메뉴 건너뛰기




Volumn 25, Issue 5, 2005, Pages 851-867

Morphological alterations and cell death provoked by the branched-chain α-amino acids accumulating in maple syrup urine disease in astrocytes from rat cerebral cortex

Author keywords

Actin; Branched chain amino acids; Creatine; Cytoskeleton; Lysophosphatidic acid; Maple syrup urine disease

Indexed keywords

ALPHA AMINO ACID; BRANCHED CHAIN AMINO ACID; CREATINE; ISOLEUCINE; LEUCINE; LYSOPHOSPHATIDIC ACID; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; VALINE;

EID: 23844540128     PISSN: 02724340     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10571-005-4938-6     Document Type: Article
Times cited : (16)

References (57)
  • 1
    • 0034471963 scopus 로고    scopus 로고
    • Neuron-astrocyte interactions: Implications for cellular energetics and antioxidant levels
    • Aschner, M. (2000). Neuron-astrocyte interactions: Implications for cellular energetics and antioxidant levels. Neurotoxicology 21:1101-1107.
    • (2000) Neurotoxicology , vol.21 , pp. 1101-1107
    • Aschner, M.1
  • 2
    • 0013966190 scopus 로고
    • Inhibition of brain protein synthesis: An approach to a biochemical basis of neurological dysfunction in the amino-acidurias
    • Appel, S. H. (1966). Inhibition of brain protein synthesis: an approach to a biochemical basis of neurological dysfunction in the amino-acidurias. Trans. N. Y. Acad. Sci. 29:63-70.
    • (1966) Trans. N. Y. Acad. Sci. , vol.29 , pp. 63-70
    • Appel, S.H.1
  • 4
    • 2842533302 scopus 로고
    • Incidence and sources of mycoplasma contamination: A brief review
    • McGarrity, G. J., Murphy, D. G., and Nichols, W. W. (eds.), Plenum Press, New York
    • Barile, M. F., Hopps, H. E., and Grabowski, M. (1978). Incidence and sources of mycoplasma contamination: a brief review. In McGarrity, G. J., Murphy, D. G., and Nichols, W. W. (eds.), Mycoplasma Infection of Cell Cultures, Plenum Press, New York, pp. 35-46.
    • (1978) Mycoplasma Infection of Cell Cultures , pp. 35-46
    • Barile, M.F.1    Hopps, H.E.2    Grabowski, M.3
  • 5
    • 0017183193 scopus 로고
    • The astroglial response to stabbing. Immunofluorescence studies with antibodies to astrocyte-specific protein (GFAP) in mammalian and submammalian vertebrates
    • Bignami, A., and Dahl, D. (1976). The astroglial response to stabbing. Immunofluorescence studies with antibodies to astrocyte-specific protein (GFAP) in mammalian and submammalian vertebrates. Neuropathol. Appl. Neurobiol. 2:99-111.
    • (1976) Neuropathol. Appl. Neurobiol. , vol.2 , pp. 99-111
    • Bignami, A.1    Dahl, D.2
  • 6
    • 0002977005 scopus 로고    scopus 로고
    • Maple syrup urine disease (branched-chain ketoaciduria)
    • Scriver, C. R., Beaudet, A. L., Sly, W. L., and Valle. D. (eds.), McGraw-Hill, New York
    • Chuang, D. T., and Shih, V. E. (2001). Maple syrup urine disease (branched-chain ketoaciduria). In Scriver, C. R., Beaudet, A. L., Sly, W. L., and Valle. D. (eds.), The Metabolic and Molecular Bases of Inherited Disease, McGraw-Hill, New York, pp. 1971-2005.
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 1971-2005
    • Chuang, D.T.1    Shih, V.E.2
  • 7
    • 0035940752 scopus 로고    scopus 로고
    • An investigation of the neuroprotective effect of lithium in organotypic slice cultures of rat hippocampus exposed to oxygen and glucose deprivation
    • Cimarosti, H., Rodnight, R., Tavares, A., Paiva, R., Valentim, L., Rocha E., and Salbego, C. (2001). An investigation of the neuroprotective effect of lithium in organotypic slice cultures of rat hippocampus exposed to oxygen and glucose deprivation. Neurosci. Lett. 315:33-36.
