메뉴 건너뛰기




Volumn 11, Issue 2, 2003, Pages 495-505

The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPIDERMAL GROWTH FACTOR RECEPTOR 3; EPIDERMAL GROWTH FACTOR RECEPTOR 4; RECEPTOR PROTEIN; UNCLASSIFIED DRUG;

EID: 0037291226     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(03)00048-0     Document Type: Article
Times cited : (501)

References (58)
  • 1
    • 0023241481 scopus 로고
    • On the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptors
    • Bajaj M., Waterfield M.D., Schlessinger J., Taylor W.R., Blundell T. On the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptors. Biochim. Biophys. Acta. 916:1987;220-226.
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 220-226
    • Bajaj, M.1    Waterfield, M.D.2    Schlessinger, J.3    Taylor, W.R.4    Blundell, T.5
  • 2
    • 0000007950 scopus 로고
    • The use of vector based on gene amplification for the expression of cloned genes in mammalian cells
    • D. Glover. Oxford: IRL Press. 163-188.pp
    • Bebbington C.R., Hentschel C.C.G. The use of vector based on gene amplification for the expression of cloned genes in mammalian cells. Glover D. DNA Cloning. 1987;IRL Press, Oxford. 163-188.pp.
    • (1987) DNA Cloning
    • Bebbington, C.R.1    Hentschel, C.C.G.2
  • 3
    • 0035797362 scopus 로고    scopus 로고
    • Disabling ErbB receptors with rationally designed exocyclic mimetics of antibodies: Structure-function analysis
    • Berezov A., Zhang H.T., Greene M.I., Murali R. Disabling ErbB receptors with rationally designed exocyclic mimetics of antibodies. structure-function analysis J. Med. Chem. 44:2001;2565-2574.
    • (2001) J. Med. Chem. , vol.44 , pp. 2565-2574
    • Berezov, A.1    Zhang, H.T.2    Greene, M.I.3    Murali, R.4
  • 4
    • 0037008698 scopus 로고    scopus 로고
    • Disabling receptor ensembles with rationally designed interface peptidomimetics
    • Berezov A., Chen J., Liu Q., Zhang H.T., Greene M.I., Murali R. Disabling receptor ensembles with rationally designed interface peptidomimetics. J. Biol. Chem. 277:2002;28330-28339.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28330-28339
    • Berezov, A.1    Chen, J.2    Liu, Q.3    Zhang, H.T.4    Greene, M.I.5    Murali, R.6
  • 6
    • 0028094123 scopus 로고
    • Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution
    • Brizzard B.L., Chubet R.G., Vizard D.L. Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution. Biotechniques. 16:1994;730-735.
    • (1994) Biotechniques , vol.16 , pp. 730-735
    • Brizzard, B.L.1    Chubet, R.G.2    Vizard, D.L.3
  • 8
    • 0037162799 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER3 reveals an interdomain tether
    • Cho H.S., Leahy D.J. Structure of the extracellular region of HER3 reveals an interdomain tether. Science. 297:2002;1330-1333.
    • (2002) Science , vol.297 , pp. 1330-1333
    • Cho, H.S.1    Leahy, D.J.2
  • 9
    • 0030768379 scopus 로고    scopus 로고
    • Neu differentiation factor induces ErbB2 down-regulation and apoptosis of ErbB2-overexpressing breast tumor cells
    • Daly J.M., Jannot C.B., Beerli R.R., Graus-Porta D., Maurer F.G., Hynes N.E. Neu differentiation factor induces ErbB2 down-regulation and apoptosis of ErbB2-overexpressing breast tumor cells. Cancer Res. 57:1997;3804-3811.
    • (1997) Cancer Res. , vol.57 , pp. 3804-3811
    • Daly, J.M.1    Jannot, C.B.2    Beerli, R.R.3    Graus-Porta, D.4    Maurer, F.G.5    Hynes, N.E.6
  • 10
    • 0036214044 scopus 로고    scopus 로고
    • The ErbB receptor family: A therapeutic target for cancer
    • Suppl) S
    • de Bono J.S., Rowinsky E.K. The ErbB receptor family. a therapeutic target for cancer Trends Mol. Med. 8:2002;19-S26. Suppl) S.
