scopus 로고    scopus 로고
    • Palmitoylation controls trafficking of GAD65 from Golgi membranes to axon-specific endosomes and a Rab5a-dependent pathway to presynaptic clusters
    • J. Kanaani, M.J. Diacovo, A. El-Husseini, D.S. Bredt, and S. Baekkeskov Palmitoylation controls trafficking of GAD65 from Golgi membranes to axon-specific endosomes and a Rab5a-dependent pathway to presynaptic clusters J. Cell Sci. 117 2004 2001 2013
    • (2004) J. Cell Sci. , vol.117 , pp. 2001-2013
    • Kanaani, J.1    Diacovo, M.J.2    El-Husseini, A.3    Bredt, D.S.4    Baekkeskov, S.5
  • 70
    • 77956383991 scopus 로고    scopus 로고
    • Two distinct mechanisms target GAD67 to vesicular pathways and presynaptic clusters
    • J. Kanaani, J. Kolibachuk, H. Martinez, and S. Baekkeskov Two distinct mechanisms target GAD67 to vesicular pathways and presynaptic clusters J. Cell Biol. 190 2010 911 925
    • (2010) J. Cell Biol. , vol.190 , pp. 911-925
    • Kanaani, J.1    Kolibachuk, J.2    Martinez, H.3    Baekkeskov, S.4
  • 71
    • 0034634742 scopus 로고    scopus 로고
    • Elevation of the γ-aminobutyric acid transaminase expression in the gerbil CA1 area after ischemia-reperfusion damage
    • T.C. Kang, S.K. Park, J.H. Bahn, J.S. Chang, W.S. Koh, S.M. Jo, and et al. Elevation of the γ-aminobutyric acid transaminase expression in the gerbil CA1 area after ischemia-reperfusion damage Neurosci. Lett. 294 2000 33 36
    • (2000) Neurosci. Lett. , vol.294 , pp. 33-36
    • Kang, T.C.1    Park, S.K.2    Bahn, J.H.3    Chang, J.S.4    Koh, W.S.5    Jo, S.M.6
  • 72
    • 0037135140 scopus 로고    scopus 로고
    • Spatial and temporal alterations in the GABA shunt in the gerbil hippocampus following transient ischemia
    • T.C. Kang, S.K. Park, I.K. Hwang, S.J. An, S.Y. Choi, S.W. Cho, and et al. Spatial and temporal alterations in the GABA shunt in the gerbil hippocampus following transient ischemia Brain Res. 944 2002 10 18
    • (2002) Brain Res. , vol.944 , pp. 10-18
    • Kang, T.C.1    Park, S.K.2    Hwang, I.K.3    An, S.J.4    Choi, S.Y.5    Cho, S.W.6
  • 73
    • 0037290227 scopus 로고    scopus 로고
    • The altered expression of GABA shunt enzymes in the gerbil hippocampus before and after seizure generation
    • T.C. Kang, S.K. Park, I.K. Hwang, S.J. An, S.Y. Choi, O.S. Kwon, and et al. The altered expression of GABA shunt enzymes in the gerbil hippocampus before and after seizure generation Neurochem. Int. 42 2003 239 249
    • (2003) Neurochem. Int. , vol.42 , pp. 239-249
    • Kang, T.C.1    Park, S.K.2    Hwang, I.K.3    An, S.J.4    Choi, S.Y.5    Kwon, O.S.6
  • 74
    • 0025944441 scopus 로고
    • An overview of γ-hydroxybutyrate catabolism: The role of the cytosolic NADP(+)-dependent oxidoreductase EC 1.1.1.19 and of a mitochondrial hydroxyacid-oxoacid transhydrogenase in the initial, rate-limiting step in this pathway
    • E.E. Kaufman, and T. Nelson An overview of γ-hydroxybutyrate catabolism: the role of the cytosolic NADP(+)-dependent oxidoreductase EC 1.1.1.19 and of a mitochondrial hydroxyacid-oxoacid transhydrogenase in the initial, rate-limiting step in this pathway Neurochem. Res. 16 1991 965 974
    • (1991) Neurochem. Res. , vol.16 , pp. 965-974
    • Kaufman, E.E.1    Nelson, T.2
  • 75
    • 0037106619 scopus 로고    scopus 로고
    • Novel homodimeric and heterodimeric rat γ-hydroxybutyrate synthases that associate with the Golgi apparatus define a distinct subclass of aldo-keto reductase 7 family proteins
    • V.P. Kelly, P.J. Sherratt, D.H. Crouch, and J.D. Hayes Novel homodimeric and heterodimeric rat γ-hydroxybutyrate synthases that associate with the Golgi apparatus define a distinct subclass of aldo-keto reductase 7 family proteins Biochem. J. 366 2002 847 861
    • (2002) Biochem. J. , vol.366 , pp. 847-861
    • Kelly, V.P.1    Sherratt, P.J.2    Crouch, D.H.3    Hayes, J.D.4
  • 76
    • 77951188459 scopus 로고    scopus 로고
    • A single acute pharmacological dose of γ-hydroxybutyrate modifies multiple gene expression patterns in rat hippocampus and frontal cortex
    • V. Kemmel, C. Klein, D. Dembele, B. Jost, O. Taleb, D. Aunis, and et al. A single acute pharmacological dose of γ-hydroxybutyrate modifies multiple gene expression patterns in rat hippocampus and frontal cortex Physiol. Genomics 41 2010 146 160
    • (2010) Physiol. Genomics , vol.41 , pp. 146-160
    • Kemmel, V.1    Klein, C.2    Dembele, D.3    Jost, B.4    Taleb, O.5    Aunis, D.6
  • 77
    • 33644614520 scopus 로고    scopus 로고
    • HIF-1-mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia
    • J.W. Kim, I. Tchernyshyov, G.L. Semenza, and C.V. Dang HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia Cell. Metab. 3 2006 177 185
    • (2006) Cell. Metab. , vol.3 , pp. 177-185
    • Kim, J.W.1    Tchernyshyov, I.2    Semenza, G.L.3    Dang, C.V.4
  • 78
    • 79959964863 scopus 로고    scopus 로고
    • Succinic semialdehyde dehydrogenase: Biochemical-molecular-clinical disease mechanisms, redox regulation, and functional significance
    • K.J. Kim, P.L. Pearl, K. Jensen, O.C. Snead, P. Malaspina, C. Jakobs, and et al. Succinic semialdehyde dehydrogenase: biochemical-molecular-clinical disease mechanisms, redox regulation, and functional significance Antioxid. Redox Signal 15 2011 691 718
    • (2011) Antioxid. Redox Signal , vol.15 , pp. 691-718
    • Kim, K.J.1    Pearl, P.L.2    Jensen, K.3    Snead, O.C.4    Malaspina, P.5    Jakobs, C.6
  • 79
    • 65449160629 scopus 로고    scopus 로고
    • Redox-switch modulation of human SSADH by dynamic catalytic loop
    • Y.G. Kim, S. Lee, O.S. Kwon, S.Y. Park, S.J. Lee, B.J. Park, and et al. Redox-switch modulation of human SSADH by dynamic catalytic loop EMBO J. 28 2009 959 968
    • (2009) EMBO J. , vol.28 , pp. 959-968
    • Kim, Y.G.1    Lee, S.2    Kwon, O.S.3    Park, S.Y.4    Lee, S.J.5    Park, B.J.6
  • 81
    • 67650421510 scopus 로고    scopus 로고
    • Pharmacological doses of γ-hydroxybutyrate (GHB) potentiate histone acetylation in the rat brain by histone deacetylase inhibition
    • C. Klein, V. Kemmel, O. Taleb, D. Aunis, and M. Maitre Pharmacological doses of γ-hydroxybutyrate (GHB) potentiate histone acetylation in the rat brain by histone deacetylase inhibition Neuropharmacology 57 2009 137 147
    • (2009) Neuropharmacology , vol.57 , pp. 137-147
    • Klein, C.1    Kemmel, V.2    Taleb, O.3    Aunis, D.4    Maitre, M.5
  • 82
    • 84922771242 scopus 로고    scopus 로고
    • γ-Hydroxybutyrate (Xyrem) ameliorates clinical symptoms and neuropathology in a mouse model of Alzheimer's disease
    • C. Klein, C. Mathis, G. Leva, C. Patte-Mensah, J.C. Cassel, M. Maitre, and et al. γ-Hydroxybutyrate (Xyrem) ameliorates clinical symptoms and neuropathology in a mouse model of Alzheimer's disease Neurobiol. Aging 36 2015 832 844
    • (2015) Neurobiol. Aging , vol.36 , pp. 832-844
    • Klein, C.1    Mathis, C.2    Leva, G.3    Patte-Mensah, C.4    Cassel, J.C.5    Maitre, M.6
  • 83
    • 0035704857 scopus 로고    scopus 로고
    • Selective loss of KGDHC-enriched neurons in Alzheimer temporal cortex: Does mitochondrial variation contribute to selective vulnerability?