    • (2001) Neurosci. Lett. , vol.315 , pp. 33-36
    • Cimarosti, H.1    Rodnight, R.2    Tavares, A.3    Paiva, R.4    Valentim, L.5    Rocha, E.6    Salbego, C.7
  • 8
    • 0032213261 scopus 로고    scopus 로고
    • Cytoskeletal assembly and ATP release regulate astrocytic calcium signaling
    • Cotrina, M. L., Lin J. H., and Nedergaard, M. (1998). Cytoskeletal assembly and ATP release regulate astrocytic calcium signaling. J. Neurosci. 18:8794-8804.
    • (1998) J. Neurosci. , vol.18 , pp. 8794-8804
    • Cotrina, M.L.1    Lin, J.H.2    Nedergaard, M.3
  • 9
    • 0035001341 scopus 로고    scopus 로고
    • Glutamate uptake
    • Danbolt, N. C. (2001). Glutamate uptake. Progr. Neurobiol. 65:1-105.
    • (2001) Progr. Neurobiol. , vol.65 , pp. 1-105
    • Danbolt, N.C.1
  • 10
    • 0000299656 scopus 로고
    • Disorders of branched chain amino acid and keto acid metabolism
    • Scriver, C. R., Beaudet, A. L., Sly, W. S., and Valle, D. (eds). Mc Graw Hill, New York
    • Danner, D. J., and Elsas, J. L. (1989). Disorders of branched chain amino acid and keto acid metabolism. In Scriver, C. R., Beaudet, A. L., Sly, W. S., and Valle, D. (eds). The Metabolic Basis of Inherited Disease. Mc Graw Hill, New York, pp. 671-692.
    • (1989) The Metabolic Basis of Inherited Disease , pp. 671-692
    • Danner, D.J.1    Elsas, J.L.2
  • 11
    • 0141953237 scopus 로고    scopus 로고
    • Cytoskeletal dynamics and transport in growth cone motility and axon guidance
    • Dent, E. W., and Gestler, F. B. (2003). Cytoskeletal dynamics and transport in growth cone motility and axon guidance. Neuron 40:209-227.
    • (2003) Neuron , vol.40 , pp. 209-227
    • Dent, E.W.1    Gestler, F.B.2
  • 12
    • 0033501641 scopus 로고    scopus 로고
    • Glutamate induces rapid upregulation of astrocyte glutamate transport and cell-surface expression of GLAST
    • Duan, S., Anderson, C. M., Stein B. A., and Swanson, R. A. (1999). Glutamate induces rapid upregulation of astrocyte glutamate transport and cell-surface expression of GLAST. J. Neurosci. 19:10193-10200.
    • (1999) J. Neurosci. , vol.19 , pp. 10193-10200
    • Duan, S.1    Anderson, C.M.2    Stein, B.A.3    Swanson, R.A.4
  • 13
    • 0000130718 scopus 로고
    • Aminoaciduria
    • Efron, M. L. (1965). Aminoaciduria. N. Engl. J. Med. 272:1058-1067.
    • (1965) N. Engl. J. Med. , vol.272 , pp. 1058-1067
    • Efron, M.L.1
  • 14
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville, S., and Hall, A. (2002). Rho GTPases in cell biology. Nature 420:629-635.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 15
    • 0032568613 scopus 로고    scopus 로고
    • A single receptor encoded by vzg-l/IpAl/edg-2 couples to G proteins and mediates multiple cellular responses to lysophosphatidic acid
    • Fukushima, N., Kimura, Y., and Chun, J. (1998). A single receptor encoded by vzg-l/IpAl/edg-2 couples to G proteins and mediates multiple cellular responses to lysophosphatidic acid. Proc. Natl. Acad. Sci. U.S.A. 95:6151-6156.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6151-6156
    • Fukushima, N.1    Kimura, Y.2    Chun, J.3
  • 17
    • 9244261568 scopus 로고    scopus 로고
    • Evidence that the branched chain α-keto acids accumulating in maple syrup urine disease induce morphological alterations and death in cultured astrocytes from rat cerebral cortex
    • Funchal, C., Gottfried, C., Almeida, L. M. V., Wajner, M., and Pessoa-Pureur, R. (2004). Evidence that the branched chain α-keto acids accumulating in maple syrup urine disease induce morphological alterations and death in cultured astrocytes from rat cerebral cortex. Glia 48:230-240.
