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Volumn 91, Issue 8, 2013, Pages 1007-1017

Deregulation of glutamate dehydrogenase in human neurologic disorders

Author keywords

Dystonia; GLUD1 and GLUD2 deregulation; Parkinson's disease

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALPHA SYNUCLEIN; ESTROGEN; GLUTAMATE DEHYDROGENASE; GLUTAMATE SYNTHASE (NADH); GUANOSINE TRIPHOSPHATE; HALOPERIDOL; NEUROLEPTIC AGENT; SPERMIDINE;

EID: 84879604039     PISSN: 03604012     EISSN: 10974547     Source Type: Journal    
DOI: 10.1002/jnr.23176     Document Type: Review
Times cited : (26)

References (75)
  • 2
    • 0023572285 scopus 로고
    • Glial glutamate dehydrogenase: ultrastructural localization and regional distribution in relation to the mitochondrial enzyme, cytochrome oxidase
    • Aoki C, Milner T, Berger S, Sheu K, Blass J, Pickel V. 1987. Glial glutamate dehydrogenase: ultrastructural localization and regional distribution in relation to the mitochondrial enzyme, cytochrome oxidase. JNeurosci Res 18:305-318.
    • (1987) JNeurosci Res , vol.18 , pp. 305-318
    • Aoki, C.1    Milner, T.2    Berger, S.3    Sheu, K.4    Blass, J.5    Pickel, V.6
  • 3
    • 1842558602 scopus 로고    scopus 로고
    • Molecular mechanisms of glutamate-dependent neurodegeneration in ischemia and traumatic brain injury
    • Arundine M, Tymianski M. 2004. Molecular mechanisms of glutamate-dependent neurodegeneration in ischemia and traumatic brain injury. Cell Mol Life Sci 61:657-668.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 657-668
    • Arundine, M.1    Tymianski, M.2
  • 6
    • 0344837307 scopus 로고    scopus 로고
    • Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation
    • Banerjee S, Schmidt T, Fang J, Stanley CA, Smith TJ. 2003. Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation. Biochemistry 42:3446-3456.
    • (2003) Biochemistry , vol.42 , pp. 3446-3456
    • Banerjee, S.1    Schmidt, T.2    Fang, J.3    Stanley, C.A.4    Smith, T.J.5
  • 7
    • 0031466522 scopus 로고    scopus 로고
    • Measurement of glutamate and glutamine in the medial prefrontal cortex of never-treated schizophrenic patients and healthy controls by proton magnetic resonance spectroscopy
    • Bartha R, Williamson PC, Drost DJ, Malla A, Carr TJ, Cortese L, Canaran G, Rylett RJ, Neufeld RW. 1997. Measurement of glutamate and glutamine in the medial prefrontal cortex of never-treated schizophrenic patients and healthy controls by proton magnetic resonance spectroscopy. Arch Gen Psychiatry 54:959-965.
    • (1997) Arch Gen Psychiatry , vol.54 , pp. 959-965
    • Bartha, R.1    Williamson, P.C.2    Drost, D.J.3    Malla, A.4    Carr, T.J.5    Cortese, L.6    Canaran, G.7    Rylett, R.J.8    Neufeld, R.W.9
  • 8
    • 0028224736 scopus 로고
    • Regulation of enzymatic activity by active site fatty acylation. A new role for long chain fatty acid acylation of proteins
    • Berthiaume L, Deichaite I, Peseckis S, Resh MD. 1994. Regulation of enzymatic activity by active site fatty acylation. A new role for long chain fatty acid acylation of proteins. J Biol Chem 4269:6498-6505.
    • (1994) J Biol Chem , vol.4269 , pp. 6498-6505
    • Berthiaume, L.1    Deichaite, I.2    Peseckis, S.3    Resh, M.D.4
  • 12
    • 6944242766 scopus 로고    scopus 로고
    • Birth and adaptive evolution of a hominoid gene that supports high neurotransmitter flux
    • Burki F, Kaessmann H. 2004. Birth and adaptive evolution of a hominoid gene that supports high neurotransmitter flux. Nat Genet 36:1061-1063.
