메뉴 건너뛰기




Volumn 55, Issue 1-3, 2009, Pages 76-84

A novel glutaminase isoform in mammalian tissues

Author keywords

Glutamate; Glutaminase genes; Glutamine; Mammalian isoenzymes; Neurone; Transcript variants

Indexed keywords

GLUTAMINASE; KIDNEY TYPE GLUTAMINASE; LIVER TYPE GLUTAMINASE; UNCLASSIFIED DRUG;

EID: 64949158435     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2009.02.021     Document Type: Article
Times cited : (56)

References (68)
  • 1
    • 0032440805 scopus 로고    scopus 로고
    • Early differential expression of two glutaminase mRNAs in mouse spleen after tumor implantation
    • Aledo J.C., Segura J.A., Barbero L.G., and Márquez J. Early differential expression of two glutaminase mRNAs in mouse spleen after tumor implantation. Cancer Lett. 133 (1998) 95-99
    • (1998) Cancer Lett. , vol.133 , pp. 95-99
    • Aledo, J.C.1    Segura, J.A.2    Barbero, L.G.3    Márquez, J.4
  • 3
    • 0033661413 scopus 로고    scopus 로고
    • Identification of two human glutaminase loci and tissue-specific expression of the two related genes
    • Aledo J.C., Gómez-Fabre P.M., Olalla L., and Márquez J. Identification of two human glutaminase loci and tissue-specific expression of the two related genes. Mamm. Genome 11 (2000) 1107-1110
    • (2000) Mamm. Genome , vol.11 , pp. 1107-1110
    • Aledo, J.C.1    Gómez-Fabre, P.M.2    Olalla, L.3    Márquez, J.4
  • 5
    • 0038305531 scopus 로고    scopus 로고
    • Expression of recombinant human L-glutaminase in Escherichia coli: polyclonal antibodies production and immunological analysis of mouse tissues
    • Campos J.A., Aledo J.C., Segura J.A., Alonso F.J., Gómez-Fabre P.M., Núñez de Castro I., and Márquez J. Expression of recombinant human L-glutaminase in Escherichia coli: polyclonal antibodies production and immunological analysis of mouse tissues. Biochim. Biophys. Acta 1648 (2003) 17-23
    • (2003) Biochim. Biophys. Acta , vol.1648 , pp. 17-23
    • Campos, J.A.1    Aledo, J.C.2    Segura, J.A.3    Alonso, F.J.4    Gómez-Fabre, P.M.5    Núñez de Castro, I.6    Márquez, J.7
  • 7
    • 1842778890 scopus 로고    scopus 로고
    • Granule localization of glutaminase in human neutrophils and the consequence of glutamine utilization for neutrophil activity
    • Castell L., Vance C., Abbott R., Márquez J., and Eggleton P. Granule localization of glutaminase in human neutrophils and the consequence of glutamine utilization for neutrophil activity. J. Biol. Chem. 279 (2004) 13305-13310
    • (2004) J. Biol. Chem. , vol.279 , pp. 13305-13310
    • Castell, L.1    Vance, C.2    Abbott, R.3    Márquez, J.4    Eggleton, P.5
  • 8
    • 0018521699 scopus 로고
    • Cow brain glutaminase: partial purification and mechanism of action
    • Chiu J.F., and Boeker E.A. Cow brain glutaminase: partial purification and mechanism of action. Arch. Biochem. Biophys. 196 (1979) 493-500
    • (1979) Arch. Biochem. Biophys. , vol.196 , pp. 493-500
    • Chiu, J.F.1    Boeker, E.A.2
  • 9
    • 0030996902 scopus 로고    scopus 로고
    • Rat hepatic glutaminase: identification of the full coding sequence and characterization of a functional promoter
    • Chung-Bok M.-I., Vincent N., Jhala U., and Watford M. Rat hepatic glutaminase: identification of the full coding sequence and characterization of a functional promoter. Biochem. J. 324 (1997) 193-200
    • (1997) Biochem. J. , vol.324 , pp. 193-200
    • Chung-Bok, M.-I.1    Vincent, N.2    Jhala, U.3    Watford, M.4
