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Volumn 76, Issue 1, 2000, Pages 56-63

Isolation, characterization and expression of a human brain mitochondrial glutaminase cDNA

Author keywords

Baculovirus expression; cDNA; Glutaminase; Mitochondria; Stroke

Indexed keywords

COMPLEMENTARY DNA; GLUTAMINASE;

EID: 0034629261     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-328X(99)00331-9     Document Type: Article
Times cited : (35)

References (28)
  • 1
    • 0032145981 scopus 로고    scopus 로고
    • Expression, purification, and characterization of histidine-tagged rat and human flavoenzyme dihydroorotate dehydrogenase
    • Bader B., Knecht W., Fries M., Loffler M. Expression, purification, and characterization of histidine-tagged rat and human flavoenzyme dihydroorotate dehydrogenase. Protein Express. Purif. 13:1998;414-422.
    • (1998) Protein Express. Purif. , vol.13 , pp. 414-422
    • Bader, B.1    Knecht, W.2    Fries, M.3    Loffler, M.4
  • 2
    • 0017279321 scopus 로고
    • Phosphate-dependent glutaminase from rat kidney. Cause of increased activity in response to acidosis and identity with glutaminases from other tissues
    • Curthoys N.P., Kuhlenschmidt T., Godfrey S.S., Weiss R.F. Phosphate-dependent glutaminase from rat kidney. Cause of increased activity in response to acidosis and identity with glutaminases from other tissues. Arch. Biochem. Biophys. 172:1976;162-167.
    • (1976) Arch. Biochem. Biophys. , vol.172 , pp. 162-167
    • Curthoys, N.P.1    Kuhlenschmidt, T.2    Godfrey, S.S.3    Weiss, R.F.4
  • 3
    • 0029099953 scopus 로고
    • Regulation of glutaminase activity and glutamine metabolism
    • Curthoys N.P., Watford M. Regulation of glutaminase activity and glutamine metabolism. Annu. Rev. Nutr. 15:1995;133-159.
    • (1995) Annu. Rev. Nutr. , vol.15 , pp. 133-159
    • Curthoys, N.P.1    Watford, M.2
  • 4
    • 0016254181 scopus 로고
    • Regulation of renal ammoniagenesis. Subcellular localization of rat kidney glutaminase isoenzymes
    • Curthoys N.P., Weiss R. Regulation of renal ammoniagenesis. Subcellular localization of rat kidney glutaminase isoenzymes. J. Biol. Chem. 249:1974;3261-3266.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3261-3266
    • Curthoys, N.P.1    Weiss, R.2
  • 5
    • 0027429163 scopus 로고
    • Damage to neurons in culture following medium change: Role of glutamine and extracellular generation of glutamate
    • Driscoll B.F., Deibler G.E., Law M.J., Crane A.M. Damage to neurons in culture following medium change: role of glutamine and extracellular generation of glutamate. J. Neurochem. 61:1993;1795-1800.
    • (1993) J. Neurochem. , vol.61 , pp. 1795-1800
    • Driscoll, B.F.1    Deibler, G.E.2    Law, M.J.3    Crane, A.M.4
  • 6
  • 7
    • 0030018017 scopus 로고    scopus 로고
    • Wild type and mutant human heart (R)-3-hydroxybutyrate dehydrogenase expressed in insect cells
    • Green D., Marks A.R., Fleischer S., McIntyre J.O. Wild type and mutant human heart (R)-3-hydroxybutyrate dehydrogenase expressed in insect cells. Biochemistry. 35:1996;8158-8165.
    • (1996) Biochemistry , vol.35 , pp. 8158-8165
    • Green, D.1    Marks, A.R.2    Fleischer, S.3    McIntyre, J.O.4
  • 8
    • 0022416657 scopus 로고
    • Comparison of the phosphate-dependent glutaminase obtained from rat brain and kidney
    • Haser W.G., Shapiro R.A., Curthoys N.P. Comparison of the phosphate-dependent glutaminase obtained from rat brain and kidney. Biochem. J. 229:1985;399-408.