    • (2004) Nat Genet , vol.36 , pp. 1061-1063
    • Burki, F.1    Kaessmann, H.2
  • 13
    • 33646152528 scopus 로고    scopus 로고
    • A dopaminergic deficit hypothesis of schizophrenia: the path to discovery
    • Carlsson A, Carlsson ML. 2006. A dopaminergic deficit hypothesis of schizophrenia: the path to discovery. Dialogues Clin Neurosci 8:137-142.
    • (2006) Dialogues Clin Neurosci , vol.8 , pp. 137-142
    • Carlsson, A.1    Carlsson, M.L.2
  • 15
    • 0018149605 scopus 로고
    • Methodological aspects of the histochemical localization and activity of some cerebellar dehydrogenases
    • Contestabile A, Andersen H. 1978. Methodological aspects of the histochemical localization and activity of some cerebellar dehydrogenases. Histochemistry 56:117-132.
    • (1978) Histochemistry , vol.56 , pp. 117-132
    • Contestabile, A.1    Andersen, H.2
  • 16
    • 0025058979 scopus 로고
    • The inhibition of glutamate dehydrogenase by some antipsychotic drugs
    • Couée I, Tipton KF. 1990. The inhibition of glutamate dehydrogenase by some antipsychotic drugs. Biochem Pharmacol 39:827-832.
    • (1990) Biochem Pharmacol , vol.39 , pp. 827-832
    • Couée, I.1    Tipton, K.F.2
  • 17
    • 0025326250 scopus 로고
    • Activation of glutamate dehydrogenase by leucine and its nonmetabolizable analogue in rat brain synaptosomes
    • Erecinska M, Nelson D. 1990. Activation of glutamate dehydrogenase by leucine and its nonmetabolizable analogue in rat brain synaptosomes. J Neurochem 54:1335-1343.
    • (1990) J Neurochem , vol.54 , pp. 1335-1343
    • Erecinska, M.1    Nelson, D.2
  • 18
    • 0019809137 scopus 로고
    • Regulation of glutamate dehydrogenase by palmitoyl-coenzyme A
    • Fahien LA, Kiomtek E. 1981. Regulation of glutamate dehydrogenase by palmitoyl-coenzyme A. Arch Biochem Biophys 212:247-253.
    • (1981) Arch Biochem Biophys , vol.212 , pp. 247-253
    • Fahien, L.A.1    Kiomtek, E.2
  • 19
    • 80053426332 scopus 로고    scopus 로고
    • The complex mechanism of glutamate dehydrogenase in insulin secretion
    • Fahien LA, Macdonald MJ. 2011. The complex mechanism of glutamate dehydrogenase in insulin secretion. Diabetes 60:2450-2454.
    • (2011) Diabetes , vol.60 , pp. 2450-2454
    • Fahien, L.A.1    Macdonald, M.J.2
  • 20
    • 0014751081 scopus 로고
    • Effects of chlorpromazine on glutamate dehydrogenase
    • Fahien LA, Shemisa O. 1970. Effects of chlorpromazine on glutamate dehydrogenase. Mol Pharmacol 6:156-163.
    • (1970) Mol Pharmacol , vol.6 , pp. 156-163
    • Fahien, L.A.1    Shemisa, O.2
  • 21
    • 0036534464 scopus 로고    scopus 로고
    • Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations
    • Fang J, Hsu BY, MacMullen CM, Poncz M, Smith TJ, Stanley CA. 2002Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. Biochem J 363:81-87.
    • (2002) Biochem J , vol.363 , pp. 81-87
    • Fang, J.1    Hsu, B.Y.2    MacMullen, C.M.3    Poncz, M.4    Smith, T.J.5    Stanley, C.A.6
  • 22
    • 0036307527 scopus 로고    scopus 로고
    • Implications for altered glutamate and GABA metabolism in the dorsolateral prefrontal cortex of aged schizophrenic patients
    • Gluck MR, Thomas RG, Davis KL, Haroutunian V. 2002. Implications for altered glutamate and GABA metabolism in the dorsolateral prefrontal cortex of aged schizophrenic patients. Am J Psychiatry 159:1165-1173.