  • 10
    • 0033215089 scopus 로고    scopus 로고
    • Shaping excitation at glutamatergic synapses
    • Conti F., and Weinberg R.J. Shaping excitation at glutamatergic synapses. Trends Neurosci. 22 (1999) 451-458
    • (1999) Trends Neurosci. , vol.22 , pp. 451-458
    • Conti, F.1    Weinberg, R.J.2
  • 11
    • 0017183620 scopus 로고
    • Regulation of renal ammoniagenesis. Purification and characterization of phosphate-dependent glutaminase from rat kidney
    • Curthoys N.P., Kuhlenschmidt T., and Godfrey S.S. Regulation of renal ammoniagenesis. Purification and characterization of phosphate-dependent glutaminase from rat kidney. Arch. Biochem. Biophys. 174 (1976) 82-89
    • (1976) Arch. Biochem. Biophys. , vol.174 , pp. 82-89
    • Curthoys, N.P.1    Kuhlenschmidt, T.2    Godfrey, S.S.3
  • 12
    • 0017279321 scopus 로고
    • Phosphate-dependent glutaminase from rat kidney. Cause of increased activity in response to acidosis and identity with glutaminase from other tissues
    • Curthoys N.P., Kuhlenschmidt T., Godfrey S.S., and Weiss R.F. Phosphate-dependent glutaminase from rat kidney. Cause of increased activity in response to acidosis and identity with glutaminase 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
  • 13
    • 0029099953 scopus 로고
    • Regulation of glutaminase activity and glutamine metabolism
    • Curthoys N.P., and 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
  • 14
    • 0032515065 scopus 로고    scopus 로고
    • The role of C/EBP genes in adipocyte differentiation
    • Darlington G.J., Ross S.E., and MacDougald O.A. The role of C/EBP genes in adipocyte differentiation. J. Biol. Chem. 273 (1998) 30057-30060
    • (1998) J. Biol. Chem. , vol.273 , pp. 30057-30060
    • Darlington, G.J.1    Ross, S.E.2    MacDougald, O.A.3
  • 15
    • 0033620972 scopus 로고    scopus 로고
    • Cloning and analysis of unique human glutaminase isoforms generated by tissue-specific alternative splicing
    • Elgadi K.M., Meguid R.A., Qian M., Souba W.W., and Abcouwer S.F. Cloning and analysis of unique human glutaminase isoforms generated by tissue-specific alternative splicing. Physiol. Genomics 1 (1999) 51-62
    • (1999) Physiol. Genomics , vol.1 , pp. 51-62
    • Elgadi, K.M.1    Meguid, R.A.2    Qian, M.3    Souba, W.W.4    Abcouwer, S.F.5
  • 16
    • 0025196959 scopus 로고
    • Metabolism and role of glutamate in mammalian brain
    • Erecinska M., and Silver I.A. Metabolism and role of glutamate in mammalian brain. Prog. Neurobiol. 35 (1990) 245-296
    • (1990) Prog. Neurobiol. , vol.35 , pp. 245-296
    • Erecinska, M.1    Silver, I.A.2
  • 17
    • 0042945133 scopus 로고
    • Phosphate-activated glutaminase in kidney and other tissues
    • Errera M., and Greenstein J.P. Phosphate-activated glutaminase in kidney and other tissues. J. Biol. Chem. 178 (1949) 495-502
    • (1949) J. Biol. Chem. , vol.178 , pp. 495-502
    • Errera, M.1    Greenstein, J.P.2
  • 18
    • 0021330769 scopus 로고
    • Glutamate: a neurotransmitter in mammalian brain
    • Fonnum F. Glutamate: a neurotransmitter in mammalian brain. J. Neurochem. 42 (1984) 1-11
    • (1984) J. Neurochem. , vol.42 , pp. 1-11
    • Fonnum, F.1
  • 19
    • 0024725630 scopus 로고
    • CCAAT/enhancer binding protein activates the promoter of the serum albumin gene in cultured hepatoma cells
