메뉴 건너뛰기




Volumn 2, Issue 3, 2002, Pages 169-186

Signaling revealed by mapping molecular interactions: Implications for ErbB-targeted cancer immunotherapies

Author keywords

Breast cancer; ErbB family; Fluorescence resonance energy transfer; Herceptin ; Immunoliposomes; Lipid rafts; Receptor tyrosine kinases; Scanning nearfield optical microscopy; Trastuzumab

Indexed keywords

ANSAMYCIN DERIVATIVE; ANTHRACYCLINE; ANTISENSE OLIGONUCLEOTIDE; CANCER VACCINE; CHOLERA TOXIN B SUBUNIT; DOXORUBICIN; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR ANTIBODY; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; IMMUNOLIPOSOME; MACROGOL; MONOCLONAL ANTIBODY; PACLITAXEL; PROTEIN TYROSINE KINASE; RECEPTOR SUBUNIT; TRANSFORMING GROWTH FACTOR ALPHA; TRASTUZUMAB;

EID: 0036625779     PISSN: 15291049     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1529-1049(02)00044-2     Document Type: Review
Times cited : (10)

References (95)
  • 1
    • 0032577051 scopus 로고    scopus 로고
    • The phosphorylation of proteins on tyrosine: Its role in cell growth and disease
    • The Croonian Lecture 1997
    • Hunter T. The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and disease. Philos Trans R Soc Lond B Biol Sci 1998;353:583-605.
    • (1998) Philos. Trans. R. Soc. Lond. B. Biol. Sci. , vol.353 , pp. 583-605
    • Hunter, T.1
  • 3
    • 0031034106 scopus 로고    scopus 로고
    • HER-2/neu signal transduction in human breast and ovarian cancer
    • Reese DM, Slamon DJ. HER-2/neu signal transduction in human breast and ovarian cancer. Stem Cells 1997;15:1-8.
    • (1997) Stem Cells , vol.15 , pp. 1-8
    • Reese, D.M.1    Slamon, D.J.2
  • 5
    • 0032227735 scopus 로고    scopus 로고
    • The role of tyrosine phosphorylation in cell growth and disease
    • Hunter T. The role of tyrosine phosphorylation in cell growth and disease. Harvey Lect 1998;94:81-119.
    • (1998) Harvey Lect. , vol.94 , pp. 81-119
    • Hunter, T.1
  • 6
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen P, Hunter T. Oncogenic kinase signalling. Nature 2001;411:355-65.
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 7
    • 0033367737 scopus 로고    scopus 로고
    • Complexity of signal transduction mediated by ErbB2: Clues to the potential of receptor-targeted cancer therapy
    • Nagy P, Jenei A, Damjanovich S, Jovin TM, Szöll″osi J. Complexity of signal transduction mediated by ErbB2: clues to the potential of receptor-targeted cancer therapy. Pathol Oncol Res 1999;5:255-71.
    • (1999) Pathol. Oncol. Res. , vol.5 , pp. 255-271
    • Nagy, P.1    Jenei, A.2    Damjanovich, S.3    Jovin, T.M.4    Szöllosi, J.5
  • 9
    • 0019474922 scopus 로고
    • Transforming genes of carcinomas and neuroblastomas introduced into mouse fibroblasts
    • Shih C, Padhy LC, Murray M, Weinberg RA. Transforming genes of carcinomas and neuroblastomas introduced into mouse fibroblasts. Nature 1981;290:261-4.
    • (1981) Nature , vol.290 , pp. 261-264
    • Shih, C.1    Padhy, L.C.2    Murray, M.3    Weinberg, R.A.4
  • 10
    • 0012597802 scopus 로고
    • Increased tyrosine kinase activity associated with the protein encoded by the activated neu oncogene
    • Bargmann CI, Weinberg RA. Increased tyrosine kinase activity associated with the protein encoded by the activated neu oncogene. Proc Natl Acad Sci USA 1988;85:5394-8.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5394-5398
    • Bargmann, C.I.1    Weinberg, R.A.2
  • 11
    • 0030633566 scopus 로고    scopus 로고
    • HER-2/neu protein: A target for antigen-specific immunotherapy of human cancer
    • Disis ML, Cheever MA. HER-2/neu protein: a target for antigen-specific immunotherapy of human cancer. Adv Cancer Res 1997;71:343-71.
    • (1997) Adv. Cancer Res. , vol.71 , pp. 343-371
    • Disis, M.L.1    Cheever, M.A.2
  • 12
    • 0025318271 scopus 로고
    • Characterization of murine monoclonal antibodies reactive to either the human epidermal growth factor receptor or HER2/neu gene product
    • Fendly BM, Winget M, Hudziak RM, Lipari MT, Napier MA, Ullrich A. Characterization of murine monoclonal antibodies reactive to either the human epidermal growth factor receptor or HER2/neu gene product. Cancer Res 1990;50:1550-8.