    • (2002) Trends Mol. Med. , vol.8
    • De Bono, J.S.1    Rowinsky, E.K.2
  • 11
    • 0035979381 scopus 로고    scopus 로고
    • Identification of a determinant of epidermal growth factor receptor ligand-binding specificity using a truncated, high-affinity form of the ectodomain
    • Elleman T.C., Domagala T., McKern N.M., Nerrie M., Lonnqvist B., Adams T.E., Lewis J., Lovrecz G.O., Hoyne P.A., Richards K.M.et al. Identification of a determinant of epidermal growth factor receptor ligand-binding specificity using a truncated, high-affinity form of the ectodomain. Biochemistry. 40:2001;8930-8939.
    • (2001) Biochemistry , vol.40 , pp. 8930-8939
    • Elleman, T.C.1    Domagala, T.2    McKern, N.M.3    Nerrie, M.4    Lonnqvist, B.5    Adams, T.E.6    Lewis, J.7    Lovrecz, G.O.8    Hoyne, P.A.9    Richards, K.M.10
  • 12
    • 0031454062 scopus 로고    scopus 로고
    • ErbB3 is required for normal cerebellar and cardiac development: A comparison with ErbB2-and heregulin-deficient mice
    • Erickson S.L., O'Shea K.S., Ghaboosi N., Loverro L., Frantz G., Bauer M., Lu L.H., Moore M.W. ErbB3 is required for normal cerebellar and cardiac development. a comparison with ErbB2-and heregulin-deficient mice Development. 124:1997;4999-5011.
    • (1997) Development , vol.124 , pp. 4999-5011
    • Erickson, S.L.1    O'Shea, K.S.2    Ghaboosi, N.3    Loverro, L.4    Frantz, G.5    Bauer, M.6    Lu, L.H.7    Moore, M.W.8
  • 13
    • 0034282556 scopus 로고    scopus 로고
    • Extracellular domains drive homo- but not heterodimerization of erbB receptors
    • Ferguson K.M., Darling P.J., Mohan M.J., Macatee T.L., Lemmon M.A. Extracellular domains drive homo- but not heterodimerization of erbB receptors. EMBO J. 19:2000;4632-4643.
    • (2000) EMBO J. , vol.19 , pp. 4632-4643
    • Ferguson, K.M.1    Darling, P.J.2    Mohan, M.J.3    Macatee, T.L.4    Lemmon, M.A.5
  • 14
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that auto-inhibit ectodomain dimerization
    • this issue
    • Ferguson K.M., Berger M.B., Mendrola J.M., Cho H.-S., Leahy D.J., Lemmon M.A. EGF activates its receptor by removing interactions that auto-inhibit ectodomain dimerization. Mol. Cell. 11:2003;507-517. this issue.
    • (2003) Mol. Cell , vol.11 , pp. 507-517
    • Ferguson, K.M.1    Berger, M.B.2    Mendrola, J.M.3    Cho, H.-S.4    Leahy, D.J.5    Lemmon, M.A.6
  • 17
    • 0028785406 scopus 로고
    • Aberrant neural and cardiac development in mice lacking the ErbB4 neuregulin receptor
    • Gassmann M., Casagranda F., Orioli D., Simon H., Lai C., Klein R., Lemke G. Aberrant neural and cardiac development in mice lacking the ErbB4 neuregulin receptor. Nature. 378:1995;390-394.
    • (1995) Nature , vol.378 , pp. 390-394
    • Gassmann, M.1    Casagranda, F.2    Orioli, D.3    Simon, H.4    Lai, C.5    Klein, R.6    Lemke, G.7
  • 18
    • 0030944455 scopus 로고    scopus 로고
    • ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling
    • Graus-Porta D., Beerli R.R., Daly J.M., Hynes N.E. ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling. EMBO J. 16:1997;1647-1655.
    • (1997) EMBO J. , vol.16 , pp. 1647-1655
    • Graus-Porta, D.1    Beerli, R.R.2    Daly, J.M.3    Hynes, N.E.4
  • 19
    • 0034638925 scopus 로고    scopus 로고
    • Molecular mechanisms underlying ErbB2/HER2 action in breast cancer
    • Harari D., Yarden Y. Molecular mechanisms underlying ErbB2/HER2 action in breast cancer. Oncogene. 19:2000;6102-6114.