    • Friedman A.D., Landschulz W.H., and McKnight S.L. CCAAT/enhancer binding protein activates the promoter of the serum albumin gene in cultured hepatoma cells. Genes Dev. 3 (1989) 1314-1322
    • (1989) Genes Dev. , vol.3 , pp. 1314-1322
    • Friedman, A.D.1    Landschulz, W.H.2    McKnight, S.L.3
  • 20
    • 0029128586 scopus 로고
    • Glutamine synthetase and hepatocarcinogenesis
    • Gebhardt R., and Williams G.M. Glutamine synthetase and hepatocarcinogenesis. Carcinogenesis 16 (1995) 1673-1681
    • (1995) Carcinogenesis , vol.16 , pp. 1673-1681
    • Gebhardt, R.1    Williams, G.M.2
  • 22
    • 0022416657 scopus 로고
    • Comparison of the phosphate-dependent glutaminase obtained from rat brain and kidney
    • Haser W.G., Shapiro R.A., and 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
  • 23
    • 0023095943 scopus 로고
    • Purification and characterization of rat liver glutaminase
    • Heini H.G., Gebhardt R., and Mecke D. Purification and characterization of rat liver glutaminase. Eur. J. Biochem. 162 (1987) 541-546
    • (1987) Eur. J. Biochem. , vol.162 , pp. 541-546
    • Heini, H.G.1    Gebhardt, R.2    Mecke, D.3
  • 24
    • 0028815804 scopus 로고
    • 15N nuclear magnetic resonance
    • 15N nuclear magnetic resonance. Biochem. J. 305 (1995) 329-336
    • (1995) Biochem. J. , vol.305 , pp. 329-336
    • Kanamori, K.1    Ross, B.D.2
  • 25
    • 0023088452 scopus 로고
    • Production, characterization, and immunohistochemical application of monoclonal antibodies to glutaminase purified from rat brain
    • Kaneko T., Urade Y., Watanabe Y., and Mizuno N. Production, characterization, and immunohistochemical application of monoclonal antibodies to glutaminase purified from rat brain. J. Neurosci. 7 (1987) 302-309
    • (1987) J. Neurosci. , vol.7 , pp. 302-309
    • Kaneko, T.1    Urade, Y.2    Watanabe, Y.3    Mizuno, N.4
  • 26
    • 0034212232 scopus 로고    scopus 로고
    • Glutamine-enriched parenteral nutrition regulates the activity and expression of intestinal glutaminase
    • Kong S.E., Hall J.C., Cooper D., and McCauley R.D. Glutamine-enriched parenteral nutrition regulates the activity and expression of intestinal glutaminase. Biochim. Biophys. Acta 1 (2000) 67-75
    • (2000) Biochim. Biophys. Acta , vol.1 , pp. 67-75
    • Kong, S.E.1    Hall, J.C.2    Cooper, D.3    McCauley, R.D.4
  • 27
    • 0020536675 scopus 로고
    • Mitochondrial metabolism of glutamine and glutamate and its physiological significance
    • Kovacevic Z., and McGivan J.D. Mitochondrial metabolism of glutamine and glutamate and its physiological significance. Physiol. Rev. 63 (1983) 547-605
    • (1983) Physiol. Rev. , vol.63 , pp. 547-605
    • Kovacevic, Z.1    McGivan, J.D.2
  • 28
    • 0001062019 scopus 로고
    • Metabolism of amino acids. IV. The synthesis of glutamine from glutamic acid and ammonia and the enzymic hydrolysis of glutamine in animal tissues
    • Krebs H.A. Metabolism of amino acids. IV. The synthesis of glutamine from glutamic acid and ammonia and the enzymic hydrolysis of glutamine in animal tissues. Biochem. J. 29 (1935) 1951-1969
    • (1935) Biochem. J. , vol.29 , pp. 1951-1969
    • Krebs, H.A.1
  • 29
    • 0002709177 scopus 로고
    • Enzymes of cerebral glutamine metabolism
    • Häussinger D., and Sies H. (Eds), Springer Verlag, Berlin
    • Kvamme E. Enzymes of cerebral glutamine metabolism. In: Häussinger D., and Sies H. (Eds). Glutamine Metabolism in Mammalian Tissues (1984), Springer Verlag, Berlin 32-48