    • L.W. Ko, K.F. Sheu, H.T. Thaler, W.R. Markesbery, and J.P. Blass Selective loss of KGDHC-enriched neurons in Alzheimer temporal cortex: does mitochondrial variation contribute to selective vulnerability? J. Mol. Neurosci. 17 2001 361 369
    • (2001) J. Mol. Neurosci. , vol.17 , pp. 361-369
    • Ko, L.W.1    Sheu, K.F.2    Thaler, H.T.3    Markesbery, W.R.4    Blass, J.P.5
  • 85
    • 84886311261 scopus 로고    scopus 로고
    • Astrocytes and glutamate homoeostasis in Alzheimer's disease: A decrease in glutamine synthetase, but not in glutamate transporter-1, in the prefrontal cortex
    • M. Kulijewicz-Nawrot, E. Sykova, A. Chvatal, A. Verkhratsky, and J.J. Rodriguez Astrocytes and glutamate homoeostasis in Alzheimer's disease: a decrease in glutamine synthetase, but not in glutamate transporter-1, in the prefrontal cortex ASN Neuro 5 2013 273 282
    • (2013) ASN Neuro , vol.5 , pp. 273-282
    • Kulijewicz-Nawrot, M.1    Sykova, E.2    Chvatal, A.3    Verkhratsky, A.4    Rodriguez, J.J.5
  • 86
    • 4043070505 scopus 로고    scopus 로고
    • GABAergic function in Alzheimer's disease: Evidence for dysfunction and potential as a therapeutic target for the treatment of behavioural and psychological symptoms of dementia
    • K.L. Lanctot, N. Herrmann, P. Mazzotta, L.R. Khan, and N. Ingber GABAergic function in Alzheimer's disease: evidence for dysfunction and potential as a therapeutic target for the treatment of behavioural and psychological symptoms of dementia Can. J. Psychiatry 49 2004 439 453
    • (2004) Can. J. Psychiatry , vol.49 , pp. 439-453
    • Lanctot, K.L.1    Herrmann, N.2    Mazzotta, P.3    Khan, L.R.4    Ingber, N.5
  • 87
    • 35248813789 scopus 로고    scopus 로고
    • Evidence for oxidative stress in tissues derived from succinate semialdehyde dehydrogenase-deficient mice
    • A. Latini, K. Scussiato, G. Leipnitz, K.M. Gibson, and M. Wajner Evidence for oxidative stress in tissues derived from succinate semialdehyde dehydrogenase-deficient mice J. Inherit. Metab. Dis. 30 2007 800 810
    • (2007) J. Inherit. Metab. Dis. , vol.30 , pp. 800-810
    • Latini, A.1    Scussiato, K.2    Leipnitz, G.3    Gibson, K.M.4    Wajner, M.5
  • 88
    • 0017640526 scopus 로고
    • Evidence for the β-oxidation of orally administered 4-hydroxybutyrate in humans
    • C.R. Lee Evidence for the β-oxidation of orally administered 4-hydroxybutyrate in humans Biochem. Med. 17 1977 284 291
    • (1977) Biochem. Med. , vol.17 , pp. 284-291
    • Lee, C.R.1
  • 89
    • 78349279184 scopus 로고    scopus 로고
    • Astrocytes are GABAergic cells that modulate microglial activity
    • M. Lee, C. Schwab, and P.L. McGeer Astrocytes are GABAergic cells that modulate microglial activity Glia 59 2011 152 165
    • (2011) Glia , vol.59 , pp. 152-165
    • Lee, M.1    Schwab, C.2    McGeer, P.L.3
  • 90
    • 84866003024 scopus 로고    scopus 로고
    • Lipid peroxidation dysregulation in ischemic stroke: Plasma 4-HNE as a potential biomarker?
    • W.C. Lee, H.Y. Wong, Y.Y. Chai, C.W. Shi, N. Amino, S. Kikuchi, and et al. Lipid peroxidation dysregulation in ischemic stroke: plasma 4-HNE as a potential biomarker? Biochem. Biophys. Res. Commun. 425 2012 842 847
    • (2012) Biochem. Biophys. Res. Commun. , vol.425 , pp. 842-847
    • Lee, W.C.1    Wong, H.Y.2    Chai, Y.Y.3    Shi, C.W.4    Amino, N.5    Kikuchi, S.6
  • 91
    • 0036080614 scopus 로고    scopus 로고
    • Reactive species mechanisms of cellular hypoxia-reoxygenation injury
    • C. Li, and R.M. Jackson Reactive species mechanisms of cellular hypoxia-reoxygenation injury Am. J. Physiol. Cell Physiol. 282 2002 C227 C241
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282 , pp. C227-C241
    • Li, C.1    Jackson, R.M.2
  • 92
    • 77957934065 scopus 로고    scopus 로고
    • Increased GAD expression in the striatum after transient cerebral ischemia
    • Y. Li, G.D. Blanco, Z. Lei, and Z.C. Xu Increased GAD expression in the striatum after transient cerebral ischemia Mol. Cell. Neurosci. 45 2010 370 377
    • (2010) Mol. Cell. Neurosci. , vol.45 , pp. 370-377
    • Li, Y.1    Blanco, G.D.2    Lei, Z.3    Xu, Z.C.4
  • 93
    • 84901218395 scopus 로고    scopus 로고
    • Glutaminase 2 negatively regulates the PI3K/AKT signaling and shows tumor suppression activity in human hepatocellular carcinoma
    • J. Liu, C. Zhang, M. Lin, W. Zhu, Y. Liang, X. Hong, and et al. Glutaminase 2 negatively regulates the PI3K/AKT signaling and shows tumor suppression activity in human hepatocellular carcinoma Oncotarget 5 2014 2635 2647
    • (2014) Oncotarget , vol.5 , pp. 2635-2647
    • Liu, J.1    Zhang, C.2    Lin, M.3    Zhu, W.4    Liang, Y.5    Hong, X.6
  • 95
    • 84922051564 scopus 로고    scopus 로고
    • Central and peripheral metabolic changes induced by γ-hydroxybutyrate
    • G. Luca, J. Vienne, A. Vaucher, S. Jimenez, and M. Tafti Central and peripheral metabolic changes induced by γ-hydroxybutyrate Sleep 38 2015 305 313
    • (2015) Sleep , vol.38 , pp. 305-313
    • Luca, G.1    Vienne, J.2    Vaucher, A.3    Jimenez, S.4    Tafti, M.5
  • 96
    • 40649126330 scopus 로고    scopus 로고
    • Detection of changed regional cerebral blood flow in mild cognitive impairment and early Alzheimer's dementia by perfusion-weighted magnetic resonance imaging
    • C. Luckhaus, M.O. Flub, H.J. Wittsack, B. Grass-Kapanke, M. Jänner, R. Khalili-Amiri, and et al. Detection of changed regional cerebral blood flow in mild cognitive impairment and early Alzheimer's dementia by perfusion-weighted magnetic resonance imaging Neuroimage 40 2008 495 503
    • (2008) Neuroimage , vol.40 , pp. 495-503
    • Luckhaus, C.1    Flub, M.O.2    Wittsack, H.J.3    Grass-Kapanke, B.4    Jänner, M.5    Khalili-Amiri, R.6
  • 97
    • 34548831366 scopus 로고    scopus 로고
    • Synthesis and catabolism of γ-hydroxybutyrate in SH-SY5Y human neuroblastoma cells: Role of the aldo-keto reductase AKR7A2
    • R.C. Lyon, S.M. Johnston, D.G. Watson, G. McGarvie, and E.M. Ellis Synthesis and catabolism of γ-hydroxybutyrate in SH-SY5Y human neuroblastoma cells: role of the aldo-keto reductase AKR7A2 J. Biol. Chem. 282 2007 25986 25992
    • (2007) J. Biol. Chem. , vol.282 , pp. 25986-25992
    • Lyon, R.C.1    Johnston, S.M.2    Watson, D.G.3    McGarvie, G.4    Ellis, E.M.5
  • 98
    • 0034015710 scopus 로고    scopus 로고
    • Glutamate dependence of GABA levels in neurons of hypoxic and hypoglycemic rat hippocampal slices
    • J.E. Madl, and S.M. Royer Glutamate dependence of GABA levels in neurons of hypoxic and hypoglycemic rat hippocampal slices Neuroscience 96 2000 657 664
    • (2000) Neuroscience , vol.96 , pp. 657-664
    • Madl, J.E.1    Royer, S.M.2
  • 99
    • 0030895783 scopus 로고    scopus 로고
    • The γ-hydroxybutyrate signalling system in brain: Organization and functional implications
    • M. Maitre The γ-hydroxybutyrate signalling system in brain: organization and functional implications Prog. Neurobiol. 51 1997 337 361
    • (1997) Prog. Neurobiol. , vol.51 , pp. 337-361
    • Maitre, M.1
  • 100
    • 65249092500 scopus 로고    scopus 로고
    • Comparative genomics of aldehyde dehydrogenase 5a1 (succinate semialdehyde dehydrogenase) and accumulation of γ-hydroxybutyrate associated with its deficiency
