메뉴 건너뛰기




Volumn 20, Issue 10, 2004, Pages 942-947

Essential fatty acids in Huntington's disease

Author keywords

amyloid fibrils; apoptosis; docosahexaenoic acid; eicosapentaenoic acid; essential fatty acids; huntingtin; Huntington's disease; polyQ peptides; ubiquitin proteasome system

Indexed keywords

ESSENTIAL FATTY ACID;

EID: 4944230131     PISSN: 08999007     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nut.2004.06.017     Document Type: Article
Times cited : (29)

References (54)
  • 2
    • 0033757718 scopus 로고    scopus 로고
    • Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice
    • Dragatsis I., Levine M.S., Zeitlin S. Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice. Nat Genet. 26:2000;300-306
    • (2000) Nat Genet , vol.26 , pp. 300-306
    • Dragatsis, I.1    Levine, M.S.2    Zeitlin, S.3
  • 3
    • 0038701684 scopus 로고    scopus 로고
    • Huntingtin aggregation and toxicity in Huntington's disease
    • Bates G. Huntingtin aggregation and toxicity in Huntington's disease. Lancet. 361:2003;1642-1644
    • (2003) Lancet , vol.361 , pp. 1642-1644
    • Bates, G.1
  • 4
    • 0036850529 scopus 로고    scopus 로고
    • Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells
    • Yang W., Dunlap J.R., Andrews R.B., Wetzel R. Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells. Hum Mol Genet. 11:2002;2905-2917
    • (2002) Hum Mol Genet , vol.11 , pp. 2905-2917
    • Yang, W.1    Dunlap, J.R.2    Andrews, R.B.3    Wetzel, R.4
  • 5
    • 0035800572 scopus 로고    scopus 로고
    • Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity
    • Chen S., Berthelier V., Yang W., Wetzel R. Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity. J Mol Biol. 311:2001;173-182
    • (2001) J Mol Biol , vol.311 , pp. 173-182
    • Chen, S.1    Berthelier, V.2    Yang, W.3    Wetzel, R.4
  • 6
    • 0035084096 scopus 로고    scopus 로고
    • Solubilization and disaggregation of polyglutamine peptides
    • Chen S., Wetzel R. Solubilization and disaggregation of polyglutamine peptides. Protein Sci. 10:2001;887-891
    • (2001) Protein Sci , vol.10 , pp. 887-891
    • Chen, S.1    Wetzel, R.2
  • 7
    • 0033551063 scopus 로고    scopus 로고
    • Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: Implications for Huntington's disease pathology
    • Scherzinger E., Sittler A., Schweiger K., et al. Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology. Proc Natl Acad Sci USA. 96:1999;4604-4609
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4604-4609
    • Scherzinger, E.1    Sittler, A.2    Schweiger, K.3
  • 8
    • 18544379477 scopus 로고    scopus 로고
    • A bivalent Huntingtin binding peptide suppresses polyglutamine aggregation and pathogenesis in Drosophila
    • Kazantsev A., Walker H.A., Slepko N., et al. A bivalent Huntingtin binding peptide suppresses polyglutamine aggregation and pathogenesis in Drosophila. Nat Genet. 30:2002;367-376
    • (2002) Nat Genet , vol.30 , pp. 367-376
    • Kazantsev, A.1    Walker, H.A.2    Slepko, N.3
  • 9
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • Sanchez I., Mahlke C., Yuan J. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature. 421:2003;373-379
    • (2003) Nature , vol.421 , pp. 373-379
    • Sanchez, I.1    Mahlke, C.2    Yuan, J.3
  • 10
    • 0035937523 scopus 로고    scopus 로고
    • Interference by huntingtin and atophin-1 with CBP-mediated transcription leading to cellular toxicity
