메뉴 건너뛰기




Volumn 7, Issue 10, 2008, Pages 3275-3284

Antitumor activity and molecular effects of the novel heat shock protein 90 inhibitor, IPI-504, in pancreatic cancer

Author keywords

[No Author keywords available]

Indexed keywords

CALM1 PROTEIN; FAM84B PROTEIN; FDPS PROTEIN; GOLPH2 PROTEIN; HBA1 PROTEIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; HIST1H1C PROTEIN; HLA B ANTIGEN; HSPA 1B PROTEIN; LGALS3 PROTEIN; MARCKS PROTEIN; PROTEIN DERIVATIVE; TANESPIMYCIN HYDROQUINONE; UNCLASSIFIED DRUG; 17-(ALLYLAMINO)-17-DEMETHOXYGELDANAMYCIN; ANTINEOPLASTIC AGENT; BENZOQUINONE DERIVATIVE; MACROCYCLIC LACTAM; TANESPIMYCIN; TUMOR PROTEIN;

EID: 55749110744     PISSN: 15357163     EISSN: None     Source Type: Journal    
DOI: 10.1158/1535-7163.MCT-08-0508     Document Type: Article
Times cited : (67)

References (47)
  • 2
    • 0029868667 scopus 로고    scopus 로고
    • National patterns of care for pancreatic cancer. Results of a survey by the Commission on Cancer
    • Janes RH, Jr., Niederhuber JE, Chmiel JS, et al. National patterns of care for pancreatic cancer. Results of a survey by the Commission on Cancer. Ann Surg 1996;223:261-72.
    • (1996) Ann Surg , vol.223 , pp. 261-272
    • Janes Jr., R.H.1    Niederhuber, J.E.2    Chmiel, J.S.3
  • 3
    • 0027370407 scopus 로고
    • Prognostic indicators for survival after resection of pancreatic adenocarcinoma
    • discussion -3
    • Geer RJ, Brennan MF. Prognostic indicators for survival after resection of pancreatic adenocarcinoma. Am J Surg 1993;165:68-72; discussion -3.
    • (1993) Am J Surg , vol.165 , pp. 68-72
    • Geer, R.J.1    Brennan, M.F.2
  • 4
    • 0026460892 scopus 로고
    • Mammalian stress response: Cell physiology, structure/function of stress proteins, and implications for medicine and disease
    • Welch WJ. Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease. Physiol Rev 1992;72:1063-81.
    • (1992) Physiol Rev , vol.72 , pp. 1063-1081
    • Welch, W.J.1
  • 6
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • Isaacs JS, Xu W, Neckers L. Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell 2003;3:213-7.
    • (2003) Cancer Cell , vol.3 , pp. 213-217
    • Isaacs, J.S.1    Xu, W.2    Neckers, L.3
  • 7
    • 15544385359 scopus 로고    scopus 로고
    • Miyata Y. Hsp90 inhibitor geldanamycin and its derivatives as novel cancer chemotherapeutic agents. Curr Pharm Des 2005;11:1131-8.
    • Miyata Y. Hsp90 inhibitor geldanamycin and its derivatives as novel cancer chemotherapeutic agents. Curr Pharm Des 2005;11:1131-8.
  • 8
    • 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;89:239-50.
    • (1997) Cell , vol.89 , 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
  • 9
    • 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
  • 10
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17- demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • Schulte TW, Neckers LM. The benzoquinone ansamycin 17-allylamino-17- demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol 1998; 42:273-9.
    • (1998) Cancer Chemother Pharmacol , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 11
    • 0033579175 scopus 로고    scopus 로고
    • DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino,17-demethoxygeldanamycin, an inhibitor of heat shock protein 90
    • Kelland LR, Sharp SY, Rogers PM, Myers TG, Workman P. DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino,17-demethoxygeldanamycin, an inhibitor of heat shock protein 90. J Natl Cancer Inst 1999;91:1940-9.
