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Volumn 5, Issue 3, 1999, Pages 195-198

The Hsp90 chaperone complex - A potential target for cancer therapy?

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EID: 0000976965     PISSN: 10079327     EISSN: None     Source Type: Journal    
DOI: 10.3748/wjg.v5.i3.195     Document Type: Article
Times cited : (17)

References (60)
  • 1
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU. Molecular chaperones in cellular protein folding. Nature, 1996;381:571-579
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 3
    • 0030907672 scopus 로고    scopus 로고
    • Proteins, RN'As, chaperones and enzyme evolution; a folding perspective
    • Csermely P. Proteins, RN'As, chaperones and enzyme evolution; a folding perspective. Trends Biochem Sci., 1997;22:147-149
    • (1997) Trends Biochem Sci. , vol.22 , pp. 147-149
    • Csermely, P.1
  • 4
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • Rutherford SL, Lindquist S. Hsp90 as a capacitor for morphological evolution. Nature, 1998;396:336-342
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 5
    • 0026460892 scopus 로고
    • Mammalian stress response: Cell physiology, structure/ function of stress proteins, and implication for medicine and disease
    • Welch WJ. Mammalian stress response: cell physiology, structure/ function of stress proteins, and implication for medicine and disease. Physiol Rev, 1992;72:1063- 1081
    • (1992) Physiol Rev , vol.72 , pp. 1063-1081
    • Welch, W.J.1
  • 6
    • 0027218599 scopus 로고
    • Heat shock proteins in relation to medicine
    • Burdon RH. Heat shock proteins in relation to medicine. Mol Aspects Med, 1993;14:83-165
    • (1993) Mol Aspects Med , vol.14 , pp. 83-165
    • Burdon, R.H.1
  • 7
    • 0030025526 scopus 로고    scopus 로고
    • Heat shock proteins: Applications in health and disease
    • Jindal S. Heat shock proteins: applications in health and disease. Trends Biotechnol , 1996;14:17-20
    • (1996) Trends Biotechnol , vol.14 , pp. 17-20
    • Jindal, S.1
  • 8
    • 0030918842 scopus 로고    scopus 로고
    • Protein processing: A role in the pathophysiology of genetic disease
    • Brooks DA. Protein processing: a role in the pathophysiology of genetic disease. FEBS Lett, 1997;409:115-120
    • (1997) FEBS Lett , vol.409 , pp. 115-120
    • Brooks, D.A.1
  • 9
    • 0031693703 scopus 로고    scopus 로고
    • The Hsp90 complex - A super-chaperone machine as a novel drug target
    • Scheibel T, Buchner J. The Hsp90 complex - a super-chaperone machine as a novel drug target. Biochem Pharmacol , 1998; 56: 675-682
    • (1998) Biochem Pharmacol , vol.56 , pp. 675-682
    • Scheibel, T.1    Buchner, J.2
  • 10
    • 0031895351 scopus 로고    scopus 로고
    • The Hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors
    • Pratt WB. The Hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exper Biol Med, 1998;217:420-434
    • (1998) Proc Soc Exper Biol Med , vol.217 , pp. 420-434
    • Pratt, W.B.1
  • 12
    • 0028171452 scopus 로고
    • Hsp90α and Hsp90β genes are present in the zebrafish and are differentially regulated in developing embryos
    • Krone PH, Sass JB. Hsp90α and Hsp90β genes are present in the zebrafish and are differentially regulated in developing embryos. Biochem Biophys Res Comm, 1994;204:746-752
    • (1994) Biochem Biophys Res Comm , vol.204 , pp. 746-752
    • Krone, P.H.1    Sass, J.B.2
  • 13
    • 0028785298 scopus 로고
    • Phylogenetic analysis of the 90kD heat shock family of protein sequences and an examination of the relationship among animals, plants, and fungi species
    • Gupta RS. Phylogenetic analysis of the 90kD heat shock family of protein sequences and an examination of the relationship among animals, plants, and fungi species. Mol Biol Evol , 1995; 12: 1063-1073
    • (1995) Mol Biol Evol , vol.12 , pp. 1063-1073