    • (2002) Am J Psychiatry , vol.159 , pp. 1165-1173
    • Gluck, M.R.1    Thomas, R.G.2    Davis, K.L.3    Haroutunian, V.4
  • 24
    • 0029051676 scopus 로고
    • The phencyclidine-glutamate model of schizophrenia
    • Halberstadt AL. 1995. The phencyclidine-glutamate model of schizophrenia. Clin Neuropharmacol 18:237-249.
    • (1995) Clin Neuropharmacol , vol.18 , pp. 237-249
    • Halberstadt, A.L.1
  • 25
    • 26844558198 scopus 로고    scopus 로고
    • Elevated glutamine/glutamate ratio in cerebrospinal fluid of first episode and drug naive schizophrenic patients
    • Hashimoto K, Engberg G, Shimizu E, Nordin C, Lindström LH, Iyo M. 2005. Elevated glutamine/glutamate ratio in cerebrospinal fluid of first episode and drug naive schizophrenic patients. BMC Psychiatry 5:6.
    • (2005) BMC Psychiatry , vol.5 , pp. 6
    • Hashimoto, K.1    Engberg, G.2    Shimizu, E.3    Nordin, C.4    Lindström, L.H.5    Iyo, M.6
  • 26
    • 0028325907 scopus 로고
    • Effect of polyamines on glutamate dehydrogenase within permeabilized kidney-cortex mitochondria and isolated renal tubules of rabbit
    • Jarzyna R, Lietz T, Brya J. 1994. Effect of polyamines on glutamate dehydrogenase within permeabilized kidney-cortex mitochondria and isolated renal tubules of rabbit. Biochem Pharmacol 47:1387-1393.
    • (1994) Biochem Pharmacol , vol.47 , pp. 1387-1393
    • Jarzyna, R.1    Lietz, T.2    Brya, J.3
  • 27
    • 64349103857 scopus 로고    scopus 로고
    • Mutations in human GLUD2 glutamate dehydrogenase affecting basal activity and regulation
    • Kanavouras K, Borompokas N, Latsoudis H, Stagourakis A, Zaganas I, Plaitakis A. 2009. Mutations in human GLUD2 glutamate dehydrogenase affecting basal activity and regulation. J Neurochem 109( Suppl 1):167-173.
    • (2009) J Neurochem , vol.109 , Issue.SUPPL 1 , pp. 167-173
    • Kanavouras, K.1    Borompokas, N.2    Latsoudis, H.3    Stagourakis, A.4    Zaganas, I.5    Plaitakis, A.6
  • 28
    • 0027905017 scopus 로고
    • Modulation of neuronal migration by NMDA receptors
    • Komuro H, Rakic P. 1993. Modulation of neuronal migration by NMDA receptors. Science 260:95-97.
    • (1993) Science , vol.260 , pp. 95-97
    • Komuro, H.1    Rakic, P.2
  • 30
    • 0027934856 scopus 로고
    • 2+ and polyamines: a possible cause for its low in vivo activity
    • 2+ and polyamines: a possible cause for its low in vivo activity. J Neurochem 63:751-757.
    • (1994) J Neurochem , vol.63 , pp. 751-757
    • Kuo, N.1    Michalik, M.2    Ereciňska, M.3
  • 31
    • 0036135109 scopus 로고    scopus 로고
    • Impaired brain GABA in focal dystonia
    • Levy LM, Hallett M. 2002. Impaired brain GABA in focal dystonia. Ann Neurol 51:93-101.
    • (2002) Ann Neurol , vol.51 , pp. 93-101
    • Levy, L.M.1    Hallett, M.2
  • 33
    • 80052271742 scopus 로고    scopus 로고
    • The structure and allosteric regulation of glutamate dehydrogenase
    • Li M, Li C, Allen A, Stanley CA, Smith TJ. 2011. The structure and allosteric regulation of glutamate dehydrogenase. Neurochem Int 59:445-455.