    • (2000) Oncogene , vol.19 , pp. 6102-6114
    • Harari, D.1    Yarden, Y.2
  • 21
    • 0026206788 scopus 로고
    • Sparse matrix sampling: A screening method for crystallization of proteins
    • Jancarik J., Kim S.-H. Sparse matrix sampling. a screening method for crystallization of proteins J. Appl. Crystallogr. 24:1991;409-411.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.-H.2
  • 22
    • 0033009389 scopus 로고    scopus 로고
    • Binding specificities and affinities of EGF domains for ErbB receptors
    • Jones J.T., Akita R.W., Sliwkowski M.X. Binding specificities and affinities of EGF domains for ErbB receptors. FEBS Lett. 447:1999;227-231.
    • (1999) FEBS Lett. , vol.447 , pp. 227-231
    • Jones, J.T.1    Akita, R.W.2    Sliwkowski, M.X.3
  • 23
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 24
    • 0020078747 scopus 로고
    • Resolution of high and low affinity epidermal growth factor receptors. Inhibition of high affinity component by low temperature, cycloheximide, and phorbol esters
    • King A.C., Cuatrecasas P. Resolution of high and low affinity epidermal growth factor receptors. Inhibition of high affinity component by low temperature, cycloheximide, and phorbol esters. J. Biol. Chem. 257:1982;3053-3060.
    • (1982) J. Biol. Chem. , vol.257 , pp. 3053-3060
    • King, A.C.1    Cuatrecasas, P.2
  • 25
    • 0024326947 scopus 로고
    • Isolation and characterization of ERBB3, a third member of the ERBB/epidermal growth factor receptor family: Evidence for overexpression in a subset of human mammary tumors
    • Kraus M.H., Issing W., Miki T., Popescu N.C., Aaronson S.A. Isolation and characterization of ERBB3, a third member of the ERBB/epidermal growth factor receptor family. evidence for overexpression in a subset of human mammary tumors Proc. Natl. Acad. Sci. USA. 86:1989;9193-9197.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9193-9197
    • Kraus, M.H.1    Issing, W.2    Miki, T.3    Popescu, N.C.4    Aaronson, S.A.5
  • 26
    • 0035826533 scopus 로고    scopus 로고
    • The role of distinct p185neu extracellular subdomains for dimerization with the epidermal growth factor (EGF) receptor and EGF-mediated signaling
    • Kumagai T., Davis J.G., Horie T., O'Rourke D.M., Greene M.I. The role of distinct p185neu extracellular subdomains for dimerization with the epidermal growth factor (EGF) receptor and EGF-mediated signaling. Proc. Natl. Acad. Sci. USA. 98:2001;5526-5531.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5526-5531
    • Kumagai, T.1    Davis, J.G.2    Horie, T.3    O'Rourke, D.M.4    Greene, M.I.5
  • 27
    • 0028884413 scopus 로고
    • Requirement for neuregulin receptor erbB2 in neural and cardiac development
    • Lee K.F., Simon H., Chen H., Bates B., Hung M.C., Hauser C. Requirement for neuregulin receptor erbB2 in neural and cardiac development. Nature. 378:1995;394-398.
    • (1995) Nature , vol.378 , pp. 394-398
    • Lee, K.F.1    Simon, H.2    Chen, H.3    Bates, B.4    Hung, M.C.5    Hauser, C.6
  • 28
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence M.C., Colman P.M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234:1993;946-950.
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 29
    • 0023930686 scopus 로고
    • Chicken epidermal growth factor (EGF) receptor: CDNA cloning, expression in mouse cells, and differential binding of EGF and transforming growth factor alpha
    • Lax I., Johnson A., Howk R., Sap J., Bellot F., Winkler M., Ullrich A., Vennstrom B., Schlessinger J., Givol D. Chicken epidermal growth factor (EGF) receptor. cDNA cloning, expression in mouse cells, and differential binding of EGF and transforming growth factor alpha Mol. Cell. Biol. 8:1988;1970-1978.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 1970-1978
    • Lax, I.1    Johnson, A.2    Howk, R.3    Sap, J.4    Bellot, F.5    Winkler, M.6    Ullrich, A.7    Vennstrom, B.8    Schlessinger, J.9    Givol, D.10
  • 30
    • 0034722889 scopus 로고    scopus 로고
    • The EGF receptor family as targets for cancer therapy
    • Mendelsohn J., Baselga J. The EGF receptor family as targets for cancer therapy. Oncogene. 19:2000;6550-6565.