    • (1990) Cancer Res. , vol.50 , pp. 1550-1558
    • Fendly, B.M.1    Winget, M.2    Hudziak, R.M.3    Lipari, M.T.4    Napier, M.A.5    Ullrich, A.6
  • 15
    • 0032850677 scopus 로고    scopus 로고
    • Multinational study of the efficacy and safety of humanized anti-HER2 monoclonal antibody in women who have HER2-overexpressing metastatic breast cancer that has progressed after chemotherapy for metastatic disease
    • Cobleigh MA, Vogel CL, Tripathy D, Robert NJ, Scholl S, Fehrenbacher L, et al. Multinational study of the efficacy and safety of humanized anti-HER2 monoclonal antibody in women who have HER2-overexpressing metastatic breast cancer that has progressed after chemotherapy for metastatic disease. J Clin Oncol 1999;17:2639-48.
    • (1999) J. Clin. Oncol. , vol.17 , pp. 2639-2648
    • Cobleigh, M.A.1    Vogel, C.L.2    Tripathy, D.3    Robert, N.J.4    Scholl, S.5    Fehrenbacher, L.6
  • 16
    • 0033770667 scopus 로고    scopus 로고
    • Clinical trials of single-agent trastuzumab (Herceptin)
    • Baselga J. Clinical trials of single-agent trastuzumab (Herceptin). Semin Oncol 2000;27:20-6.
    • (2000) Semin. Oncol. , vol.27 , pp. 20-26
    • Baselga, J.1
  • 17
    • 0035869407 scopus 로고    scopus 로고
    • Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2
    • Slamon DJ, Leyland-Jones B, Shak S, Fuchs H, Paton V, Bajamonde A, et al. Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2. N Engl J Med 2001;344:783-92.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 783-792
    • Slamon, D.J.1    Leyland-Jones, B.2    Shak, S.3    Fuchs, H.4    Paton, V.5    Bajamonde, A.6
  • 18
    • 0035125614 scopus 로고    scopus 로고
    • Clinical trials of Herceptin (trastuzumab)
    • Baselga J. Clinical trials of Herceptin (trastuzumab). Eur J Cancer 2001;37(Suppl 1):S18-24.
    • (2001) Eur. J. Cancer , vol.37 , Issue.SUPPL. 1
    • Baselga, J.1
  • 19
    • 0028176477 scopus 로고
    • A neu acquaintance for erbB3 and erbB4: A role for receptor heterodimerization in growth signaling
    • Carraway III KL, Cantley LC. A neu acquaintance for erbB3 and erbB4: a role for receptor heterodimerization in growth signaling. Cell 1994;78:5-8.
    • (1994) Cell , vol.78 , pp. 5-8
    • Carraway K.L. III1    Cantley, L.C.2
  • 20
    • 0034708598 scopus 로고    scopus 로고
    • A natural ErbB4 isoform that does not activate phosphoinositide 3-kinase mediates proliferation but not survival or chemotaxis
    • Kainulainen V, Sundvall M, Maatta JA, Santiestevan E, Klagsbrun M, Elenius K. A natural ErbB4 isoform that does not activate phosphoinositide 3-kinase mediates proliferation but not survival or chemotaxis. J Biol Chem 2000;275:8641-9.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8641-8649
    • Kainulainen, V.1    Sundvall, M.2    Maatta, J.A.3    Santiestevan, E.4    Klagsbrun, M.5    Elenius, K.6
  • 21
    • 0031028273 scopus 로고    scopus 로고
    • Two EGF molecules contribute additively to stabilization of the EGFR dimer
    • Lemmon MA, Bu Z, Ladbury JE, Zhou M, Pinchasi D, Lax I, et al. Two EGF molecules contribute additively to stabilization of the EGFR dimer. EMBO J 1997;16:281-94.
    • (1997) EMBO J. , vol.16 , pp. 281-294
    • Lemmon, M.A.1    Bu, Z.2    Ladbury, J.E.3    Zhou, M.4    Pinchasi, D.5    Lax, I.6
  • 22
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation
    • Gadella Jr. TW, Jovin TM. Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation. J Cell Biol 1995;129:1543-58.
    • (1995) J. Cell Biol. , vol.129 , pp. 1543-1558
    • Gadella T.W., Jr.1    Jovin, T.M.2
  • 23
    • 0032101894 scopus 로고    scopus 로고
    • EGF-induced redistribution of erbB2 on breast tumor cells: Flow and image cytometric energy transfer measurements
    • Nagy P, Bene L, Balázs M, Hyun WC, Lockett SJ, Chiang NY, et al. EGF-induced redistribution of erbB2 on breast tumor cells: flow and image cytometric energy transfer measurements. Cytometry 1998;32:120-31.