    • (2004) Glia , vol.48 , pp. 230-240
    • Funchal, C.1    Gottfried, C.2    Almeida, L.M.V.3    Wajner, M.4    Pessoa-Pureur, R.5
  • 19
    • 0033519890 scopus 로고    scopus 로고
    • Regulation of protein phosphorylation in astrocyte cultures by external calcium ions: Specific effects on the phosphorylation of GFAP, vimentin and heat shock protein 27 (HSP 27)
    • Gottfried, C., Valentim, L., Salbego, C., Karl, J., Wofchuk, S. T., and Rodnight, R. (1999). Regulation of protein phosphorylation in astrocyte cultures by external calcium ions: Specific effects on the phosphorylation of GFAP, vimentin and heat shock protein 27 (HSP 27). Brain Res. 833:142-149.
    • (1999) Brain Res. , vol.833 , pp. 142-149
    • Gottfried, C.1    Valentim, L.2    Salbego, C.3    Karl, J.4    Wofchuk, S.T.5    Rodnight, R.6
  • 20
    • 0242516021 scopus 로고    scopus 로고
    • Rho a and lysophosphatidic acid are involved in the actin cytoskeleton reorganization of astrocytes exposed to ethanol
    • Guasch, R. M., Tomas, M., Miñambres, R., Valles, S., Renau-Piqueras, J., and Guerri, C. (2003). Rho A and lysophosphatidic acid are involved in the actin cytoskeleton reorganization of astrocytes exposed to ethanol. J. Neurosci. Res. 72:487-502.
    • (2003) J. Neurosci. Res. , vol.72 , pp. 487-502
    • Guasch, R.M.1    Tomas, M.2    Miñambres, R.3    Valles, S.4    Renau-Piqueras, J.5    Guerri, C.6
  • 21
    • 0016259467 scopus 로고
    • Inhibition of mitochondrial pyruvate transport by phenylpyruvate and α-ketoisocaproate
    • Halestrap, A., Brand M. D., and Denton, R. M. (1974). Inhibition of mitochondrial pyruvate transport by phenylpyruvate and α-ketoisocaproate. Biochem. Biophys. Acta 367:102-108.
    • (1974) Biochem. Biophys. Acta , vol.367 , pp. 102-108
    • Halestrap, A.1    Brand, M.D.2    Denton, R.M.3
  • 22
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. (1998). Rho GTPases and the actin cytoskeleton. Science 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 23
    • 1642503683 scopus 로고    scopus 로고
    • Intermediate filaments are dynamic and motile elements of cellular architecture
    • Helfand, B. T., Chang, L., and Goldman, R. D. (2004). Intermediate filaments are dynamic and motile elements of cellular architecture. J. Cell Sci. 117:133-141.
    • (2004) J. Cell Sci. , vol.117 , pp. 133-141
    • Helfand, B.T.1    Chang, L.2    Goldman, R.D.3
  • 24
    • 0001234745 scopus 로고
    • Influence of alpha-ketoacids on the respiration of brain in vitro
    • Howell, R. K., and Lee, M. (1963). Influence of alpha-ketoacids on the respiration of brain in vitro. Proc. Soc. Exp. Biol. Med. 113:660-663.
    • (1963) Proc. Soc. Exp. Biol. Med. , vol.113 , pp. 660-663
    • Howell, R.K.1    Lee, M.2
  • 25
    • 0034108632 scopus 로고    scopus 로고
    • Branched chain amino acids induce apoptosis in neural cells without mitochondrial membrane depolarization or cytochrome c release: Implications for neurological impairment associated with maple syrup urine disease
    • Jouvet, P., Rustin, P., Taylor, D. L., Pocock, J. M., Felderhoff-Mueser, U., Mazarakis, N. D., Sarrat, C., Joashi, U., Kozma, M., Greewood, K., Edwards A. D., and Mehmet, H. (2000). Branched chain amino acids induce apoptosis in neural cells without mitochondrial membrane depolarization or cytochrome c release: Implications for neurological impairment associated with maple syrup urine disease. Mol. Biol. Cell 11:1919-1932.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1919-1932
    • Jouvet, P.1    Rustin, P.2    Taylor, D.L.3    Pocock, J.M.4    Felderhoff-Mueser, U.5    Mazarakis, N.D.6    Sarrat, C.7    Joashi, U.8    Kozma, M.9    Greewood, K.10    Edwards, A.D.11    Mehmet, H.12
  • 26
    • 0026608780 scopus 로고
    • Transient ischemia stimulate glial fibrillary acidic protein and vimentin gene expression in the gerbil neocortex, striatum and hippocampus
    • Kindy, M. S., Bhat, A. N., and Bhat, N. R. (1992). Transient ischemia stimulate glial fibrillary acidic protein and vimentin gene expression in the gerbil neocortex, striatum and hippocampus. Mol. Brain Res. 13:199-206.
