메뉴 건너뛰기




Volumn 16, Issue 2, 2013, Pages 177-189

Targeting the calmodulin-regulated ErbB/Grb7 signaling axis in cancer therapy

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CALMODULIN; CALMODULIN INHIBITOR; CYSTEINE; DOXORUBICIN; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPIDERMAL GROWTH FACTOR RECEPTOR 2 INHIBITOR; GROWTH FACTOR RECEPTOR BOUND PROTEIN 7; PEPTIDE DERIVATIVE; PROTEIN INHIBITOR; SMALL INTERFERING RNA; THREONINE; TRASTUZUMAB; TRYPTOPHYLPHENYLALANYLGLUTAMYLGLYCYLTYROSYLASPARTYLASPARAGINYLTHREONYLPHENYLALANYLPROLYLCYSTEINE; UNCLASSIFIED DRUG;

EID: 84889880020     PISSN: None     EISSN: 14821826     Source Type: Journal    
DOI: 10.18433/J3V59V     Document Type: Article
Times cited : (15)

References (136)
  • 1
    • 0021204118 scopus 로고
    • Autophosphorylation sites on the epidermal growth factor receptor
    • Downward J, Parker P, Waterfield MD. Autophosphorylation sites on the epidermal growth factor receptor. Nature, 1984; 311:483-485.
    • (1984) Nature , vol.311 , pp. 483-485
    • Downward, J.1    Parker, P.2    Waterfield, M.D.3
  • 2
    • 0023082137 scopus 로고
    • Receptors for epidermal growth factor and other polypeptide mitogens
    • Carpenter G. Receptors for epidermal growth factor and other polypeptide mitogens. Annu Rev Biochem, 1987; 56:881-914.
    • (1987) Annu Rev Biochem , vol.56 , pp. 881-914
    • Carpenter, G.1
  • 3
    • 0024316019 scopus 로고
    • All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails: Identification of a novel site in EGF receptor
    • Margolis BL, Lax I, Kris R, Dombalagian M, Honegger AM, Howk R, Givol D, Ullrich A, Schlessinger J. All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails: identification of a novel site in EGF receptor. J Biol Chem, 1989; 264:10667-10671.
    • (1989) J Biol Chem , vol.264 , pp. 10667-10671
    • Margolis, B.L.1    Lax, I.2    Kris, R.3    Dombalagian, M.4    Honegger, A.M.5    Howk, R.6    Givol, D.7    Ullrich, A.8    Schlessinger, J.9
  • 5
    • 0030795612 scopus 로고    scopus 로고
    • The ErbB signaling network in embryogenesis and oncogenesis: Signal diversification through combinatorial ligand-receptor interactions
    • Alroy I, Yarden Y. The ErbB signaling network in embryogenesis and oncogenesis: signal diversification through combinatorial ligand-receptor interactions. FEBS Lett, 1997; 410:83-86.
    • (1997) FEBS Lett , vol.410 , pp. 83-86
    • Alroy, I.1    Yarden, Y.2
  • 7
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang X, Gureasko J, Shen K, Cole PA, Kuriyan J. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell, 2006; 125:1137-1149.
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 8
    • 0037429779 scopus 로고    scopus 로고
    • The deaf and the dumb: The biology of ErbB-2 and ErbB-3
    • Citri A, Skaria KB, Yarden Y. The deaf and the dumb: the biology of ErbB-2 and ErbB-3. Exp Cell Res, 2003; 284:54-65.
    • (2003) Exp Cell Res , vol.284 , pp. 54-65
    • Citri, A.1    Skaria, K.B.2    Yarden, Y.3
  • 9
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: Towards the systems level
    • Citri A, Yarden Y. EGF-ERBB signalling: towards the systems level. Nat Rev Mol Cell Biol, 2006; 7:505-515.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 505-515
    • Citri, A.1    Yarden, Y.2
  • 10
    • 33645130990 scopus 로고    scopus 로고
    • Signaling through ERBB receptors: Multiple layers of diversity and control
    • Warren CM, Landgraf R. Signaling through ERBB receptors: multiple layers of diversity and control. Cell Signal, 2006; 18:923-933.
    • (2006) Cell Signal , vol.18 , pp. 923-933
    • Warren, C.M.1    Landgraf, R.2
  • 11
    • 0041816011 scopus 로고    scopus 로고
    • Ligand-induced lysosomal epidermal growth factor receptor (EGFR) degradation is preceded by proteasome-dependent EGFR de-ubiquitination
    • Alwan HAJ, van Zoelen EJJ, van Leeuwen JEM. Ligand-induced lysosomal epidermal growth factor receptor (EGFR) degradation is preceded by proteasome-dependent EGFR de-ubiquitination. J Biol Chem, 2003; 278:35781-35790.
    • (2003) J Biol Chem , vol.278 , pp. 35781-35790
    • Alwan, H.A.J.1    van Zoelen, E.J.J.2    van Leeuwen, J.E.M.3
  • 12
    • 0037429692 scopus 로고    scopus 로고
    • Trafficking of the ErbB receptors and its influence on signaling
    • Wiley HS. Trafficking of the ErbB receptors and its influence on signaling. Exp Cell Res, 2003; 284:78-88.
    • (2003) Exp Cell Res , vol.284 , pp. 78-88
    • Wiley, H.S.1
  • 13
    • 34748860356 scopus 로고    scopus 로고
    • Epidermal growth factor receptor degradation: An alternative view of oncogenic pathways
    • Kirisits A, Pils D, Krainer M. Epidermal growth factor receptor degradation: an alternative view of oncogenic pathways. Int J Biochem Cell Biol, 2007; 39:2173-2182.
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 2173-2182
    • Kirisits, A.1    Pils, D.2    Krainer, M.3
  • 15
    • 33751328082 scopus 로고    scopus 로고
    • ErbB receptors: New insights on mechanisms and biology
    • Linggi B, Carpenter G. ErbB receptors: new insights on mechanisms and biology. Trends Cell Biol, 2006; 16:649-656.