    • P. Malaspina, M.J. Picklo, C. Jakobs, O.C. Snead, and K.M. Gibson Comparative genomics of aldehyde dehydrogenase 5a1 (succinate semialdehyde dehydrogenase) and accumulation of γ-hydroxybutyrate associated with its deficiency Hum. Genomics 3 2009 106 120
    • (2009) Hum. Genomics , vol.3 , pp. 106-120
    • Malaspina, P.1    Picklo, M.J.2    Jakobs, C.3    Snead, O.C.4    Gibson, K.M.5
  • 101
    • 84865613285 scopus 로고    scopus 로고
    • Sporadic Alzheimer's disease: The starving brain
    • M. Mamelak Sporadic Alzheimer's disease: the starving brain J. Alzheimers Dis. 31 2012 459 474
    • (2012) J. Alzheimers Dis. , vol.31 , pp. 459-474
    • Mamelak, M.1
  • 102
    • 34447569486 scopus 로고    scopus 로고
    • Alzheimer's disease, oxidative stress and γ-hydroxybutyrate
    • M. Mamelak Alzheimer's disease, oxidative stress and γ-hydroxybutyrate Neurobiol. Aging 28 2007 1340 1360
    • (2007) Neurobiol. Aging , vol.28 , pp. 1340-1360
    • Mamelak, M.1
  • 104
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • W.R. Markesbery Oxidative stress hypothesis in Alzheimer's disease Free Radic. Biol. Med. 23 1997 134 147
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 105
    • 0023475544 scopus 로고
    • Regulatory properties of brain glutamate decarboxylase
    • D.L. Martin Regulatory properties of brain glutamate decarboxylase Cell. Mol. Neurobiol. 7 1987 237 253
    • (1987) Cell. Mol. Neurobiol. , vol.7 , pp. 237-253
    • Martin, D.L.1
  • 106
    • 12244289642 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase complex: Metabolic link to ischemic brain injury and target of oxidative stress
    • E. Martin, R.E. Rosenthal, and G. Fiskum Pyruvate dehydrogenase complex: metabolic link to ischemic brain injury and target of oxidative stress J. Neurosci. Res. 79 2005 240 247
    • (2005) J. Neurosci. Res. , vol.79 , pp. 240-247
    • Martin, E.1    Rosenthal, R.E.2    Fiskum, G.3
  • 107
    • 0027332651 scopus 로고
    • Brain α-ketoglutarate dehydrogenase complex activity in Alzheimer's disease
    • F. Mastrogiacomo, C. Bergeron, and S.J. Kish Brain α-ketoglutarate dehydrogenase complex activity in Alzheimer's disease J. Neurochem. 61 1993 2007 2014
    • (1993) J. Neurochem. , vol.61 , pp. 2007-2014
    • Mastrogiacomo, F.1    Bergeron, C.2    Kish, S.J.3
  • 108
    • 0034612075 scopus 로고    scopus 로고
    • A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients
    • I. Maurer, S. Zierz, and H.J. Möller A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients Neurobiol. Aging 21 2000 455 462
    • (2000) Neurobiol. Aging , vol.21 , pp. 455-462
    • Maurer, I.1    Zierz, S.2    Möller, H.J.3
  • 109
    • 84933059889 scopus 로고    scopus 로고
    • Imaging biomarkers associated with cognitive decline: A review
    • J. McConathy, and Y.I. Sheline Imaging biomarkers associated with cognitive decline: a review Biol. Psychiatry 77 2015 685 692
    • (2015) Biol. Psychiatry , vol.77 , pp. 685-692
    • McConathy, J.1    Sheline, Y.I.2
  • 110
    • 35848947733 scopus 로고    scopus 로고
    • The glutamate-glutamine cycle is not stoichiometric: Fates of glutamate in brain
    • M.C. McKenna The glutamate-glutamine cycle is not stoichiometric: fates of glutamate in brain J. Neurosci. Res. 85 2007 3347 3358
    • (2007) J. Neurosci. Res. , vol.85 , pp. 3347-3358
    • McKenna, M.C.1
  • 111
    • 0034889080 scopus 로고    scopus 로고
    • 4-Hydroxynonenal immunoreactivity is increased in human hippocampus after global ischemia
    • E. McKracken, D.I. Graham, M. Nilsen, J. Stewart, J.A. Nicoll, and K. Horsburgh 4-Hydroxynonenal immunoreactivity is increased in human hippocampus after global ischemia Brain Pathol. 11 2001 414 421
    • (2001) Brain Pathol. , vol.11 , pp. 414-421
    • McKracken, E.1    Graham, D.I.2    Nilsen, M.3    Stewart, J.4    Nicoll, J.A.5    Horsburgh, K.6
  • 112
    • 0034065936 scopus 로고    scopus 로고
    • Glutamate as a neurotransmitter in the brain: Review of physiology and pathology
    • B.S. Meldrum Glutamate as a neurotransmitter in the brain: review of physiology and pathology J. Nutr. 130 2000 1007S 1015S
    • (2000) J. Nutr. , vol.130 , pp. 1007S-1015S
    • Meldrum, B.S.1
  • 113
    • 79960894781 scopus 로고    scopus 로고
    • A mitochondrial GABA permease connects the GABA shunt and the TCA cycle, and is essential for normal carbon metabolism
    • S. Michaeli, A. Fait, K. Lagor, A. Nunes-Nesi, N. Grillich, A. Yellin, and et al. A mitochondrial GABA permease connects the GABA shunt and the TCA cycle, and is essential for normal carbon metabolism Plant J. 67 2011 485 498
    • (2011) Plant J. , vol.67 , pp. 485-498
    • Michaeli, S.1    Fait, A.2    Lagor, K.3    Nunes-Nesi, A.4    Grillich, N.5    Yellin, A.6
  • 114
    • 0037188309 scopus 로고    scopus 로고
    • Homocysteine, vitamin B6, and vascular disease in AD patients
    • J.W. Miller, R. Green, D.M. Mungas, B.R. Reed, and W.J. Jagust Homocysteine, vitamin B6, and vascular disease in AD patients Neurology 58 2002 1471 1475
    • (2002) Neurology , vol.58 , pp. 1471-1475
    • Miller, J.W.1    Green, R.2    Mungas, D.M.3    Reed, B.R.4    Jagust, W.J.5
  • 115
    • 70350787143 scopus 로고    scopus 로고
    • Aldo-keto reductase (AKR) superfamily: Genomics and annotation
    • R.D. Mindnich, and T.M. Penning Aldo-keto reductase (AKR) superfamily: genomics and annotation Hum. Genomics 3 2009 362 370
    • (2009) Hum. Genomics , vol.3 , pp. 362-370
    • Mindnich, R.D.1    Penning, T.M.2
  • 116
    • 84901014330 scopus 로고    scopus 로고
    • Polyamines and abiotic stress in plants: A complex relationship
    • R. Minocha, R. Majumdar, and S.C. Minocha Polyamines and abiotic stress in plants: a complex relationship Front. Plant Sci. 5 2014 175
    • (2014) Front. Plant Sci. , vol.5 , pp. 175
    • Minocha, R.1    Majumdar, R.2    Minocha, S.C.3
  • 118
    • 84942193326 scopus 로고    scopus 로고
    • Transcriptional regulation of GAD1 GABA synthesis gene in the prefrontal cortex of subjects with schizophrenia
    • A.C. Mitchell, Y. Jiang, C. Peter, and S. Akbarian Transcriptional regulation of GAD1 GABA synthesis gene in the prefrontal cortex of subjects with schizophrenia Schizophr. Res. 167 2015 28 34
    • (2015) Schizophr. Res. , vol.167 , pp. 28-34
    • Mitchell, A.C.1    Jiang, Y.2    Peter, C.3    Akbarian, S.4
  • 119
    • 0029051691 scopus 로고
    • Brain polyamine levels are altered in Alzheimer's disease
    • L.D. Morrison, and S.J. Kish Brain polyamine levels are altered in Alzheimer's disease Neurosci. Lett. 197 1995 5 8
    • (1995) Neurosci. Lett. , vol.197 , pp. 5-8
    • Morrison, L.D.1    Kish, S.J.2
  • 120
    • 0027254187 scopus 로고
    • Brain S-adenosylmethionine decarboxylase activity is increased in Alzheimer's disease
    • L.D. Morrison, C. Bergeron, and S.J. Kish Brain S-adenosylmethionine decarboxylase activity is increased in Alzheimer's disease Neurosci. Lett. 154 1993 141 144
    • (1993) Neurosci. Lett. , vol.154 , pp. 141-144
    • Morrison, L.D.1    Bergeron, C.2    Kish, S.J.3
  • 122
    • 0017112561 scopus 로고
