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Volumn 11, Issue 5, 2005, Pages 545-550

Diverse compounds mimic Alzheimer disease-causing mutations by augmenting Aβ42 production

Author keywords

[No Author keywords available]

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; 6 (2,4 DIFLUOROPHENYLTHIO) 5 METHANESULFONAMIDO 1 INDANONE; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; ANTILIPEMIC AGENT; CELECOXIB; CYCLOOXYGENASE 2 INHIBITOR; ETORICOXIB; FARNESYL DIPHOSPHATE; FENOFIBRATE; FT 1; GAMMA SECRETASE; GERANYLGERANYL PYROPHOSPHATE; INDOMETACIN; INDOMETACIN DERIVATIVE; ISOPRENOID; LM 4114; LM 4414; LUMIRACOXIB; MECLOFENAMIC ACID; NONSTEROID ANTIINFLAMMATORY AGENT; PRESENILIN DERIVATIVE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; ROFECOXIB; S 2474; TILMACOXIB; UNCLASSIFIED DRUG; VALDECOXIB;

EID: 21044458540     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm1235     Document Type: Article
Times cited : (266)

References (48)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81, 741-766 (2001).
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 2
    • 0034718027 scopus 로고    scopus 로고
    • Biochemical detection of Abeta isoforms: Implications for pathogenesis, diagnosis, and treatment of Alzheimer's disease
    • Golde, T.E., Eckman, C.B. & Younkin, S.G. Biochemical detection of Abeta isoforms: implications for pathogenesis, diagnosis, and treatment of Alzheimer's disease. Biochim. Biophys. Acta 1502, 172-187 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 172-187
    • Golde, T.E.1    Eckman, C.B.2    Younkin, S.G.3
  • 3
    • 0032105394 scopus 로고    scopus 로고
    • The role of a beta 42 in Alzheimer's disease
    • Younkin, S.G. The role of A beta 42 in Alzheimer's disease. J. Physiol. Paris 92, 289-292 (1998).
    • (1998) J. Physiol. Paris , vol.92 , pp. 289-292
    • Younkin, S.G.1
  • 4
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner, D. et al. Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat. Med. 2, 864-870 (1996).
    • (1996) Nat. Med. , vol.2 , pp. 864-870
    • Scheuner, D.1
  • 5
    • 16044366039 scopus 로고    scopus 로고
    • Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1
    • Duff, K. et al. Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1. Nature 383, 710-713 (1996).
    • (1996) Nature , vol.383 , pp. 710-713
    • Duff, K.1
  • 6
    • 2342473791 scopus 로고    scopus 로고
    • Dissecting the pathological effects of human Abeta40 and Abeta42 in Drosophila: A potential model for Alzheimer's disease
    • Iijima, K. et al. Dissecting the pathological effects of human Abeta40 and Abeta42 in Drosophila: a potential model for Alzheimer's disease. Proc. Natl. Acad. Sci. USA 101, 6623-6628 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6623-6628
    • Iijima, K.1
  • 7
    • 18844402004 scopus 로고    scopus 로고
    • Selective Overexpression of Abeta42, but not Abeta40, in the secretory pathway is sufficient for plaque deposition in mice
    • 877.14
    • McGowan, E. et al. Selective Overexpression of Abeta42, but not Abeta40, in the secretory pathway is sufficient for plaque deposition in mice. Abstr. Soc. Neurosci. 877.14 (2003).
    • (2003) Abstr. Soc. Neurosci.
    • McGowan, E.1
  • 8
    • 85047691727 scopus 로고    scopus 로고
    • NSAIDs and enantiomers of flurbiprofen target gamma-secretase and lower Abeta 42 in vivo
    • Eriksen, J.L. et al. NSAIDs and enantiomers of flurbiprofen target gamma-secretase and lower Abeta 42 in vivo. J. Clin. Invest. 112, 440-449 (2003).
    • (2003) J. Clin. Invest. , vol.112 , pp. 440-449
    • Eriksen, J.L.1
  • 9
    • 0035829592 scopus 로고    scopus 로고
    • A subset of NSAIDs lower amyloidogenic Abeta42 independently of cyclooxygenase activity
    • Weggen, S. et al. A subset of NSAIDs lower amyloidogenic Abeta42 independently of cyclooxygenase activity. Nature 414, 212-216 (2001).