    • Gupta, R.S.1
  • 14
    • 0030324952 scopus 로고    scopus 로고
    • A pathway of multi-chaperone interactions common to diverse regulatory proteins-estrogen receptor, fes tyrosine kinase, heat shock transcription factor, HSF1, and the aryl hydrocarbon receptor
    • Nair SC, Toran EJ, Rimerman RA, Hjermstad S, Smithgall TE, Smith DF. A pathway of multi-chaperone interactions common to diverse regulatory proteins-estrogen receptor, fes tyrosine kinase, heat shock transcription factor, HSF1, and the aryl hydrocarbon receptor. Cell Stress Chaperones, 1996;1:237-250
    • (1996) Cell Stress Chaperones , vol.1 , pp. 237-250
    • Nair, S.C.1    Toran, E.J.2    Rimerman, R.A.3    Hjermstad, S.4    Smithgall, T.E.5    Smith, D.F.6
  • 15
    • 0030809270 scopus 로고    scopus 로고
    • Protein folding in vivo: Unraveling complex pathways
    • Johnson JL, Craig EA. Protein folding in vivo: unraveling complex pathways. Cell, 1997;90:201-204
    • (1997) Cell , vol.90 , pp. 201-204
    • Johnson, J.L.1    Craig, E.A.2
  • 16
    • 0030667932 scopus 로고    scopus 로고
    • In vivo function of the Saccharomyces cerevisiae Hsp90 chaperone
    • Nathan DF, Vos MH, Lindquist S. In vivo function of the Saccharomyces cerevisiae Hsp90 chaperone. Proc Natl Acad Sci USA, 1997;94:12949-12956
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12949-12956
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 17
    • 12044259947 scopus 로고
    • Steroid receptors and their associated proteins
    • Smith DF, Toft DO. Steroid receptors and their associated proteins. MolEndo, 1993;7:4-11
    • (1993) MolEndo , vol.7 , pp. 4-11
    • Smith, D.F.1    Toft, D.O.2
  • 18
    • 0002830140 scopus 로고
    • Modulation of steroid receptor signal transduction by heat-shock proteins
    • Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Bohen SP, Yamamoto KR. Modulation of steroid receptor signal transduction by heat-shock proteins. In: The biology of heat-shock proteins and molecular chaperones. Cold Spring Harbor: Cold Spring Harbor Laboratory Press, 1994:313-334
    • (1994) : the Biology of Heat-shock Proteins and Molecular Chaperones. , pp. 313-334
    • Bohen, S.P.1    Yamamoto, K.R.2
  • 19
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat-shock protein and immunophilin chaperones
    • Pratt WB, Toft DO. Steroid receptor interactions with heat-shock protein and immunophilin chaperones. Endo Rev, 1997;18:306-360
    • (1997) Endo Rev , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 20
    • 0030982641 scopus 로고    scopus 로고
    • The role of the Hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase
    • Pratt WB. The role of the Hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase. Annu Rev Pharmacol Toxicol , 1997;37:297-326
    • (1997) Annu Rev Pharmacol Toxicol , vol.37 , pp. 297-326
    • Pratt, W.B.1
  • 21
    • 0028892084 scopus 로고
    • A role for Hsp90 in retinoid receptor signal transduction
    • Holley SJ, Yamamoto KR. A role for Hsp90 in retinoid receptor signal transduction. Mol Biol Cell, 1995;6:1833-1842
    • (1995) Mol Biol Cell , vol.6 , pp. 1833-1842
    • Holley, S.J.1    Yamamoto, K.R.2
  • 22
    • 0026631538 scopus 로고
    • Dual roles of the 90-kDa heat shock protein Hsp90 in modulating functional activities of the dioxin receptor. Evidence that the dioxin receptor functionally belongs to a subclass of nuclear receptors which require Hsp90 both for ligand binding activity and repression of intrinsic DNA binding activity
    • Pongratz I, Mason GG, Poellinger L. Dual roles of the 90-kDa heat shock protein Hsp90 in modulating functional activities of the dioxin receptor. Evidence that the dioxin receptor functionally belongs to a subclass of nuclear receptors which require Hsp90 both for ligand binding activity and repression of intrinsic DNA binding activity. J Biol Chem, 1992;267:13728-13734