    • (1999) J Natl Cancer Inst , vol.91 , pp. 1940-1949
    • Kelland, L.R.1    Sharp, S.Y.2    Rogers, P.M.3    Myers, T.G.4    Workman, P.5
  • 13
    • 33750711384 scopus 로고    scopus 로고
    • A phase I trial of twice-weekly 17-allylamino-demethoxy-geldanamycin in patients with advanced cancer
    • Nowakowski GS, McCollum AK, Ames MM, et al. A phase I trial of twice-weekly 17-allylamino-demethoxy-geldanamycin in patients with advanced cancer. Clin Cancer Res 2006;12:6087-93.
    • (2006) Clin Cancer Res , vol.12 , pp. 6087-6093
    • Nowakowski, G.S.1    McCollum, A.K.2    Ames, M.M.3
  • 15
    • 33751258297 scopus 로고    scopus 로고
    • Development of 17-allylamino-17- demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anti-cancer agent directed against Hsp90
    • Sydor JR, Normant E, Pien CS, et al. Development of 17-allylamino-17- demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anti-cancer agent directed against Hsp90. Proc Natl Acad Sci U S A 2006;103:17408-13.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 17408-17413
    • Sydor, J.R.1    Normant, E.2    Pien, C.S.3
  • 16
    • 33745086222 scopus 로고    scopus 로고
    • Identification of new biomarkers for clinical trials of Hsp90 inhibitors
    • Zhang H, Chung D, Yang YC, et al. Identification of new biomarkers for clinical trials of Hsp90 inhibitors. Mol Cancer Ther 2006;5:1256-64.
    • (2006) Mol Cancer Ther , vol.5 , pp. 1256-1264
    • Zhang, H.1    Chung, D.2    Yang, Y.C.3
  • 17
    • 35948962411 scopus 로고    scopus 로고
    • Gene expression profiles in HPV-infected head and neck cancer
    • Schlecht NF, Burk RD, Adrien L, et al. Gene expression profiles in HPV-infected head and neck cancer. J Pathol 2007;213:283-93.
    • (2007) J Pathol , vol.213 , pp. 283-293
    • Schlecht, N.F.1    Burk, R.D.2    Adrien, L.3
  • 18
    • 34147150867 scopus 로고    scopus 로고
    • Gene and protein expression profiling of human ovarian cancer cells treated with the heat shock protein 90 inhibitor 17-allylamino-17-demethoxygeldanamycin
    • Maloney A, Clarke PA, Naaby-Hansen S, et al. Gene and protein expression profiling of human ovarian cancer cells treated with the heat shock protein 90 inhibitor 17-allylamino-17-demethoxygeldanamycin. Cancer Res 2007;67:3239-53.
    • (2007) Cancer Res , vol.67 , pp. 3239-3253
    • Maloney, A.1    Clarke, P.A.2    Naaby-Hansen, S.3
  • 19
    • 0034710542 scopus 로고    scopus 로고
    • Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17-demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone
    • Clarke PA, Hostein I, Banerji U, et al. Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17-demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone. Oncogene 2000;19:4125-33.
    • (2000) Oncogene , vol.19 , pp. 4125-4133
    • Clarke, P.A.1    Hostein, I.2    Banerji, U.3
  • 20
    • 34548118760 scopus 로고    scopus 로고
    • Use of a cytokine gene expression signature in lung adenocarcinoma and the surrounding tissue as a prognostic classifier
    • Seike M, Yanaihara N, Bowman ED, et al. Use of a cytokine gene expression signature in lung adenocarcinoma and the surrounding tissue as a prognostic classifier. J Natl Cancer Inst 2007;99:1257-69.
    • (2007) J Natl Cancer Inst , vol.99 , pp. 1257-1269
    • Seike, M.1    Yanaihara, N.2    Bowman, E.D.3
  • 21
    • 33847340190 scopus 로고    scopus 로고
    • Technical, experimental, and biological variations in isobaric tags for relative and absolute quantitation (iTRAQ)
    • Gan CS, Chong PK, Pham TK, Wright PC. Technical, experimental, and biological variations in isobaric tags for relative and absolute quantitation (iTRAQ). J Proteome Res 2007;6:821-7.
    • (2007) J Proteome Res , vol.6 , pp. 821-827
    • Gan, C.S.1    Chong, P.K.2    Pham, T.K.3    Wright, P.C.4
  • 22
    • 33748088524 scopus 로고    scopus 로고
    • An in vivo platform for translational drug development in pancreatic cancer
    • Rubio-Viqueira B, Jimeno A, Cusatis G, et al. An in vivo platform for translational drug development in pancreatic cancer. Clin Cancer Res 2006;12:4652-61.