    • (1985) Biochem. J. , vol.229 , pp. 399-408
    • Haser, W.G.1    Shapiro, R.A.2    Curthoys, N.P.3
  • 10
    • 0031928862 scopus 로고    scopus 로고
    • Genes involved in hereditary ataxias
    • Klockgether T., Evert B. Genes involved in hereditary ataxias. Trends Neurosci. 21:1998;413-418.
    • (1998) Trends Neurosci. , vol.21 , pp. 413-418
    • Klockgether, T.1    Evert, B.2
  • 11
    • 0031172843 scopus 로고    scopus 로고
    • Rat dihydroorotate dehydrogenase: Isolation of the recombinant enzyme from mitochondria of insect cells
    • Knecht W., Altekruse D., Rotgeri A., Gonski S., Loffler M. Rat dihydroorotate dehydrogenase: isolation of the recombinant enzyme from mitochondria of insect cells. Protein Express. Purif. 10:1997;89-99.
    • (1997) Protein Express. Purif. , vol.10 , pp. 89-99
    • Knecht, W.1    Altekruse, D.2    Rotgeri, A.3    Gonski, S.4    Loffler, M.5
  • 14
    • 0028897733 scopus 로고
    • Clinical experience with excitatory amino acid antagonist drugs
    • Muir K.W., Lees K.R. Clinical experience with excitatory amino acid antagonist drugs. Stroke. 26:1995;503-513.
    • (1995) Stroke , vol.26 , pp. 503-513
    • Muir, K.W.1    Lees, K.R.2
  • 15
    • 0032583209 scopus 로고    scopus 로고
    • Characterization of mitochondrial glutaminase and amino acids at prolonged times after experimental focal cerebral ischemia
    • Newcomb R., Pierce A.R., Kano T., Meng W., Bosque-Hamilton P., Taylor L., Curthoys N., Lo E.H. Characterization of mitochondrial glutaminase and amino acids at prolonged times after experimental focal cerebral ischemia. Brain Res. 813:1998;103-111.
    • (1998) Brain Res. , vol.813 , pp. 103-111
    • Newcomb, R.1    Pierce, A.R.2    Kano, T.3    Meng, W.4    Bosque-Hamilton, P.5    Taylor, L.6    Curthoys, N.7    Lo, E.H.8
  • 16
    • 0030893024 scopus 로고    scopus 로고
    • Increased production of extracellular glutamate by the mitochondrial glutaminase following neuronal death
    • Newcomb R., Sun X., Taylor L., Curthoys N., Gifford R.G. Increased production of extracellular glutamate by the mitochondrial glutaminase following neuronal death. J. Biol. Chem. 272:1997;11276-11282.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11276-11282
    • Newcomb, R.1    Sun, X.2    Taylor, L.3    Curthoys, N.4    Gifford, R.G.5
  • 17
    • 0025080859 scopus 로고
    • Biosynthesis and processing of renal mitochondrial glutaminase in cultured proximal tubule epithelial cells and in isolated mitochondria
    • Perera S., Chen T.C., Curthoys N.P. Biosynthesis and processing of renal mitochondrial glutaminase in cultured proximal tubule epithelial cells and in isolated mitochondria. J. Biol. Chem. 265:1990;17764-17770.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17764-17770
    • Perera, S.1    Chen, T.C.2    Curthoys, N.P.3
  • 18
    • 0026068739 scopus 로고
    • Biosynthesis and processing of mitochondrial glutaminase in HTC-hepatoma cells
    • Perera S.Y., Voith D.M., Curthoys N.P. Biosynthesis and processing of mitochondrial glutaminase in HTC-hepatoma cells. Biochem. J. 273:1991;265-270.
    • (1991) Biochem. J. , vol.273 , pp. 265-270
    • Perera, S.Y.1    Voith, D.M.2    Curthoys, N.P.3
  • 20
    • 0033010987 scopus 로고    scopus 로고
    • Recent advances in understanding the pathogenesis of Huntington's disease
    • Reddy P.H., Williams M., Tagle D.A. Recent advances in understanding the pathogenesis of Huntington's disease. Trends Neurosci. 22:1999;248-255.