    • (1984) Glutamine Metabolism in Mammalian Tissues , pp. 32-48
    • Kvamme, E.1
  • 30
    • 0034305620 scopus 로고    scopus 로고
    • Phosphate activated glutaminase and mitochondrial glutamine transport in the brain
    • Kvamme E., Roberg B., and Torgner I.Aa. Phosphate activated glutaminase and mitochondrial glutamine transport in the brain. Neurochem. Res. 25 (2000) 1407-1419
    • (2000) Neurochem. Res. , vol.25 , pp. 1407-1419
    • Kvamme, E.1    Roberg, B.2    Torgner, I.Aa.3
  • 31
    • 0014961888 scopus 로고
    • Glutaminase from pig renal cortex. I. Purification and general properties
    • Kvamme E., Tveit B., and Svenneby G. Glutaminase from pig renal cortex. I. Purification and general properties. J. Biol. Chem. 245 (1970) 1871-1877
    • (1970) J. Biol. Chem. , vol.245 , pp. 1871-1877
    • Kvamme, E.1    Tveit, B.2    Svenneby, G.3
  • 32
    • 0030923984 scopus 로고    scopus 로고
    • Identification of an mRNA-binding protein and the specific elements that may mediate the pH-responsive induction of renal glutaminase mRNA
    • Laterza O.F., Hansen W.R., Taylor L., and Curthoys N.P. Identification of an mRNA-binding protein and the specific elements that may mediate the pH-responsive induction of renal glutaminase mRNA. J. Biol. Chem. 272 (1997) 22481-22488
    • (1997) J. Biol. Chem. , vol.272 , pp. 22481-22488
    • Laterza, O.F.1    Hansen, W.R.2    Taylor, L.3    Curthoys, N.P.4
  • 35
    • 0026532176 scopus 로고
    • Glutaminase and glutamine synthetase activities in human cirrhotic liver and hepatocellular carcinoma
    • Matsuno T., and Goto I. Glutaminase and glutamine synthetase activities in human cirrhotic liver and hepatocellular carcinoma. Cancer Res. 52 (1992) 1192-1194
    • (1992) Cancer Res. , vol.52 , pp. 1192-1194
    • Matsuno, T.1    Goto, I.2
  • 38
    • 0032585352 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro
    • Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nombra N., and Ohara O. Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 5 (1998) 355-364
    • (1998) DNA Res. , vol.5 , pp. 355-364
    • Nagase, T.1    Ishikawa, K.2    Suyama, M.3    Kikuno, R.4    Hirosawa, M.5    Miyajima, N.6    Tanaka, A.7    Kotani, H.8    Nombra, N.9    Ohara, O.10
  • 39
    • 0023322754 scopus 로고
    • Interactions between neurons and glia in glutamate/glutamine compartmentation
    • Nicklas W.J., Zeevalk G., and Hyndman A. Interactions between neurons and glia in glutamate/glutamine compartmentation. Biochem. Soc. Trans. 15 (1987) 208-210
    • (1987) Biochem. Soc. Trans. , vol.15 , pp. 208-210
    • Nicklas, W.J.1    Zeevalk, G.2    Hyndman, A.3
  • 40
    • 0018872447 scopus 로고
    • Purification of soluble glutaminase from pig brain
    • Nimmo G.A., and Tipton K.F. Purification of soluble glutaminase from pig brain. Biochem. Pharmacol. 29 (1980) 359-367
    • (1980) Biochem. Pharmacol. , vol.29 , pp. 359-367
    • Nimmo, G.A.1    Tipton, K.F.2
  • 42
    • 0035910506 scopus 로고    scopus 로고
    • The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins
    • Olalla L., Aledo J.C., Bannenberg G., and Márquez J. The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins. FEBS Lett. 488 (2001) 116-122
    • (2001) FEBS Lett. , vol.488 , pp. 116-122
    • Olalla, L.1    Aledo, J.C.2    Bannenberg, G.3    Márquez, J.4
  • 45
    • 0021248977 scopus 로고
    • Partial purification and properties of rat liver glutaminase