    • γ-Hydroxybutyrate degradation in the brain in vivo: Negligible direct conversion to GABA
    • H. Möhler, A.J. Patel, and R. Balazs γ-Hydroxybutyrate degradation in the brain in vivo: negligible direct conversion to GABA J. Neurochem. 27 1976 253 258
    • (1976) J. Neurochem. , vol.27 , pp. 253-258
    • Möhler, H.1    Patel, A.J.2    Balazs, R.3
  • 123
    • 0018229454 scopus 로고
    • Alterations of putative neurotransmitters and enzymes during ischemia in gerbil cerebral cortex
    • B.B. Mrsulja, B.J. Mrsulja, V. Cvejic, B.M. Djuriciic, and L. Rogac Alterations of putative neurotransmitters and enzymes during ischemia in gerbil cerebral cortex J. Neural Transm. Suppl. 14 1978 23 30
    • (1978) J. Neural Transm. Suppl. , vol.14 , pp. 23-30
    • Mrsulja, B.B.1    Mrsulja, B.J.2    Cvejic, V.3    Djuriciic, B.M.4    Rogac, L.5
  • 124
    • 0037627824 scopus 로고    scopus 로고
    • Oxidation of 4-hydroxy-2-nonenal by succinic semialdehyde dehydrogenase (ALDH5A)
    • T.C. Murphy, V. Amarnath, K.M. Gibson, and M.J. Picklo Sr. Oxidation of 4-hydroxy-2-nonenal by succinic semialdehyde dehydrogenase (ALDH5A) J. Neurochem. 86 2003 298 305
    • (2003) J. Neurochem. , vol.86 , pp. 298-305
    • Murphy, T.C.1    Amarnath, V.2    Gibson, K.M.3    Picklo, M.J.4
  • 125
    • 33750301141 scopus 로고    scopus 로고
    • Expression of glutamic acid decarboxylase and identification of GABAergic cells in the ischemic rat dentate gyrus
    • G.J. Müller, A.M. Dogonowski, B. Finsen, and F.F. Johansen Expression of glutamic acid decarboxylase and identification of GABAergic cells in the ischemic rat dentate gyrus Exp. Brain Res. 175 2006 556 566
    • (2006) Exp. Brain Res. , vol.175 , pp. 556-566
    • Müller, G.J.1    Dogonowski, A.M.2    Finsen, B.3    Johansen, F.F.4
  • 126
    • 84922631542 scopus 로고    scopus 로고
    • The GAD65 knock out mouse - A model for GABAergic processes in fear- and stress-induced psychopathology
    • I. Müller, G. Caliskan, and O. Stork The GAD65 knock out mouse - a model for GABAergic processes in fear- and stress-induced psychopathology Genes Brain Behav. 14 2015 37 45
    • (2015) Genes Brain Behav. , vol.14 , pp. 37-45
    • Müller, I.1    Caliskan, G.2    Stork, O.3
  • 127
    • 84882252310 scopus 로고    scopus 로고
    • Hypoxia-inducible factor prolyl 4-hydroxylases: Common and specific roles
    • J. Myllyharju, and P. Koivunen Hypoxia-inducible factor prolyl 4-hydroxylases: common and specific roles Biol. Chem. 394 2013 435 448
    • (2013) Biol. Chem. , vol.394 , pp. 435-448
    • Myllyharju, J.1    Koivunen, P.2
  • 128
    • 0032973069 scopus 로고    scopus 로고
    • Mitochondrial enzyme expression in the hippocampus in relation to Alzheimer-type pathology
    • Z. Nagy, M.M. Esiri, M. LeGris, and P.M. Matthews Mitochondrial enzyme expression in the hippocampus in relation to Alzheimer-type pathology Acta Neuropathol. 97 1999 346 354
    • (1999) Acta Neuropathol. , vol.97 , pp. 346-354
    • Nagy, Z.1    Esiri, M.M.2    Legris, M.3    Matthews, P.M.4
  • 129
    • 77956592294 scopus 로고    scopus 로고
    • γ-Hydroxybutyrate and the GABAergic footprint: A metabolomic approach to unpicking the actions of GHB
    • F.A. Nasrallah, A.D. Maher, J.R. Hanrahan, V.J. Balcar, and C.D. Rae γ-Hydroxybutyrate and the GABAergic footprint: a metabolomic approach to unpicking the actions of GHB J. Neurochem. 115 2010 58 67
    • (2010) J. Neurochem. , vol.115 , pp. 58-67
    • Nasrallah, F.A.1    Maher, A.D.2    Hanrahan, J.R.3    Balcar, V.J.4    Rae, C.D.5
  • 130
    • 0037454660 scopus 로고    scopus 로고
    • Inhibition of succinic semialdehyde dehydrogenase activity by alkenal products of lipid peroxidation
    • E. Nguyen, and M.J. Picklo Sr Inhibition of succinic semialdehyde dehydrogenase activity by alkenal products of lipid peroxidation Biochim. Biophys. Acta 1637 2003 107 112
    • (2003) Biochim. Biophys. Acta , vol.1637 , pp. 107-112
    • Nguyen, E.1    Picklo, M.J.2
  • 131
    • 84855549573 scopus 로고    scopus 로고
    • Overview of glutamatergic neurotransmission in the nervous system
    • M.J. Niciu, B. Kelmendi, and G. Sanacora Overview of glutamatergic neurotransmission in the nervous system Pharmacol. Biochem. Behav. 100 2012 656 664
    • (2012) Pharmacol. Biochem. Behav. , vol.100 , pp. 656-664
    • Niciu, M.J.1    Kelmendi, B.2    Sanacora, G.3
  • 132
    • 79960887452 scopus 로고    scopus 로고
    • Age-dependent decrease in glutamine synthetase expression in the hippocampal astroglia of the triple transgenic Alzheimer's disease mouse model: Mechanism for deficient glutamatergic transmission?
    • M. Olabarria, H.N. Noristani, A. Verkhratsky, and J.J. Rodríguez Age-dependent decrease in glutamine synthetase expression in the hippocampal astroglia of the triple transgenic Alzheimer's disease mouse model: mechanism for deficient glutamatergic transmission? Mol. Neurodegener. 6 2011 55
    • (2011) Mol. Neurodegener. , vol.6 , pp. 55
    • Olabarria, M.1    Noristani, H.N.2    Verkhratsky, A.3    Rodríguez, J.J.4
  • 135
    • 1642578910 scopus 로고    scopus 로고
    • Effect of late treatment with γ-hydroxybutyrate on the histological and behavioral consequences of transient brain ischemia in the rat
    • A. Ottani, A.V. Vergoni, S. Saltini, C. Mioni, D. Giuliani, M. Bartiromo, and et al. Effect of late treatment with γ-hydroxybutyrate on the histological and behavioral consequences of transient brain ischemia in the rat Eur. J. Pharmacol. 485 2004 183 191
    • (2004) Eur. J. Pharmacol. , vol.485 , pp. 183-191
    • Ottani, A.1    Vergoni, A.V.2    Saltini, S.3    Mioni, C.4    Giuliani, D.5    Bartiromo, M.6
  • 136
    • 61849168093 scopus 로고    scopus 로고
    • Proteomics-determined differences in the concanavalin-A-fractionated proteome of hippocampus and inferior parietal lobule in subjects with Alzheimer's disease and mild cognitive impairment: Implications for progression of AD
    • J.B. Owen, F. Di Domenico, R. Sultana, M. Perluigi, C. Cini, W.M. Pierce, and et al. Proteomics-determined differences in the concanavalin-A-fractionated proteome of hippocampus and inferior parietal lobule in subjects with Alzheimer's disease and mild cognitive impairment: implications for progression of AD J. Proteome Res. 8 2009 471 482
    • (2009) J. Proteome Res. , vol.8 , pp. 471-482
    • Owen, J.B.1    Di Domenico, F.2    Sultana, R.3    Perluigi, M.4    Cini, C.5    Pierce, W.M.6
  • 138
    • 0031960218 scopus 로고    scopus 로고
    • Glutamate, glutamine, and GABA as substrates for the neuronal and glial compartments after focal cerebral ischemia in rats
    • J.M. Pascual, F. Carceller, J.M. Roda, and S. Cerdan Glutamate, glutamine, and GABA as substrates for the neuronal and glial compartments after focal cerebral ischemia in rats Stroke 29 1998 1048 1056
    • (1998) Stroke , vol.29 , pp. 1048-1056
    • Pascual, J.M.1    Carceller, F.2    Roda, J.M.3    Cerdan, S.4
  • 141
    • 0035914218 scopus 로고    scopus 로고
    • Elevation of AKR7A2 (succinic semialdehyde reductase) in neurodegenerative disease
    • M.J. Picklo Sr., S.J. Olson, J.D. Hayes, W.R. Markesbery, and T.J. Montine Elevation of AKR7A2 (succinic semialdehyde reductase) in neurodegenerative disease Brain Res. 916 2001 229 238