    • (2006) Trends Cell Biol , vol.16 , pp. 649-656
    • Linggi, B.1    Carpenter, G.2
  • 16
    • 70349305428 scopus 로고    scopus 로고
    • Epidermal growth factor receptor signaling in liver cell proliferation and apoptosis
    • Reinehr R, Häussinger D. Epidermal growth factor receptor signaling in liver cell proliferation and apoptosis. Biol Chem, 2009; 390:1033-1037.
    • (2009) Biol Chem , vol.390 , pp. 1033-1037
    • Reinehr, R.1    Häussinger, D.2
  • 17
    • 62649114637 scopus 로고    scopus 로고
    • ErbB receptors and cell polarity: New pathways and paradigms for understanding cell migration and invasion
    • Feigin ME, Muthuswamy SK. ErbB receptors and cell polarity: new pathways and paradigms for understanding cell migration and invasion. Exp Cell Res, 2009; 315:707-716.
    • (2009) Exp Cell Res , vol.315 , pp. 707-716
    • Feigin, M.E.1    Muthuswamy, S.K.2
  • 18
    • 63749086305 scopus 로고    scopus 로고
    • ErbB receptors and signaling pathways in cancer
    • Hynes NE, MacDonald G. ErbB receptors and signaling pathways in cancer. Curr Opi Cell Biol, 2009; 21:177-184.
    • (2009) Curr Opi Cell Biol , vol.21 , pp. 177-184
    • Hynes, N.E.1    Macdonald, G.2
  • 19
    • 84855275538 scopus 로고    scopus 로고
    • Endosomal accumulation of the activated epidermal growth factor receptor (EGFR) induces apoptosis
    • Rush JS, Quinalty LM, Engelman L, Sherry DM, Ceresa BP. Endosomal accumulation of the activated epidermal growth factor receptor (EGFR) induces apoptosis. J Biol Chem, 2012; 287:712-722.
    • (2012) J Biol Chem , vol.287 , pp. 712-722
    • Rush, J.S.1    Quinalty, L.M.2    Engelman, L.3    Sherry, D.M.4    Ceresa, B.P.5
  • 20
    • 0028252996 scopus 로고
    • The GRB family of SH2 domain proteins
    • Margolis B. The GRB family of SH2 domain proteins. Prog Biophys Mol Biol, 1994; 62:223-244.
    • (1994) Prog Biophys Mol Biol , vol.62 , pp. 223-244
    • Margolis, B.1
  • 21
    • 0031713878 scopus 로고    scopus 로고
    • The Grb7 family of signalling proteins
    • Daly RJ. The Grb7 family of signalling proteins. Cell Signal, 1998; 10:613-618.
    • (1998) Cell Signal , vol.10 , pp. 613-618
    • Daly, R.J.1
  • 22
    • 0035473462 scopus 로고    scopus 로고
    • The Grb7 family proteins: Structure, interactions with other signaling molecules and potential cellular functions
    • Han DC, Shen T-L, Guan J-L. The Grb7 family proteins: structure, interactions with other signaling molecules and potential cellular functions. Oncogene, 2001; 20:6315-6321.
    • (2001) Oncogene , vol.20 , pp. 6315-6321
    • Han, D.C.1    Shen, T.-L.2    Guan, J.-L.3
  • 25
    • 0025332945 scopus 로고
    • Mutations affecting embryonic cell migrations in Caenorhabditis elegans
    • Manser J, Wood WB. Mutations affecting embryonic cell migrations in Caenorhabditis elegans. Dev Genet, 1990; 11:49-64.
    • (1990) Dev Genet , vol.11 , pp. 49-64
    • Manser, J.1    Wood, W.B.2
  • 26
    • 0031128420 scopus 로고    scopus 로고
    • C elegans cell migration gene mig-10 shares similarities with a family of SH2 domain proteins and acts cell nonautonomously in excretory canal development
    • Manser J, Roonprapunt C, Margolis B. C. elegans cell migration gene mig-10 shares similarities with a family of SH2 domain proteins and acts cell nonautonomously in excretory canal development. Dev Biol, 1997; 184:150-164.
    • (1997) Dev Biol , vol.184 , pp. 150-164
    • Manser, J.1    Roonprapunt, C.2    Margolis, B.3
  • 27
    • 0000226650 scopus 로고    scopus 로고
    • Association of focal adhesion kinase with Grb7 and its role in cell migration
    • Han DC, Guan J-L. Association of focal adhesion kinase with Grb7 and its role in cell migration. J Biol Chem, 1999; 274:24425-24430.
    • (1999) J Biol Chem , vol.274 , pp. 24425-24430
    • Han, D.C.1    Guan, J.-L.2
  • 28
    • 0037160059 scopus 로고    scopus 로고
    • EphB1 associates with Grb7 and regulates cell migration
    • Han DC, Shen T-L, Miao H, Wang B, Guan J-L. EphB1 associates with Grb7 and regulates cell migration. J Biol Chem, 2002; 277:45655-45661.
    • (2002) J Biol Chem , vol.277 , pp. 45655-45661
    • Han, D.C.1    Shen, T.-L.2    Miao, H.3    Wang, B.4    Guan, J.-L.5
  • 31
    • 77951758017 scopus 로고    scopus 로고
    • Differential functions of growth factor receptor-bound protein 7 (GRB7) and its variant GRB7v in ovarian carcinogenesis
    • Wang Y, Chan DW, Liu VWS, Chu PM, Ngan HYS. Differential functions of growth factor receptor-bound protein 7 (GRB7) and its variant GRB7v in ovarian carcinogenesis. Clin Cancer Res, 2010; 16:2529-2539.
    • (2010) Clin Cancer Res , vol.16 , pp. 2529-2539
    • Wang, Y.1    Chan, D.W.2    Liu, V.W.S.3    Chu, P.M.4    Ngan, H.Y.S.5
  • 34
    • 67749099777 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of growth factor receptor-bound protein-7 by focal adhesion kinase in the regulation of cell migration, proliferation, and tumorigenesis
    • Chu P-Y, Huang L-Y, Hsu C-H, Liang C-C, Guan J-L, Hung T-H, Shen T-L. Tyrosine phosphorylation of growth factor receptor-bound protein-7 by focal adhesion kinase in the regulation of cell migration, proliferation, and tumorigenesis. J Biol Chem, 2009; 284:20215-20226.