    • (1999) Trends Neurosci. , vol.22 , pp. 248-255
    • Reddy, P.H.1    Williams, M.2    Tagle, D.A.3
  • 21
    • 0025929460 scopus 로고
    • Accumulation of extracellular glutamate and neuronal death in astrocyte-poor cultures exposed to glutamine
    • Rosenburg P.A. Accumulation of extracellular glutamate and neuronal death in astrocyte-poor cultures exposed to glutamine. Glia. 4:1991;91-100.
    • (1991) Glia , vol.4 , pp. 91-100
    • Rosenburg, P.A.1
  • 23
    • 0026052695 scopus 로고
    • Isolation, characterization, and in vitro expression of a cDNA that encodes the kidney isoenzyme of the mitochondrial glutaminase
    • Shapiro R.A., Farrell L., Srinivasan M., Curthoys N.P. Isolation, characterization, and in vitro expression of a cDNA that encodes the kidney isoenzyme of the mitochondrial glutaminase. J. Biol. Chem. 266:1991;18792-18796.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18792-18796
    • Shapiro, R.A.1    Farrell, L.2    Srinivasan, M.3    Curthoys, N.P.4
  • 24
    • 0028817567 scopus 로고
    • In vitro characterization of the mitochondrial processing and potential function of the 68-kDa subunit of renal glutaminase
    • Srinivasan M., Kalousek F., Curthoys N.P. In vitro characterization of the mitochondrial processing and potential function of the 68-kDa subunit of renal glutaminase. J. Biol. Chem. 270:1995;1185-1190.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1185-1190
    • Srinivasan, M.1    Kalousek, F.2    Curthoys, N.P.3
  • 25
    • 0028838956 scopus 로고
    • Role of N-terminal 118 amino acids in the processing of the rat renal mitochondrial glutaminase
    • Srinivasan M., Kalousek F., Farrell L., Curthoys N.P. Role of N-terminal 118 amino acids in the processing of the rat renal mitochondrial glutaminase. J. Biol. Chem. 270:1995;1191-1197.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1191-1197
    • Srinivasan, M.1    Kalousek, F.2    Farrell, L.3    Curthoys, N.P.4
  • 26
    • 0032502659 scopus 로고    scopus 로고
    • Definition of regulatory sequence elements in the promoter region and the first intron of the myotonic dystrophy protein kinase gene
    • Storbeck C.J., Sabourin L.A., Waring J.D., Korneluk R.G. Definition of regulatory sequence elements in the promoter region and the first intron of the myotonic dystrophy protein kinase gene. J. Biol. Chem. 273:1998;9139-9147.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9139-9147
    • Storbeck, C.J.1    Sabourin, L.A.2    Waring, J.D.3    Korneluk, R.G.4
  • 27
    • 0015606174 scopus 로고
    • Purification of phosphate dependent pig brain glutaminase
    • Svenneby G., Torgner I.A., Kvemme E. Purification of phosphate dependent pig brain glutaminase. J. Neurochem. 20:1973;1217-1224.
    • (1973) J. Neurochem. , vol.20 , pp. 1217-1224
    • Svenneby, G.1    Torgner, I.A.2    Kvemme, E.3
  • 28
    • 0029079129 scopus 로고
    • Purification and reconstitution of murine mitochondrial glycerol-3-phosphate acyltransferase. Functional expression in baculovirus-infected insect cells
    • Yet S.F., Moon Y.K., Sul H.S. Purification and reconstitution of murine mitochondrial glycerol-3-phosphate acyltransferase. Functional expression in baculovirus-infected insect cells. Biochemistry. 34:1995;7303-7310.
    • (1995) Biochemistry , vol.34 , pp. 7303-7310
    • Yet, S.F.1    Moon, Y.K.2    Sul, H.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.