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Volumn 110, Issue 6, 2002, Pages 775-787

Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE KINASE;

EID: 18644386251     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(02)00963-7     Document Type: Article
Times cited : (970)

References (62)
  • 2
    • 0033554674 scopus 로고    scopus 로고
    • Atomic structure of the GCSF-receptor complex showing a new cytokine-receptor recognition scheme
    • Aritomi M., Kunishima N., Okamoto T., Kuroki R., Ota Y., Morikawa K. Atomic structure of the GCSF-receptor complex showing a new cytokine-receptor recognition scheme. Nature. 401:1999;713-717.
    • (1999) Nature , vol.401 , pp. 713-717
    • Aritomi, M.1    Kunishima, N.2    Okamoto, T.3    Kuroki, R.4    Ota, Y.5    Morikawa, K.6
  • 3
    • 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
  • 5
    • 0028145271 scopus 로고
    • The extracellular domain of the epidermal growth factor receptor. Studies on the affinity and stoichiometry of binding, receptor dimerization and a binding-domain mutant
    • Brown P.M., Debanne M.T., Grothe S., Bergsma D., Caron M., Kay C., O'Connor-McCourt M.D. The extracellular domain of the epidermal growth factor receptor. Studies on the affinity and stoichiometry of binding, receptor dimerization and a binding-domain mutant. Eur. J. Biochem. 225:1994;223-233.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 223-233
    • Brown, P.M.1    Debanne, M.T.2    Grothe, S.3    Bergsma, D.4    Caron, M.5    Kay, C.6    O'Connor-McCourt, M.D.7
  • 7
    • 0025134280 scopus 로고
    • Biochemical properties of site-directed mutants of human epidermal growth factor: Importance of solvent-exposed hydrophobic residues of the amino-terminal domain in receptor binding
    • Campion S.R., Matsunami R.K., Engler D.A., Niyogi S.K. Biochemical properties of site-directed mutants of human epidermal growth factor. importance of solvent-exposed hydrophobic residues of the amino-terminal domain in receptor binding Biochemistry. 29:1990;9988-9993.
    • (1990) Biochemistry , vol.29 , pp. 9988-9993
    • Campion, S.R.1    Matsunami, R.K.2    Engler, D.A.3    Niyogi, S.K.4
  • 9
    • 0025321157 scopus 로고
    • Epidermal growth factor
    • Carpenter G., Cohen S. Epidermal growth factor. J. Biol. Chem. 265:1990;7709-7712.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7709-7712
    • Carpenter, G.1    Cohen, S.2
  • 10
    • 0028103275 scopus 로고
    • The CCP4 (Collaborative Computational Project 4) suite: Programs for protein crystallography
    • CCP4 The CCP4 (Collaborative Computational Project 4) suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 11
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos A.M., Ultsch M., Kossiakoff A.A. Human growth hormone and extracellular domain of its receptor. crystal structure of the complex Science. 255:1992;306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 13
    • 0021752924 scopus 로고
    • Human transforming growth factor-α: Precursor structure and expression in E. coli
    • Derynck R., Roberts A.B., Winkler M.E., Chen E.Y., Goeddel D.V. Human transforming growth factor-α precursor structure and expression in E. coli Cell. 38:1984;287-297.