    • Patel M., and McGivan J.D. Partial purification and properties of rat liver glutaminase. Biochem. J. 220 (1984) 583-590
    • (1984) Biochem. J. , vol.220 , pp. 583-590
    • Patel, M.1    McGivan, J.D.2
  • 46
    • 0025080859 scopus 로고
    • Biosynthesis and processing of renal mitochondrial glutaminase in cultured proximal tubular epithelial cells and in isolated mitochondria
    • Perera S.Y., Chen T.C., and Curthoys N.P. Biosynthesis and processing of renal mitochondrial glutaminase in cultured proximal tubular epithelial cells and in isolated mitochondria. J. Biol. Chem. 265 (1990) 17764-17770
    • (1990) J. Biol. Chem. , vol.265 , pp. 17764-17770
    • Perera, S.Y.1    Chen, T.C.2    Curthoys, N.P.3
  • 50
    • 0347370301 scopus 로고    scopus 로고
    • Complexity and species variation of the kidney-type glutaminase gene
    • Porter L.D., Ibrahim H., Taylor L., and Curthoys N.P. Complexity and species variation of the kidney-type glutaminase gene. Physiol. Genomics 9 (2002) 57-66
    • (2002) Physiol. Genomics , vol.9 , pp. 57-66
    • Porter, L.D.1    Ibrahim, H.2    Taylor, L.3    Curthoys, N.P.4
  • 52
    • 34548789512 scopus 로고    scopus 로고
    • Novel mechanism of inhibition of rat kidney-type glutaminase by bis-2-(5-phenylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide (BPTES)
    • Robinson M.M., McBryant S.J., Tsukamoto T., Rojas C., Ferraris D.V., Hamilton S.K., Hansen J.C., and Curthoys N.P. Novel mechanism of inhibition of rat kidney-type glutaminase by bis-2-(5-phenylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide (BPTES). Biochem J. 406 (2007) 407-414
    • (2007) Biochem J. , vol.406 , pp. 407-414
    • Robinson, M.M.1    McBryant, S.J.2    Tsukamoto, T.3    Rojas, C.4    Ferraris, D.V.5    Hamilton, S.K.6    Hansen, J.C.7    Curthoys, N.P.8
  • 54
    • 0026725883 scopus 로고
    • Glucocorticoids regulate intestinal glutaminase expression
    • Sarantos P., Abouhamze A., and Souba W.W. Glucocorticoids regulate intestinal glutaminase expression. Surgery 112 (1992) 278-283
    • (1992) Surgery , vol.112 , pp. 278-283
    • Sarantos, P.1    Abouhamze, A.2    Souba, W.W.3
  • 55
    • 0027182604 scopus 로고
    • Endotoxin stimulates lymphocyte glutaminase expression
    • Sarantos P., Ockert K., and Souba W.W. Endotoxin stimulates lymphocyte glutaminase expression. Arch. Surg. 128 (1993) 920-924
    • (1993) Arch. Surg. , vol.128 , pp. 920-924
    • Sarantos, P.1    Ockert, K.2    Souba, W.W.3
  • 57
    • 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., and 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
  • 58
    • 0032056406 scopus 로고    scopus 로고
    • Triplet-repeat transcripts: a role for DNA in disease
    • Singer R.H. Triplet-repeat transcripts: a role for DNA in disease. Science 280 (1998) 696-697
    • (1998) Science , vol.280 , pp. 696-697
    • Singer, R.H.1
  • 59
    • 0023848212 scopus 로고
    • Rat hepatic glutaminase: purification and immunochemical characterization
    • Smith E.M., and Watford M. Rat hepatic glutaminase: purification and immunochemical characterization. Arch. Biochem. Biophys. 260 (1988) 740-751
    • (1988) Arch. Biochem. Biophys. , vol.260 , pp. 740-751
    • Smith, E.M.1    Watford, M.2
  • 60
    • 0025333864 scopus 로고
    • Molecular cloning of a cDNA for rat hepatic glutaminase. Sequence similarity to kidney-type glutaminase