    • (2011) Neurochem Int , vol.59 , pp. 445-455
    • Li, M.1    Li, C.2    Allen, A.3    Stanley, C.A.4    Smith, T.J.5
  • 34
    • 0020063951 scopus 로고
    • Lack of effect on glutamate dehydrogenase activity after in vivo administration of pharmacological doses of haloperidol
    • Luengo de Borges E, Ryder E, Campos G. 1982. Lack of effect on glutamate dehydrogenase activity after in vivo administration of pharmacological doses of haloperidol. Biochem Pharmacol 31:1446-1448.
    • (1982) Biochem Pharmacol , vol.31 , pp. 1446-1448
    • Luengo de Borges, E.1    Ryder, E.2    Campos, G.3
  • 35
    • 0027390458 scopus 로고
    • Quantitative synaptic alterations in the human neocortex during normal aging
    • Masliah E, Mallory M, Hansen L, DeTeresa R, Terry RD. 1993. Quantitative synaptic alterations in the human neocortex during normal aging. Neurology 43:192-197.
    • (1993) Neurology , vol.43 , pp. 192-197
    • Masliah, E.1    Mallory, M.2    Hansen, L.3    DeTeresa, R.4    Terry, R.D.5
  • 36
    • 0027302996 scopus 로고
    • Glutamate: its role in learning, memory, and the aging brain
    • McEntee WJ, Crook TH. 1993. Glutamate: its role in learning, memory, and the aging brain. Psychopharmacology 111:391-401.
    • (1993) Psychopharmacology , vol.111 , pp. 391-401
    • McEntee, W.J.1    Crook, T.H.2
  • 37
    • 80052290024 scopus 로고    scopus 로고
    • Glutamate dehydrogenase in brain mitochondria: do lipid modifications and transient metabolon formation influence enzyme activity?
    • McKenna MC. 2011. Glutamate dehydrogenase in brain mitochondria: do lipid modifications and transient metabolon formation influence enzyme activity?Neurochem Int 59:525-533.
    • (2011) Neurochem Int , vol.59 , pp. 525-533
    • McKenna, M.C.1
  • 38
    • 0029972176 scopus 로고    scopus 로고
    • New insights into the compartmentation of glutamate and glutamine in cultured rat brain astrocytes
    • McKenna M, Tildon J, Stevenson J, Huang X. 1996. New insights into the compartmentation of glutamate and glutamine in cultured rat brain astrocytes. Dev Neurosci 18:380-390.
    • (1996) Dev Neurosci , vol.18 , pp. 380-390
    • McKenna, M.1    Tildon, J.2    Stevenson, J.3    Huang, X.4
  • 39
    • 0032473367 scopus 로고    scopus 로고
    • Molecular biology of glutamate receptors in the central nervous system and their role in excitotoxicity, oxidative stress and aging
    • Michaelis EK. 1998. Molecular biology of glutamate receptors in the central nervous system and their role in excitotoxicity, oxidative stress and aging. Prog Neurobiol 54:369-415.
    • (1998) Prog Neurobiol , vol.54 , pp. 369-415
    • Michaelis, E.K.1
  • 41
    • 0347990591 scopus 로고    scopus 로고
    • Familial hyperinsulinemic hypoglycemia caused by a defect in the SCHAD enzyme of mitochondrial fatty acid oxidation
    • Molven A, Matre GE, Duran M, Wanders RJ, Rishaug U, Njlstad PR, Jellum E, Svik O. 2004. Familial hyperinsulinemic hypoglycemia caused by a defect in the SCHAD enzyme of mitochondrial fatty acid oxidation. Diabetes 53:221-227.
    • (2004) Diabetes , vol.53 , pp. 221-227
    • Molven, A.1    Matre, G.E.2    Duran, M.3    Wanders, R.J.4    Rishaug, U.5    Njlstad, P.R.6    Jellum, E.7    Svik, O.8
  • 42
    • 0030698871 scopus 로고    scopus 로고
    • Life and death of neurons in the aging brain
    • Morrison JH, Hof PR. 1997. Life and death of neurons in the aging brain. Science 278:412-419.