    • (1992) J Biol Chem , vol.267 , pp. 13728-13734
    • Pongratz, I.1    Mason, G.G.2    Poellinger, L.3
  • 24
    • 0027359404 scopus 로고
    • Isolation of Hsp90 mutants by screening for decreased steroid function
    • Bohen SP, Yamamoto KR. Isolation of Hsp90 mutants by screening for decreased steroid function. Proc Natl Acad Sci USA, 1993;11424-11428
    • (1993) Proc Natl Acad Sci USA , pp. 11424-11428
    • Bohen, S.P.1    Yamamoto, K.R.2
  • 25
    • 0029037110 scopus 로고
    • Mutational analysis of Hsp90 function; interactions with a steroid receptor and a protein kinase
    • Nathan DF, Lindquist S. Mutational analysis of Hsp90 function; interactions with a steroid receptor and a protein kinase. Mol Cell Biol , 1995;15:3917-3925
    • (1995) Mol Cell Biol , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 26
  • 27
    • 0027291238 scopus 로고
    • Heat-shock protein Hsp90 governs the activity of pp60v-src kinase
    • Xu Y, Lindquist S. Heat-shock protein Hsp90 governs the activity of pp60v-src kinase. Proc Natl Acad Sci USA, 1993;90:7074-7078
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7074-7078
    • Xu, Y.1    Lindquist, S.2
  • 28
    • 0030896688 scopus 로고    scopus 로고
    • The heat shock protein 83 ( Hsp83 ) is required for Raf-mediated signalling in Drosophila
    • van der Straten A, Rommel C, Dickson B, Hafen E. The heat shock protein 83 ( Hsp83 ) is required for Raf-mediated signalling in Drosophila. EMBO J, 1997; 16:1961-1969
    • (1997) EMBO J , vol.16 , pp. 1961-1969
    • Straten, A.1    Rommel, C.2    Dickson, B.3    Hafen, E.4
  • 29
    • 0030997120 scopus 로고    scopus 로고
    • Hsp90 is obligatory for the hemeregulated eIF-2α kinase to acquire and maintain an activable conformation
    • Uma S, Hartson SD, Chen JJ, Matts RL. Hsp90 is obligatory for the hemeregulated eIF-2α kinase to acquire and maintain an activable conformation. J Biol Chem , 1997;272:11648-11656
    • (1997) J Biol Chem , vol.272 , pp. 11648-11656
    • Uma, S.1    Hartson, S.D.2    Chen, J.J.3    Matts, R.L.4
  • 30
    • 0026669310 scopus 로고
    • The 90-kDa heat shock protein, Hsp90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity
    • Miyata Y, Yaharal. The 90-kDa heat shock protein, Hsp90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. J Biol Chem , 1992;267:7042-7047
    • (1992) J Biol Chem , vol.267 , pp. 7042-7047
    • Miyata, Y.1    Yaharal2
  • 31
    • 0031054517 scopus 로고    scopus 로고
    • The Hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase
    • Stancato LF, Silverstein AM, Owens-Grillo JK, Chow YH, Jove R, Pratt WB. The Hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase. J Biol Chem , 1997;272:4013-4020
    • (1997) J Biol Chem , vol.272 , pp. 4013-4020
    • Stancato, L.F.1    Silverstein, A.M.2    Owens-Grillo, J.K.3    Chow, Y.H.4    Jove, R.5    Pratt, W.B.6
  • 32
    • 0029838168 scopus 로고    scopus 로고
    • Physical interaction of mammalian CDC37 with CDK4
    • Dai K, Kobayashi R, Beach D. Physical interaction of mammalian CDC37 with CDK4. J Biol Chem , 1996;271:22030-22034
    • (1996) J Biol Chem , vol.271 , pp. 22030-22034
    • Dai, K.1    Kobayashi, R.2    Beach, D.3
  • 33
    • 0029665779 scopus 로고    scopus 로고
    • Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
    • Stephanova L, Leng X, Parker SB, Harper JW. Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes Dev, 1996;10:1491-1502
    • (1996) Genes Dev , vol.10 , pp. 1491-1502
    • Stephanova, L.1    Leng, X.2    Parker, S.B.3    Harper, J.W.4
  • 34
    • 0028589101 scopus 로고
    • A role for Hsp90 in cell cycle control; wee 1 tyrosine kinase requires interaction with Hsp90
    • Aligue R, Akhavan-Niak H, Russell P. A role for Hsp90 in cell cycle control; wee 1 tyrosine kinase requires interaction with Hsp90. EMBO J, 1994;13:6099-6106
    • (1994) EMBO J , vol.13 , pp. 6099-6106