    • (2009) J Biol Chem , vol.284 , pp. 20215-20226
    • Chu, P.-Y.1    Huang, L.-Y.2    Hsu, C.-H.3    Liang, C.-C.4    Guan, J.-L.5    Hung, T.-H.6    Shen, T.-L.7
  • 35
    • 77956556826 scopus 로고    scopus 로고
    • EGF-induced Grb7 recruits and promotes Ras activity essential for the tumorigenicity of Sk-Br3 breast cancer cells
    • Chu P-Y, Li T-K, Ding S-T, Lai I-R, Shen T-L. EGF-induced Grb7 recruits and promotes Ras activity essential for the tumorigenicity of Sk-Br3 breast cancer cells. J Biol Chem, 2010; 285:29279-29285.
    • (2010) J Biol Chem , vol.285 , pp. 29279-29285
    • Chu, P.-Y.1    Li, T.-K.2    Ding, S.-T.3    Lai, I.-R.4    Shen, T.-L.5
  • 36
    • 33745686009 scopus 로고    scopus 로고
    • RNA interference-based functional dissection of the 17q12 amplicon in breast cancer reveals contribution of coamplified genes
    • Kao J, Pollack J-R. RNA interference-based functional dissection of the 17q12 amplicon in breast cancer reveals contribution of coamplified genes. Genes Chrom Cancer, 2006; 45:761-769.
    • (2006) Genes Chrom Cancer , vol.45 , pp. 761-769
    • Kao, J.1    Pollack, J.-R.2
  • 37
    • 34248525627 scopus 로고    scopus 로고
    • Combination treatment with Grb7 peptide and Doxorubicin or Trastuzumab (Herceptin) results in cooperative cell growth inhibition in breast cancer cells
    • Pero SC, Shukla GS, Cookson MM, Flemer S Jr, Krag DN. Combination treatment with Grb7 peptide and Doxorubicin or Trastuzumab (Herceptin) results in cooperative cell growth inhibition in breast cancer cells. Br J Cancer, 2007; 96:1520-1525.
    • (2007) Br J Cancer , vol.96 , pp. 1520-1525
    • Pero, S.C.1    Shukla, G.S.2    Cookson, M.M.3    Flemer Jr., S.4    Krag, D.N.5
  • 38
    • 84882242399 scopus 로고    scopus 로고
    • Nuclear magnetic resonance imaging of tumour growth and neovasculature performance in vivo reveals Grb7 as a novel antiangiogenic target
    • doi: 10.1002/nbm.2918
    • García-Palmero I, López-Larrubia P, Cerdán S, Villalobo A. Nuclear magnetic resonance imaging of tumour growth and neovasculature performance in vivo reveals Grb7 as a novel antiangiogenic target. NMR Biomed, 2013; doi: 10.1002/nbm.2918.
    • (2013) NMR Biomed
    • García-Palmero, I.1    López-Larrubia, P.2    Cerdán, S.3    Villalobo, A.4
  • 39
    • 33947577607 scopus 로고    scopus 로고
    • The adaptor Grb7 links netrin-1 signaling to regulation of mRNA translation
    • Tsai N-P, Bi J, Wei L-N. The adaptor Grb7 links netrin-1 signaling to regulation of mRNA translation. EMBO J, 2007; 26:1522-1531.
    • (2007) EMBO J , vol.26 , pp. 1522-1531
    • Tsai, N.-P.1    Bi, J.2    Wei, L.-N.3
  • 40
    • 40949135034 scopus 로고    scopus 로고
    • Regulation of stress granule dynamics by Grb7 and FAK signaling pathway
    • Tsai N-P, Ho P-C, Wei L-N. Regulation of stress granule dynamics by Grb7 and FAK signaling pathway. EMBO J, 2008; 27:715-726.
    • (2008) EMBO J , vol.27 , pp. 715-726
    • Tsai, N.-P.1    Ho, P.-C.2    Wei, L.-N.3
  • 43
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • Chin D, Means AR. Calmodulin: a prototypical calcium sensor. Trends Cell Biol, 2000; 10:322-328.
    • (2000) Trends Cell Biol , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 44
    • 0033548680 scopus 로고    scopus 로고
    • 2+- calmodulin in intact cells
    • 2+- calmodulin in intact cells. J Biol Chem, 1999; 274:6827-6830.
    • (1999) J Biol Chem , vol.274 , pp. 6827-6830
    • Persechini, A.1    Cronk, B.2
  • 45
    • 79955659147 scopus 로고    scopus 로고
    • A general strategy to characterize calmodulin-calcium complexes in CaM-target recognition: DAPK and EGFR calmodulin binding domains interact with different calmodulin-calcium complexes
    • Dagher R, Peng S, Gioria S, Fève M, Zeniou M, Zimmermann M, Pigault C, Haiech J, Kilhoffer M-C. A general strategy to characterize calmodulin-calcium complexes in CaM-target recognition: DAPK and EGFR calmodulin binding domains interact with different calmodulin-calcium complexes. Biochim Biophys Acta, 2011; 1813:1059-1067.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1059-1067
    • Dagher, R.1    Peng, S.2    Gioria, S.3    Fève, M.4    Zeniou, M.5    Zimmermann, M.6    Pigault, C.7    Haiech, J.8    Kilhoffer, M.-C.9
  • 48
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: Sequence independent recognition of amphiphilic α-helices
    • O'Neil KT, DeGrado WF. How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helices. Trends Biochem Sci, 1990; 15:59-64.
    • (1990) Trends Biochem Sci , vol.15 , pp. 59-64
    • O'Neil, K.T.1    Degrado, W.F.2
  • 49
    • 0030945196 scopus 로고    scopus 로고
    • Sequence motifs for calmodulin recognition
    • Rhoads AR, Friedberg F. Sequence motifs for calmodulin recognition. FASEB J, 1997; 11:331-340.
    • (1997) FASEB J , vol.11 , pp. 331-340
    • Rhoads, A.R.1    Friedberg, F.2
  • 50
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • Hoeflich KP, Ikura M. Calmodulin in action: diversity in target recognition and activation mechanisms. Cell, 2002; 108:739-742.