    • (1997) Science , vol.278 , pp. 412-419
    • Morrison, J.H.1    Hof, P.R.2
  • 43
    • 0024411518 scopus 로고
    • Role of aspartate aminotransferase and mitochondrial dicarboxylate transport for release of endogenously and exogenously supplied neurotrasmitter in glutamatergic neurons
    • Palaiologos G, Hertz L, Schousboe A. 1989. Role of aspartate aminotransferase and mitochondrial dicarboxylate transport for release of endogenously and exogenously supplied neurotrasmitter in glutamatergic neurons. Neurochem Res 14:359-366.
    • (1989) Neurochem Res , vol.14 , pp. 359-366
    • Palaiologos, G.1    Hertz, L.2    Schousboe, A.3
  • 44
    • 0033565447 scopus 로고    scopus 로고
    • The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery
    • Peterson PE, Smith TJ. 1999. The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery. Structure 7:769-782.
    • (1999) Structure , vol.7 , pp. 769-782
    • Peterson, P.E.1    Smith, T.J.2
  • 45
    • 0020164840 scopus 로고
    • The chymotrypsin-catalysed activation of bovine liver glutamate dehydrogenase
    • Place GA, Beynon RJ. 1982. The chymotrypsin-catalysed activation of bovine liver glutamate dehydrogenase. Biochem J 205:75-80.
    • (1982) Biochem J , vol.205 , pp. 75-80
    • Place, G.A.1    Beynon, R.J.2
  • 46
    • 0020322196 scopus 로고
    • Abnormal glutamate metabolism in an adult onset degenerative neurological disorder
    • Plaitakis A, Berl S, Yahr MD. 1982. Abnormal glutamate metabolism in an adult onset degenerative neurological disorder. Science 216:193-196.
    • (1982) Science , vol.216 , pp. 193-196
    • Plaitakis, A.1    Berl, S.2    Yahr, M.D.3
  • 47
    • 0021340557 scopus 로고
    • Neurological disorders associated with deficiency of glutamate dehydrogenase
    • Plaitakis A, Berl S, Yahr M. 1984. Neurological disorders associated with deficiency of glutamate dehydrogenase. Ann Neurol 15:144-153.
    • (1984) Ann Neurol , vol.15 , pp. 144-153
    • Plaitakis, A.1    Berl, S.2    Yahr, M.3
  • 49
    • 80052265272 scopus 로고    scopus 로고
    • The human GLUD2 glutamate dehydrogenase and its regulation in health and disease
    • Plaitakis A, Latsoudis H, Spanaki C. 2011. The human GLUD2 glutamate dehydrogenase and its regulation in health and disease. Neurochem Int 59:495-509.
    • (2011) Neurochem Int , vol.59 , pp. 495-509
    • Plaitakis, A.1    Latsoudis, H.2    Spanaki, C.3
  • 50
    • 14844302859 scopus 로고    scopus 로고
    • Central nervous system hyperexcitability associated with glutamate dehydrogenase gain of function mutations. J
    • Raizen DM, Brooks-Kayal A, Steinkrauss L, Tennekoon GI, Stanley CA, Kelly A. 2005. Central nervous system hyperexcitability associated with glutamate dehydrogenase gain of function mutations. J. Pediatr 146:388-394.
    • (2005) Pediatr , vol.146 , pp. 388-394
    • Raizen, D.M.1    Brooks-Kayal, A.2    Steinkrauss, L.3    Tennekoon, G.I.4    Stanley, C.A.5    Kelly, A.6
  • 51
    • 79951659203 scopus 로고    scopus 로고
    • GABA transport inhibitors and seizure protection: the past and future
    • Schousboe A, Madsen KK, White HS. 2011. GABA transport inhibitors and seizure protection: the past and future. Future Med Chem 3:183-187.