    • (2001) Brain Res. , vol.916 , pp. 229-238
    • Picklo, M.J.1    Olson, S.J.2    Hayes, J.D.3    Markesbery, W.R.4    Montine, T.J.5
  • 142
    • 84888015942 scopus 로고    scopus 로고
    • Sporadic Alzheimer's disease begins as episodes of brain ischemia and ischemically dysregulated Alzheimer's disease genes
    • R. Pluta, M. Jablonski, M. Ulamek-Koziol, J. Kocki, J. Brzozowska, S. Januszewski, and et al. Sporadic Alzheimer's disease begins as episodes of brain ischemia and ischemically dysregulated Alzheimer's disease genes Mol. Neurobiol. 48 2013 500 515
    • (2013) Mol. Neurobiol. , vol.48 , pp. 500-515
    • Pluta, R.1    Jablonski, M.2    Ulamek-Koziol, M.3    Kocki, J.4    Brzozowska, J.5    Januszewski, S.6
  • 143
    • 84876325985 scopus 로고    scopus 로고
    • Oxygen sensing and hypoxia signalling pathways in animals: The implications of physiology for cancer
    • P.J. Ratcliffe Oxygen sensing and hypoxia signalling pathways in animals: the implications of physiology for cancer J. Physiol. 591 2013 2027 2042
    • (2013) J. Physiol. , vol.591 , pp. 2027-2042
    • Ratcliffe, P.J.1
  • 144
    • 67849126232 scopus 로고    scopus 로고
    • Proteomic identification of nitrated brain proteins in early Alzheimer's disease inferior parietal lobule
    • T.T. Reed, W.M. Pierce Jr., D.M. Turner, W.R. Markesbery, and D.A. Butterfield Proteomic identification of nitrated brain proteins in early Alzheimer's disease inferior parietal lobule J. Cell. Mol. Med. 13 2009 2019 2029
    • (2009) J. Cell. Mol. Med. , vol.13 , pp. 2019-2029
    • Reed, T.T.1    Pierce, W.M.2    Turner, D.M.3    Markesbery, W.R.4    Butterfield, D.A.5
  • 145
    • 67349279818 scopus 로고    scopus 로고
    • Proteomic identification of HNE-bound proteins in early Alzheimer disease: Insights into the role of lipid peroxidation in the progression of AD
    • T.T. Reed, W.M. Pierce, W.R. Markesbery, and D.A. Butterfield Proteomic identification of HNE-bound proteins in early Alzheimer disease: insights into the role of lipid peroxidation in the progression of AD Brain Res. 1274 2009 66 76
    • (2009) Brain Res. , vol.1274 , pp. 66-76
    • Reed, T.T.1    Pierce, W.M.2    Markesbery, W.R.3    Butterfield, D.A.4
  • 146
    • 77954697566 scopus 로고    scopus 로고
    • Isocitrate dehydrogenase 1 and 2 mutations in cancer: Alterations at a crossroads of cellular metabolism
    • Z.J. Reitman, and H. Yan Isocitrate dehydrogenase 1 and 2 mutations in cancer: alterations at a crossroads of cellular metabolism J. Natl. Cancer Inst. 102 2010 932 941
    • (2010) J. Natl. Cancer Inst. , vol.102 , pp. 932-941
    • Reitman, Z.J.1    Yan, H.2
  • 147
    • 84871601359 scopus 로고    scopus 로고
    • Glutamate system, amyloid ß peptides and tau protein: Functional interrelationships and relevance to Alzheimer disease pathology
    • T.J. Revett, G.B. Baker, J. Jhamandas, and S. Kar Glutamate system, amyloid ß peptides and tau protein: functional interrelationships and relevance to Alzheimer disease pathology J. Psychiatry Neurosci. 38 2013 6 23
    • (2013) J. Psychiatry Neurosci. , vol.38 , pp. 6-23
    • Revett, T.J.1    Baker, G.B.2    Jhamandas, J.3    Kar, S.4
  • 148
    • 0033963901 scopus 로고    scopus 로고
    • Neuronal expression of glutamine synthetase in Alzheimer's disease indicates a profound impairment of metabolic interactions with astrocytes
    • S.R. Robinson Neuronal expression of glutamine synthetase in Alzheimer's disease indicates a profound impairment of metabolic interactions with astrocytes Neurochem. Int. 36 2000 471 482
    • (2000) Neurochem. Int. , vol.36 , pp. 471-482
    • Robinson, S.R.1
  • 149
    • 0018634441 scopus 로고
    • Effects of 2,4-dihydroxybutyrate on lipogenesis in rat hepatocytes
    • R. Rognstad, and J. Katz Effects of 2,4-dihydroxybutyrate on lipogenesis in rat hepatocytes J. Biol. Chem. 254 1979 11969 11972
    • (1979) J. Biol. Chem. , vol.254 , pp. 11969-11972
    • Rognstad, R.1    Katz, J.2
  • 150
    • 31844435663 scopus 로고    scopus 로고
    • Inhibitors of the α-ketoglutarate dehydrogenase complex alter [1-13C]glucose and [U-13C]glutamate metabolism in cerebellar granule neurons
    • S.S. Santos, G.E. Gibson, A.J. Cooper, T.T. Denton, C.M. Thompson, V.I. Bunik, and et al. Inhibitors of the α-ketoglutarate dehydrogenase complex alter [1-13C]glucose and [U-13C]glutamate metabolism in cerebellar granule neurons J. Neurosci. Res. 83 2006 450 458
    • (2006) J. Neurosci. Res. , vol.83 , pp. 450-458
    • Santos, S.S.1    Gibson, G.E.2    Cooper, A.J.3    Denton, T.T.4    Thompson, C.M.5    Bunik, V.I.6
  • 151
    • 0033231456 scopus 로고    scopus 로고
    • Cloning and expression of succinic semialdehyde reductase from human brain. Identity with aflatoxin B1 aldehyde reductase
    • M. Schaller, M. Schaffhauser, N. Sans, and B. Wermuth Cloning and expression of succinic semialdehyde reductase from human brain. Identity with aflatoxin B1 aldehyde reductase Eur. J. Biochem. 265 1999 1056 1060
    • (1999) Eur. J. Biochem. , vol.265 , pp. 1056-1060
    • Schaller, M.1    Schaffhauser, M.2    Sans, N.3    Wermuth, B.4
  • 152
    • 0017581544 scopus 로고
    • Inhibition and alternate-substrate studies on the mechanism of malic enzyme
    • M.I. Schimerlik, and W.W. Cleland Inhibition and alternate-substrate studies on the mechanism of malic enzyme Biochemistry 16 1977 565 570
    • (1977) Biochemistry , vol.16 , pp. 565-570
    • Schimerlik, M.I.1    Cleland, W.W.2
  • 153
    • 47049095632 scopus 로고    scopus 로고
    • Routes to 4-hydroxynonenal: Fundamental issues in the mechanisms of lipid peroxidation
    • C. Schneider, N.A. Porter, and A.R. Brash Routes to 4-hydroxynonenal: fundamental issues in the mechanisms of lipid peroxidation J. Biol. Chem. 283 2008 15539 15543
    • (2008) J. Biol. Chem. , vol.283 , pp. 15539-15543
    • Schneider, C.1    Porter, N.A.2    Brash, A.R.3
  • 154
    • 84884299230 scopus 로고    scopus 로고
    • Astrocytic control of biosynthesis and turnover of the neurotransmitters glutamate and GABA
    • A. Schousboe, L.K. Bak, and H.S. Waagepetersen Astrocytic control of biosynthesis and turnover of the neurotransmitters glutamate and GABA Front. Endocrinol. (Lausanne) 4 2013 102
    • (2013) Front. Endocrinol. (Lausanne) , vol.4 , pp. 102
    • Schousboe, A.1    Bak, L.K.2    Waagepetersen, H.S.3
  • 155
    • 0038403903 scopus 로고    scopus 로고
    • Differential roles of alanine in GABAergic and glutamatergic neurons
    • A. Schousboe, U. Sonnewald, and H.S. Waagepetersen Differential roles of alanine in GABAergic and glutamatergic neurons Neurochem. Int. 43 2003 311 315
    • (2003) Neurochem. Int. , vol.43 , pp. 311-315
    • Schousboe, A.1    Sonnewald, U.2    Waagepetersen, H.S.3
  • 156
    • 0016144610 scopus 로고
    • Subunit structure and kinetic properties of 4-aminobutyrate-2-ketoglutarate transaminase purified from mouse brain
    • A. Schousboe, J.Y. Wu, and E. Roberts Subunit structure and kinetic properties of 4-aminobutyrate-2-ketoglutarate transaminase purified from mouse brain J. Neurochem. 23 1974 1189 1195
    • (1974) J. Neurochem. , vol.23 , pp. 1189-1195