    • (1998) Cytometry , vol.32 , pp. 120-131
    • Nagy, P.1    Bene, L.2    Balázs, M.3    Hyun, W.C.4    Lockett, S.J.5    Chiang, N.Y.6
  • 25
    • 0029814271 scopus 로고    scopus 로고
    • A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor
    • Tzahar E, Waterman H, Chen X, Levkowitz G, Karunagaran D, Lavi S, et al. A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor. Mol Cell Biol 1996;16:5276-87.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 5276-5287
    • Tzahar, E.1    Waterman, H.2    Chen, X.3    Levkowitz, G.4    Karunagaran, D.5    Lavi, S.6
  • 26
    • 0028603296 scopus 로고
    • Fluorescence lifetime imaging microscopy: Pixel-by-pixel analysis of phase-modulation data
    • Gadella Jr. TW, Clegg RM, Jovin TM. Fluorescence lifetime imaging microscopy: pixel-by-pixel analysis of phase-modulation data. Bioimaging 1994;2:139-59.
    • (1994) Bioimaging , vol.2 , pp. 139-159
    • Gadella T.W., Jr.1    Clegg, R.M.2    Jovin, T.M.3
  • 27
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder T, Scheiffele P, Verkade P, Simons K. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J Cell Biol 1998;141:929-42.
    • (1998) J. Cell Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 28
    • 34250965243 scopus 로고
    • Energiewanderung und Fluoreszenz
    • Förster T. Energiewanderung und Fluoreszenz. Naturwissenschaften 1946;6:166-75.
    • (1946) Naturwissenschaften , vol.6 , pp. 166-175
    • Förster, T.1
  • 29
    • 0021243527 scopus 로고
    • Fluorescence energy transfer measurements on cell surfaces: A critical comparison of steady-state fluorimetric and flow cytometric methods
    • Szöll″osi J, Tron L, Damjanovich S, Helliwell SH, Arndt-Jovin D, Jovin TM. Fluorescence energy transfer measurements on cell surfaces: a critical comparison of steady-state fluorimetric and flow cytometric methods. Cytometry 1984;5:210-6.
    • (1984) Cytometry , vol.5 , pp. 210-216
    • Szöllosi, J.1    Tron, L.2    Damjanovich, S.3    Helliwell, S.H.4    Arndt-Jovin, D.5    Jovin, T.M.6
  • 30
    • 0028799667 scopus 로고
    • Structural hierarchy in the clustering of HLA class I molecules in the plasma membrane of human lymphoblastoid cells
    • Damjanovich S, Vereb Jr. G, Schaper A, Jenei A, Matkó J, Starink JP, et al. Structural hierarchy in the clustering of HLA class I molecules in the plasma membrane of human lymphoblastoid cells. Proc Natl Acad Sci USA 1995;92:1122-6.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1122-1126
    • Damjanovich, S.1    Vereb G., Jr.2    Schaper, A.3    Jenei, A.4    Matkó, J.5    Starink, J.P.6
  • 32
    • 0011977802 scopus 로고    scopus 로고
    • Novel microscope-based approaches for the investigation of protein-protein interactions in signal transduction
    • Heilmeyer Jr LMG, editor. NATO ASI series. New York, Springer-Verlag
    • Vereb G, Meyer CK, Jovin TM. Novel microscope-based approaches for the investigation of protein-protein interactions in signal transduction. In: Heilmeyer Jr LMG, editor. Interacting protein domains, their role in signal and energy transduction. NATO ASI series. New York, Springer-Verlag, 1997:49-52.
    • (1997) Interacting Protein Domains, Their Role in Signal and Energy Transduction , pp. 49-52
    • Vereb, G.1    Meyer, C.K.2    Jovin, T.M.3
  • 34
    • 0033534459 scopus 로고    scopus 로고
    • Domain-specific interactions between the p185(neu) and epidermal growth factor receptor kinases determine differential signaling outcomes
    • Qian X, O'Rourke DM, Fei Z, Zhang HT, Kao CC, Greene MI. Domain-specific interactions between the p185(neu) and epidermal growth factor receptor kinases determine differential signaling outcomes. J Biol Chem 1999;274:574-83.
    • (1999) J. Biol. Chem. , vol.274 , pp. 574-583
    • Qian, X.1    O'Rourke, D.M.2    Fei, Z.3    Zhang, H.T.4    Kao, C.C.5    Greene, M.I.6
  • 35
    • 0030969251 scopus 로고    scopus 로고
    • Transmembrane domain sequence requirements for activation of the p185c- neu receptor tyrosine kinase
    • Chen LI, Webster MK, Meyer AN, Donoghue DJ. Transmembrane domain sequence requirements for activation of the p185c- neu receptor tyrosine kinase. J Cell Biol 1997;137:619-31.
    • (1997) J. Cell Biol. , vol.137 , pp. 619-631
    • Chen, L.I.1    Webster, M.K.2    Meyer, A.N.3    Donoghue, D.J.4
  • 36
    • 0027203585 scopus 로고
    • Specific short transmembrane sequences can inhibit transformation by the mutant neu growth factor receptor in vitro and in vivo
    • Lofts FJ, Hurst HC, Sternberg MJ, Gullick WJ. Specific short transmembrane sequences can inhibit transformation by the mutant neu growth factor receptor in vitro and in vivo. Oncogene 1993;8:2813-20.