    • (2011) Future Med Chem , vol.3 , pp. 183-187
    • Schousboe, A.1    Madsen, K.K.2    White, H.S.3
  • 52
    • 0021869650 scopus 로고
    • Excitatory aminoacid antagonists provide a therapeutic approach to neurological disorders
    • Schwarcz R, Meldrum B. 1985. Excitatory aminoacid antagonists provide a therapeutic approach to neurological disorders. Lancet 2:140-143.
    • (1985) Lancet , vol.2 , pp. 140-143
    • Schwarcz, R.1    Meldrum, B.2
  • 53
    • 84865722357 scopus 로고
    • Association of putrescine, spermidine, spermine andGABA with structural elements of brain cells
    • Seiler N, Deckardt K. 1978. Association of putrescine, spermidine, spermine andGABA with structural elements of brain cells. Neurochem Res 1:161-167.
    • (1978) Neurochem Res , vol.1 , pp. 161-167
    • Seiler, N.1    Deckardt, K.2
  • 54
    • 0028341884 scopus 로고
    • Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene
    • Shashidharan P, Michaelidis TM, Robakis NK, Kresovali A, Papamattheakis J, Plaitakis A. 1994. Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene. J Biol Chem 269:16971-16976.
    • (1994) J Biol Chem , vol.269 , pp. 16971-16976
    • Shashidharan, P.1    Michaelidis, T.M.2    Robakis, N.K.3    Kresovali, A.4    Papamattheakis, J.5    Plaitakis, A.6
  • 55
    • 0031003604 scopus 로고    scopus 로고
    • Nerve tissue-specific human glutamate dehydrogenase that is thermolabile and highly regulated by ADP
    • Shashidharan P, Clarke DD, Ahmed N, Moschonas N, Plaitakis A. 1997. Nerve tissue-specific human glutamate dehydrogenase that is thermolabile and highly regulated by ADP. J Neurochem 68:1804-1811.
    • (1997) J Neurochem , vol.68 , pp. 1804-1811
    • Shashidharan, P.1    Clarke, D.D.2    Ahmed, N.3    Moschonas, N.4    Plaitakis, A.5
  • 56
    • 0014979144 scopus 로고
    • Modifications of glutamate dehydrogenase by various drugs which affect behavior
    • Shemisa OA, Fahien LA. 1971. Modifications of glutamate dehydrogenase by various drugs which affect behavior. Mol Pharmacol 7:8-25.
    • (1971) Mol Pharmacol , vol.7 , pp. 8-25
    • Shemisa, O.A.1    Fahien, L.A.2
  • 57
    • 28444497046 scopus 로고    scopus 로고
    • In vivo carbon-13 magnetization transfer effect. Detection of aspartate amitransferase reaction
    • Shen J. 2005. In vivo carbon-13 magnetization transfer effect. Detection of aspartate amitransferase reaction. Magn Reson Med 54:1321-1326.
    • (2005) Magn Reson Med , vol.54 , pp. 1321-1326
    • Shen, J.1
  • 58
    • 54249092318 scopus 로고    scopus 로고
    • Untangling the glutamate dehydrogenase allosteric nightmare
    • Smith T, Stanley C. 2008. Untangling the glutamate dehydrogenase allosteric nightmare. Trends Biochem Sci 33:557-564.
    • (2008) Trends Biochem Sci , vol.33 , pp. 557-564
    • Smith, T.1    Stanley, C.2
  • 59
    • 0036304611 scopus 로고    scopus 로고
    • The structure of apo human glutamate dehydrogenase details subunit communication and allostery
    • Smith TJ, Schmidt T, Fang J, Wu J, Siuzdak G, Stanley CA. 2002. The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol 318:765-777.
    • (2002) J Mol Biol , vol.318 , pp. 765-777
    • Smith, T.J.1    Schmidt, T.2    Fang, J.3    Wu, J.4    Siuzdak, G.5    Stanley, C.A.6
  • 60
    • 0031239422 scopus 로고    scopus 로고
    • Glutamate transport and metabolism in astrocytes
    • Sonnewald U, Westergaard N, Schousboe A. 1997. Glutamate transport and metabolism in astrocytes. Glia 21:56-63.