    • (2001) Nature , vol.414 , pp. 212-216
    • Weggen, S.1
  • 10
    • 0041876229 scopus 로고    scopus 로고
    • Evidence that nonsteroidal anti-inflammatory drugs decrease amyloid beta 42 production by direct modulation of gamma-secretase activity
    • Weggen, S. et al. Evidence that nonsteroidal anti-inflammatory drugs decrease amyloid beta 42 production by direct modulation of gamma-secretase activity. J. Biol. Chem. 278, 31831-31837 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 31831-31837
    • Weggen, S.1
  • 11
    • 0042878457 scopus 로고    scopus 로고
    • The non-cyclooxygenase targets of non-steroidal anti-inflammatory drugs, lipoxygenases, peroxisome proliferator-activated receptor, inhibitor of kappa B kinase, and NF kappa B, do not reduce amyloid beta 42 production
    • Sagi, S.A., Weggen, S., Eriksen, J., Golde, T.E. & Koo, E.H. The non-cyclooxygenase targets of non-steroidal anti-inflammatory drugs, lipoxygenases, peroxisome proliferator-activated receptor, inhibitor of kappa B kinase, and NF kappa B, do not reduce amyloid beta 42 production. J. Biol. Chem. 278, 31825-31830 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 31825-31830
    • Sagi, S.A.1    Weggen, S.2    Eriksen, J.3    Golde, T.E.4    Koo, E.H.5
  • 12
    • 0038719688 scopus 로고    scopus 로고
    • Sulindac sulfide is a noncompetitive gamma-secretase inhibitor that preferentially reduces Abeta 42 generation
    • Takahashi, Y. et al. Sulindac sulfide is a noncompetitive gamma-secretase inhibitor that preferentially reduces Abeta 42 generation. J. Biol. Chem. 278, 18664-18670 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 18664-18670
    • Takahashi, Y.1
  • 13
    • 6344233805 scopus 로고    scopus 로고
    • Selected non-steroidal anti-inflammatory drugs and their derivatives target gamma -secretase at a novel site-evidence for an allosteric mechanism
    • Beher, D. et al. Selected non-steroidal anti-inflammatory drugs and their derivatives target gamma -secretase at a novel site-evidence for an allosteric mechanism. J. Biol. Chem. 279, 43419-43426 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 43419-43426
    • Beher, D.1
  • 14
    • 7044254509 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs lower Abeta42 and change presenilin 1 conformation
    • Lleo, A. et al. Nonsteroidal anti-inflammatory drugs lower Abeta42 and change presenilin 1 conformation. Nat. Med. 10, 1065-1066 (2004).
    • (2004) Nat. Med. , vol.10 , pp. 1065-1066
    • Lleo, A.1
  • 15
    • 0026661730 scopus 로고
    • Induction of the peroxisome proliferator activated receptor by fenofibrate in rat liver
    • Gebel, T., Arand, M. & Oesch, F. Induction of the peroxisome proliferator activated receptor by fenofibrate in rat liver. FEBS Lett. 309, 37-40 (1992).
    • (1992) FEBS Lett. , vol.309 , pp. 37-40
    • Gebel, T.1    Arand, M.2    Oesch, F.3
  • 16
    • 0034721194 scopus 로고    scopus 로고
    • Ester and amide derivatives of the nonsteroidal antiinflammatory drug, indomethacin, as selective cyclooxygenase-2 inhibitors
    • Kalgutkar, A.S., Marnett, A.B., Crews, B.C., Remmel, P.P. & Marnett, L.J. Ester and amide derivatives of the nonsteroidal antiinflammatory drug, indomethacin, as selective cyclooxygenase-2 inhibitors. J. Med. Chem. 43, 2860-2870 (2000).
    • (2000) J. Med. Chem. , vol.43 , pp. 2860-2870
    • Kalgutkar, A.S.1    Marnett, A.B.2    Crews, B.C.3    Remmel, P.P.4    Marnett, L.J.5
  • 17
    • 0034681109 scopus 로고    scopus 로고
    • Biochemically based design of cyclooxygenase-2 (COX-2) inhibitors: Facile conversion of nonsteroidal antiinflammatory drugs to potent and highly selective COX-2 inhibitors
    • Kalgutkar, A.S. et al. Biochemically based design of cyclooxygenase-2 (COX-2) inhibitors: facile conversion of nonsteroidal antiinflammatory drugs to potent and highly selective COX-2 inhibitors. Proc. Natl. Acad. Sci. USA 97, 925-930 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 925-930
    • Kalgutkar, A.S.1
  • 18
    • 0242414463 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs can lower amyloidogenic Abeta42 by inhibiting Rho
    • Zhou, Y. et al. Nonsteroidal anti-inflammatory drugs can lower amyloidogenic Abeta42 by inhibiting Rho. Science 302, 1215-1217 (2003).