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 51
    • 0020638179 scopus 로고
    • Inhibition of human breast cancer colony formation by anticalmodulin agents: Trifluoperazine, W-7, and W-13
    • Wei JW, Hickie RZ, Klaassen DJ. Inhibition of human breast cancer colony formation by anticalmodulin agents: trifluoperazine, W-7, and W-13. Cancer Chemother Pharmacol, 1983; 11:86-90.
    • (1983) Cancer Chemother Pharmacol , vol.11 , pp. 86-90
    • Wei, J.W.1    Hickie, R.Z.2    Klaassen, D.J.3
  • 52
    • 0022516721 scopus 로고
    • Calmodulin: A potential target for cancer chemotherapeutic agents
    • Hait WN, Lazo JS. Calmodulin: a potential target for cancer chemotherapeutic agents. J Clin Oncol, 1986; 4:994-1012.
    • (1986) J Clin Oncol , vol.4 , pp. 994-1012
    • Hait, W.N.1    Lazo, J.S.2
  • 53
    • 33749531924 scopus 로고    scopus 로고
    • New anti-mitotic drugs with distinct anti-calmodulin activity
    • Orosz F, Horváth I, Ovádi J. New anti-mitotic drugs with distinct anti-calmodulin activity. Mini Rev Med Chem, 2006; 6:1145-1157.
    • (2006) Mini Rev Med Chem , vol.6 , pp. 1145-1157
    • Orosz, F.1    Horváth, I.2    Ovádi, J.3
  • 54
    • 33845386823 scopus 로고    scopus 로고
    • Targeting calmodulin in reversing multi drug resistance in cancer cells
    • Mayur YC, Jagadeesh S, Thimmaiah KN. Targeting calmodulin in reversing multi drug resistance in cancer cells. Mini Rev Med Chem, 2006; 6:1383-1389.
    • (2006) Mini Rev Med Chem , vol.6 , pp. 1383-1389
    • Mayur, Y.C.1    Jagadeesh, S.2    Thimmaiah, K.N.3
  • 55
    • 0019947482 scopus 로고
    • Interaction of drugs with calmodulin: Biochemical, pharmacological and clinical implications
    • Weiss B, Prozialeck WC, Wallace TL. Interaction of drugs with calmodulin: biochemical, pharmacological and clinical implications. Biochem Pharmacol, 1982; 31:2217-2226.
    • (1982) Biochem Pharmacol , vol.31 , pp. 2217-2226
    • Weiss, B.1    Prozialeck, W.C.2    Wallace, T.L.3
  • 57
    • 0022211395 scopus 로고
    • Calmodulin: Structure-function relations and inhibitors
    • Walsh MP. Calmodulin: structure-function relations and inhibitors. Rev Clin Basic Pharm, 1985; 5:35-69.
    • (1985) Rev Clin Basic Pharm , vol.5 , pp. 35-69
    • Walsh, M.P.1
  • 58
    • 0024401656 scopus 로고
    • The use and limitations of calmodulin antagonists
    • Veigl ML, Klevit RE, Sedwick WD. The use and limitations of calmodulin antagonists. Pharmacol Ther, 1989; 44:181-239.
    • (1989) Pharmacol Ther , vol.44 , pp. 181-239
    • Veigl, M.L.1    Klevit, R.E.2    Sedwick, W.D.3
  • 59
    • 0026708937 scopus 로고
    • Molecular pharmacology of calmodulin pathways in the cell functions
    • Hidaka H, Ishikawa T. Molecular pharmacology of calmodulin pathways in the cell functions. Cell Calcium, 1992; 13:465-472.
    • (1992) Cell Calcium , vol.13 , pp. 465-472
    • Hidaka, H.1    Ishikawa, T.2
  • 60
  • 61
    • 0028914706 scopus 로고
    • Calcium, calmodulin and cell cycle progression
    • Takuwa N, Zhow W, Takuwa Y. Calcium, calmodulin and cell cycle progression. Cell Signal, 1995; 7:93-104.
    • (1995) Cell Signal , vol.7 , pp. 93-104
    • Takuwa, N.1    Zhow, W.2    Takuwa, Y.3
  • 62
    • 74549204565 scopus 로고    scopus 로고
    • Calmodulin-mediated regulation of the epidermal growth factor receptor
    • Sánchez-González P, Jellali K, Villalobo A. Calmodulin-mediated regulation of the epidermal growth factor receptor. FEBS J, 2010; 277:327-342.
    • (2010) FEBS J , vol.277 , pp. 327-342
    • Sánchez-González, P.1    Jellali, K.2    Villalobo, A.3
  • 63
    • 0026637981 scopus 로고
    • Calmodulin inhibits the epidermal growth factor receptor tyrosine kinase
    • San José E, Benguría A, Geller P, Villalobo A. Calmodulin inhibits the epidermal growth factor receptor tyrosine kinase. J Biol Chem, 1992; 267:15237-15245.
    • (1992) J Biol Chem , vol.267 , pp. 15237-15245
    • San, J.E.1    Benguría, A.2    Geller, P.3    Villalobo, A.4
  • 64
    • 0345195976 scopus 로고    scopus 로고
    • The human epidermal growth factor receptor contains a juxtamembrane calmodulin-binding site
    • Martín-Nieto J, Villalobo A. The human epidermal growth factor receptor contains a juxtamembrane calmodulin-binding site. Biochemistry, 1998; 37:227-236.
    • (1998) Biochemistry , vol.37 , pp. 227-236
    • Martín-Nieto, J.1    Villalobo, A.2
  • 65
    • 0036888526 scopus 로고    scopus 로고
    • Interactions between the juxtamembrane domain of the EGFR and calmodulin measured by surface plasmon resonance
    • Aifa S, Johansen K, Nilsson UK, Liedberg B, Lundström I, Svensson SPS. Interactions between the juxtamembrane domain of the EGFR and calmodulin measured by surface plasmon resonance. Cell Signal, 2002; 14:1005-1013.