    • Nucifora F.C., Sasaki M., Peters M.F., et al. Interference by huntingtin and atophin-1 with CBP-mediated transcription leading to cellular toxicity. Science. 291:2001;2423-2428
    • (2001) Science , vol.291 , pp. 2423-2428
    • Nucifora, F.C.1    Sasaki, M.2    Peters, M.F.3
  • 11
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science. 292:2001;1552-1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 12
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • Perutz M.F., Johnson T., Suzuki M., Finch J.T. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc Natl Acad Sci USA. 91:1994;5355-5358
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 13
    • 0033613212 scopus 로고    scopus 로고
    • Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cells
    • Kazantsev A., Preisinger E., Dranovsky A., Goldgaber D., Housman D. Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cells. Proc Natl Acad Sci USA. 96:1999;11404-11409
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11404-11409
    • Kazantsev, A.1    Preisinger, E.2    Dranovsky, A.3    Goldgaber, D.4    Housman, D.5
  • 14
    • 0034285017 scopus 로고    scopus 로고
    • CREB-binding protein sequestration by expanded polyglutamine
    • McCampbell A., Taylor J.P., Taye A.A., et al. CREB-binding protein sequestration by expanded polyglutamine. Hum Mol Genet. 9:2000;2197-2202
    • (2000) Hum Mol Genet , vol.9 , pp. 2197-2202
    • McCampbell, A.1    Taylor, J.P.2    Taye, A.A.3
  • 15
    • 0033818112 scopus 로고    scopus 로고
    • Expanded polyglutamine stretches interact with TAFII130, interfering with CREB-dependent transcription
    • Shimohata T., Nakajima T., Yamada M., et al. Expanded polyglutamine stretches interact with TAFII130, interfering with CREB-dependent transcription. Nat Genet. 26:2000;29-36
    • (2000) Nat Genet , vol.26 , pp. 29-36
    • Shimohata, T.1    Nakajima, T.2    Yamada, M.3
  • 16
    • 12944263711 scopus 로고    scopus 로고
    • The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription
    • Steffan J.S., Kazantsev A., Spasic-Boskovic O., et al. The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc Natl Acad Sci USA. 97:2000;6763-6768
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6763-6768
    • Steffan, J.S.1    Kazantsev, A.2    Spasic-Boskovic, O.3
  • 17
    • 0034702030 scopus 로고    scopus 로고
    • Decreased expression of striatal signaling genes in a mouse model of Huntington's disease
    • Luthi-Carter R., Strand A., Peters N.L., et al. Decreased expression of striatal signaling genes in a mouse model of Huntington's disease. Hum Mol Genet. 9:2000;1259-1271
    • (2000) Hum Mol Genet , vol.9 , pp. 1259-1271
    • Luthi-Carter, R.1    Strand, A.2    Peters, N.L.3
  • 18
    • 0028957560 scopus 로고
    • Reduced expression of preproenkephalin in striated neurons from Huntington's disease patients
    • Richfield E.K., Maguire-Zeiss K.A., Cox C., Gilmore J., Voorn P. Reduced expression of preproenkephalin in striated neurons from Huntington's disease patients. Ann Neurol. 37:1995;335-343
    • (1995) Ann Neurol , vol.37 , pp. 335-343
    • Richfield, E.K.1    Maguire-Zeiss, K.A.2    Cox, C.3    Gilmore, J.4    Voorn, P.5
  • 19
    • 0034595722 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor in Huntington disease
    • Ferrer I., Goutan E., Marin C., Rey M.J., Ribalta T. Brain-derived neurotrophic factor in Huntington disease. Brain Res. 866:2000;257-261