    • (1984) Cell , vol.38 , pp. 287-297
    • Derynck, R.1    Roberts, A.B.2    Winkler, M.E.3    Chen, E.Y.4    Goeddel, D.V.5
  • 16
    • 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
  • 17
    • 0026787356 scopus 로고
    • Critical functional requirement for the guanidinium group of the arginine 41 side chain of human epidermal growth factor as revealed by mutagenic inactivation and chemical reactivation
    • Engler D.A., Campion S.R., Hauser M.R., Cook J.S., Niyogi S.K. Critical functional requirement for the guanidinium group of the arginine 41 side chain of human epidermal growth factor as revealed by mutagenic inactivation and chemical reactivation. J. Biol. Chem. 267:1992;2274-2281.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2274-2281
    • Engler, D.A.1    Campion, S.R.2    Hauser, M.R.3    Cook, J.S.4    Niyogi, S.K.5
  • 19
    • 18644370411 scopus 로고    scopus 로고
    • Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor-α
    • Garrett T.P.J., McKern N.M., Lou M., Elleman T.C., Adams T.E., Lovrecz G.O., Zhu H.-J., Walker F., Frenkel M.J., Hoyne P.A.et al. Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor-α Cell. 110:2002;763-773. this issue,
    • (2002) Cell , vol.110 , Issue.THIS ISSUE , pp. 763-773
    • Garrett, T.P.J.1    McKern, N.M.2    Lou, M.3    Elleman, T.C.4    Adams, T.E.5    Lovrecz, G.O.6    Zhu, H.-J.7    Walker, F.8    Frenkel, M.J.9    Hoyne, P.A.10
  • 20
    • 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
  • 21
    • 0028618937 scopus 로고
    • Structure-function relationships for the EGF/TGF-α family of mitogens
    • Groenen L.C., Nice E.C., Burgess A.W. Structure-function relationships for the EGF/TGF-α family of mitogens. Growth Factors. 11:1994;235-257.
    • (1994) Growth Factors , vol.11 , pp. 235-257
    • Groenen, L.C.1    Nice, E.C.2    Burgess, A.W.3
  • 22
    • 0025668419 scopus 로고
    • The secreted form of the epidermal growth factor receptor. Characterization and crystallization of the receptor-ligand complex
    • Gunther N., Betzel C., Weber W. The secreted form of the epidermal growth factor receptor. Characterization and crystallization of the receptor-ligand complex. J. Biol. Chem. 265:1990;22082-22085.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22082-22085
    • Gunther, N.1    Betzel, C.2    Weber, W.3
  • 23
    • 0024542564 scopus 로고
    • Analysis of mammalian fibroblast transformation by normal and mutated human EGF receptors
    • Haley J.D., Hsuan J.J., Waterfield M.D. Analysis of mammalian fibroblast transformation by normal and mutated human EGF receptors. Oncogene. 4:1989;273-283.
    • (1989) Oncogene , vol.4 , pp. 273-283
    • Haley, J.D.1    Hsuan, J.J.2    Waterfield, M.D.3
  • 25
    • 14444288522 scopus 로고    scopus 로고
    • The enhanced tumorigenic activity of a mutant epidermal growth factor receptor common in human cancers is mediated by threshold levels of constitutive tyrosine phosphorylation and unattenuated signaling
    • Huang H.S., Nagane M., Klingbeil C.K., Lin H., Nishikawa R., Ji X.D., Huang C.M., Gill G.N., Wiley H.S., Cavenee W.K. The enhanced tumorigenic activity of a mutant epidermal growth factor receptor common in human cancers is mediated by threshold levels of constitutive tyrosine phosphorylation and unattenuated signaling. J. Biol. Chem. 272:1997;2927-2935.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2927-2935
    • Huang, H.S.1    Nagane, M.2    Klingbeil, C.K.3    Lin, H.4    Nishikawa, R.5    Ji, X.D.6    Huang, C.M.7    Gill, G.N.8    Wiley, H.S.9    Cavenee, W.K.10
  • 26
    • 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
  • 27
    • 0036093854 scopus 로고    scopus 로고
    • Chimeric receptor analyses of the interactions of the ectodomains of ErbB-1 with epidermal growth factor and of those of ErbB-4 with neuregulin
    • Kim J.-H., Saito K., Yokoyama S. Chimeric receptor analyses of the interactions of the ectodomains of ErbB-1 with epidermal growth factor and of those of ErbB-4 with neuregulin. Eur. J. Biochem. 269:2002;2323-2329.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2323-2329
    • Kim, J.-H.1    Saito, K.2    Yokoyama, S.3
  • 28
    • 0026464730 scopus 로고
    • Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions
    • Kohda D., Inagaki F. Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions. Biochemistry. 31:1992;11928-11939.