    • (1992) Mol. Brain Res. , vol.13 , pp. 199-206
    • Kindy, M.S.1    Bhat, A.N.2    Bhat, N.R.3
  • 27
    • 0035052469 scopus 로고    scopus 로고
    • Enhanced neuronal protection from oxidative stress by coculture with glutamic acid decarboxylase-expression astrocytes
    • Lamigeon, C., Bellier, J. P., Sacchettoni, S., Rujano, M., and Jacquemont, B. (2001). Enhanced neuronal protection from oxidative stress by coculture with glutamic acid decarboxylase-expression astrocytes. J. Neurochem. 77:598-606.
    • (2001) J. Neurochem. , vol.77 , pp. 598-606
    • Lamigeon, C.1    Bellier, J.P.2    Sacchettoni, S.3    Rujano, M.4    Jacquemont, B.5
  • 28
    • 0017258183 scopus 로고
    • Control of pyruvate and β-hydroxy-butyrate utilization in rat brain mitochondria and its relevance to phenylketonuria and maple syrup urine disease
    • Land, J. M., Mowbray, J., and Clark, J. B. (1976). Control of pyruvate and β-hydroxy-butyrate utilization in rat brain mitochondria and its relevance to phenylketonuria and maple syrup urine disease. J. Neurochem. 26:823-830.
    • (1976) J. Neurochem. , vol.26 , pp. 823-830
    • Land, J.M.1    Mowbray, J.2    Clark, J.B.3
  • 30
    • 0036441201 scopus 로고    scopus 로고
    • Actin cytoskeleton regulation in neuronal morpho genesis and structural plasticity
    • Luo, L. (2002). Actin cytoskeleton regulation in neuronal morpho genesis and structural plasticity. Annu. Rev. Cell Dev. Biol. 18:601-635.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 601-635
    • Luo, L.1
  • 32
    • 2642640420 scopus 로고    scopus 로고
    • Lysophosphatidic acid stimulates actomyosin contraction in astrocytes
    • Manning, T. J., Rosenfeld, S. S., and Sontheimer, H. (1998). Lysophosphatidic acid stimulates actomyosin contraction in astrocytes. J. Neurosci. Res. 53:343-352.
    • (1998) J. Neurosci. Res. , vol.53 , pp. 343-352
    • Manning, T.J.1    Rosenfeld, S.S.2    Sontheimer, H.3
  • 33
    • 0141533205 scopus 로고    scopus 로고
    • New roles for astrocytes: Redefining the functional architecture of the brain
    • Nedergaard, M., Ranson, B., and Goldman, S. A. (2003). New roles for astrocytes: Redefining the functional architecture of the brain. Trends Neurosci. 26:523-530.
    • (2003) Trends Neurosci. , vol.26 , pp. 523-530
    • Nedergaard, M.1    Ranson, B.2    Goldman, S.A.3
  • 34
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D., and Hall, A. (1995). Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 36
    • 0037403502 scopus 로고    scopus 로고
    • Creatine kinase activity from rat brain is inhibited by branched-chain amino acids in vitro
    • Pilla, C., Cardozo, R. F., Dutra-Filho, C. S., Wyse, A. T., Wajner, M., and Wannmacher, C. M. (2003). Creatine kinase activity from rat brain is inhibited by branched-chain amino acids in vitro. Neurochem. Res. 28:675-679.