    • (2000) Brain Res , vol.866 , pp. 257-261
    • Ferrer, I.1    Goutan, E.2    Marin, C.3    Rey, M.J.4    Ribalta, T.5
  • 20
    • 0033614761 scopus 로고    scopus 로고
    • Altered neurotransmitter receptor expression in transgenic mouse models of Huntington's disease
    • Cha J.H., Frey A.S., Alsdorf S.A., et al. Altered neurotransmitter receptor expression in transgenic mouse models of Huntington's disease. Phil Trans R Soc Lond B Biol Sci. 354:1999;981-989
    • (1999) Phil Trans R Soc Lond B Biol Sci , vol.354 , pp. 981-989
    • Cha, J.H.1    Frey, A.S.2    Alsdorf, S.A.3
  • 21
    • 0034048845 scopus 로고    scopus 로고
    • Decrease in striatal enkephalin mRNA in mouse models of Huntington's disease
    • Menalled L., Zanjani H., MacKenzie L., et al. Decrease in striatal enkephalin mRNA in mouse models of Huntington's disease. Exp Neurol. 162:2000;328-342
    • (2000) Exp Neurol , vol.162 , pp. 328-342
    • Menalled, L.1    Zanjani, H.2    MacKenzie, L.3
  • 22
    • 0035348156 scopus 로고    scopus 로고
    • Aberrant amplification of A92A receptor signaling in striatal cells expressing mutant huntingtin
    • Varani K., Rigamonti D., Sipione S., et al. Aberrant amplification of A92A receptor signaling in striatal cells expressing mutant huntingtin. FASEB J. 15:2001;1245-1247
    • (2001) FASEB J , vol.15 , pp. 1245-1247
    • Varani, K.1    Rigamonti, D.2    Sipione, S.3
  • 23
    • 0038231381 scopus 로고    scopus 로고
    • Adenosine receptors and Huntington's disease: Implications for pathogenesis and therapeutics
    • Blum D., Hourez R., Galas M.C., Popoli P., Schiffmann S.N. Adenosine receptors and Huntington's disease: implications for pathogenesis and therapeutics. Lancet Neurol. 2:2003;366-374
    • (2003) Lancet Neurol , vol.2 , pp. 366-374
    • Blum, D.1    Hourez, R.2    Galas, M.C.3    Popoli, P.4    Schiffmann, S.N.5
  • 24
    • 0029205479 scopus 로고
    • The nervous system has an absolute molecular species requirement for proper function
    • Salem N., Niebylski C.D. The nervous system has an absolute molecular species requirement for proper function. Mol Membr Biol. 12:1995;131-134
    • (1995) Mol Membr Biol , vol.12 , pp. 131-134
    • Salem, N.1    Niebylski, C.D.2
  • 25
    • 0034653210 scopus 로고    scopus 로고
    • Essential fatty acids, lipid membrane abnormalities and the diagnosis and treatment of schizophrenia
    • Fenton W.S., Hibbeln J., Knable M. Essential fatty acids, lipid membrane abnormalities and the diagnosis and treatment of schizophrenia. Biol Psychiatry. 47:2000;8-21
    • (2000) Biol Psychiatry , vol.47 , pp. 8-21
    • Fenton, W.S.1    Hibbeln, J.2    Knable, M.3
  • 26
    • 0026337465 scopus 로고
    • Essential fatty acids: Biology and their clinical implications
    • Das U.N. Essential fatty acids: biology and their clinical implications. Asian Pac J Pharmacol. 6:1991;317-330
    • (1991) Asian Pac J Pharmacol , vol.6 , pp. 317-330
    • Das, U.N.1
  • 27
    • 0342635463 scopus 로고    scopus 로고
    • Striatal oxidative damage parallels the expression of a neurological phenotype in mice transgenic for the mutation of Huntington's disease
    • Perez-Severiano F., Rios C., Segovia J. Striatal oxidative damage parallels the expression of a neurological phenotype in mice transgenic for the mutation of Huntington's disease. Brain Res. 862:2000;234-237