    • (1993) Oncogene , vol.8 , pp. 2813-2820
    • Lofts, F.J.1    Hurst, H.C.2    Sternberg, M.J.3    Gullick, W.J.4
  • 37
    • 0031842104 scopus 로고    scopus 로고
    • Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface
    • Burke CL, Stern DF. Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface. Mol Cell Biol 1998;18:5371-9.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 5371-5379
    • Burke, C.L.1    Stern, D.F.2
  • 39
    • 0002193007 scopus 로고    scopus 로고
    • Integration of optical techniques in scanning probe microscopes: The scanning near-field optical microscope (SNOM)
    • Kohen E, Kirschberg JG, editors. Miami, FL. Oct. 14-18 1995 New York, Plenum Press
    • Kirsch A, Meyer C, Jovin TM. Integration of optical techniques in scanning probe microscopes: the scanning near-field optical microscope (SNOM). In: Kohen E, Kirschberg JG, editors. Proceedings of NATO Advanced Research Workshop: analytical use of fluorescent probes in oncology, Miami, FL. Oct. 14-18 1995. New York, Plenum Press, 1996:317-23.
    • (1996) Proceedings of NATO Advanced Research Workshop: Analytical Use of Fluorescent Probes in Oncology , pp. 317-323
    • Kirsch, A.1    Meyer, C.2    Jovin, T.M.3
  • 40
    • 0030822255 scopus 로고    scopus 로고
    • Lipid microdomains in cell surface membranes
    • Edidin M. Lipid microdomains in cell surface membranes. Curr Opin Struct Biol 1997;7:528-32.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 528-532
    • Edidin, M.1
  • 41
    • 0033014064 scopus 로고    scopus 로고
    • Activation-dependent clustering of the erbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy
    • Nagy P, Jenei A, Kirsch AK, Szöll″osi J, Damjanovich S, Jovin TM. Activation-dependent clustering of the erbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy. J Cell Sci 1999;112:1733-41.
    • (1999) J. Cell Sci. , vol.112 , pp. 1733-1741
    • Nagy, P.1    Jenei, A.2    Kirsch, A.K.3    Szöll'osi, J.4    Damjanovich, S.5    Jovin, T.M.6
  • 42
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. Functional rafts in cell membranes. Nature 1997;387:569-72.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 43
    • 0032727709 scopus 로고    scopus 로고
    • Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor
    • Janes PW, Ley SC, Magee AI. Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor. J Cell Biol 1999;147:447-61.
    • (1999) J. Cell Biol. , vol.147 , pp. 447-461
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3
  • 45
    • 0034611005 scopus 로고    scopus 로고
    • Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells
    • Pralle A, Keller P, Florin EL, Simons K, Horber JK. Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J Cell Biol 2000;148:997-1008.
    • (2000) J. Cell Biol. , vol.148 , pp. 997-1008
    • Pralle, A.1    Keller, P.2    Florin, E.L.3    Simons, K.4    Horber, J.K.5
  • 46
    • 0030878573 scopus 로고    scopus 로고
    • Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains
    • Harder T, Simons K. Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains. Curr Opin Cell Biol 1997;9:534-42.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 534-542
    • Harder, T.1    Simons, K.2
  • 48
    • 0033055564 scopus 로고    scopus 로고
    • Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae (review)
    • Hooper NM. Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae (review). Mol Membr Biol 1999;16:145-56.
    • (1999) Mol. Membr. Biol. , vol.16 , pp. 145-156
    • Hooper, N.M.1
  • 49
    • 0034707082 scopus 로고    scopus 로고
    • Insolubility of lipids in triton X-100: Physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts)
    • 1508
    • London E, Brown DA. Insolubility of lipids in triton X-100: physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts). Biochim Biophys Acta 2000;1508:182-95.