    • (2002) Cell Signal , vol.14 , pp. 1005-1013
    • Aifa, S.1    Johansen, K.2    Nilsson, U.K.3    Liedberg, B.4    Lundström, I.5    Svensson, S.P.S.6
  • 66
    • 0036499476 scopus 로고    scopus 로고
    • Evidence for the direct interaction between calmodulin and the human epidermal growth factor receptor
    • Li H, Villalobo A. Evidence for the direct interaction between calmodulin and the human epidermal growth factor receptor. Biochem J, 2002; 362:499-505.
    • (2002) Biochem J , vol.362 , pp. 499-505
    • Li, H.1    Villalobo, A.2
  • 67
    • 0442292089 scopus 로고    scopus 로고
    • Endogenous calmodulin interacts with the epidermal growth factor receptor in living cells
    • Li H, Ruano MJ, Villalobo A. Endogenous calmodulin interacts with the epidermal growth factor receptor in living cells. FEBS Lett, 2004; 559:175-180.
    • (2004) FEBS Lett , vol.559 , pp. 175-180
    • Li, H.1    Ruano, M.J.2    Villalobo, A.3
  • 68
    • 22244449320 scopus 로고    scopus 로고
    • An electrostatic engine model for autoinhibition and activation of the epidermal growth factor receptor (EGFR/ErbB) family
    • McLaughlin S, Smith SO, Hayman MJ, Murray D. An electrostatic engine model for autoinhibition and activation of the epidermal growth factor receptor (EGFR/ErbB) family. J Gen Physiol, 2005; 126:41-53.
    • (2005) J Gen Physiol , vol.126 , pp. 41-53
    • McLaughlin, S.1    Smith, S.O.2    Hayman, M.J.3    Murray, D.4
  • 71
    • 34247189583 scopus 로고    scopus 로고
    • Membrane-permeable calmodulin inhibitors (e.g., W-7/W-13) bind to membranes, changing the electrostatic surface potential: Dual effect of W-13 on EGFR activation
    • Sengupta P, Ruano MJ, Tebar F, Golebiewska U, Zaitseva I, Enrich C, McLaughlin S, Villalobo A. Membrane-permeable calmodulin inhibitors (e.g., W-7/W-13) bind to membranes, changing the electrostatic surface potential: dual effect of W-13 on EGFR activation. J Biol Chem, 2007; 282:8474-8486.
    • (2007) J Biol Chem , vol.282 , pp. 8474-8486
    • Sengupta, P.1    Ruano, M.J.2    Tebar, F.3    Golebiewska, U.4    Zaitseva, I.5    Enrich, C.6    McLaughlin, S.7    Villalobo, A.8
  • 76
    • 79955646433 scopus 로고    scopus 로고
    • Calmodulin binds HER2 and modulates HER2 signaling
    • White CD, Li Z, Sacks DB. Calmodulin binds HER2 and modulates HER2 signaling. Biochim Biophys Acta, 2011; 1813:1074-1082.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1074-1082
    • White, C.D.1    Li, Z.2    Sacks, D.B.3
  • 78
    • 84859243184 scopus 로고    scopus 로고
    • The nuclear epidermal growth factor receptor signaling network and its role in cancer
    • Brand TM, Iida M, Li C, Wheeler DL. The nuclear epidermal growth factor receptor signaling network and its role in cancer. Discov Med, 2011; 12:419-432.
    • (2011) Discov Med , vol.12 , pp. 419-432
    • Brand, T.M.1    Iida, M.2    Li, C.3    Wheeler, D.L.4
  • 79
    • 84864589406 scopus 로고    scopus 로고
    • Nuclear functions and subcellular trafficking mechanisms of the epidermal growth factor receptor family
    • Wang Y-N, Hung M-C. Nuclear functions and subcellular trafficking mechanisms of the epidermal growth factor receptor family. Cell Biosci, 2012; 2:13.
    • (2012) Cell Biosci , vol.2 , pp. 13
    • Wang, Y.-N.1    Hung, M.-C.2
  • 81
    • 33749072019 scopus 로고    scopus 로고
    • Nuclear signaling by receptor tyrosine kinases: The first robin of spring
    • Schlessinger J, Lemmon MA. Nuclear signaling by receptor tyrosine kinases: the first robin of spring. Cell, 2006; 127:45-48.
    • (2006) Cell , vol.127 , pp. 45-48
    • Schlessinger, J.1    Lemmon, M.A.2
  • 82
    • 0033604516 scopus 로고    scopus 로고
    • The role of the epidermal growth factor receptor family in mammary tumorigenesis and metastasis
    • Kim H, Muller WJ. The role of the epidermal growth factor receptor family in mammary tumorigenesis and metastasis. Exp Cell Res, 1999; 253:78-87.
    • (1999) Exp Cell Res , vol.253 , pp. 78-87
    • Kim, H.1    Muller, W.J.2
  • 83
    • 0034638917 scopus 로고    scopus 로고
    • Overexpression of ErbB2 in cancer and ErbB2-targeting strategies
    • Yu D, Hung MC. Overexpression of ErbB2 in cancer and ErbB2-targeting strategies. Oncogene, 2000; 19:6115-6121.
    • (2000) Oncogene , vol.19 , pp. 6115-6121
    • Yu, D.1    Hung, M.C.2
  • 84
    • 0034954124 scopus 로고    scopus 로고
    • The type III epidermal growth factor receptor mutation: Biological significance and potential target for anti-cancer therapy
    • Pedersen MW, Meltorn M, Damstrup L, Poulsen HS. The type III epidermal growth factor receptor mutation: biological significance and potential target for anti-cancer therapy. Ann Oncol, 2001; 12:745-760.
    • (2001) Ann Oncol , vol.12 , pp. 745-760
    • Pedersen, M.W.1    Meltorn, M.2    Damstrup, L.3    Poulsen, H.S.4
  • 85
    • 2442701289 scopus 로고    scopus 로고
    • The ErbB/HER receptor protein-tyrosine kinases and cancer
    • Roskoski R Jr. The ErbB/HER receptor protein-tyrosine kinases and cancer. Biochem Biophys Res Commun, 2004; 319:1-11.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 1-11
    • Roskoski Jr., R.1
  • 89
    • 67349137902 scopus 로고    scopus 로고
    • The EGFRvIII variant in glioblastoma multiforme
    • Gan HK, Kave AH, Luwor RB. The EGFRvIII variant in glioblastoma multiforme. J Clin Neurosci, 2009; 16:748-754.