    • (2000) Brain Res , vol.862 , pp. 234-237
    • Perez-Severiano, F.1    Rios, C.2    Segovia, J.3
  • 28
    • 0021235056 scopus 로고
    • Essential fatty acids and neuroleptic drug induced tardive dyskinesia-preliminary clinical observations
    • Vaddadi K.S. Essential fatty acids and neuroleptic drug induced tardive dyskinesia-preliminary clinical observations. IRCS Med Sci. 12:1984;678-679
    • (1984) IRCS Med Sci , vol.12 , pp. 678-679
    • Vaddadi, K.S.1
  • 29
    • 0029421079 scopus 로고
    • Schizophrenic symptoms and dietary intake of N-3 fatty acids
    • Mellor J.E., Laugharne D.E.J., Peet M. Schizophrenic symptoms and dietary intake of N-3 fatty acids. Schizophr Res. 18:1995;85-86
    • (1995) Schizophr Res , vol.18 , pp. 85-86
    • Mellor, J.E.1    Laugharne, D.E.J.2    Peet, M.3
  • 30
    • 0002293456 scopus 로고
    • Tardive dyskinesia and essential fatty acids: An animal model study
    • D.F. Horrobin. Montreal, Canada: Eden Press
    • Nohria V., Vaddadi K.S. Tardive dyskinesia and essential fatty acids: an animal model study. Horrobin D.F. Clinical uses of essential fatty acids. 1982;199-204 Eden Press, Montreal, Canada
    • (1982) Clinical Uses of Essential Fatty Acids , pp. 199-204
    • Nohria, V.1    Vaddadi, K.S.2
  • 31
    • 0021717997 scopus 로고
    • The antidyskinetic action of dihomo-gamma-linolenic acid in rodent
    • Costall B.M., Kelly E., Naylor R.J. The antidyskinetic action of dihomo-gamma-linolenic acid in rodent. Br J Pharmacol. 83:1984;733-740
    • (1984) Br J Pharmacol , vol.83 , pp. 733-740
    • Costall, B.M.1    Kelly, E.2    Naylor, R.J.3
  • 32
    • 0024602813 scopus 로고
    • A double-blind trial of essential fatty acid supplementation in patients with tardive dyskinesia
    • Vaddadi K.S., Courtney P., Gilleard C.J., Manku M.S., Horrobin D.F. A double-blind trial of essential fatty acid supplementation in patients with tardive dyskinesia. Psychiatry Res. 27:1989;313-323
    • (1989) Psychiatry Res , vol.27 , pp. 313-323
    • Vaddadi, K.S.1    Courtney, P.2    Gilleard, C.J.3    Manku, M.S.4    Horrobin, D.F.5
  • 34
    • 0002376807 scopus 로고    scopus 로고
    • Essential fatty acids and movement disorders
    • M. Peet, I. Glen, & D.F. Horrobin. Carnforth, UK: Marius Press
    • Vaddadi K. Essential fatty acids and movement disorders. Peet M., Glen I., Horrobin D.F. Phospholipids spectrum disorders in psychiatry. 1999;285-296 Marius Press, Carnforth, UK
    • (1999) Phospholipids Spectrum Disorders in Psychiatry , pp. 285-296
    • Vaddadi, K.1
  • 35
    • 0029767060 scopus 로고    scopus 로고
    • Dyskinesias and their treatment with essential fatty acids
    • Vaddadi K.S. Dyskinesias and their treatment with essential fatty acids. Prostaglandins Leukot Essen Fatty Acids. 55:1996;89-94
    • (1996) Prostaglandins Leukot Essen Fatty Acids , vol.55 , pp. 89-94
    • Vaddadi, K.S.1
  • 36
    • 0037148140 scopus 로고    scopus 로고
    • A randomized, placebo-controlled, double-blind study of treatment of Huntington's disease with unsaturated fatty acids
    • Vaddadi K.S., Soosai E., Chiu E., Dingjan P. A randomized, placebo-controlled, double-blind study of treatment of Huntington's disease with unsaturated fatty acids. Neuroreport. 13:2002;29-33
    • (2002) Neuroreport , vol.13 , pp. 29-33
    • Vaddadi, K.S.1    Soosai, E.2    Chiu, E.3    Dingjan, P.4
  • 37
    • 0037148131 scopus 로고    scopus 로고