    • Schousboe, A.1    Wu, J.Y.2    Roberts, E.3
  • 157
    • 0017363065 scopus 로고
    • Intramitochondrial localization of the 4-aminobutyrate-2-oxoglutarate transaminase from ox brain
    • I. Schousboe, B. Bro, and A. Schousboe Intramitochondrial localization of the 4-aminobutyrate-2-oxoglutarate transaminase from ox brain Biochem. J. 162 1977 303 307
    • (1977) Biochem. J. , vol.162 , pp. 303-307
    • Schousboe, I.1    Bro, B.2    Schousboe, A.3
  • 158
    • 0035044262 scopus 로고    scopus 로고
    • γ-Aminobutyric acid (A) neurotransmission and cerebral ischemia
    • R.D. Schwartz-Bloom, and R. Sah γ-Aminobutyric acid (A) neurotransmission and cerebral ischemia J. Neurochem. 77 2001 353 371
    • (2001) J. Neurochem. , vol.77 , pp. 353-371
    • Schwartz-Bloom, R.D.1    Sah, R.2
  • 159
    • 0029965257 scopus 로고    scopus 로고
    • Polyamines in frontal cortex of patients with Down syndrome and Alzheimer disease
    • R. Seidl, S. Beninati, N. Cairns, N. Singewald, D. Risser, H. Bavan, and et al. Polyamines in frontal cortex of patients with Down syndrome and Alzheimer disease Neurosci. Lett. 206 1996 193 195
    • (1996) Neurosci. Lett. , vol.206 , pp. 193-195
    • Seidl, R.1    Beninati, S.2    Cairns, N.3    Singewald, N.4    Risser, D.5    Bavan, H.6
  • 160
    • 0035095970 scopus 로고    scopus 로고
    • Differences between GABA levels in Alzheimer's disease and Down syndrome with Alzheimer-like neuropathology
    • R. Seidl, N. Cairns, N. Singewald, S.T. Kaehler, and G. Lubec Differences between GABA levels in Alzheimer's disease and Down syndrome with Alzheimer-like neuropathology Naunyn Schmiedeb. Arch. Pharmacol. 363 2001 139 145
    • (2001) Naunyn Schmiedeb. Arch. Pharmacol. , vol.363 , pp. 139-145
    • Seidl, R.1    Cairns, N.2    Singewald, N.3    Kaehler, S.T.4    Lubec, G.5
  • 161
    • 84856739946 scopus 로고    scopus 로고
    • Hypoxia-inducible factors in physiology and medicine
    • G.L. Semenza Hypoxia-inducible factors in physiology and medicine Cell 148 2012 399 408
    • (2012) Cell , vol.148 , pp. 399-408
    • Semenza, G.L.1
  • 162
    • 69549135250 scopus 로고    scopus 로고
    • Neuroprotection of ebselen against ischemia/reperfusion injury involves GABA shunt enzymes
    • J.Y. Seo, C.H. Lee, J.H. Cho, J.H. Choi, K.Y. Yoo, D.W. Kim, and et al. Neuroprotection of ebselen against ischemia/reperfusion injury involves GABA shunt enzymes J. Neurol. Sci. 285 2009 88 94
    • (2009) J. Neurol. Sci. , vol.285 , pp. 88-94
    • Seo, J.Y.1    Lee, C.H.2    Cho, J.H.3    Choi, J.H.4    Yoo, K.Y.5    Kim, D.W.6
  • 163
    • 0032731314 scopus 로고    scopus 로고
    • Metabolism and functions of γ-aminobutyric acid
    • B.J. Shelp, A.W. Bown, and M.D. McLean Metabolism and functions of γ-aminobutyric acid Trends Plant Sci. 4 1999 446 452
    • (1999) Trends Plant Sci. , vol.4 , pp. 446-452
    • Shelp, B.J.1    Bown, A.W.2    McLean, M.D.3
  • 164
    • 0026562226 scopus 로고
    • Brain γ-aminobutyrate aminotransferase (GABA-T) and monoamine oxidase (MAO) in patients with Alzheimer's disease
    • F. Sherif, C.G. Gottfries, I. Alafuzoff, and L. Oreland Brain γ-aminobutyrate aminotransferase (GABA-T) and monoamine oxidase (MAO) in patients with Alzheimer's disease J. Neural Transm. Park. Dis. Dement. Sect. 4 1992 227 240
    • (1992) J. Neural Transm. Park. Dis. Dement. Sect. , vol.4 , pp. 227-240
    • Sherif, F.1    Gottfries, C.G.2    Alafuzoff, I.3    Oreland, L.4
  • 165
    • 0033387202 scopus 로고    scopus 로고
    • The α-ketoglutarate dehydrogenase complex
    • K.F. Sheu, and J.P. Blass The α-ketoglutarate dehydrogenase complex Ann. N. Y. Acad. Sci. 893 1999 61 78
    • (1999) Ann. N. Y. Acad. Sci. , vol.893 , pp. 61-78
    • Sheu, K.F.1    Blass, J.P.2
  • 166
    • 64349124515 scopus 로고    scopus 로고
    • Mild reduction in the activity of the α-ketoglutarate dehydrogenase complex elevates GABA shunt and glycolysis
    • Q. Shi, O. Risa, U. Sonnewald, and G.E. Gibson Mild reduction in the activity of the α-ketoglutarate dehydrogenase complex elevates GABA shunt and glycolysis J. Neurochem. 109 Suppl. 1 2009 214 221
    • (2009) J. Neurochem. , vol.109 , pp. 214-221
    • Shi, Q.1    Risa, O.2    Sonnewald, U.3    Gibson, G.E.4
  • 167
    • 40849133924 scopus 로고    scopus 로고
    • Novel functions of the α-ketoglutarate dehydrogenase complex may mediate diverse oxidant-induced changes in mitochondrial enzymes associated with Alzheimer's disease
    • Q. Shi, H. Xu, W.A. Kleinman, and G.E. Gibson Novel functions of the α-ketoglutarate dehydrogenase complex may mediate diverse oxidant-induced changes in mitochondrial enzymes associated with Alzheimer's disease Biochim. Biophys. Acta 1782 2008 229 238
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 229-238
    • Shi, Q.1    Xu, H.2    Kleinman, W.A.3    Gibson, G.E.4
  • 168
    • 0037173959 scopus 로고    scopus 로고
    • Rapid and sensitive detection of urinary 4-hydroxybutyric acid and its related compounds by gas chromatography-mass spectrometry in a patient with succinic semialdehyde dehydrogenase deficiency
    • T. Shinka, Y. Inoue, M. Ohse, A. Ito, M. Ohfu, S. Hirose, and et al. Rapid and sensitive detection of urinary 4-hydroxybutyric acid and its related compounds by gas chromatography-mass spectrometry in a patient with succinic semialdehyde dehydrogenase deficiency J. Chromatogr. B. Anal. Technol. Biomed. Life Sci. 776 2002 57 63
    • (2002) J. Chromatogr. B. Anal. Technol. Biomed. Life Sci. , vol.776 , pp. 57-63
    • Shinka, T.1    Inoue, Y.2    Ohse, M.3    Ito, A.4    Ohfu, M.5    Hirose, S.6
  • 169
    • 0026670061 scopus 로고
    • γ-Vinyl GABA prevents hippocampal and substantia nigra reticulata damage in repetitive transient forebrain ischemia
    • A. Shuaib, S. Ijaz, S. Hasan, and J. Kalra γ-Vinyl GABA prevents hippocampal and substantia nigra reticulata damage in repetitive transient forebrain ischemia Brain Res. 590 1992 13 17
    • (1992) Brain Res. , vol.590 , pp. 13-17
    • Shuaib, A.1    Ijaz, S.2    Hasan, S.3    Kalra, J.4
  • 170
    • 0030019916 scopus 로고    scopus 로고
    • The neuroprotective effects of γ-vinyl GABA in transient global ischemia: A morphological study with early and delayed evaluations
    • A. Shuaib, M.A. Murabit, R. Kanthan, W. Howlett, and T. Wishart The neuroprotective effects of γ-vinyl GABA in transient global ischemia: a morphological study with early and delayed evaluations Neurosci. Lett. 204 1996 1 4
    • (1996) Neurosci. Lett. , vol.204 , pp. 1-4
    • Shuaib, A.1    Murabit, M.A.2    Kanthan, R.3    Howlett, W.4    Wishart, T.5
  • 171
    • 0027420891 scopus 로고
    • Functional alterations in Alzheimer's disease: Diminution of cytochrome oxidase in the hippocampal formation
    • N.A. Simonian, and B.T. Hyman Functional alterations in Alzheimer's disease: diminution of cytochrome oxidase in the hippocampal formation J. Neuropathol. Exp. Neurol. 52 1993 580 585
    • (1993) J. Neuropathol. Exp. Neurol. , vol.52 , pp. 580-585
    • Simonian, N.A.1    Hyman, B.T.2
  • 172
  • 173
    • 84922395267 scopus 로고    scopus 로고
    • Glutamate synthesis has to be matched by its degradation - Where do all the carbons go?