    • (2000) Biochim. Biophys. Acta , pp. 182-195
    • London, E.1    Brown, D.A.2
  • 50
    • 0034075971 scopus 로고    scopus 로고
    • High-resolution FRET microscopy of cholera toxin B-subunit and GPI- anchored proteins in cell plasma membranes
    • Kenworthy AK, Petranova N, Edidin M. High-resolution FRET microscopy of cholera toxin B-subunit and GPI- anchored proteins in cell plasma membranes. Mol Biol Cell 2000;11:1645-55.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1645-1655
    • Kenworthy, A.K.1    Petranova, N.2    Edidin, M.3
  • 51
    • 0032516835 scopus 로고    scopus 로고
    • Cholesterol depletion of caveolae causes hyperactivation of extracellular signalrelated kinase (ERK)
    • Furuchi T, Anderson RG. Cholesterol depletion of caveolae causes hyperactivation of extracellular signalrelated kinase (ERK). J Biol Chem 1998;273:21099-104.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21099-21104
    • Furuchi, T.1    Anderson, R.G.2
  • 52
    • 0032696038 scopus 로고    scopus 로고
    • Regulated migration of epidermal growth factor receptor from caveolae
    • Mineo C, Gill GN, Anderson RG. Regulated migration of epidermal growth factor receptor from caveolae. J Biol Chem 1999;274:30636-43.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30636-30643
    • Mineo, C.1    Gill, G.N.2    Anderson, R.G.3
  • 53
    • 0030731231 scopus 로고    scopus 로고
    • Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities
    • Couet J, Sargiacomo M, Lisanti MP. Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities. J Biol Chem 1997;272:30429-38.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30429-30438
    • Couet, J.1    Sargiacomo, M.2    Lisanti, M.P.3
  • 54
    • 17344363636 scopus 로고    scopus 로고
    • Reciprocal regulation of neu tyrosine kinase activity and caveolin-1 protein expression in vitro and in vivo. Implications for human breast cancer
    • Engelman JA, Lee RJ, Karnezis A, Bearss DJ, Webster M, Siegel P, et al. Reciprocal regulation of neu tyrosine kinase activity and caveolin-1 protein expression in vitro and in vivo. Implications for human breast cancer. J Biol Chem 1998;273:20448-55.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20448-20455
    • Engelman, J.A.1    Lee, R.J.2    Karnezis, A.3    Bearss, D.J.4    Webster, M.5    Siegel, P.6
  • 55
    • 0032546319 scopus 로고    scopus 로고
    • Tumor cell growth inhibition by caveolin re-expression in human breast cancer cells
    • Lee SW, Reimer CL, Oh P, Campbell DB, Schnitzer JE. Tumor cell growth inhibition by caveolin re-expression in human breast cancer cells. Oncogene 1998;16:1391-7.
    • (1998) Oncogene , vol.16 , pp. 1391-1397
    • Lee, S.W.1    Reimer, C.L.2    Oh, P.3    Campbell, D.B.4    Schnitzer, J.E.5
  • 56
    • 0033082833 scopus 로고    scopus 로고
    • Epidermal growth factor receptor activation is localized within low- buoyant density, non-caveolar membrane domains
    • Waugh MG, Lawson D, Hsuan JJ. Epidermal growth factor receptor activation is localized within low- buoyant density, non-caveolar membrane domains. Biochem J 1999;337:591-7.
    • (1999) Biochem. J. , vol.337 , pp. 591-597
    • Waugh, M.G.1    Lawson, D.2    Hsuan, J.J.3
  • 58
    • 0011983272 scopus 로고    scopus 로고
    • Lipid rafts and the local density of ErbB proteins influence the biological role of homo- and heteroassociations of ErbB2
    • Manuscript in preparation
    • Nagy P, Vereb G, Sebestyén Z, Horváth G, Lockett SJ, Damjanovich S, et al. Lipid rafts and the local density of ErbB proteins influence the biological role of homo- and heteroassociations of ErbB2. Manuscript in preparation, 2002
    • (2002)
    • Nagy, P.1    Vereb, G.2    Sebestyén, Z.3    Horváth, G.4    Lockett, S.J.5    Damjanovich, S.6
  • 59
    • 12944328730 scopus 로고    scopus 로고
    • Cholesterol-dependent clustering of IL-2Rα and its colocalization with HLA and CD48 on T lymphoma cells suggest their functional association with lipid rafts
    • Vereb Jr. G, Matkó J, Vamosi G, Ibrahim SM, Magyar E, Varga S, et al. Cholesterol-dependent clustering of IL-2Rα and its colocalization with HLA and CD48 on T lymphoma cells suggest their functional association with lipid rafts. Proc Natl Acad Sci USA 2000;97:6013-8.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6013-6018
    • Vereb G., Jr.1    Matkó, J.2    Vamosi, G.3    Ibrahim, S.M.4    Magyar, E.5    Varga, S.6
  • 60
    • 0029671427 scopus 로고    scopus 로고
    • p120cbl is a cytosolic adapter protein that associates with phosphoinositide 3-kinase in response to epidermal growth factor in PC12 and other cells
    • Soltoff SP, Cantley LC. p120cbl is a cytosolic adapter protein that associates with phosphoinositide 3-kinase in response to epidermal growth factor in PC12 and other cells. J Biol Chem 1996;271:563-7.