    • (2003) Neurochem. Res. , vol.28 , pp. 675-679
    • Pilla, C.1    Cardozo, R.F.2    Dutra-Filho, C.S.3    Wyse, A.T.4    Wajner, M.5    Wannmacher, C.M.6
  • 37
    • 0029834061 scopus 로고    scopus 로고
    • Selective N-type calcium channel antagonist omega-conotoxin MVIIA is neuroprotective against hypoxic neurodegeneration in organotypic hippocampal slices cultures
    • Pringle, A., Benhan, C., Sim, L., Kennedy, J., Iannoti, F., and Sundstrom, L. (1996). Selective N-type calcium channel antagonist omega-conotoxin MVIIA is neuroprotective against hypoxic neurodegeneration in organotypic hippocampal slices cultures. Stroke 27:2124-2130.
    • (1996) Stroke , vol.27 , pp. 2124-2130
    • Pringle, A.1    Benhan, C.2    Sim, L.3    Kennedy, J.4    Iannoti, F.5    Sundstrom, L.6
  • 38
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J., and Hall, A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 39
    • 0028321785 scopus 로고
    • Signal transduction pathways regulating Rho-mediated stress fiber formation: Requirement for tyrosine kinase
    • Ridley, A. J., and Hall, A. (1994). Signal transduction pathways regulating Rho-mediated stress fiber formation: Requirement for tyrosine kinase. EMBO J. 13:2600-2610.
    • (1994) EMBO J. , vol.13 , pp. 2600-2610
    • Ridley, A.J.1    Hall, A.2
  • 40
    • 0035960736 scopus 로고    scopus 로고
    • An epithelial cell destined for apoptosis signals its neighbors to extrude it by an actin- and myosin-dependent mechanism
    • Rosenblatt, J., Raff, M. C., and Cramer, L. P. (2001). An epithelial cell destined for apoptosis signals its neighbors to extrude it by an actin- and myosin-dependent mechanism. Curr. Biol. 11:1847-1857.
    • (2001) Curr. Biol. , vol.11 , pp. 1847-1857
    • Rosenblatt, J.1    Raff, M.C.2    Cramer, L.P.3
  • 41
  • 42
    • 0036785111 scopus 로고    scopus 로고
    • Diffusion magnetic resonance imaging in intermediate form of maple syrup urine disease
    • Sener, R. N. (2002). Diffusion magnetic resonance imaging in intermediate form of maple syrup urine disease. J. Neuroimaging 12:368-370.
    • (2002) J. Neuroimaging , vol.12 , pp. 368-370
    • Sener, R.N.1
  • 45
    • 0001760204 scopus 로고
    • Maple syrup urine disease, with particular reference to dietotherapy
    • Snyderman, E., Norton, P. M., and Roitman, B. (1964). Maple syrup urine disease, with particular reference to dietotherapy. Pediatrics 34:454-472.
    • (1964) Pediatrics , vol.34 , pp. 454-472
    • Snyderman, E.1    Norton, P.M.2    Roitman, B.3
  • 46
    • 0023951297 scopus 로고
    • Molecular and cellular biology of intermediate filaments
    • Steinert, P. M., and Roop, D. R. (1988). Molecular and cellular biology of intermediate filaments. Annu. Ver. Biochem. 57:593-625.
    • (1988) Annu. Ver. Biochem. , vol.57 , pp. 593-625
    • Steinert, P.M.1    Roop, D.R.2
  • 47
    • 0031260271 scopus 로고    scopus 로고
    • Astrocyte spreading in response to thrombin and lysophosphatidic acid is dependent on the Rho GTPase
    • Suidan, H. S., Nobes, C. D., Hall, A., and Monard, D. (1997). Astrocyte spreading in response to thrombin and lysophosphatidic acid is dependent on the Rho GTPase. Glia 21:244-252.
    • (1997) Glia , vol.21 , pp. 244-252
    • Suidan, H.S.1    Nobes, C.D.2    Hall, A.3    Monard, D.4
  • 48
    • 0020606605 scopus 로고
    • Abnormal protein and lipidic composition of the cerebral myelin of a patient with maple syrup urine disease
    • Taketomi, T., Kunishita, T., Hara, A., and Mizushima, S. (1983). Abnormal protein and lipidic composition of the cerebral myelin of a patient with maple syrup urine disease. Jpn. J. Exp. Med. 53:109-116.