    • (2009) J Clin Neurosci , vol.16 , pp. 748-754
    • Gan, H.K.1    Kave, A.H.2    Luwor, R.B.3
  • 90
    • 77953133384 scopus 로고    scopus 로고
    • Oncogenic mutant forms of EGFR: Lessons in signal transduction and targets for cancer therapy
    • Pines G, Köstler WJ, Yarden Y. Oncogenic mutant forms of EGFR: lessons in signal transduction and targets for cancer therapy. FEBS Lett, 2010; 584:2699-2706.
    • (2010) FEBS Lett , vol.584 , pp. 2699-2706
    • Pines, G.1    Köstler, W.J.2    Yarden, Y.3
  • 93
    • 80055089812 scopus 로고    scopus 로고
    • Epidermal growth factor receptor pathway mutations and colorectal cancer therapy
    • Grossmann AH, Samowitz WS. Epidermal growth factor receptor pathway mutations and colorectal cancer therapy. Arch Pathol Lab Med, 2011; 135:1278-1282.
    • (2011) Arch Pathol Lab Med , vol.135 , pp. 1278-1282
    • Grossmann, A.H.1    Samowitz, W.S.2
  • 94
    • 0036720103 scopus 로고    scopus 로고
    • ErbB receptor tyrosine kinase inhibitors as therapeutic agents
    • Anderson NG, Ahmad T. ErbB receptor tyrosine kinase inhibitors as therapeutic agents. Front Biosci, 2002; 7:d1926-d1940.
    • (2002) Front Biosci , vol.7
    • Anderson, N.G.1    Ahmad, T.2
  • 95
    • 0037211253 scopus 로고    scopus 로고
    • Epidermal growth factor receptor tyrosine kinase inhibitors (EGFR-TKIs): Simple drugs with a complex mechanism of action?
    • Normanno N, Maiello MR, De Luca A. Epidermal growth factor receptor tyrosine kinase inhibitors (EGFR-TKIs): simple drugs with a complex mechanism of action? J Cell Physiol, 2002; 194:13-19.
    • (2002) J Cell Physiol , vol.194 , pp. 13-19
    • Normanno, N.1    Maiello, M.R.2    de Luca, A.3
  • 96
    • 11244334282 scopus 로고    scopus 로고
    • Small molecule epidermal growth factor receptor tyrosine kinase inhibitors: An overview
    • Normanno N, Maiello MR, Mancino M, De Luca A. Small molecule epidermal growth factor receptor tyrosine kinase inhibitors: an overview. J Chemother, 2004; 16 Suppl 4:36-40.
    • (2004) J Chemother , vol.16 , Issue.4 SUPPL. , pp. 36-40
    • Normanno, N.1    Maiello, M.R.2    Mancino, M.3    de Luca, A.4
  • 97
    • 3042782959 scopus 로고    scopus 로고
    • Epidermal growth factor receptor tyrosine kinase inhibitors
    • Ranson M. Epidermal growth factor receptor tyrosine kinase inhibitors. Br J Cancer, 2004; 90:2250-2255.
    • (2004) Br J Cancer , vol.90 , pp. 2250-2255
    • Ranson, M.1
  • 98
    • 33746485766 scopus 로고    scopus 로고
    • Epidermal growth factor receptor targeting in cancer
    • Mendelson J, Baselga J. Epidermal growth factor receptor targeting in cancer. Semin Oncol, 2006; 33:369-385.
    • (2006) Semin Oncol , vol.33 , pp. 369-385
    • Mendelson, J.1    Baselga, J.2
  • 99
    • 34147107009 scopus 로고    scopus 로고
    • Second-generation epidermal growth factor receptor tyrosine kinase inhibitors in non-small cell lung cancer
    • Sequist LV. Second-generation epidermal growth factor receptor tyrosine kinase inhibitors in non-small cell lung cancer. Oncologist, 2007; 12:325-330.
    • (2007) Oncologist , vol.12 , pp. 325-330
    • Sequist, L.V.1
  • 100
    • 84857088600 scopus 로고    scopus 로고
    • Epidermal growth factor receptor tyrosine kinase inhibitors in the treatment of epidermal growth factor receptor-mutant non-small cell lung cancer metastatic to the brain
    • Jamal-Hanjani M, Spicer J. Epidermal growth factor receptor tyrosine kinase inhibitors in the treatment of epidermal growth factor receptor-mutant non-small cell lung cancer metastatic to the brain. Clin Cancer Res, 2012; 18:938-944.
    • (2012) Clin Cancer Res , vol.18 , pp. 938-944
    • Jamal-Hanjani, M.1    Spicer, J.2
  • 101
    • 84861330461 scopus 로고    scopus 로고
    • In silico screening of epidermal growth factor receptor (EGFR) in the tyrosine kinase domain through a medicinal plant compound database
    • Sawatdichaikul O, Hannongbua S, Sangma C, Wolschann P, Choowongkomon K. In silico screening of epidermal growth factor receptor (EGFR) in the tyrosine kinase domain through a medicinal plant compound database. J Mol Model, 2012; 18:1241-1254.
    • (2012) J Mol Model , vol.18 , pp. 1241-1254
    • Sawatdichaikul, O.1    Hannongbua, S.2    Sangma, C.3    Wolschann, P.4    Choowongkomon, K.5
  • 102
    • 84889887686 scopus 로고    scopus 로고
    • EGFR-targeted cancer research: Continuing progress and changing views (Editorial)
    • Lipton A, Villalobo A. EGFR-targeted cancer research: continuing progress and changing views (Editorial). Signal, 2001; 2:2-3.
    • (2001) Signal , vol.2 , pp. 2-3
    • Lipton, A.1    Villalobo, A.2
  • 103
    • 17844372539 scopus 로고    scopus 로고
    • Critical update and emerging trends in epidermal growth factor receptor targeting in cancer
    • Baselga J, Arteaga CL. Critical update and emerging trends in epidermal growth factor receptor targeting in cancer. J Clin Oncol, 2005; 23:2445-2459.