    • (1996) J. Biol. Chem. , vol.271 , pp. 563-567
    • Soltoff, S.P.1    Cantley, L.C.2
  • 61
    • 0029782738 scopus 로고    scopus 로고
    • An epidermal growth factor receptor/Jak2 tyrosine kinase domain chimera induces tyrosine phosphorylation of Stat5 and transduces a growth signal in hematopoietic cells
    • Nakamura N, Chin H, Miyasaka N, Miura O. An epidermal growth factor receptor/Jak2 tyrosine kinase domain chimera induces tyrosine phosphorylation of Stat5 and transduces a growth signal in hematopoietic cells. J Biol Chem 1996;271:19483-8.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19483-19488
    • Nakamura, N.1    Chin, H.2    Miyasaka, N.3    Miura, O.4
  • 62
    • 0033546315 scopus 로고    scopus 로고
    • ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases
    • Olayioye MA, Beuvink I, Horsch K, Daly JM, Hynes NE. ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases. J Biol Chem 1999;274:17209-18.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17209-17218
    • Olayioye, M.A.1    Beuvink, I.2    Horsch, K.3    Daly, J.M.4    Hynes, N.E.5
  • 63
    • 0029912203 scopus 로고    scopus 로고
    • All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired
    • Baulida J, Kraus MH, Alimandi M, Di Fiore PP, Carpenter G. All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired. J Biol Chem 1996;271:5251-7.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5251-5257
    • Baulida, J.1    Kraus, M.H.2    Alimandi, M.3    Di Fiore, P.P.4    Carpenter, G.5
  • 64
    • 0029917264 scopus 로고    scopus 로고
    • Coupling of the c-Cbl protooncogene product to ErbB-1/EGF-receptor but not to other ErbB proteins
    • Levkowitz G, Klapper LN, Tzahar E, Freywald A, Sela M, Yarden Y. Coupling of the c-Cbl protooncogene product to ErbB-1/EGF-receptor but not to other ErbB proteins. Oncogene 1996;12:1117-25.
    • (1996) Oncogene , vol.12 , pp. 1117-1125
    • Levkowitz, G.1    Klapper, L.N.2    Tzahar, E.3    Freywald, A.4    Sela, M.5    Yarden, Y.6
  • 65
    • 0032526729 scopus 로고    scopus 로고
    • Differential endocytic routing of homo- and hetero-dimeric ErbB tyrosine kinases confers signaling superiority to receptor heterodimers
    • Lenferink AE, Pinkas-Kramarski R, van de Poll ML, van Vugt MJ, Klapper LN, Tzahar E, et al. Differential endocytic routing of homo- and hetero-dimeric ErbB tyrosine kinases confers signaling superiority to receptor heterodimers. EMBO J 1998;17:3385-97.
    • (1998) EMBO J. , vol.17 , pp. 3385-3397
    • Lenferink, A.E.1    Pinkas-Kramarski, R.2    van de Poll, M.L.3    van Vugt, M.J.4    Klapper, L.N.5    Tzahar, E.6
  • 66
    • 7144261725 scopus 로고    scopus 로고
    • The class III variant of the epidermal growth factor receptor (EGFRvIII): Characterization and utilization as an immunotherapeutic target
    • Wikstrand CJ, Reist CJ, Archer GE, Zalutsky MR, Bigner DD. The class III variant of the epidermal growth factor receptor (EGFRvIII): characterization and utilization as an immunotherapeutic target. J Neurovirol 1998;4:148-58.
    • (1998) J. Neurovirol. , vol.4 , pp. 148-158
    • Wikstrand, C.J.1    Reist, C.J.2    Archer, G.E.3    Zalutsky, M.R.4    Bigner, D.D.5
  • 69
    • 0028848397 scopus 로고
    • ERBB-2 (HER2/neu) gene copy number, p185HER-2 overexpression, and intratumor heterogeneity in human breast cancer
    • Szöll″osi J, Balázs M, Feuerstein BG, Benz CC, Waldman FM. ERBB-2 (HER2/neu) gene copy number, p185HER-2 overexpression, and intratumor heterogeneity in human breast cancer. Cancer Res 1995;55:5400-7.
    • (1995) Cancer Res. , vol.55 , pp. 5400-5407
    • Szöllosi, J.1    Balázs, M.2    Feuerstein, B.G.3    Benz, C.C.4    Waldman, F.M.5
  • 70
    • 0033372557 scopus 로고    scopus 로고
    • Combination of EGFR, HER-2/neu, and HER-3 is a stronger predictor for the outcome of oral squamous cell carcinoma than any individual family members
    • Xia W, Lau YK, Zhang HZ, Xiao FY, Johnston DA, Liu AR, et al. Combination of EGFR, HER-2/neu, and HER-3 is a stronger predictor for the outcome of oral squamous cell carcinoma than any individual family members. Clin Cancer Res 1999;5:4164-74.
    • (1999) Clin. Cancer Res. , vol.5 , pp. 4164-4174
    • Xia, W.1    Lau, Y.K.2    Zhang, H.Z.3    Xiao, F.Y.4    Johnston, D.A.5    Liu, A.R.6
  • 71
    • 0030933521 scopus 로고    scopus 로고
    • Tissue expression of neu differentiation factor/heregulin and its receptor complex in prostate cancer and its biologic effects on prostate cancer cells in vitro
    • Lyne JC, Melhem MF, Finley GG, Wen D, Liu N, Deng DH, et al. Tissue expression of neu differentiation factor/heregulin and its receptor complex in prostate cancer and its biologic effects on prostate cancer cells in vitro. Cancer J Sci Am 1997;3:21-30.