    • Aligue, R.1    Akhavan-Niak, H.2    Russell, P.3
  • 36
    • 0032230323 scopus 로고    scopus 로고
    • Calcium/calmodulin kinase inhibitors and immunosuppressant macrolides rapamycin and FK506 inhibit progestin-and glucocorticosteroid receptor-mediated transcription in human breast cancer T47D cells
    • Le Bihan S, Marsaud V, Mercier Bodard C, Baulieu EE, Mader S, White JH, Renoir JM. Calcium/calmodulin kinase inhibitors and immunosuppressant macrolides rapamycin and FK506 inhibit progestin-and glucocorticosteroid receptor-mediated transcription in human breast cancer T47D cells. Mol Endo, 1998;12:986-1001
    • (1998) Mol Endo , vol.12 , pp. 986-1001
    • Le Bihan, S.1    Marsaud, V.2    Mercier Bodard, C.3    Baulieu, E.E.4    Mader, S.5    White, J.H.6    Renoir, J.M.7
  • 37
    • 0031826823 scopus 로고    scopus 로고
    • The molecular chaperones in cell cycle control
    • Sato N, Torigoe T. The molecular chaperones in cell cycle control. Annals New York Acad Sci , 1998;851:61 -66
    • (1998) Annals New York Acad Sci , vol.851 , pp. 61-66
    • Sato, N.1    Torigoe, T.2
  • 38
    • 0030218025 scopus 로고    scopus 로고
    • The role of the 90-kDa heat shock protein in cell cycle control and differentiation of the monoblastoid cell line U937
    • Galea-Lauri J, Latchman DS, Katz DR. The role of the 90-kDa heat shock protein in cell cycle control and differentiation of the monoblastoid cell line U937. Exp Cell Res , 1996;226:243-254
    • (1996) Exp Cell Res , vol.226 , pp. 243-254
    • Galea-Lauri, J.1    Latchman, D.S.2    Katz, D.R.3
  • 39
    • 15844363948 scopus 로고    scopus 로고
    • Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell
    • Sepehmia B, Paz IB, Dasgupta G, Momand J. Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell. J Biol Chem , 1996;271:15084-15090
    • (1996) J Biol Chem , vol.271 , pp. 15084-15090
    • Sepehmia, B.1    Paz, I.B.2    Dasgupta, G.3    Momand, J.4
  • 41
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat-shock proteins in human tumor cells
    • Ferrarini M, Heltai S, Zocchi MR, Rugarli C. Unusual expression and localization of heat-shock proteins in human tumor cells. Int J Cancer, 1992;51:613-619
    • (1992) Int J Cancer , vol.51 , pp. 613-619
    • Ferrarini, M.1    Heltai, S.2    Zocchi, M.R.3    Rugarli, C.4
  • 42
    • 0026664393 scopus 로고
    • High constitutive expression of heat shock protein 90a in human acute leukemia cells
    • Yufu Y, Nishimura J, Nawata H. High constitutive expression of heat shock protein 90a in human acute leukemia cells. Leuk Res, 1992;16:597-605
    • (1992) Leuk Res , vol.16 , pp. 597-605
    • Yufu, Y.1    Nishimura, J.2    Nawata, H.3
  • 45
    • 0001148491 scopus 로고    scopus 로고
    • Down-regulation of Hsp90 could change cell cycle distribution and increase drug sensitivity of tumor cells
    • Liu XL, Xiao B, Yu ZC, Guo JC, Zhao QC, Xu L, Shi YQ, Fan DM. Down-regulation of Hsp90 could change cell cycle distribution and increase drug sensitivity of tumor cells. WJG , 1999;199-208
    • (1999) WJG , pp. 199-208
    • Liu, X.L.1    Xiao, B.2    Yu, Z.C.3    Guo, J.C.4    Zhao, Q.C.5    Xu, L.6    Shi, Y.Q.7    Fan, D.M.8
  • 46
    • 0030613625 scopus 로고    scopus 로고
    • Intratumoral heterogeneity for Hsp90 beta mRNA levels in a breast cancer cell line
    • Luparello C, Noel A, Pucci-Minafra I. Intratumoral heterogeneity for Hsp90 beta mRNA levels in a breast cancer cell line. DNA Cell Biol , 1997; 16: 1231-1236
    • (1997) DNA Cell Biol , vol.16 , pp. 1231-1236
    • Luparello, C.1    Noel, A.2    Pucci-Minafra, I.3
  • 47
    • 0031789983 scopus 로고    scopus 로고
    • Signal-transduction cascades as targets for therapeutic intervention by natural products
    • Cardenas ME, Sanfridson A, Cutler NS, Heitman J. Signal-transduction cascades as targets for therapeutic intervention by natural products. Trends Biotechn , 1998;16:427-433