    • U. Sonnewald Glutamate synthesis has to be matched by its degradation - where do all the carbons go? J. Neurochem. 131 2014 399 406
    • (2014) J. Neurochem. , vol.131 , pp. 399-406
    • Sonnewald, U.1
  • 174
    • 84864838550 scopus 로고    scopus 로고
    • Alanine and aspartate aminotransferase and glutamine-cycling pathway: Their roles in pathogenesis of metabolic syndrome
    • S. Sookoian, and C.J. Pirola Alanine and aspartate aminotransferase and glutamine-cycling pathway: their roles in pathogenesis of metabolic syndrome World J. Gastroenterol. 18 2012 3775 3781
    • (2012) World J. Gastroenterol. , vol.18 , pp. 3775-3781
    • Sookoian, S.1    Pirola, C.J.2
  • 175
    • 0020685951 scopus 로고
    • Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain
    • S. Sorbi, E.D. Bird, and J.P. Blass Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain Ann. Neurol. 13 1983 72 78
    • (1983) Ann. Neurol. , vol.13 , pp. 72-78
    • Sorbi, S.1    Bird, E.D.2    Blass, J.P.3
  • 176
    • 77956555564 scopus 로고    scopus 로고
    • Quantitative proteomics and metabolomics analysis of normal human cerebrospinal fluid samples
    • M.P. Stoop, L. Coulier, T. Rosenling, S. Shi, A.M. Smolinska, L. Buydens, and et al. Quantitative proteomics and metabolomics analysis of normal human cerebrospinal fluid samples Mol. Cell. Proteomics 9 2010 2063 2075
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2063-2075
    • Stoop, M.P.1    Coulier, L.2    Rosenling, T.3    Shi, S.4    Smolinska, A.M.5    Buydens, L.6
  • 177
    • 65349123514 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function
    • D.F. Stowe, and A.K. Camara Mitochondrial reactive oxygen species production in excitable cells: modulators of mitochondrial and cell function Antioxid. Redox Signal 11 2009 1373 1414
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 1373-1414
    • Stowe, D.F.1    Camara, A.K.2
  • 178
    • 32544441880 scopus 로고    scopus 로고
    • Metabolism of γ-hydroxybutyrate to d-2-hydroxyglutarate in mammals: Further evidence for d-2-hydroxyglutarate transhydrogenase
    • E.A. Struys, N.M. Verhoeven, E.E. Jansen, H.J. Ten Brink, M. Gupta, T.G. Burlingame, and et al. Metabolism of γ-hydroxybutyrate to d-2-hydroxyglutarate in mammals: further evidence for d-2-hydroxyglutarate transhydrogenase Metabolism 55 2006 353 358
    • (2006) Metabolism , vol.55 , pp. 353-358
    • Struys, E.A.1    Verhoeven, N.M.2    Jansen, E.E.3    Ten Brink, H.J.4    Gupta, M.5    Burlingame, T.G.6
  • 179
    • 84884877254 scopus 로고    scopus 로고
    • Lipid peroxidation triggers neurodegeneration: A redox proteomics view into the Alzheimer disease brain
    • R. Sultana, M. Perluigi, and D.A. Butterfield Lipid peroxidation triggers neurodegeneration: a redox proteomics view into the Alzheimer disease brain Free Radic. Biol. Med. 62 2013 157 169
    • (2013) Free Radic. Biol. Med. , vol.62 , pp. 157-169
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 180
    • 64549148367 scopus 로고    scopus 로고
    • β-Hydroxybutyrate alters GABA-transaminase activity in cultured astrocytes
    • Y. Suzuki, H. Takahashi, M. Fukuda, H. Hino, K. Kobayashi, J. Tanaka, and et al. β-Hydroxybutyrate alters GABA-transaminase activity in cultured astrocytes Brain Res. 1268 2009 17 23
    • (2009) Brain Res. , vol.1268 , pp. 17-23
    • Suzuki, Y.1    Takahashi, H.2    Fukuda, M.3    Hino, H.4    Kobayashi, K.5    Tanaka, J.6
  • 181
    • 84875195795 scopus 로고    scopus 로고
    • Alcohol dehydrogenase, iron containing, 1 promoter hypermethylation associated with colorectal cancer differentiation
    • C.H. Tae, K.J. Ryu, S.H. Kim, H.C. Kim, H.K. Chun, B.H. Min, and et al. Alcohol dehydrogenase, iron containing, 1 promoter hypermethylation associated with colorectal cancer differentiation BMC Cancer 13 2013 142
    • (2013) BMC Cancer , vol.13 , pp. 142
    • Tae, C.H.1    Ryu, K.J.2    Kim, S.H.3    Kim, H.C.4    Chun, H.K.5    Min, B.H.6
  • 182
    • 0016618178 scopus 로고
    • Gas-chromatographic/mass-spectrometric identification and quantitation of tetronic and deoxytetronic acids in urine from normal adults and neonates
    • J.A. Thompson, S.P. Markey, and P.V. Fennessey Gas-chromatographic/mass-spectrometric identification and quantitation of tetronic and deoxytetronic acids in urine from normal adults and neonates Clin. Chem. 21 1975 1892 1898
    • (1975) Clin. Chem. , vol.21 , pp. 1892-1898
    • Thompson, J.A.1    Markey, S.P.2    Fennessey, P.V.3
  • 184
    • 0034671429 scopus 로고    scopus 로고
    • Inhibition of Krebs cycle enzymes by hydrogen peroxide: A key role of α-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress
    • L. Tretter, and V. Adam-Vizi Inhibition of Krebs cycle enzymes by hydrogen peroxide: a key role of α-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress J. Neurosci. 20 2000 8972 8979
    • (2000) J. Neurosci. , vol.20 , pp. 8972-8979
    • Tretter, L.1    Adam-Vizi, V.2
  • 185
    • 0033392347 scopus 로고    scopus 로고
    • Inhibition of α-ketoglutarate dehydrogenase due to H2O2-induced oxidative stress in nerve terminals
    • L. Tretter, and V. Adam-Vizi Inhibition of α-ketoglutarate dehydrogenase due to H2O2-induced oxidative stress in nerve terminals Ann. N. Y. Acad. Sci. 893 1999 412 416
    • (1999) Ann. N. Y. Acad. Sci. , vol.893 , pp. 412-416
    • Tretter, L.1    Adam-Vizi, V.2
  • 186
    • 84871268346 scopus 로고    scopus 로고
    • Consequences of the α-ketoglutarate dehydrogenase inhibition for neuronal metabolism and survival: Implications for neurodegenerative diseases
    • L.K. Trofimova, W.L. Araujo, A.A. Strokina, A.R. Fernie, L. Bettendorff, and V.I. Bunik Consequences of the α-ketoglutarate dehydrogenase inhibition for neuronal metabolism and survival: implications for neurodegenerative diseases Curr. Med. Chem. 19 2012 5895 5906
    • (2012) Curr. Med. Chem. , vol.19 , pp. 5895-5906
    • Trofimova, L.K.1    Araujo, W.L.2    Strokina, A.A.3    Fernie, A.R.4    Bettendorff, L.5    Bunik, V.I.6
  • 187
    • 84877888815 scopus 로고    scopus 로고
    • Identification of altered metabolic pathways in plasma and CSF in mild cognitive impairment and Alzheimer's disease using metabolomics
    • E. Trushina, T. Dutta, X.M. Persson, M.M. Mielke, and R.C. Petersen Identification of altered metabolic pathways in plasma and CSF in mild cognitive impairment and Alzheimer's disease using metabolomics PLoS One 8 2013 e63644
    • (2013) PLoS One , vol.8
    • Trushina, E.1    Dutta, T.2    Persson, X.M.3    Mielke, M.M.4    Petersen, R.C.5
  • 188
    • 84863245760 scopus 로고    scopus 로고
    • Defects in mitochondrial dynamics and metabolomic signatures of evolving energetic stress in mouse models of familial Alzheimer's disease
    • E. Trushina, E. Nemutlu, S. Zhang, T. Christensen, J. Camp, J. Mesa, and et al. Defects in mitochondrial dynamics and metabolomic signatures of evolving energetic stress in mouse models of familial Alzheimer's disease PLoS One 7 2012 e32737
    • (2012) PLoS One , vol.7
    • Trushina, E.1    Nemutlu, E.2    Zhang, S.3    Christensen, T.4    Camp, J.5    Mesa, J.6
  • 189
    • 84857388905 scopus 로고    scopus 로고
    • Possible long-term effects of γ-hydroxybutyric acid (GHB) due to neurotoxicity and overdose
    • J.G. van Amsterdam, T.M. Brunt, M.T. McMaster, and R.J. Niesink Possible long-term effects of γ-hydroxybutyric acid (GHB) due to neurotoxicity and overdose Neurosci. Biobehav. Rev. 36 2012 1217 1227
    • (2012) Neurosci. Biobehav. Rev. , vol.36 , pp. 1217-1227
    • Van Amsterdam, J.G.1    Brunt, T.M.2    McMaster, M.T.3    Niesink, R.J.4
  • 190
  • 191
    • 0023836072 scopus 로고
    • γ-Hydroxybutyrate distribution and turnover rates in discrete brain regions of the rat
    • P. Vayer, J.D. Ehrhardt, S. Gobaille, P. Mandel, and M. Maitre γ-Hydroxybutyrate distribution and turnover rates in discrete brain regions of the rat Neurochem. Int. 12 1988 53 59
    • (1988) Neurochem. Int. , vol.12 , pp. 53-59
    • Vayer, P.1    Ehrhardt, J.D.2    Gobaille, S.3    Mandel, P.4    Maitre, M.5
  • 193
    • 0031791971 scopus 로고    scopus 로고
    • Distribution of Aβ-associated proteins in cerebrovascular amyloid of Alzheimer's disease
    • M.M. Verbeek, I. Otte-Höller, R. Veerhuis, D.J. Ruiter, and R.M. De Waal Distribution of Aβ-associated proteins in cerebrovascular amyloid of Alzheimer's disease Acta Neuropathol. 96 1998 628 636