    • (1992) Biochemistry , vol.31 , pp. 11928-11939
    • Kohda, D.1    Inagaki, F.2
  • 29
    • 0027519152 scopus 로고
    • A 40-kDa epidermal growth factor/transforming growth factor α-binding domain produced by limited proteolysis of the extracellular domain of the epidermal growth factor receptor
    • Kohda D., Odaka M., Lax I., Kawasaki H., Suzuki K., Ullrich A., Schlessinger J., Inagaki F. A 40-kDa epidermal growth factor/transforming growth factor α-binding domain produced by limited proteolysis of the extracellular domain of the epidermal growth factor receptor. J. Biol. Chem. 268:1993;1976-1981.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1976-1981
    • Kohda, D.1    Odaka, M.2    Lax, I.3    Kawasaki, H.4    Suzuki, K.5    Ullrich, A.6    Schlessinger, J.7    Inagaki, F.8
  • 30
    • 17644444217 scopus 로고
    • Recognition of an antiparallel beta-sheet structure of human epidermal growth factor by its receptor. Site-directed mutagenesis studies of Ala-30 and Asn-32
    • Koide H., Muto Y., Kasai H., Hoshi K., Takusari H., Kohri K., Takahashi S., Sasaki T., Tsukumo K., Miyake T.et al. Recognition of an antiparallel beta-sheet structure of human epidermal growth factor by its receptor. Site-directed mutagenesis studies of Ala-30 and Asn-32. FEBS Lett. 302:1992;39-42. a.
    • (1992) FEBS Lett. , vol.302 , pp. 39-42
    • Koide, H.1    Muto, Y.2    Kasai, H.3    Hoshi, K.4    Takusari, H.5    Kohri, K.6    Takahashi, S.7    Sasaki, T.8    Tsukumo, K.9    Miyake, T.10
  • 32
    • 0024342417 scopus 로고
    • Functional analysis of the ligand binding site of EGF-receptor utilizing chimeric chicken/human receptor molecules
    • Lax I., Bellot F., Howk R., Ullrich A., Givol D., Schlessinger J. Functional analysis of the ligand binding site of EGF-receptor utilizing chimeric chicken/human receptor molecules. EMBO J. 8:1989;421-427.
    • (1989) EMBO J. , vol.8 , pp. 421-427
    • Lax, I.1    Bellot, F.2    Howk, R.3    Ullrich, A.4    Givol, D.5    Schlessinger, J.6
  • 34
    • 0035860766 scopus 로고    scopus 로고
    • Crystal structure of human epidermal growth factor and its dimerization
    • Lu H.S., Chai J.J., Li M., Huang B.R., He C.H., Bi R.C. Crystal structure of human epidermal growth factor and its dimerization. J. Biol. Chem. 276:2001;34913-34917.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34913-34917
    • Lu, H.S.1    Chai, J.J.2    Li, M.3    Huang, B.R.4    He, C.H.5    Bi, R.C.6
  • 35
    • 0021360015 scopus 로고
    • Rat transforming growth factor type 1: Structure and relation to epidermal growth factor
    • Marquardt H., Hunkapiller M.W., Hood L.E., Todaro G.J. Rat transforming growth factor type 1. structure and relation to epidermal growth factor Science. 223:1984;1079-1082.
    • (1984) Science , vol.223 , pp. 1079-1082
    • Marquardt, H.1    Hunkapiller, M.W.2    Hood, L.E.3    Todaro, G.J.4
  • 36
    • 0034016522 scopus 로고    scopus 로고
    • NMR study of the differential contributions of residues of transforming growth factor alpha to association with its receptor
    • McInnes C., Grothe S., O'Connor-McCourt M., Sykes B.D. NMR study of the differential contributions of residues of transforming growth factor alpha to association with its receptor. Protein Eng. 13:2000;143-147.