    • (2003) Science , vol.302 , pp. 1215-1217
    • Zhou, Y.1
  • 19
    • 0033765588 scopus 로고    scopus 로고
    • Rho-kinase is involved in macrophage-mediated formation of coronary vascular lesions in pigs in vivo
    • Miyata, K. et al. Rho-kinase is involved in macrophage-mediated formation of coronary vascular lesions in pigs in vivo. Arterioscler. Thromb. Vasc. Biol. 20, 2351-2358 (2000).
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 2351-2358
    • Miyata, K.1
  • 20
    • 0033777071 scopus 로고    scopus 로고
    • Determination of GTP loading on Rho
    • Ren, X.D. & Schwartz, M.A. Determination of GTP loading on Rho. Methods Enzymol. 325, 264-272 (2000).
    • (2000) Methods Enzymol. , vol.325 , pp. 264-272
    • Ren, X.D.1    Schwartz, M.A.2
  • 21
    • 0034602419 scopus 로고    scopus 로고
    • Presenilin-1 and -2 are molecular targets for gamma-secretase inhibitors
    • Seiffert, D. et al. Presenilin-1 and -2 are molecular targets for gamma-secretase inhibitors. J. Biol. Chem. 275, 34086-34091 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 34086-34091
    • Seiffert, D.1
  • 22
    • 0036922497 scopus 로고    scopus 로고
    • Fenofibrate in the treatment of dyslipidemia: A review of the data as they relate to the new suprabioavailable tablet formulation
    • Najib, J. Fenofibrate in the treatment of dyslipidemia: a review of the data as they relate to the new suprabioavailable tablet formulation. Clin. Ther. 24, 2022-2050 (2002).
    • (2002) Clin. Ther. , vol.24 , pp. 2022-2050
    • Najib, J.1
  • 23
    • 0033569840 scopus 로고    scopus 로고
    • The four murine peroxisomal ABC-transporter genes differ in constitutive, inducible and developmental expression
    • Berger, J. et al. The four murine peroxisomal ABC-transporter genes differ in constitutive, inducible and developmental expression. Eur. J. Biochem. 265, 719-727 (1999).
    • (1999) Eur. J. Biochem. , vol.265 , pp. 719-727
    • Berger, J.1
  • 24
    • 0035966125 scopus 로고    scopus 로고
    • Dual mechanisms of ABCA1 regulation by geranylgeranyl pyrophosphate
    • Gan, X. et al. Dual mechanisms of ABCA1 regulation by geranylgeranyl pyrophosphate. J. Biol. Chem. 276, 48702-48708 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 48702-48708
    • Gan, X.1
  • 25
    • 0033538474 scopus 로고    scopus 로고
    • New insights into the interaction of Ras with the plasma membrane
    • Magee, T. & Marshall, C. New insights into the interaction of Ras with the plasma membrane. Cell 98, 9-12 (1999).
    • (1999) Cell , vol.98 , pp. 9-12
    • Magee, T.1    Marshall, C.2
  • 26
    • 0036180950 scopus 로고    scopus 로고
    • Cholesterol-dependent gamma-secretase activity in buoyant cholesterol- rich membrane microdomains
    • Wahrle, S. et al. Cholesterol-Dependent gamma-Secretase Activity in Buoyant Cholesterol- Rich Membrane Microdomains. Neurobiol. Dis. 9, 11-23 (2002).
    • (2002) Neurobiol. Dis. , vol.9 , pp. 11-23
    • Wahrle, S.1
  • 27
    • 7244258941 scopus 로고    scopus 로고
    • Association of gamma -secretase with lipid rafts in post-golgi and endosome membranes
    • Vetrivel, K.S. et al. Association of gamma -secretase with lipid rafts in post-golgi and endosome membranes. J. Biol. Chem. 279, 44945-44954 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 44945-44954
    • Vetrivel, K.S.1
  • 28
    • 0030592525 scopus 로고    scopus 로고
    • Squalene synthase inhibition alters metabolism of nonsterols in rat liver
    • Keller, R.K. Squalene synthase inhibition alters metabolism of nonsterols in rat liver. Biochim. Biophys. Acta 1303, 169-179 (1996).