    • (1983) Jpn. J. Exp. Med. , vol.53 , pp. 109-116
    • Taketomi, T.1    Kunishita, T.2    Hara, A.3    Mizushima, S.4
  • 49
    • 0000819855 scopus 로고
    • Inhibition of brain glutamic acid descarboxylase by phenylalanine, leucine and valine derivates: A suggestion concerning the neurological defect in phenylketonuria and branched-chain keto aciduria
    • Tashian, R. (1961). Inhibition of brain glutamic acid descarboxylase by phenylalanine, leucine and valine derivates: A suggestion concerning the neurological defect in phenylketonuria and branched-chain keto aciduria. Metabolism 10:393-400.
    • (1961) Metabolism , vol.10 , pp. 393-400
    • Tashian, R.1
  • 50
    • 0026553444 scopus 로고
    • Maple syrup urine disease: Interrelations between branched-chain amino-, oxo- and hydroxyacids; implications for treatment; associations with CNS dysmyelination
    • Treacy, E., Clow, C. L., Reade, T. R., Chitayat, D., Mamer, O. A., and Scriver, C. R. (1992). Maple syrup urine disease: Interrelations between branched-chain amino-, oxo- and hydroxyacids; implications for treatment; associations with CNS dysmyelination. J. Inherit. Metab. Dis. 15:121-135.
    • (1992) J. Inherit. Metab. Dis. , vol.15 , pp. 121-135
    • Treacy, E.1    Clow, C.L.2    Reade, T.R.3    Chitayat, D.4    Mamer, O.A.5    Scriver, C.R.6
  • 51
    • 0020552907 scopus 로고
    • Myelin proteins: Degradation in rat brain initiated by metabolites causative of maple syrup urine disease
    • Tribble, D., and Shapira, R. (1983). Myelin proteins: Degradation in rat brain initiated by metabolites causative of maple syrup urine disease. Biochem. Biophys. Res. Commun. 114:440-446.
    • (1983) Biochem. Biophys. Res. Commun. , vol.114 , pp. 440-446
    • Tribble, D.1    Shapira, R.2
  • 52
    • 0023845966 scopus 로고
    • CT and MRI in maple syrup urine disease
    • Uziel, G., Savoiardo, M., and Nardocci. N. (1988). CT and MRI in maple syrup urine disease. Neurology 38:486-488.
    • (1988) Neurology , vol.38 , pp. 486-488
    • Uziel, G.1    Savoiardo, M.2    Nardocci, N.3
  • 54
    • 0032989964 scopus 로고    scopus 로고
    • Reduction of plasma concentrations of large neutral amino acids in patients with maple urine disease during crises
    • Wajner, M., and Vargas, C. R. (1999). Reduction of plasma concentrations of large neutral amino acids in patients with maple urine disease during crises. Arch. Dis. Child 80:579.
    • (1999) Arch. Dis. Child , vol.80 , pp. 579
    • Wajner, M.1    Vargas, C.R.2
  • 55
    • 0033913801 scopus 로고    scopus 로고
    • Reduction of large neutral amino acid concentration in plasma and CSF of patients with maple syrup urine disease during crises
    • Wajner, M., Coelho, D. M., Barschak, A. G., Araújo, P. R., Pires, R. F., Lulhier, F. L. G., and Vargas, C. R. (2000). Reduction of large neutral amino acid concentration in plasma and CSF of patients with maple syrup urine disease during crises. J. Inher. Met. Dis. 23:505-512.
    • (2000) J. Inher. Met. Dis. , vol.23 , pp. 505-512
    • Wajner, M.1    Coelho, D.M.2    Barschak, A.G.3    Araújo, P.R.4    Pires, R.F.5    Lulhier, F.L.G.6    Vargas, C.R.7
  • 56
    • 0031239010 scopus 로고    scopus 로고
    • Brain metabolism of branched-chain amino acids
    • Yudkoff, M. (1997). Brain metabolism of branched-chain amino acids. Glia 21:92-98.
    • (1997) Glia , vol.21 , pp. 92-98
    • Yudkoff, M.1
  • 57
    • 0030021649 scopus 로고    scopus 로고
    • Signal transduction and actin filament organization
    • Zigmond, S. H. (1996). Signal transduction and actin filament organization. Curr. Opin. Cell Biol. 8:66-73.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 66-73
    • Zigmond, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.