    • Smith E.M., and Watford M. Molecular cloning of a cDNA for rat hepatic glutaminase. Sequence similarity to kidney-type glutaminase. J. Biol. Chem. 265 (1990) 10631-10636
    • (1990) J. Biol. Chem. , vol.265 , pp. 10631-10636
    • Smith, E.M.1    Watford, M.2
  • 61
    • 0027145124 scopus 로고
    • Glutamine and cancer
    • Souba W.W. Glutamine and cancer. Ann. Surg. 218 (1993) 715-728
    • (1993) Ann. Surg. , vol.218 , pp. 715-728
    • Souba, W.W.1
  • 62
    • 0028817567 scopus 로고
    • In vitro characterization of the mitochondrial processing and the potential function of the 68-kDa subunit of renal glutaminase
    • Srinivasan M., Kalousek F., and Curthoys N.P. In vitro characterization of the mitochondrial processing and the 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
  • 63
    • 64949148042 scopus 로고    scopus 로고
    • Szeliga, M., Obara-Michlewska, M., Matyja, E., Lazarczyk, M., Lobo, C., Hilgier, W., Alonso, F., Márquez, J., Albrecht, J., 2008. Transfection with liver-type glutaminase (LGA) cDNA alters gene expression and reduces viability, migration and proliferation of T98G glioma cells. Glia., ahead of print, PMID: 19062176.
    • Szeliga, M., Obara-Michlewska, M., Matyja, E., Lazarczyk, M., Lobo, C., Hilgier, W., Alonso, F., Márquez, J., Albrecht, J., 2008. Transfection with liver-type glutaminase (LGA) cDNA alters gene expression and reduces viability, migration and proliferation of T98G glioma cells. Glia., ahead of print, PMID: 19062176.
  • 64
    • 0015606174 scopus 로고
    • Purification of phosphate-dependent pig brain glutaminase
    • Svenneby G., Torgner I.Aa., and Kvamme 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.Aa.2    Kvamme, E.3
  • 65
    • 0035877665 scopus 로고    scopus 로고
    • Identification of zeta-crystallin/NADPH:quinone reductase as a renal glutaminase mRNA pH response element-binding protein
    • Tang A., and Curthoys N.P. Identification of zeta-crystallin/NADPH:quinone reductase as a renal glutaminase mRNA pH response element-binding protein. J. Biol. Chem. 276 (2001) 21375-21380
    • (2001) J. Biol. Chem. , vol.276 , pp. 21375-21380
    • Tang, A.1    Curthoys, N.P.2
  • 66
    • 0037337447 scopus 로고    scopus 로고
    • Glutaminase isoform expression in cell lines derived from human colorectal adenomas and carcinomas
    • Turner A., and McGivan J.D. Glutaminase isoform expression in cell lines derived from human colorectal adenomas and carcinomas. Biochem. J. 370 (2003) 403-408
    • (2003) Biochem. J. , vol.370 , pp. 403-408
    • Turner, A.1    McGivan, J.D.2
  • 67
    • 0027132540 scopus 로고
    • Hepatic glutaminase expression: relationship to kidney-type glutaminase and to the urea cycle
    • Watford M. Hepatic glutaminase expression: relationship to kidney-type glutaminase and to the urea cycle. FASEB J. 7 (1993) 1468-1474
    • (1993) FASEB J. , vol.7 , pp. 1468-1474
    • Watford, M.1
  • 68
    • 0028334861 scopus 로고
    • Transcriptional control of rat hepatic glutaminase expression by dietary protein level and starvation
    • Watford M., Vincent N., Zhan Z., Fannelli J., Kowalski T., and Kovacevic Z. Transcriptional control of rat hepatic glutaminase expression by dietary protein level and starvation. J. Nutr. 124 (1994) 493-499
    • (1994) J. Nutr. , vol.124 , pp. 493-499
    • Watford, M.1    Vincent, N.2    Zhan, Z.3    Fannelli, J.4    Kowalski, T.5    Kovacevic, Z.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.