    • (2000) Oncogene , vol.19 , pp. 6550-6565
    • Mendelsohn, J.1    Baselga, J.2
  • 31
    • 0029165834 scopus 로고
    • Direct and specific interaction of c-Src with Neu is involved in signalling by the epidermal growth factor receptor
    • Muthuswamy S.K., Muller W.J. Direct and specific interaction of c-Src with Neu is involved in signalling by the epidermal growth factor receptor. Oncogene. 11:1995;271-279.
    • (1995) Oncogene , vol.11 , pp. 271-279
    • Muthuswamy, S.K.1    Muller, W.J.2
  • 32
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;281-295.
    • (1991) Proteins , vol.11 , pp. 281-295
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 34
    • 0034600849 scopus 로고    scopus 로고
    • The ErbB signaling network: Receptor heterodimerization in development and cancer
    • Olayioye M.A., Neve R.M., Lane H.A., Hynes N.E. The ErbB signaling network. receptor heterodimerization in development and cancer EMBO J. 19:2000;3159-3167.
    • (2000) EMBO J. , vol.19 , pp. 3159-3167
    • Olayioye, M.A.1    Neve, R.M.2    Lane, H.A.3    Hynes, N.E.4
  • 35
    • 0030700883 scopus 로고    scopus 로고
    • A linear region of a monoclonal antibody conformational epitope mapped on p185HER2 oncoprotein
    • Orlandi R., Formantici C., Menard S., Boyer C.M., Wiener J.R., Colnaghi M. A linear region of a monoclonal antibody conformational epitope mapped on p185HER2 oncoprotein. Biol. Chem. 378:1997;1387-1392.
    • (1997) Biol. Chem. , vol.378 , pp. 1387-1392
    • Orlandi, R.1    Formantici, C.2    Menard, S.3    Boyer, C.M.4    Wiener, J.R.5    Colnaghi, M.6
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 0037047402 scopus 로고    scopus 로고
    • Identification of a region within the EerbB2/HER2 intracellular domain that is necessary for ligand-independent association
    • Penuel E., Akita R.W., Sliwkowski M.X. Identification of a region within the EerbB2/HER2 intracellular domain that is necessary for ligand-independent association. J. Biol. Chem. 277:2002;28468-28473.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28468-28473
    • Penuel, E.1    Akita, R.W.2    Sliwkowski, M.X.3
  • 41
    • 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 D.M., Fei Z., Zhang H.T., Kao C.C., Greene M.I. Domain-specific interactions between the p185(neu) and epidermal growth factor receptor kinases determine differential signaling outcomes. J. Biol. Chem. 274:1999;574-583.
    • (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
  • 43
    • 0037144523 scopus 로고    scopus 로고
    • Decorin binds to a narrow region of the EGF receptor, partially overlapping with, but distinct from, the EGF-binding epitope
    • Santra M., Reed C.C., Iozzo R.V. Decorin binds to a narrow region of the EGF receptor, partially overlapping with, but distinct from, the EGF-binding epitope. J. Biol. Chem. 277:2002;35671-35681.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35671-35681
    • Santra, M.1    Reed, C.C.2    Iozzo, R.V.3
  • 44
    • 0033215237 scopus 로고    scopus 로고
    • Mutagenesis reveals a role for epidermal growth factor receptor extracellular subdomain IV in ligand binding
    • Saxon M.L., Lee D.C. Mutagenesis reveals a role for epidermal growth factor receptor extracellular subdomain IV in ligand binding. J. Biol. Chem. 274:1999;28356-28362.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28356-28362
    • Saxon, M.L.1    Lee, D.C.2
  • 45
    • 0033534480 scopus 로고    scopus 로고
    • A discrete three-amino acid segment (LVI) at the C-terminal end of kinase-impaired ErbB3 is required for transactivation of ErbB2
    • Schaefer G., Akita R.W., Sliwkowski M.X. A discrete three-amino acid segment (LVI) at the C-terminal end of kinase-impaired ErbB3 is required for transactivation of ErbB2. J. Biol. Chem. 274:1999;859-866.
    • (1999) J. Biol. Chem. , vol.274 , pp. 859-866
    • Schaefer, G.1    Akita, R.W.2    Sliwkowski, M.X.3
  • 47
    • 0034732721 scopus 로고    scopus 로고
    • Val(659)-> Glu mutation within the transmembrane domain of ErbB-2: Effects measured by H-2 NMR in fluid phospholipid bilayers
    • Sharpe S., Barber K.R., Grant C.W.M. Val(659)-> Glu mutation within the transmembrane domain of ErbB-2. Effects measured by H-2 NMR in fluid phospholipid bilayers Biochemistry. 39:2000;6572-6580.