    • MRI and neuropsychological improvement in Huntington disease following ethyl-EPA treatment
    • Puri B.K., Bydder G.M., Counsell S.J., et al. MRI and neuropsychological improvement in Huntington disease following ethyl-EPA treatment. Neuroreport. 13:2002;1-4
    • (2002) Neuroreport , vol.13 , pp. 1-4
    • Puri, B.K.1    Bydder, G.M.2    Counsell, S.J.3
  • 38
    • 4944236582 scopus 로고    scopus 로고
    • Essential fatty acids in the treatment of Huntington's disease
    • M. Peet, I. Glen, & D.F. Horrobin. Carnforth, UK: Marius Press
    • Vaddadi K. Essential fatty acids in the treatment of Huntington's disease. Peet M., Glen I., Horrobin D.F. Phospholipids spectrum disorders in psychiatry and neurology. 2nd ed.:2003;565-574 Marius Press, Carnforth, UK
    • (2003) Phospholipids Spectrum Disorders in Psychiatry and Neurology 2nd Ed. , pp. 565-574
    • Vaddadi, K.1
  • 39
    • 0037126988 scopus 로고    scopus 로고
    • Essential fatty acids given from conception prevent topographies of motor deficit in a transgenic model of Huntington's disease
    • Clifford J.J., Drago J., Natoli A.L., et al. Essential fatty acids given from conception prevent topographies of motor deficit in a transgenic model of Huntington's disease. Neuroscience. 109:2002;81-88
    • (2002) Neuroscience , vol.109 , pp. 81-88
    • Clifford, J.J.1    Drago, J.2    Natoli, A.L.3
  • 41
    • 0242664799 scopus 로고    scopus 로고
    • Identification of residues and domains of Raf important for function in vivo and in vitro
    • Harding A., Hsu V., Kornfeld K., Hancock J.F. Identification of residues and domains of Raf important for function in vivo and in vitro. J Biol Chem. 278:2003;45519-45527
    • (2003) J Biol Chem , vol.278 , pp. 45519-45527
    • Harding, A.1    Hsu, V.2    Kornfeld, K.3    Hancock, J.F.4
  • 43
    • 0030014380 scopus 로고    scopus 로고
    • Phospholipase A(2) and lipids as potential modulators of c-Raf 1 kinase
    • Bonventre J.V., Kyriakis J.M., Spech R., Witzgall R., Force T. Phospholipase A(2) and lipids as potential modulators of c-Raf 1 kinase. Am J Ther. 3:1996;287-293
    • (1996) Am J Ther , vol.3 , pp. 287-293
    • Bonventre, J.V.1    Kyriakis, J.M.2    Spech, R.3    Witzgall, R.4    Force, T.5
  • 44
    • 0034634590 scopus 로고    scopus 로고
    • Inhibition of neuronal apoptosis by docosahexaenoic acid (22: 6 n-3)
    • Kim H.-Y., Akbar M., Lau A., Edsall L. Inhibition of neuronal apoptosis by docosahexaenoic acid (22: 6 n-3). J Biol Chem. 275:2000;35215-35223
    • (2000) J Biol Chem , vol.275 , pp. 35215-35223
    • Kim, H.-Y.1    Akbar, M.2    Lau, A.3    Edsall, L.4
  • 45
    • 0037072813 scopus 로고    scopus 로고
    • Apoptotic changes in the aged brain are triggered by interlukin-1β- induced activation of p38 and reversed by treatment with eicosapentaenoic acid
    • Martin D.S.D., Lonergan P.E., Boland B., et al. Apoptotic changes in the aged brain are triggered by interlukin-1β-induced activation of p38 and reversed by treatment with eicosapentaenoic acid. J Biol Chem. 277:2002;34239-34246
    • (2002) J Biol Chem , vol.277 , pp. 34239-34246
    • Martin, D.S.D.1    Lonergan, P.E.2    Boland, B.3
  • 46
    • 0037036429 scopus 로고    scopus 로고
    • Neuroprotective effect of eicosapentaenoic acid in hippocampus of rats exposed to γ-irradiation
    • Lonergan P.E., Martin D.S.D., Horrobin D.F., Lynch M.A. Neuroprotective effect of eicosapentaenoic acid in hippocampus of rats exposed to γ-irradiation. J Biol Chem. 277:2002;20804-20811