    • (2006) Clin Cancer Res , vol.12 , pp. 4652-4661
    • Rubio-Viqueira, B.1    Jimeno, A.2    Cusatis, G.3
  • 23
    • 0033569406 scopus 로고    scopus 로고
    • Molecular classification of cancer: Class discovery and class prediction by gene expression monitoring
    • Golub TR, Slonim DK, Tamayo P, et al. Molecular classification of cancer: class discovery and class prediction by gene expression monitoring. Science 1999;286:531-7.
    • (1999) Science , vol.286 , pp. 531-537
    • Golub, T.R.1    Slonim, D.K.2    Tamayo, P.3
  • 24
    • 27344435774 scopus 로고    scopus 로고
    • Gene set enrichment analysis: A knowledge-based approach for interpreting genome-wide expression profiles
    • Subramanian A, Tamayo P, Mootha VK, et al. Gene set enrichment analysis: a knowledge-based approach for interpreting genome-wide expression profiles. Proc Natl Acad Sci U S A 2005;102:15545-50.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 15545-15550
    • Subramanian, A.1    Tamayo, P.2    Mootha, V.K.3
  • 25
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: The story unfolds
    • Maloney A, Workman P. HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert Opin Biol Ther 2002;2:3-24.
    • (2002) Expert Opin Biol Ther , vol.2 , pp. 3-24
    • Maloney, A.1    Workman, P.2
  • 26
    • 13844314055 scopus 로고    scopus 로고
    • Higher farnesyl diphosphate synthase activity in human colorectal cancer inhibition of cellular apoptosis
    • Notarnicola M, Messa C, Cavallini A, et al. Higher farnesyl diphosphate synthase activity in human colorectal cancer inhibition of cellular apoptosis. Oncology 2004;67:351-8.
    • (2004) Oncology , vol.67 , pp. 351-358
    • Notarnicola, M.1    Messa, C.2    Cavallini, A.3
  • 27
    • 0036614561 scopus 로고    scopus 로고
    • Expression of GP73, a resident Golgi membrane protein, in viral and nonviral liver disease
    • Kladney RD, Cui X, Bulla GA, Brunt EM, Fimmel CJ. Expression of GP73, a resident Golgi membrane protein, in viral and nonviral liver disease. Hepatology 2002;35:1431-40.
    • (2002) Hepatology , vol.35 , pp. 1431-1440
    • Kladney, R.D.1    Cui, X.2    Bulla, G.A.3    Brunt, E.M.4    Fimmel, C.J.5
  • 28
    • 27744539432 scopus 로고    scopus 로고
    • GP73, a resident Golgi glycoprotein, is a novel serum marker for hepatocellular carcinoma
    • Marrero JA, Romano PR, Nikolaeva O, et al. GP73, a resident Golgi glycoprotein, is a novel serum marker for hepatocellular carcinoma. J Hepatol 2005;43:1007-12.
    • (2005) J Hepatol , vol.43 , pp. 1007-1012
    • Marrero, J.A.1    Romano, P.R.2    Nikolaeva, O.3
  • 29
    • 1942536127 scopus 로고    scopus 로고
    • HLA alleles and lung cancer in a Turkish population
    • Ozbek N, Birinci A, Karaoglanoglu O, et al. HLA alleles and lung cancer in a Turkish population. Ann Saudi Med 2004;24:106-11.
    • (2004) Ann Saudi Med , vol.24 , pp. 106-111
    • Ozbek, N.1    Birinci, A.2    Karaoglanoglu, O.3
  • 31
    • 14844291701 scopus 로고    scopus 로고
    • Naturally processed and HLA-B8-presented HPV16 E7 epitope recognized by T cells from patients with cervical cancer
    • Oerke S, Hohn H, Zehbe I, et al. Naturally processed and HLA-B8-presented HPV16 E7 epitope recognized by T cells from patients with cervical cancer. Int J Cancer 2005;114:766-78.