    • (2000) Protein Eng. , vol.13 , pp. 143-147
    • McInnes, C.1    Grothe, S.2    O'Connor-McCourt, M.3    Sykes, B.D.4
  • 37
    • 0032860819 scopus 로고    scopus 로고
    • Controlled dimerization of ErbB receptors provides evidence for differential signaling by homo- and heterodimers
    • Muthuswamy S.K., Gilman M., Brugge J.S. Controlled dimerization of ErbB receptors provides evidence for differential signaling by homo- and heterodimers. Mol. Cell. Biol. 19:1999;6845-6857.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6845-6857
    • Muthuswamy, S.K.1    Gilman, M.2    Brugge, J.S.3
  • 38
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe. an automated package for molecular replacement Acta Crystallogr. A. 50:1994;157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 39
    • 0030737618 scopus 로고    scopus 로고
    • Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor
    • Odaka M., Kohda D., Lax I., Schlessinger J., Inagaki F. Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor. J. Biochem. (Tokyo). 122:1997;116-121.
    • (1997) J. Biochem. (Tokyo) , vol.122 , pp. 116-121
    • Odaka, M.1    Kohda, D.2    Lax, I.3    Schlessinger, J.4    Inagaki, F.5
  • 40
    • 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
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collection in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collection in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 42
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • Pellegrini L., Burke D.F., von Delft F., Mulloy B., Blundell T.L. Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. Nature. 407:2000;1029-1034.
    • (2000) Nature , vol.407 , pp. 1029-1034
    • Pellegrini, L.1    Burke, D.F.2    Von Delft, F.3    Mulloy, B.4    Blundell, T.L.5
  • 43
    • 0033520472 scopus 로고    scopus 로고
    • Structural basis for FGF receptor dimerization and activation
    • Plotnikov A.N., Schlessinger J., Hubbard S.R., Mohammadi M. Structural basis for FGF receptor dimerization and activation. Cell. 98:1999;641-650.
    • (1999) Cell , vol.98 , pp. 641-650
    • Plotnikov, A.N.1    Schlessinger, J.2    Hubbard, S.R.3    Mohammadi, M.4
  • 44
    • 0034640103 scopus 로고    scopus 로고
    • Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity
    • Plotnikov A.N., Hubbard S.R., Schlessinger J., Mohammadi M. Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity. Cell. 101:2000;413-424.
    • (2000) Cell , vol.101 , pp. 413-424
    • Plotnikov, A.N.1    Hubbard, S.R.2    Schlessinger, J.3    Mohammadi, M.4
  • 45
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • Sako Y., Minoghchi S., Yanagida T. Single-molecule imaging of EGFR signalling on the surface of living cells. Nat. Cell Biol. 2:2000;168-172.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 46
    • 0033950717 scopus 로고    scopus 로고
    • Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor
    • Sato C., Kim J.-H., Abe Y., Saito K., Yokoyama S., Kohda D. Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor. J. Biochem. (Tokyo). 127:2000;65-72.
    • (2000) J. Biochem. (Tokyo) , vol.127 , pp. 65-72
    • Sato, C.1    Kim, J.-H.2    Abe, Y.3    Saito, K.4    Yokoyama, S.5    Kohda, D.6
  • 48
  • 49
    • 0029810873 scopus 로고    scopus 로고
    • Identification of residues of the epidermal growth factor receptor proximal to residue 45 of bound epidermal growth factor
    • Summerfield A.E., Hudnall A.K., Lukas T.J., Guyer C.A., Staros J.V. Identification of residues of the epidermal growth factor receptor proximal to residue 45 of bound epidermal growth factor. J. Biol. Chem. 271:1996;19656-19659.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19656-19659
    • Summerfield, A.E.1    Hudnall, A.K.2    Lukas, T.J.3    Guyer, C.A.4    Staros, J.V.5
  • 51
    • 0027157416 scopus 로고
    • The functional importance of hydrophobicity of the tyrosine at position 13 of human epidermal growth factor in receptor binding
    • Tadaki D.K., Niyogi S.K. The functional importance of hydrophobicity of the tyrosine at position 13 of human epidermal growth factor in receptor binding. J. Biol. Chem. 268:1993;10114-10119.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10114-10119
    • Tadaki, D.K.1    Niyogi, S.K.2
  • 52
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallogr. D. 56:2000;965-972.