    • (1996) Biochim. Biophys. Acta , vol.1303 , pp. 169-179
    • Keller, R.K.1
  • 29
    • 0036322869 scopus 로고    scopus 로고
    • Isoprenoids as mediators of the biological effects of statins
    • Liao, J.K. Isoprenoids as mediators of the biological effects of statins. J. Clin. Invest. 110, 285-288 (2002).
    • (2002) J. Clin. Invest. , vol.110 , pp. 285-288
    • Liao, J.K.1
  • 30
    • 4344566427 scopus 로고    scopus 로고
    • Statins inhibit HIV-1 infection by down-regulating Rho activity
    • del Real, G. et al. Statins inhibit HIV-1 infection by down-regulating Rho activity. J. Exp. Med. 200, 541-547 (2004).
    • (2004) J. Exp. Med. , vol.200 , pp. 541-547
    • Del Real, G.1
  • 31
    • 0033772113 scopus 로고    scopus 로고
    • Decreased prevalence of Alzheimer disease associated with 3-hydroxy-3- methyglutaryl coenzyme A reductase inhibitors
    • Wolozin, B., Kellman, W., Ruosseau, P., Celesia, G.G. & Siegel, G. Decreased prevalence of Alzheimer disease associated with 3-hydroxy-3- methyglutaryl coenzyme A reductase inhibitors. Arch. Neurol. 57, 1439-1443 (2000).
    • (2000) Arch. Neurol. , vol.57 , pp. 1439-1443
    • Wolozin, B.1    Kellman, W.2    Ruosseau, P.3    Celesia, G.G.4    Siegel, G.5
  • 32
    • 0032568552 scopus 로고    scopus 로고
    • Cholesterol depletion inhibits the generation of beta-amyloid in hippocampal neurons
    • Simons, M. et al. Cholesterol depletion inhibits the generation of beta-amyloid in hippocampal neurons. Proc. Natl. Acad. Sci. USA 95, 6460-6464 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6460-6464
    • Simons, M.1
  • 33
    • 0035160066 scopus 로고    scopus 로고
    • A cholesterol-lowering drug reduces beta-amyloid pathology in a transgenic mouse model of Alzheimer's disease
    • Refolo, L.M. et al. A cholesterol-lowering drug reduces beta-amyloid pathology in a transgenic mouse model of Alzheimer's disease. Neurobiol. Dis. 8, 890-899 (2001).
    • (2001) Neurobiol. Dis. , vol.8 , pp. 890-899
    • Refolo, L.M.1
  • 34
    • 0034612175 scopus 로고    scopus 로고
    • Inflammation and Alzheimer's disease
    • Akiyama, H. et al. Inflammation and Alzheimer's disease. Neurobiol. Aging 21, 383-421 (2000).
    • (2000) Neurobiol. Aging , vol.21 , pp. 383-421
    • Akiyama, H.1
  • 35
    • 9144219644 scopus 로고    scopus 로고
    • Cyclooxygenase (COX)-2 and COX-1 potentiate beta-amyloid peptide generation through mechanisms that involve gamma-secretase activity
    • Qin, W. et al. Cyclooxygenase (COX)-2 and COX-1 potentiate beta-amyloid peptide generation through mechanisms that involve gamma-secretase activity. J. Biol. Chem. 278, 50970-50977 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 50970-50977
    • Qin, W.1
  • 36
    • 0036424134 scopus 로고    scopus 로고
    • Cyclooxygenase-2 promotes amyloid plaque deposition in a mouse model of Alzheimer's disease neuropathology
    • Xiang, Z. et al. Cyclooxygenase-2 promotes amyloid plaque deposition in a mouse model of Alzheimer's disease neuropathology. Gene Expr. 10, 271-278 (2002).
    • (2002) Gene Expr. , vol.10 , pp. 271-278
    • Xiang, Z.1
  • 37
    • 0034062275 scopus 로고    scopus 로고
    • Clinical pharmacokinetics and pharmacodynamics of celecoxib: A selective cyclo-oxygenase-2 inhibitor
    • Davies, N.M., McLachlan, A.J., Day, R.O. & Williams, K.M. Clinical pharmacokinetics and pharmacodynamics of celecoxib: a selective cyclo-oxygenase-2 inhibitor. Clin. Pharmacokinet. 38, 225-242 (2000).