    • (2002) J Biol Chem , vol.277 , pp. 20804-20811
    • Lonergan, P.E.1    Martin, D.S.D.2    Horrobin, D.F.3    Lynch, M.A.4
  • 47
    • 0037155879 scopus 로고    scopus 로고
    • The oxidized lipid and lipoxygenase product 12(S)-hydroxyeicosatetraenoic acid induces hypertrophy and fibronectin transcription in vascular smooth muscle cells via p38 MAPK and cAMP response element-binding protein activation
    • Reddy M.A., Pushpa-Rekha T., Lanting L., Nadler J.L., Fatima S., Natarajan R. The oxidized lipid and lipoxygenase product 12(S)- hydroxyeicosatetraenoic acid induces hypertrophy and fibronectin transcription in vascular smooth muscle cells via p38 MAPK and cAMP response element-binding protein activation. J Biol Chem. 277:2002;9920-9928
    • (2002) J Biol Chem , vol.277 , pp. 9920-9928
    • Reddy, M.A.1    Pushpa-Rekha, T.2    Lanting, L.3    Nadler, J.L.4    Fatima, S.5    Natarajan, R.6
  • 48
    • 0035902487 scopus 로고    scopus 로고
    • Prostaglandins are required for CREB activation and cellular proliferation during liver regeneration
    • Rudnick D.A., Perlmutter D.H., Muglia L.J. Prostaglandins are required for CREB activation and cellular proliferation during liver regeneration. Proc Natl Acad Sci USA. 98:2001;8885-8890
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8885-8890
    • Rudnick, D.A.1    Perlmutter, D.H.2    Muglia, L.J.3
  • 49
    • 0037223545 scopus 로고    scopus 로고
    • Long-chain polyunsaturated fatty acids in the growth and development of the brain and memory
    • Das U.N. Long-chain polyunsaturated fatty acids in the growth and development of the brain and memory. Nutrition. 19:2003;62-65
    • (2003) Nutrition , vol.19 , pp. 62-65
    • Das, U.N.1
  • 50
    • 0034652238 scopus 로고    scopus 로고
    • Proteasome inhibition of neuronal cells induces proinflammatory response manifested by upregulation of cyclooxygenase-2, its accumulation as ubiquitin conjugates, and production of the prostaglandin PGE(2)
    • Rockwell P., Yuan H., Magnusson R., Figueiredo-Pereira M.E. Proteasome inhibition of neuronal cells induces proinflammatory response manifested by upregulation of cyclooxygenase-2, its accumulation as ubiquitin conjugates, and production of the prostaglandin PGE(2). Arch Biochem Biophys. 374:2000;325-333
    • (2000) Arch Biochem Biophys , vol.374 , pp. 325-333
    • Rockwell, P.1    Yuan, H.2    Magnusson, R.3    Figueiredo-Pereira, M.E.4
  • 51
    • 0034817082 scopus 로고    scopus 로고
    • Downregulation of ubiquitin-dependent proteolysis by eicosapentaenoic acid in acute starvation
    • Whitehouse A.S., Tisdale M.J. Downregulation of ubiquitin-dependent proteolysis by eicosapentaenoic acid in acute starvation. Biochem Biophys Res Commun. 285:2001;598-602
    • (2001) Biochem Biophys Res Commun , vol.285 , pp. 598-602
    • Whitehouse, A.S.1    Tisdale, M.J.2
  • 54
    • 0025074323 scopus 로고
    • Effects of membrane polyunsaturated fatty acids on adenosine receptor function in intact N1E-115 neuroblastoma cells
    • Murphy M.G., Byczko Z. Effects of membrane polyunsaturated fatty acids on adenosine receptor function in intact N1E-115 neuroblastoma cells. Biochem Cell Biol. 68:1990;392-395
    • (1990) Biochem Cell Biol , vol.68 , pp. 392-395
    • Murphy, M.G.1    Byczko, Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.