    • (2000) Acta Crystallogr. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 53
    • 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., Ratzkin B.J., Yarden Y. A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor. Mol. Cell. Biol. 16:1996;5276-5287.
    • (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    Ratzkin, B.J.7    Yarden, Y.8
  • 54
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich A., Schlessinger J. Signal transduction by receptors with tyrosine kinase activity. Cell. 61:1990;203-212.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 55
    • 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
  • 56
    • 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
  • 57
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB v2.0
    • Weeks C.M., Miller R. The design and implementation of SnB v2.0. J. Appl. Crystallogr. 32:1999;120-124.
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 58
    • 0033539065 scopus 로고    scopus 로고
    • Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor
    • Wiesmann C., Ultsch M.H., Bass S.H., de Vos A.M. Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor. Nature. 401:1999;184-188.
    • (1999) Nature , vol.401 , pp. 184-188
    • Wiesmann, C.1    Ultsch, M.H.2    Bass, S.H.3    De Vos, A.M.4
  • 59
    • 0026687755 scopus 로고
    • Direct identification of residues of the epidermal growth factor receptor in close proximity to the amino terminus of bound epidermal growth factor
    • Woltjer R.L., Lukas T.J., Staros J.V. Direct identification of residues of the epidermal growth factor receptor in close proximity to the amino terminus of bound epidermal growth factor. Proc. Natl. Acad. Sci. USA. 89:1992;7801-7805.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7801-7805
    • Woltjer, R.L.1    Lukas, T.J.2    Staros, J.V.3
  • 60
    • 0024325767 scopus 로고
    • Human epidermal growth factor (EGF) receptor sequence recognized by EGF competitive monoclonal antibodies. Evidence for the localization of the EGF-binding site
    • Wu D.G., Wang L.H., Sato G.H., West K.A., Harris W.R., Crabb J.W., Sato J.D. Human epidermal growth factor (EGF) receptor sequence recognized by EGF competitive monoclonal antibodies. Evidence for the localization of the EGF-binding site. J. Biol. Chem. 264:1989;17469-17475.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17469-17475
    • Wu, D.G.1    Wang, L.H.2    Sato, G.H.3    West, K.A.4    Harris, W.R.5    Crabb, J.W.6    Sato, J.D.7
  • 61
    • 0025246227 scopus 로고
    • Human epidermal growth factor receptor residue covalently cross-linked to epidermal growth factor
    • Wu D.G., Wang L.H., Chi Y., Sato G.H., Sato J.D. Human epidermal growth factor receptor residue covalently cross-linked to epidermal growth factor. Proc. Natl. Acad. Sci. USA. 87:1990;3151-3155.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3151-3155
    • Wu, D.G.1    Wang, L.H.2    Chi, Y.3    Sato, G.H.4    Sato, J.D.5
  • 62
    • 0021055658 scopus 로고
    • The erbB gene of avian erythroblastosis virus is a member of the src gene family
    • Yamamoto T., Nishida T., Miyajima N., Kawai S., Ooi T., Toyoshima K. The erbB gene of avian erythroblastosis virus is a member of the src gene family. Cell. 35:1983;71-78.
    • (1983) Cell , vol.35 , pp. 71-78
    • Yamamoto, T.1    Nishida, T.2    Miyajima, N.3    Kawai, S.4    Ooi, T.5    Toyoshima, K.6


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