    • (2005) Int J Cancer , vol.114 , pp. 766-778
    • Oerke, S.1    Hohn, H.2    Zehbe, I.3
  • 32
    • 0037099735 scopus 로고    scopus 로고
    • Two distinct pathways mediated by PA28 and hsp90 in major histocompatibility complex class I antigen processing
    • Yamano T, Murata S, Shimbara N, et al. Two distinct pathways mediated by PA28 and hsp90 in major histocompatibility complex class I antigen processing. J Exp Med 2002;196:185-96.
    • (2002) J Exp Med , vol.196 , pp. 185-196
    • Yamano, T.1    Murata, S.2    Shimbara, N.3
  • 33
    • 13244296915 scopus 로고    scopus 로고
    • Transforming growth factor-β (TGF-β) type I receptor/ALK5-dependent activation of the GADD45β gene mediates the induction of biglycan expression by TGF-β
    • Ungefroren H, Groth S, Ruhnke M, Kalthoff H, Fandrich F. Transforming growth factor-β (TGF-β) type I receptor/ALK5-dependent activation of the GADD45β gene mediates the induction of biglycan expression by TGF-β. J Biol Chem 2005;280:2644-52.
    • (2005) J Biol Chem , vol.280 , pp. 2644-2652
    • Ungefroren, H.1    Groth, S.2    Ruhnke, M.3    Kalthoff, H.4    Fandrich, F.5
  • 34
    • 34248202726 scopus 로고    scopus 로고
    • Differential expression of galectins in normal, benign and malignant prostate epithelial cells: Silencing of galectin-3 expression in prostate cancer by its promoter methylation
    • Ahmed H, Banerjee PP, Vasta GR. Differential expression of galectins in normal, benign and malignant prostate epithelial cells: silencing of galectin-3 expression in prostate cancer by its promoter methylation. Biochem Biophys Res Commun 2007;358:241-6.
    • (2007) Biochem Biophys Res Commun , vol.358 , pp. 241-246
    • Ahmed, H.1    Banerjee, P.P.2    Vasta, G.R.3
  • 35
    • 34249001015 scopus 로고    scopus 로고
    • Association of nuclear, cytoplasmic expression of galectin-3 with β-catenin/Wnt-pathway activation in thyroid carcinoma
    • Weinberger PM, Adam BL, Gourin CG, et al. Association of nuclear, cytoplasmic expression of galectin-3 with β-catenin/Wnt-pathway activation in thyroid carcinoma. Arch Otolaryngol Head Neck Surg 2007;133: 503-10.
    • (2007) Arch Otolaryngol Head Neck Surg , vol.133 , pp. 503-510
    • Weinberger, P.M.1    Adam, B.L.2    Gourin, C.G.3
  • 36
    • 31344480709 scopus 로고    scopus 로고
    • Decreased galectin-3 expression during the progression of cervical neoplasia
    • Lee JW, Song SY, Choi JJ, et al. Decreased galectin-3 expression during the progression of cervical neoplasia. J Cancer Res Clin Oncol 2006;132:241-7.
    • (2006) J Cancer Res Clin Oncol , vol.132 , pp. 241-247
    • Lee, J.W.1    Song, S.Y.2    Choi, J.J.3
  • 37
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 1998; 94:471-80.
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 38
    • 28544433004 scopus 로고    scopus 로고
    • Abrogation of heat shock protein 70 induction as a strategy to increase antileukemia activity of heat shock protein 90 inhibitor 17-allylamino-demethoxy geldanamycin
    • Guo F, Rocha K, Bali P, et al. Abrogation of heat shock protein 70 induction as a strategy to increase antileukemia activity of heat shock protein 90 inhibitor 17-allylamino-demethoxy geldanamycin. Cancer Res 2005;65:10536-44.
    • (2005) Cancer Res , vol.65 , pp. 10536-10544
    • Guo, F.1    Rocha, K.2    Bali, P.3
  • 39
    • 31944445649 scopus 로고    scopus 로고
    • Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation
    • Kim TS, Jang CY, Kim HD, Lee JY, Ahn BY, Kim J. Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation. Mol Biol Cell 2006;17:824-33.
    • (2006) Mol Biol Cell , vol.17 , pp. 824-833
    • Kim, T.S.1    Jang, C.Y.2    Kim, H.D.3    Lee, J.Y.4    Ahn, B.Y.5    Kim, J.6
  • 40
    • 0036091221 scopus 로고    scopus 로고
    • 17-Allylamino-17- demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts
    • Solit DB, Zheng FF, Drobnjak M, et al. 17-Allylamino-17- demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts. Clin Cancer Res 2002;8:986-93.