    • (1998) Trends Biotechn , vol.16 , pp. 427-433
    • Cardenas, M.E.1    Sanfridson, A.2    Cutler, N.S.3    Heitman, J.4
  • 48
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex; targeting of a protein chaperone by an antitumor agent
    • Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP. Crystal structure of an Hsp90-geldanamycin complex; targeting of a protein chaperone by an antitumor agent. Cell, 1997;898:239-250
    • (1997) Cell , vol.898 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 50
    • 0032554763 scopus 로고    scopus 로고
    • Targeting of the protein chaperone, Hsp90, by the transformation suppressing agent, radicicol
    • Sharma SV, Agatsuma T, Nakano H. Targeting of the protein chaperone, Hsp90, by the transformation suppressing agent, radicicol. Oncogene, 1998;16:2639-2645
    • (1998) Oncogene , vol.16 , pp. 2639-2645
    • Sharma, S.V.1    Agatsuma, T.2    Nakano, H.3
  • 51
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for the inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe SM, Prodromou C, O'Brian R, Ladbury JE, Piper PW, Pearl LH. Structural basis for the inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem , 1999;42:260-262
    • (1999) J Med Chem , vol.42 , pp. 260-262
    • Roe, S.M.1    Prodromou, C.2    O'Brian, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 52
    • 0029729308 scopus 로고    scopus 로고
    • Increase of P-glycoprotein-mediated drug resistance by Hsp90 beta
    • Bertram J, Palfner K, Hiddemann W, Kneba M. Increase of P-glycoprotein-mediated drug resistance by Hsp90 beta. Anti-Cancer Drugs, 1996;7:838-845
    • (1996) Anti-Cancer Drugs , vol.7 , pp. 838-845
    • Bertram, J.1    Palfner, K.2    Hiddemann, W.3    Kneba, M.4
  • 53
    • 0032927941 scopus 로고    scopus 로고
    • Cancer multidrug resistance
    • Persidis A. Cancer multidrug resistance. Nature Biotech , 1999;17:94-95
    • (1999) Nature Biotech , vol.17 , pp. 94-95
    • Persidis, A.1
  • 54
    • 0031764330 scopus 로고    scopus 로고
    • Clinical relevance of transmembrane drug efflux as a mechanism of multidrug resistance
    • Bradshaw DM, Arceci RJ. Clinical relevance of transmembrane drug efflux as a mechanism of multidrug resistance. J Clinic Oncol, 1998; 16:3674-3690
    • (1998) J Clinic Oncol , vol.16 , pp. 3674-3690
    • Bradshaw, D.M.1    Arceci, R.J.2
  • 56
    • 0031843013 scopus 로고    scopus 로고
    • Multidrug resistance and its reversal
    • Volm M. Multidrug resistance and its reversal. Anticancer Res, 1998; 18:2905-2917
    • (1998) Anticancer Res , vol.18 , pp. 2905-2917
    • Volm, M.1
  • 57
    • 0029759985 scopus 로고    scopus 로고
    • Molecular mechanisms of multidrug resistance in cancer chemotherapy
    • Nooter K, Stoter G. Molecular mechanisms of multidrug resistance in cancer chemotherapy. Pathol Res Practice, 1996;192:768-780
    • (1996) Pathol Res Practice , vol.192 , pp. 768-780
    • Nooter, K.1    Stoter, G.2
  • 58
    • 0031925152 scopus 로고    scopus 로고
    • The role of heat shock proteins in the stimulation of an immune response
    • Multhoff G, Botzler C, Issels R. The role of heat shock proteins in the stimulation of an immune response. Biol Chem , 1998;379:295-300
    • (1998) Biol Chem , vol.379 , pp. 295-300
    • Multhoff, G.1    Botzler, C.2    Issels, R.3
  • 59
    • 0029000501 scopus 로고
    • The role of tumor rejection antigens in host antitumor defense mechanisms
    • Campbell FA, Redmond HP, Bouchier-Hayes D. The role of tumor rejection antigens in host antitumor defense mechanisms. Cancer, 1995;75:2649-2655
    • (1995) Cancer , vol.75 , pp. 2649-2655
    • Campbell, F.A.1    Redmond, H.P.2    Bouchier-Hayes, D.3
  • 60
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell, 1997;90:65-75
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6


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