    • (2000) Biochemistry , vol.39 , pp. 6572-6580
    • Sharpe, S.1    Barber, K.R.2    Grant, C.W.M.3
  • 49
    • 0024559003 scopus 로고
    • Chinese hamster ovary cell mutants with multiple glycosylation defects for the production of glycoproteins with minimal carbohydrate heterogeneity
    • Stanley P. Chinese hamster ovary cell mutants with multiple glycosylation defects for the production of glycoproteins with minimal carbohydrate heterogeneity. Mol. Cell. Biol. 9:1989;377-383.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 377-383
    • Stanley, P.1
  • 50
    • 0031756437 scopus 로고    scopus 로고
    • Biological response to ErbB ligands in nontransformed cell lines correlates with a specific pattern of receptor expression
    • Sundaresan S., Roberts P.E., King K.L., Sliwkowski M.X., Mather J.P. Biological response to ErbB ligands in nontransformed cell lines correlates with a specific pattern of receptor expression. Endocrinology. 139:1998;4756-4764.
    • (1998) Endocrinology , vol.139 , pp. 4756-4764
    • Sundaresan, S.1    Roberts, P.E.2    King, K.L.3    Sliwkowski, M.X.4    Mather, J.P.5
  • 51
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • Takagi J., Petre B.M., Walz T., Springer T.A. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell. 110:2002;599-611.
    • (2002) Cell , vol.110 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 52
    • 0021273420 scopus 로고
    • Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells
    • Ullrich A., Coussens L., Hayflick J.S., Dull T.J., Gray A., Tam A.W., Lee J., Yarden Y., Libermann T.A., Schlessinger J.et al. Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells. Nature. 309:1984;418-425.
    • (1984) Nature , vol.309 , pp. 418-425
    • Ullrich, A.1    Coussens, L.2    Hayflick, J.S.3    Dull, T.J.4    Gray, A.5    Tam, A.W.6    Lee, J.7    Yarden, Y.8    Libermann, T.A.9    Schlessinger, J.10
  • 53
    • 0029060529 scopus 로고
    • Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumor necrosis factor receptor
    • Ward C.W., Hoyne P.A., Flegg R.H. Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumor necrosis factor receptor. Proteins. 22:1995;141-153.
    • (1995) Proteins , vol.22 , pp. 141-153
    • Ward, C.W.1    Hoyne, P.A.2    Flegg, R.H.3
  • 54
    • 0037039303 scopus 로고    scopus 로고
    • Effect of ErbB2 coexpression on the kinetic interactions of epidermal growth factor with its receptor in intact cells
    • Wilkinson J.C., Staros J.V. Effect of ErbB2 coexpression on the kinetic interactions of epidermal growth factor with its receptor in intact cells. Biochemistry. 41:2002;8-14.
    • (2002) Biochemistry , vol.41 , pp. 8-14
    • Wilkinson, J.C.1    Staros, J.V.2
  • 57
    • 0035675556 scopus 로고    scopus 로고
    • Anti-ErbB-2 monoclonal antibodies and ErbB-2-directed vaccines
    • Yip Y.L., Ward R.L. Anti-ErbB-2 monoclonal antibodies and ErbB-2-directed vaccines. Cancer Immunol. Immunother. 50:2002;569-587.
    • (2002) Cancer Immunol. Immunother. , vol.50 , pp. 569-587
    • Yip, Y.L.1    Ward, R.L.2
  • 58
    • 0035871618 scopus 로고    scopus 로고
    • Identification of epitope regions recognized by tumor inhibitory and stimulatory anti-ErbB-2 monoclonal antibodies: Implications for vaccine design
    • Yip Y.L., Smith G., Koch J., Dubel S., Ward R.L. Identification of epitope regions recognized by tumor inhibitory and stimulatory anti-ErbB-2 monoclonal antibodies. implications for vaccine design J. Immunol. 166:2001;5271-5278.
    • (2001) J. Immunol. , vol.166 , pp. 5271-5278
    • Yip, Y.L.1    Smith, G.2    Koch, J.3    Dubel, S.4    Ward, R.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.