    • (2005) J Clin Oncol , vol.23 , pp. 2445-2459
    • Baselga, J.1    Arteaga, C.L.2
  • 104
    • 61349158561 scopus 로고    scopus 로고
    • Human anti-ErbB2 immunoagents - immunoRNases and compact antibodies
    • De Lorenzo C, D'Alessio G. Human anti-ErbB2 immunoagents - immunoRNases and compact antibodies. FEBS J, 2009; 276:1527-1535.
    • (2009) FEBS J , vol.276 , pp. 1527-1535
    • de Lorenzo, C.1    D'Alessio, G.2
  • 105
    • 77953389316 scopus 로고    scopus 로고
    • New trends in epidermal growth factor receptor-directed monoclonal antibodies
    • Markman B, Capdevilla J, Elez E, Tabernero J. New trends in epidermal growth factor receptor-directed monoclonal antibodies. Immunotherapy, 2009; 1:965-982.
    • (2009) Immunotherapy , vol.1 , pp. 965-982
    • Markman, B.1    Capdevilla, J.2    Elez, E.3    Tabernero, J.4
  • 107
    • 84864035249 scopus 로고    scopus 로고
    • Single domain antibodies: A new concept for epidermal growth factor receptor and EGFRvIII targeting
    • Omidfar K, Shirvani Z. Single domain antibodies: a new concept for epidermal growth factor receptor and EGFRvIII targeting. DNA Cell Biol, 2012; 1015-1026.
    • (2012) DNA Cell Biol , pp. 1015-1026
    • Omidfar, K.1    Shirvani, Z.2
  • 109
    • 84856282034 scopus 로고    scopus 로고
    • Targeting epidermal growth factor receptor in tumors: From conventional antibodies via heavy chain-only antibodies to nanobodies
    • Altintas I, Kok RJ, Schiffelers RM. Targeting epidermal growth factor receptor in tumors: from conventional antibodies via heavy chain-only antibodies to nanobodies. Eur J Pharm Sci, 2012; 45:399-407.
    • (2012) Eur J Pharm Sci , vol.45 , pp. 399-407
    • Altintas, I.1    Kok, R.J.2    Schiffelers, R.M.3
  • 110
    • 33846852882 scopus 로고    scopus 로고
    • PTEN-mediated resistance to epidermal growth factor receptor kinase inhibitors
    • Mellinghoff IK, Cloughesy TF, Mischel PS. PTEN-mediated resistance to epidermal growth factor receptor kinase inhibitors. Clin Cancer Res, 2007; 13:378-381.
    • (2007) Clin Cancer Res , vol.13 , pp. 378-381
    • Mellinghoff, I.K.1    Cloughesy, T.F.2    Mischel, P.S.3
  • 111
    • 49649127657 scopus 로고    scopus 로고
    • Mechanisms of acquired resistance to epidermal growth factor receptor tyrosine kinase inhibitors in non-small cell lung cancer
    • Engelman JA, Jänne PA. Mechanisms of acquired resistance to epidermal growth factor receptor tyrosine kinase inhibitors in non-small cell lung cancer. Clin Cancer Res, 2008; 14:2895-2899.
    • (2008) Clin Cancer Res , vol.14 , pp. 2895-2899
    • Engelman, J.A.1    Jänne, P.A.2
  • 112
    • 78650208364 scopus 로고    scopus 로고
    • Mechanisms of resistance to anti-human epidermal growth factor receptor 2 agents in breast cancer
    • Mukohara T. Mechanisms of resistance to anti-human epidermal growth factor receptor 2 agents in breast cancer. Cancer Sci, 2011; 102:1-8.
    • (2011) Cancer Sci , vol.102 , pp. 1-8
    • Mukohara, T.1
  • 113
    • 84861042428 scopus 로고    scopus 로고
    • Primary and acquired resistance to epidermal growth factor receptor tyrosine kinase inhibitors in non-small cell lung cancer: An update
    • Ayoola A, Barochia A, Belani K, Belani CP. Primary and acquired resistance to epidermal growth factor receptor tyrosine kinase inhibitors in non-small cell lung cancer: an update. Cancer Invest, 2012; 30:433-446.
    • (2012) Cancer Invest , vol.30 , pp. 433-446
    • Ayoola, A.1    Barochia, A.2    Belani, K.3    Belani, C.P.4
  • 114
    • 0035160313 scopus 로고    scopus 로고
    • Cardiotoxicity in signal transduction therapeutics: ErbB2 antibodies and the heart
    • Schneider JW, Chang AY, Rocco TP. Cardiotoxicity in signal transduction therapeutics: erbB2 antibodies and the heart. Semin Oncol, 2001; 28:18-26.
    • (2001) Semin Oncol , vol.28 , pp. 18-26
    • Schneider, J.W.1    Chang, A.Y.2    Rocco, T.P.3
  • 115
    • 77954724869 scopus 로고    scopus 로고
    • Cardiovascular effects of EGFR (epidermal growth factor receptor) monoclonal antibodies
    • Chaudhary P, Gaira A. Cardiovascular effects of EGFR (epidermal growth factor receptor) monoclonal antibodies. Cardiovasc Hematol Agents Med Chem, 2010; 8:156-163.
    • (2010) Cardiovasc Hematol Agents Med Chem , vol.8 , pp. 156-163
    • Chaudhary, P.1    Gaira, A.2
  • 116
    • 0026643602 scopus 로고
    • Ligand-induced functions of the epidermal growth factor receptor require the positively charged region asymmetrically distributed across plasma membrane
    • Yamane K, Toyoshima C, Nishimura S. Ligand-induced functions of the epidermal growth factor receptor require the positively charged region asymmetrically distributed across plasma membrane. Biochem Biophys Res Commun, 1992; 184:1301-1310.
    • (1992) Biochem Biophys Res Commun , vol.184 , pp. 1301-1310
    • Yamane, K.1    Toyoshima, C.2    Nishimura, S.3
  • 118
    • 84870823045 scopus 로고    scopus 로고
    • Consequences of replacing EGFR juxtamembrane domain with an unstructured sequence
    • He L, Hristova K. Consequences of replacing EGFR juxtamembrane domain with an unstructured sequence. Sci Rep, 2012; 2:854.