    • (1998) Acta Neuropathol. , vol.96 , pp. 628-636
    • Verbeek, M.M.1    Otte-Höller, I.2    Veerhuis, R.3    Ruiter, D.J.4    De Waal, R.M.5
  • 194
    • 0034717230 scopus 로고    scopus 로고
    • Neuroprotective effect of γ-hydroxybutyrate in transient global cerebral ischemia in the rat
    • A.V. Vergoni, A. Ottani, A.R. Botticelli, D. Zaffe, L. Guano, A. Loche, and et al. Neuroprotective effect of γ-hydroxybutyrate in transient global cerebral ischemia in the rat Eur. J. Pharmacol. 397 2000 75 84
    • (2000) Eur. J. Pharmacol. , vol.397 , pp. 75-84
    • Vergoni, A.V.1    Ottani, A.2    Botticelli, A.R.3    Zaffe, D.4    Guano, L.5    Loche, A.6
  • 195
    • 0032842197 scopus 로고    scopus 로고
    • The GABA paradox: Multiple roles as metabolite, neurotransmitter, and neurodifferentiative agent
    • H.S. Waagepetersen, U. Sonnewald, and A. Schousboe The GABA paradox: multiple roles as metabolite, neurotransmitter, and neurodifferentiative agent J. Neurochem. 73 1999 1335 1342
    • (1999) J. Neurochem. , vol.73 , pp. 1335-1342
    • Waagepetersen, H.S.1    Sonnewald, U.2    Schousboe, A.3
  • 197
    • 0017192497 scopus 로고
    • Studies on the control of 4-aminobutyrate metabolism in 'synaptosomal' and free rat brain mitochondria
    • J.M. Walsh, and J.B. Clark Studies on the control of 4-aminobutyrate metabolism in 'synaptosomal' and free rat brain mitochondria Biochem. J. 160 1976 147 157
    • (1976) Biochem. J. , vol.160 , pp. 147-157
    • Walsh, J.M.1    Clark, J.B.2
  • 198
    • 84888197384 scopus 로고    scopus 로고
    • Epigenetic mechanisms in Alzheimer's disease: Implications for pathogenesis and therapy
    • J. Wang, J.T. Yu, M.S. Tan, T. Jiang, and L. Tan Epigenetic mechanisms in Alzheimer's disease: implications for pathogenesis and therapy Ageing Res. Rev. 12 2013 1024 1041
    • (2013) Ageing Res. Rev. , vol.12 , pp. 1024-1041
    • Wang, J.1    Yu, J.T.2    Tan, M.S.3    Jiang, T.4    Tan, L.5
  • 199
    • 46249093626 scopus 로고    scopus 로고
    • Post-translational regulation of L-glutamic acid decarboxylase in the brain
    • J. Wei, and J.Y. Wu Post-translational regulation of L-glutamic acid decarboxylase in the brain Neurochem. Res. 33 2008 1459 1465
    • (2008) Neurochem. Res. , vol.33 , pp. 1459-1465
    • Wei, J.1    Wu, J.Y.2
  • 200
    • 0021274062 scopus 로고
    • Immunocytochemical evidence for the presence of enzymes synthesizing GABA and GHB in the same neuron
    • D. Weissmann-Nanopoulos, M.F. Belin, P. Mandel, and M. Maitre Immunocytochemical evidence for the presence of enzymes synthesizing GABA and GHB in the same neuron Neurochem. Int. 6 1984 333 338
    • (1984) Neurochem. Int. , vol.6 , pp. 333-338
    • Weissmann-Nanopoulos, D.1    Belin, M.F.2    Mandel, P.3    Maitre, M.4
  • 201
    • 84908212297 scopus 로고    scopus 로고
    • Cerebral blood flow measured by arterial spin labeling MRI as a preclinical marker of Alzheimer's disease
    • C.E. Wierenga, C.C. Hays, and Z.Z. Zlatar Cerebral blood flow measured by arterial spin labeling MRI as a preclinical marker of Alzheimer's disease J. Alzheimers Dis. 42 Suppl. 4 2014 S411 S419
    • (2014) J. Alzheimers Dis. , vol.42 , pp. S411-S419
    • Wierenga, C.E.1    Hays, C.C.2    Zlatar, Z.Z.3
  • 202
    • 0346024000 scopus 로고    scopus 로고
    • From the street to the brain: Neurobiology of the recreational drug γ-hydroxybutyric acid
    • C.G. Wong, K.M. Gibson, and O.C. Snead 3rd From the street to the brain: neurobiology of the recreational drug γ-hydroxybutyric acid Trends Pharmacol. Sci. 25 2004 29 34
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 29-34
    • Wong, C.G.1    Gibson, K.M.2    Snead, O.C.3
  • 203
    • 0014313599 scopus 로고
    • The effect of hypoxia on brain γ-aminobutyric acid levels
    • J.D. Wood, W.J. Watson, and A.J. Ducker The effect of hypoxia on brain γ-aminobutyric acid levels J. Neurochem. 15 1968 603 608
    • (1968) J. Neurochem. , vol.15 , pp. 603-608
    • Wood, J.D.1    Watson, W.J.2    Ducker, A.J.3
  • 204
    • 84886925692 scopus 로고    scopus 로고
    • Mitochondrial alterations near amyloid plaques in an Alzheimer's disease mouse model
    • H. Xie, J. Guan, L.A. Borrelli, J. Xu, A. Serrano-Pozo, and B.J. Bacskai Mitochondrial alterations near amyloid plaques in an Alzheimer's disease mouse model J. Neurosci. 33 2013 17042 17051
    • (2013) J. Neurosci. , vol.33 , pp. 17042-17051
    • Xie, H.1    Guan, J.2    Borrelli, L.A.3    Xu, J.4    Serrano-Pozo, A.5    Bacskai, B.J.6
  • 205
    • 78651463452 scopus 로고    scopus 로고
    • Oncometabolite 2-hydroxyglutarate is a competitive inhibitor of α-ketoglutarate-dependent dioxygenases
    • W. Xu, H. Yang, Y. Liu, Y. Yang, P. Wang, S.H. Kim, and et al. Oncometabolite 2-hydroxyglutarate is a competitive inhibitor of α-ketoglutarate-dependent dioxygenases Cancer Cell 19 2011 17 30
    • (2011) Cancer Cell , vol.19 , pp. 17-30
    • Xu, W.1    Yang, H.2    Liu, Y.3    Yang, Y.4    Wang, P.5    Kim, S.H.6
  • 206
    • 61849173495 scopus 로고    scopus 로고
    • Elevated endogenous GABA concentration attenuates glutamate-glutamine cycling between neurons and astroglia
    • J. Yang, and J. Shen Elevated endogenous GABA concentration attenuates glutamate-glutamine cycling between neurons and astroglia J. Neural Transm. 116 2009 291 300
    • (2009) J. Neural Transm. , vol.116 , pp. 291-300
    • Yang, J.1    Shen, J.2
  • 207
    • 70149093436 scopus 로고    scopus 로고
    • Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease
    • J. Yao, R.W. Irwin, L. Zhao, J. Nilsen, R.T. Hamilton, and R.D. Brinton Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease Proc. Natl. Acad. Sci. U. S. A. 106 2009 14670 14675
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 14670-14675
    • Yao, J.1    Irwin, R.W.2    Zhao, L.3    Nilsen, J.4    Hamilton, R.T.5    Brinton, R.D.6
  • 208
    • 81855164838 scopus 로고    scopus 로고
    • Shift in brain metabolism in late onset Alzheimer's disease: Implications for biomarkers and therapeutic interventions
    • J. Yao, J.R. Rettberg, L.P. Klosinski, E. Cadenas, and R.D. Brinton Shift in brain metabolism in late onset Alzheimer's disease: implications for biomarkers and therapeutic interventions Mol. Asp. Med. 32 2011 247 257
    • (2011) Mol. Asp. Med. , vol.32 , pp. 247-257
    • Yao, J.1    Rettberg, J.R.2    Klosinski, L.P.3    Cadenas, E.4    Brinton, R.D.5
  • 210
    • 15444370317 scopus 로고    scopus 로고
    • The GABA shunt: An attractive and potential therapeutic target in the treatment of epileptic disorders
    • P. Yogeeswari, D. Sriram, and J. Vaigundaragavendran The GABA shunt: an attractive and potential therapeutic target in the treatment of epileptic disorders Curr. Drug Metab. 6 2005 127 139
    • (2005) Curr. Drug Metab. , vol.6 , pp. 127-139
    • Yogeeswari, P.1    Sriram, D.2    Vaigundaragavendran, J.3
  • 212
    • 84922119726 scopus 로고    scopus 로고
    • Glial GABA, synthesized by monoamine oxidase B, mediates tonic inhibition
    • B.E. Yoon, J. Woo, Y.E. Chun, H. Chun, S. Jo, J.Y. Bae, and et al. Glial GABA, synthesized by monoamine oxidase B, mediates tonic inhibition J. Physiol. 592 2014 4951 4968
    • (2014) J. Physiol. , vol.592 , pp. 4951-4968
    • Yoon, B.E.1    Woo, J.2    Chun, Y.E.3    Chun, H.4    Jo, S.5    Bae, J.Y.6
  • 213
    • 70450285127 scopus 로고    scopus 로고
    • Catabolism of 4-hydroxyacids and 4-hydroxynonenal via 4-hydroxy-4-phosphoacyl-CoAs
    • G.F. Zhang, R.S. Kombu, T. Kasumov, Y. Han, S. Sadhukhan, J. Zhang, and et al. Catabolism of 4-hydroxyacids and 4-hydroxynonenal via 4-hydroxy-4-phosphoacyl-CoAs J. Biol. Chem. 284 2009 33521 33534
    • (2009) J. Biol. Chem. , vol.284 , pp. 33521-33534
    • Zhang, G.F.1    Kombu, R.S.2    Kasumov, T.3    Han, Y.4    Sadhukhan, S.5    Zhang, J.6
  • 215
    • 77952549255 scopus 로고    scopus 로고
    • Pathological role of hypoxia in Alzheimer's disease
    • X. Zhang, and W. Le Pathological role of hypoxia in Alzheimer's disease Exp. Neurol. 223 2010 299 303
    • (2010) Exp. Neurol. , vol.223 , pp. 299-303
    • Zhang, X.1    Le, W.2
  • 216
    • 38149090292 scopus 로고    scopus 로고
    • The blood-brain barrier in health and chronic neurodegenerative disorders
    • B.V. Zlokovic The blood-brain barrier in health and chronic neurodegenerative disorders Neuron 57 2008 178 201
    • (2008) Neuron , vol.57 , pp. 178-201
    • Zlokovic, B.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.