    • (1997) Cancer J. Sci. Am. , vol.3 , pp. 21-30
    • Lyne, J.C.1    Melhem, M.F.2    Finley, G.G.3    Wen, D.4    Liu, N.5    Deng, D.H.6
  • 72
    • 0030741967 scopus 로고    scopus 로고
    • Prognostic significance of HER2 and HER4 coexpression in childhood medulloblastoma
    • Gilbertson RJ, Perry RH, Kelly PJ, Pearson AD, Lunec J. Prognostic significance of HER2 and HER4 coexpression in childhood medulloblastoma. Cancer Res 1997;57:3272-80.
    • (1997) Cancer Res. , vol.57 , pp. 3272-3280
    • Gilbertson, R.J.1    Perry, R.H.2    Kelly, P.J.3    Pearson, A.D.4    Lunec, J.5
  • 73
    • 0026174552 scopus 로고
    • Characterization of an antip185HER2 monoclonal antibody that stimulates receptor function and inhibits tumor cell growth
    • Sarup JC, Johnson RM, King KL, Fendly BM, Lipari MT, Napier MA, et al. Characterization of an antip185HER2 monoclonal antibody that stimulates receptor function and inhibits tumor cell growth. Growth Regul 1991;1:72-82.
    • (1991) Growth Regul. , vol.1 , pp. 72-82
    • Sarup, J.C.1    Johnson, R.M.2    King, K.L.3    Fendly, B.M.4    Lipari, M.T.5    Napier, M.A.6
  • 75
    • 0034234854 scopus 로고    scopus 로고
    • Tumor-inhibitory antibodies to HER-2/ErbB-2 may act by recruiting c-Cbl and enhancing ubiquitination of HER-2
    • Klapper LN, Waterman H, Sela M, Yarden Y. Tumor-inhibitory antibodies to HER-2/ErbB-2 may act by recruiting c-Cbl and enhancing ubiquitination of HER-2. Cancer Res 2000;60:3384-8.
    • (2000) Cancer Res. , vol.60 , pp. 3384-3388
    • Klapper, L.N.1    Waterman, H.2    Sela, M.3    Yarden, Y.4
  • 76
    • 0030959114 scopus 로고    scopus 로고
    • A subclass of tumor-inhibitory monoclonal antibodies to ErbB-2/HER2 blocks crosstalk with growth factor receptors
    • Klapper LN, Vaisman N, Hurwitz E, Pinkas-Kramarski R, Yarden Y, Sela M. A subclass of tumor-inhibitory monoclonal antibodies to ErbB-2/HER2 blocks crosstalk with growth factor receptors. Oncogene 1997;14:2099-109.
    • (1997) Oncogene , vol.14 , pp. 2099-2109
    • Klapper, L.N.1    Vaisman, N.2    Hurwitz, E.3    Pinkas-Kramarski, R.4    Yarden, Y.5    Sela, M.6
  • 77
    • 0035874981 scopus 로고    scopus 로고
    • Trastuzumab (herceptin), a humanized anti-Her2 receptor monoclonal antibody, inhibits basal and activated Her2 ectodomain cleavage in breast cancer cells
    • Molina MA, Codony-Servat J, Albanell J, Rojo F, Arribas J, Baselga J. Trastuzumab (herceptin), a humanized anti-Her2 receptor monoclonal antibody, inhibits basal and activated Her2 ectodomain cleavage in breast cancer cells. Cancer Res 2001;61:4744-9.
    • (2001) Cancer Res. , vol.61 , pp. 4744-4749
    • Molina, M.A.1    Codony-Servat, J.2    Albanell, J.3    Rojo, F.4    Arribas, J.5    Baselga, J.6
  • 79
    • 0035257549 scopus 로고    scopus 로고
    • Rationale for trastuzumab (Herceptin) in adjuvant breast cancer trials
    • Slamon D, Pegram M. Rationale for trastuzumab (Herceptin) in adjuvant breast cancer trials. Semin Oncol 2001;28:13-9.
    • (2001) Semin. Oncol. , vol.28 , pp. 13-19
    • Slamon, D.1    Pegram, M.2
  • 80
    • 0011980867 scopus 로고    scopus 로고
    • Liposome-based drug delivery in breast cancer treatment
    • In press
    • Park JW. Liposome-based drug delivery in breast cancer treatment. Breast Cancer Res 2001; In press.
    • (2001) Breast Cancer Res.
    • Park, J.W.1
  • 83
    • 13144266690 scopus 로고    scopus 로고
    • Specific, irreversible inactivation of the epidermal growth factor receptor and erbB2, by a new class of tyrosine kinase inhibitor
    • Fry DW, Bridges AJ, Denny WA, Doherty A, Greis KD, Hicks JL, et al. Specific, irreversible inactivation of the epidermal growth factor receptor and erbB2, by a new class of tyrosine kinase inhibitor. Proc Natl Acad Sci USA 1998;95:12022-7.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12022-12027
    • Fry, D.W.1    Bridges, A.J.2    Denny, W.A.3    Doherty, A.4    Greis, K.D.5    Hicks, J.L.6
  • 84
    • 0034714283 scopus 로고    scopus 로고
    • Geldanamycin induces ErbB-2 degradation by proteolytic fragmentation
    • Tikhomirov O, Carpenter G. Geldanamycin induces ErbB-2 degradation by proteolytic fragmentation. J Biol Chem 2000;275:26625-31.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26625-26631
    • Tikhomirov, O.1    Carpenter, G.2
  • 85
    • 0035359505 scopus 로고    scopus 로고
    • Exploiting cancer cell cycling for selective protection of normal cells
    • Blagosklonny MV, Pardee AB. Exploiting cancer cell cycling for selective protection of normal cells. Cancer Res 2001;61:4301-5.