    • (2012) Sci Rep , vol.2 , pp. 854
    • He, L.1    Hristova, K.2
  • 120
    • 73149115292 scopus 로고    scopus 로고
    • Somatic mutations of EGFR, ERBB2, ERBB3 and ERBB4 in juxtamembrane activating domains are rare in non-small cell lung cancers
    • Park SW, Chung NG, Han JY, Eom HS, Yoo NJ, Lee SH. Somatic mutations of EGFR, ERBB2, ERBB3 and ERBB4 in juxtamembrane activating domains are rare in non-small cell lung cancers. Acta Pathol Microbiol Immunol Scand, 2009; 118:83-84.
    • (2009) Acta Pathol Microbiol Immunol Scand , vol.118 , pp. 83-84
    • Park, S.W.1    Chung, N.G.2    Han, J.Y.3    Eom, H.S.4    Yoo, N.J.5    Lee, S.H.6
  • 122
    • 84869222520 scopus 로고    scopus 로고
    • A potential peptide therapeutic derived from the juxtamembrane domain of the epidermal growth factor receptor
    • Boran ADW, Seco J, Jayaraman V, Jayaraman G, Zhao S, Reddy S, Chen Y, Iyengar R. A potential peptide therapeutic derived from the juxtamembrane domain of the epidermal growth factor receptor. PLoS One, 2012; 7:e49702.
    • (2012) PLoS One , vol.7
    • Boran, A.D.W.1    Seco, J.2    Jayaraman, V.3    Jayaraman, G.4    Zhao, S.5    Reddy, S.6    Chen, Y.7    Iyengar, R.8
  • 123
    • 0028946005 scopus 로고
    • Irreversible inactivation of protein kinase C by a peptide-substrate analog
    • Ward NE, Gravitt KR, O'Brian CA. Irreversible inactivation of protein kinase C by a peptide-substrate analog. J Biol Chem, 1995; 270:8056-8060.
    • (1995) J Biol Chem , vol.270 , pp. 8056-8060
    • Ward, N.E.1    Gravitt, K.R.2    O'Brian, C.A.3
  • 124
    • 0021220257 scopus 로고
    • Protein kinase C phosphorylation of the EGF receptor at threonine residue close to the cytoplasmic face of the plasma membrane
    • Hunter T, Ling N, Cooper JA. (1984) Protein kinase C phosphorylation of the EGF receptor at threonine residue close to the cytoplasmic face of the plasma membrane. Nature, 1984; 311:480-483.
    • (1984) Nature , vol.311 , pp. 480-483
    • Hunter, T.1    Ling, N.2    Cooper, J.A.3
  • 125
    • 0025297583 scopus 로고
    • The signal peptide
    • von Heijne G. The signal peptide. J Membr Biol, 1990; 115:195-201
    • (1990) J Membr Biol , vol.115 , pp. 195-201
    • von Heijne, G.1
  • 126
    • 0029006149 scopus 로고
    • Inhibition of nuclear translocation of transcription factor NF-κB by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence
    • Lin Y-Z, Yao SY, Veach RA, Torgerson TR, Hawiger J. Inhibition of nuclear translocation of transcription factor NF-κB by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence. J Biol Chem, 1995; 270:14255-14258.
    • (1995) J Biol Chem , vol.270 , pp. 14255-14258
    • Lin, Y.-Z.1    Yao, S.Y.2    Veach, R.A.3    Torgerson, T.R.4    Hawiger, J.5
  • 127
    • 0029861248 scopus 로고    scopus 로고
    • Controlling epidermal growth factor (EGF)-stimulated Ras activation in intact cells by a cell-permeable peptide mimicking phosphorylated EGF receptor
    • Rojas M, Yao SY, Lin Y-Z. Controlling epidermal growth factor (EGF)-stimulated Ras activation in intact cells by a cell-permeable peptide mimicking phosphorylated EGF receptor. J Biol Chem, 1996; 271:27456-27461.
    • (1996) J Biol Chem , vol.271 , pp. 27456-27461
    • Rojas, M.1    Yao, S.Y.2    Lin, Y.-Z.3
  • 128
    • 34249845380 scopus 로고    scopus 로고
    • Characterization of a novel tripartite nuclear localization sequence in the EGFR family
    • Hsu SC, Hung MC. Characterization of a novel tripartite nuclear localization sequence in the EGFR family. J Biol Chem, 2007; 282:10432-10440.
    • (2007) J Biol Chem , vol.282 , pp. 10432-10440
    • Hsu, S.C.1    Hung, M.C.2
  • 129
    • 79551510855 scopus 로고    scopus 로고
    • EGFR nuclear translocation modulates DNA repair following cisplatin and ionizing radiation
    • Liccardi G, Hartley JA, Hochhauser D. EGFR nuclear translocation modulates DNA repair following cisplatin and ionizing radiation. Cancer Res, 2011; 71:1103-1114.
    • (2011) Cancer Res , vol.71 , pp. 1103-1114
    • Liccardi, G.1    Hartley, J.A.2    Hochhauser, D.3
  • 130
    • 84861197178 scopus 로고    scopus 로고
    • Calmodulin regulates the translocation of Grb7 into the nucleus
    • García-Palmero I, Villalobo A. Calmodulin regulates the translocation of Grb7 into the nucleus. FEBS Lett, 2012; 586:1533-1539.
    • (2012) FEBS Lett , vol.586 , pp. 1533-1539
    • García-Palmero, I.1    Villalobo, A.2
  • 133
    • 0037023768 scopus 로고    scopus 로고
    • Identification of novel non-phosphorylated ligands, which bind selectively to the SH2 domain of Grb7
    • Pero SC, Oligino L, Daly RJ, Soden AL, Liu C, Roller PP, Li P, Krag DN. Identification of novel non-phosphorylated ligands, which bind selectively to the SH2 domain of Grb7. J Biol Chem, 2002; 277:11918-11926.
    • (2002) J Biol Chem , vol.277 , pp. 11918-11926
    • Pero, S.C.1    Oligino, L.2    Daly, R.J.3    Soden, A.L.4    Liu, C.5    Roller, P.P.6    Li, P.7    Krag, D.N.8
  • 134


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.