    • (1997) Glia , vol.21 , pp. 56-63
    • Sonnewald, U.1    Westergaard, N.2    Schousboe, A.3
  • 61
    • 84856303217 scopus 로고    scopus 로고
    • The role of glutamate dehydorgenase in mammalian ammonia metabolism
    • Spanaki C, Plaitakis A. 2012. The role of glutamate dehydorgenase in mammalian ammonia metabolism. Neurotox Res 21:117-127.
    • (2012) Neurotox Res , vol.21 , pp. 117-127
    • Spanaki, C.1    Plaitakis, A.2
  • 62
    • 77952778182 scopus 로고    scopus 로고
    • Human GLUD2 glutamate dehydrogenase is expressed in neural and testicular supportive cells
    • Spanaki C, Zaganas I, Kleopas K, Plaitakis A. 2010. Human GLUD2 glutamate dehydrogenase is expressed in neural and testicular supportive cells. J Biol Chem 285:16748-16756.
    • (2010) J Biol Chem , vol.285 , pp. 16748-16756
    • Spanaki, C.1    Zaganas, I.2    Kleopas, K.3    Plaitakis, A.4
  • 63
    • 84865790575 scopus 로고    scopus 로고
    • The complex regulation of human glud1 and glud2 glutamate dehydrogenases and its implications in nerve tissue biology
    • Spanaki C, Zaganas I, Kounoupa Z, Plaitakis A. 2012. The complex regulation of human glud1 and glud2 glutamate dehydrogenases and its implications in nerve tissue biology. Neurochem Int (in press).
    • (2012) Neurochem Int
    • Spanaki, C.1    Zaganas, I.2    Kounoupa, Z.3    Plaitakis, A.4
  • 64
    • 80052259624 scopus 로고    scopus 로고
    • Two genetic forms of hyperinsulinemic hypoglycemia caused by dysregulation of glutamate dehydrogenase
    • Stanley CA. 2011. Two genetic forms of hyperinsulinemic hypoglycemia caused by dysregulation of glutamate dehydrogenase. Neurochem Int 59:465-472.
    • (2011) Neurochem Int , vol.59 , pp. 465-472
    • Stanley, C.A.1
  • 66
    • 0034855244 scopus 로고    scopus 로고
    • Changing concepts in the neurochemistry of schizophrenia
    • Tamminga CA, Frost DO. 2001. Changing concepts in the neurochemistry of schizophrenia. Am J Psychiatry 158:1365-1366.
    • (2001) Am J Psychiatry , vol.158 , pp. 1365-1366
    • Tamminga, C.A.1    Frost, D.O.2
  • 67
    • 0023276014 scopus 로고
    • Neocortical cell counts in normal human adult aging
    • Terry RD, DeTeresa R, Hansen LA. 1987. Neocortical cell counts in normal human adult aging. Ann Neurol 21:530-539.
    • (1987) Ann Neurol , vol.21 , pp. 530-539
    • Terry, R.D.1    DeTeresa, R.2    Hansen, L.A.3
  • 68
    • 7244220611 scopus 로고    scopus 로고
    • Glutamate and glutamine in the anterior cingulate and thalamus of medicated patients with chronic schizophrenia and healthy comparison subjects measured with 4.0-T proton MRS
    • Théberge J, Al-Semaan Y, Williamson PC, Menon RS, Neufeld RW, Rajakumar N, Schaefer B, Densmore M, Drost DJ. 2003. Glutamate and glutamine in the anterior cingulate and thalamus of medicated patients with chronic schizophrenia and healthy comparison subjects measured with 4.0-T proton MRS. Am J Psychiatry 160:2231-2233.