    • (2001) Cancer Res. , vol.61 , pp. 4301-4305
    • Blagosklonny, M.V.1    Pardee, A.B.2
  • 86
    • 0035489191 scopus 로고    scopus 로고
    • Selective protection of mitogenically stimulated human lymphocytes but not leukemic cells from cytosine arabinoside-induced apoptosis by LY294002, a phosphoinositol-3 kinase inhibitor
    • Du L, Smolewski P, Bedner E, Traganos F, Darzynkiewicz Z. Selective protection of mitogenically stimulated human lymphocytes but not leukemic cells from cytosine arabinoside-induced apoptosis by LY294002, a phosphoinositol-3 kinase inhibitor. Int J Oncol 2001;19:811-9.
    • (2001) Int. J. Oncol. , vol.19 , pp. 811-819
    • Du, L.1    Smolewski, P.2    Bedner, E.3    Traganos, F.4    Darzynkiewicz, Z.5
  • 87
    • 0028148050 scopus 로고
    • Intracellular expression of single chain antibodies reverts ErbB-2 transformation
    • Beerli RR, Wels W, Hynes NE. Intracellular expression of single chain antibodies reverts ErbB-2 transformation. J Biol Chem 1994;269:23931-6.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23931-23936
    • Beerli, R.R.1    Wels, W.2    Hynes, N.E.3
  • 88
    • 0033993508 scopus 로고    scopus 로고
    • Adenovirus-mediated ribozyme targeting of HER-2/neu inhibits in vivo growth of breast cancer cells
    • Suzuki T, Anderegg B, Ohkawa T, Irie A, Engebraaten O, Halks-Miller M, et al. Adenovirus-mediated ribozyme targeting of HER-2/neu inhibits in vivo growth of breast cancer cells. Gene Ther 2000;7:241-8.
    • (2000) Gene Ther. , vol.7 , pp. 241-248
    • Suzuki, T.1    Anderegg, B.2    Ohkawa, T.3    Irie, A.4    Engebraaten, O.5    Halks-Miller, M.6
  • 90
    • 0034754136 scopus 로고    scopus 로고
    • Epidermal growth factor receptor biology (IMC-C225)
    • Kim ES, Khuri FR, Herbst RS. Epidermal growth factor receptor biology (IMC-C225). Curr Opin Oncol 2001;13:506-13.
    • (2001) Curr. Opin. Oncol. , vol.13 , pp. 506-513
    • Kim, E.S.1    Khuri, F.R.2    Herbst, R.S.3
  • 91
    • 0034909841 scopus 로고    scopus 로고
    • Growth factors and their receptors: New targets for prostate cancer therapy
    • Barton J, Blackledge G, Wakeling A. Growth factors and their receptors: new targets for prostate cancer therapy. Urology 2001;58:114-22.
    • (2001) Urology , vol.58 , pp. 114-122
    • Barton, J.1    Blackledge, G.2    Wakeling, A.3
  • 92
    • 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;12:745-60.
    • (2001) Ann. Oncol. , vol.12 , pp. 745-760
    • Pedersen, M.W.1    Meltorn, M.2    Damstrup, L.3    Poulsen, H.S.4
  • 94
    • 0033919203 scopus 로고    scopus 로고
    • Antisense oligonucleotides: An evolving technology for the modulation of gene expression in human disease
    • Green DW, Roh H, Pippin J, Drebin JA. Antisense oligonucleotides: an evolving technology for the modulation of gene expression in human disease. J Am Coll Surg 2000;191:93-105.
    • (2000) J. Am. Coll. Surg. , vol.191 , pp. 93-105
    • Green, D.W.1    Roh, H.2    Pippin, J.3    Drebin, J.A.4
  • 95
    • 0343151924 scopus 로고    scopus 로고
    • Signal transduction in leukocytes via GPIanchored proteins: An experimental artefact or an aspect of immunoreceptor function?
    • Horejsi V, Cebecauer M, Cerny J, Brdicka T, Angelisova P, Drbal K. Signal transduction in leukocytes via GPIanchored proteins: an experimental artefact or an aspect of immunoreceptor function? Immunol Lett 1998;63:63-73.
    • (1998) Immunol. Lett. , vol.63 , pp. 63-73
    • Horejsi, V.1    Cebecauer, M.2    Cerny, J.3    Brdicka, T.4    Angelisova, P.5    Drbal, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.