    • (2000) Clin. Pharmacokinet. , vol.38 , pp. 225-242
    • Davies, N.M.1    McLachlan, A.J.2    Day, R.O.3    Williams, K.M.4
  • 38
    • 0036174553 scopus 로고    scopus 로고
    • Double placebo design in a prevention trial for Alzheimer's disease
    • Martin, B.K., Meinert, C.L. & Breitner, J.C. Double placebo design in a prevention trial for Alzheimer's disease. Control Clin. Trials 23, 93-99 (2002).
    • (2002) Control Clin. Trials , vol.23 , pp. 93-99
    • Martin, B.K.1    Meinert, C.L.2    Breitner, J.C.3
  • 39
    • 3042788940 scopus 로고    scopus 로고
    • COX-2 inhibition and colorectal cancer
    • Koehne, C.H. & Dubois, R.N. COX-2 inhibition and colorectal cancer. Semin. Oncol. 31, 12-21 (2004).
    • (2004) Semin. Oncol. , vol.31 , pp. 12-21
    • Koehne, C.H.1    Dubois, R.N.2
  • 40
    • 6944231391 scopus 로고    scopus 로고
    • COX-2 inhibitors and risk of heart failure
    • author reply 1487
    • Kammerl, M.C., Debler, J., Riegger, G.A. & Kramer, B.K. COX-2 inhibitors and risk of heart failure. Lancet 364, 1486-1487; author reply 1487 (2004).
    • (2004) Lancet , vol.364 , pp. 1486-1487
    • Kammerl, M.C.1    Debler, J.2    Riegger, G.A.3    Kramer, B.K.4
  • 41
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J. & Selkoe, D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356 (2002).
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 42
    • 0034714316 scopus 로고    scopus 로고
    • Presenilin 1 regulates pharmacologically distinct gamma-secretase activities. Implications for the role of presenilin in gamma -secretase cleavage
    • Murphy, M.P. et al. Presenilin 1 regulates pharmacologically distinct gamma-secretase activities. Implications for the role of presenilin in gamma -secretase cleavage. J. Biol. Chem. 275, 26277-26284 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 26277-26284
    • Murphy, M.P.1
  • 43
    • 0029752755 scopus 로고    scopus 로고
    • The profile of soluble amyloid beta protein in cultured cell media. Detection and quantification of amyloid beta protein and variants by immunoprecipitation-mass spectrometry
    • Wang, R., Sweeney, D., Gandy, S.E. & Sisodia, S.S. The profile of soluble amyloid beta protein in cultured cell media. Detection and quantification of amyloid beta protein and variants by immunoprecipitation-mass spectrometry. J. Biol. Chem. 271, 31894-31902 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 31894-31902
    • Wang, R.1    Sweeney, D.2    Gandy, S.E.3    Sisodia, S.S.4
  • 44
    • 0001468710 scopus 로고    scopus 로고
    • Inhibition of RhoA by p120 catenin
    • Anastasiadis, P.Z. et al. Inhibition of RhoA by p120 catenin. Nat. Cell Biol. 2, 637-644 (2000).
    • (2000) Nat. Cell Biol. , vol.2 , pp. 637-644
    • Anastasiadis, P.Z.1
  • 45
    • 0034576027 scopus 로고    scopus 로고
    • Cell-free assays for γ-secretase activity
    • McLendon, C. et al. Cell-free assays for γ-secretase activity. FASEB J. 14, 2383-2386 (2000).
    • (2000) FASEB J. , vol.14 , pp. 2383-2386
    • McLendon, C.1
  • 46
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice
    • Hsiao, K. et al. Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice. Science 274, 99-102 (1996).
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1
  • 47
    • 0035863055 scopus 로고    scopus 로고
    • Age-dependent changes in brain, CSF, and plasma amyloid protein in the Tg2576 transgenic mouse model of Alzheimer's disease
    • Kawarabayashi, T. et al. Age-dependent changes in brain, CSF, and plasma amyloid protein in the Tg2576 transgenic mouse model of Alzheimer's disease. J. Neurosci. 21, 372-381 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 372-381
    • Kawarabayashi, T.1
  • 48
    • 0037462769 scopus 로고    scopus 로고
    • Alzheimer's disease beta-amyloid peptide is increased in mice deficient in endothelin-converting enzyme
    • Eckman, E.A., Watson, M., Marlow, L., Sambamurti, K. & Eckman, C.B. Alzheimer's disease beta-amyloid peptide is increased in mice deficient in endothelin-converting enzyme. J. Biol. Chem. 278, 2081-2084 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 2081-2084
    • Eckman, E.A.1    Watson, M.2    Marlow, L.3    Sambamurti, K.4    Eckman, C.B.5


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