    • (2002) Clin Cancer Res , vol.8 , pp. 986-993
    • Solit, D.B.1    Zheng, F.F.2    Drobnjak, M.3
  • 41
    • 18844396087 scopus 로고    scopus 로고
    • Potent activity of a novel dimeric heat shock protein 90 inhibitor against head and neck squamous cell carcinoma in vitro and in vivo
    • Yin X, Zhang H, Burrows F, Zhang L, Shores CG. Potent activity of a novel dimeric heat shock protein 90 inhibitor against head and neck squamous cell carcinoma in vitro and in vivo. Clin Cancer Res 2005;11: 3889-96.
    • (2005) Clin Cancer Res , vol.11 , pp. 3889-3896
    • Yin, X.1    Zhang, H.2    Burrows, F.3    Zhang, L.4    Shores, C.G.5
  • 42
    • 0037012344 scopus 로고    scopus 로고
    • Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228
    • Yu X, Guo ZS, Marcu MG, et al. Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228. J Natl Cancer Inst 2002;94:504-13.
    • (2002) J Natl Cancer Inst , vol.94 , pp. 504-513
    • Yu, X.1    Guo, Z.S.2    Marcu, M.G.3
  • 43
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl LH, Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem 2006;75:271-94.
    • (2006) Annu Rev Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 44
    • 11244337455 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of 17-demethoxy 17-[(2-dimethylamino)ethyl]amino]-geldanamycin (17DMAG, NSC 707545) in C.B-17 SCID mice bearing MDA-MB-231 human breast cancer xenografts
    • Eiseman JL, Lan J, Lagattuta TF, et al. Pharmacokinetics and pharmacodynamics of 17-demethoxy 17-[(2-dimethylamino)ethyl]amino]-geldanamycin (17DMAG, NSC 707545) in C.B-17 SCID mice bearing MDA-MB-231 human breast cancer xenografts. Cancer Chemother Pharmacol 2005;55:21-32.
    • (2005) Cancer Chemother Pharmacol , vol.55 , pp. 21-32
    • Eiseman, J.L.1    Lan, J.2    Lagattuta, T.F.3
  • 45
    • 34547683376 scopus 로고    scopus 로고
    • The geldanamycin analogue 17-allylamino-17-demethoxygeldanamycin inhibits the growth of GL261 glioma cells in vitro and in vivo
    • Newcomb EW, Lukyanov Y, Schnee T, et al. The geldanamycin analogue 17-allylamino-17-demethoxygeldanamycin inhibits the growth of GL261 glioma cells in vitro and in vivo. Anticancer Drugs 2007;18: 875-82.
    • (2007) Anticancer Drugs , vol.18 , pp. 875-882
    • Newcomb, E.W.1    Lukyanov, Y.2    Schnee, T.3
  • 46
    • 49849084850 scopus 로고    scopus 로고
    • An in vitro and in vivo study of the combination of the heat shock protein inhibitor 17-allylamino-17-demethoxygeldanamycin and carboplatin in human ovarian cancer models
    • Banerji U, Sain N, Sharp SY, et al. An in vitro and in vivo study of the combination of the heat shock protein inhibitor 17-allylamino-17-demethoxygeldanamycin and carboplatin in human ovarian cancer models. Cancer Chemother Pharmacol 2008;62:769-78.
    • (2008) Cancer Chemother Pharmacol , vol.62 , pp. 769-778
    • Banerji, U.1    Sain, N.2    Sharp, S.Y.3
  • 47
    • 34548490977 scopus 로고    scopus 로고
    • Intratumor injection of the Hsp90 inhibitor 17AAG decreases tumor growth and induces apoptosis in a prostate cancer xenograft model
    • Williams CR, Tabios R, Linehan WM, Neckers L. Intratumor injection of the Hsp90 inhibitor 17AAG decreases tumor growth and induces apoptosis in a prostate cancer xenograft model. J Urol 2007; 178:1528-32.
    • (2007) J Urol , vol.178 , pp. 1528-1532
    • Williams, C.R.1    Tabios, R.2    Linehan, W.M.3    Neckers, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.