    • (2003) Am J Psychiatry , vol.160 , pp. 2231-2233
    • Théberge, J.1    Al-Semaan, Y.2    Williamson, P.C.3    Menon, R.S.4    Neufeld, R.W.5    Rajakumar, N.6    Schaefer, B.7    Densmore, M.8    Drost, D.J.9
  • 69
    • 77952626170 scopus 로고    scopus 로고
    • Systemic activation of glutamate dehydrogenase increases renal ammoniagenesis: implications for the hyperinsulinism/hyperammonemia syndrome
    • Treberg JR, Clow KA, Greene KA, Brosnan ME, Brosnan JT. 2010. Systemic activation of glutamate dehydrogenase increases renal ammoniagenesis: implications for the hyperinsulinism/hyperammonemia syndrome. Am J Physiol Endocrinol Metab 298:E1219-E1225.
    • (2010) Am J Physiol Endocrinol Metab , vol.298
    • Treberg, J.R.1    Clow, K.A.2    Greene, K.A.3    Brosnan, M.E.4    Brosnan, J.T.5
  • 71
    • 77953076614 scopus 로고    scopus 로고
    • Transcriptomic responses in mouse brain exposed to chronic excess of the neurotransmitter glutamate
    • Wang X, Bao X, Pal R, Agbas A, Michaelis EK. 2010. Transcriptomic responses in mouse brain exposed to chronic excess of the neurotransmitter glutamate. BMC Genomics 11:360.
    • (2010) BMC Genomics , vol.11 , pp. 360
    • Wang, X.1    Bao, X.2    Pal, R.3    Agbas, A.4    Michaelis, E.K.5
  • 72
    • 0037135619 scopus 로고    scopus 로고
    • Single amino acid substitution (G456A) in the vicinity of the GTP binding domain of human housekeeping glutamate dehydrogenase markedly attenuates GTP inhibition and abolishes the cooperative behavior of the enzyme
    • Zaganas I, Plaitakis A. 2002. Single amino acid substitution (G456A) in the vicinity of the GTP binding domain of human housekeeping glutamate dehydrogenase markedly attenuates GTP inhibition and abolishes the cooperative behavior of the enzyme. J Biol Chem 277:26422-26428.
    • (2002) J Biol Chem , vol.277 , pp. 26422-26428
    • Zaganas, I.1    Plaitakis, A.2
  • 73
    • 0035577775 scopus 로고    scopus 로고
    • Differential expression of glutamate dehydrogenase in cultured neurons and astrocytes from mouse cerebellum and cerebral cortex
    • Zaganas I, Waagepetersen HS, Georgopoulos P, Sonnewald U, Plaitakis A, Schousboe A. 2001. Differential expression of glutamate dehydrogenase in cultured neurons and astrocytes from mouse cerebellum and cerebral cortex. J Neurosci Res 66:909-913.
    • (2001) J Neurosci Res , vol.66 , pp. 909-913
    • Zaganas, I.1    Waagepetersen, H.S.2    Georgopoulos, P.3    Sonnewald, U.4    Plaitakis, A.5    Schousboe, A.6
  • 74
    • 0037195942 scopus 로고    scopus 로고
    • Substitution of Ser for Arg-443 in the regulatory domain of human housekeeping (GLUD1) glutamate dehydrogenase virtually abolishes basal activity and markedly alters the activation of the enzyme by ADP and L-leucine
    • Zaganas I, Spanaki C, Karpusas M, Plaitakis A. 2002. Substitution of Ser for Arg-443 in the regulatory domain of human housekeeping (GLUD1) glutamate dehydrogenase virtually abolishes basal activity and markedly alters the activation of the enzyme by ADP and L-leucine. JBiol Chem 277:46552-46558.
    • (2002) JBiol Chem , vol.277 , pp. 46552-46558
    • Zaganas, I.1    Spanaki, C.2    Karpusas, M.3    Plaitakis, A.4
  • 75
    • 84865755077 scopus 로고    scopus 로고
    • Expression of human GLUD2 glutamate dehydrogenase in human tissues: functional implications
    • Zaganas I, Spanaki C, Plaitakis A. 2012. Expression of human GLUD2 glutamate dehydrogenase in human tissues: functional implications. Neurochem Int (in press).
    • (2012) Neurochem Int
    • Zaganas, I.1    Spanaki, C.2    Plaitakis, A.3


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