메뉴 건너뛰기




Volumn 18, Issue 9, 1998, Pages 5371-7379

Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SUBSTITUTION; ARTICLE; DIMERIZATION; DISULFIDE BOND; ENZYME ACTIVITY; GENE MAPPING; HYPOTHESIS; PREDICTION; PRIORITY JOURNAL; SIGNAL TRANSDUCTION; STOICHIOMETRY;

EID: 0031842104     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.18.9.5371     Document Type: Article
Times cited : (98)

References (61)
  • 1
    • 0029847652 scopus 로고    scopus 로고
    • Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching
    • Adams, P. D., D. M. Engelman, and A. T. Brunger. 1996. Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching. Proteins 26:257-261.
    • (1996) Proteins , vol.26 , pp. 257-261
    • Adams, P.D.1    Engelman, D.M.2    Brunger, A.T.3
  • 2
    • 0022647432 scopus 로고
    • The product of the human c-erbB-2 gene: A 185-kilodalton glycoprotein with tyrosine kinase activity
    • Akiyama, T., C. Sudo, H. Ogawara, K. Toyoshima, and T. Yamamoto. 1986. The product of the human c-erbB-2 gene: a 185-kilodalton glycoprotein with tyrosine kinase activity. Science 232:1644-1646.
    • (1986) Science , vol.232 , pp. 1644-1646
    • Akiyama, T.1    Sudo, C.2    Ogawara, H.3    Toyoshima, K.4    Yamamoto, T.5
  • 3
    • 0022485548 scopus 로고
    • Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185
    • Bargmann, C. I., M.-C. Hung, and R. A. Weinberg. 1986. Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185. Cell 45:649-657.
    • (1986) Cell , vol.45 , pp. 649-657
    • Bargmann, C.I.1    Hung, M.-C.2    Weinberg, R.A.3
  • 4
    • 0022600388 scopus 로고
    • The neu oncogene encodes an epidermal growth factor receptor-related protein
    • Bargmann, C. I., M. C. Hung, and R. A. Weinberg. 1986. The neu oncogene encodes an epidermal growth factor receptor-related protein. Nature 310: 226-230.
    • (1986) Nature , vol.310 , pp. 226-230
    • Bargmann, C.I.1    Hung, M.C.2    Weinberg, R.A.3
  • 5
    • 0024042025 scopus 로고
    • Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion
    • Bargmann, C. I., and R. A. Weinberg. 1988. Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion. EMBO J. 7: 2043-2052.
    • (1988) EMBO J. , vol.7 , pp. 2043-2052
    • Bargmann, C.I.1    Weinberg, R.A.2
  • 6
    • 0024278714 scopus 로고
    • Helix geometry in proteins
    • Barlow, D., and J. Thornton. 1988. Helix geometry in proteins. J. Mol. Biol. 201:601-619.
    • (1988) J. Mol. Biol. , vol.201 , pp. 601-619
    • Barlow, D.1    Thornton, J.2
  • 8
    • 0030614530 scopus 로고    scopus 로고
    • Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation
    • Burke, C. L., M. A. Lemmon, B. A. Coren, D. M. Engelman, and D. F. Stern. 1997. Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation. Oncogene 14:687-696.
    • (1997) Oncogene , vol.14 , pp. 687-696
    • Burke, C.L.1    Lemmon, M.A.2    Coren, B.A.3    Engelman, D.M.4    Stern, D.F.5
  • 10
    • 0026511905 scopus 로고
    • A subdomain in the transmembrane domain is necessary for p185neu*activation
    • Cao, H., L. Bangalore, B. J. Bormann, and D. F. Stern. 1992. A subdomain in the transmembrane domain is necessary for p185neu*activation. EMBO J. 11:923-932.
    • (1992) EMBO J. , vol.11 , pp. 923-932
    • Cao, H.1    Bangalore, L.2    Bormann, B.J.3    Stern, D.F.4
  • 12
    • 0025778063 scopus 로고
    • TPA inhibits the tyrosine kinase activity of the neu protein in vivo and in vitro
    • Cao, H., S. Decker, and D. F. Stern. 1991. TPA inhibits the tyrosine kinase activity of the neu protein in vivo and in vitro. Oncogene 6:705-711.
    • (1991) Oncogene , vol.6 , pp. 705-711
    • Cao, H.1    Decker, S.2    Stern, D.F.3
  • 13
    • 0030969251 scopus 로고    scopus 로고
    • Transmembrane domain sequence requirements for activation of the p185c-neu receptor tyrosine kinase
    • Chen, L. I., M. K. Webster, A. N. Meyer, and D. J. Donoghue. 1997. Transmembrane domain sequence requirements for activation of the p185c-neu receptor tyrosine kinase. J. Cell Biol. 137:619-631.
    • (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
  • 14
    • 0029130732 scopus 로고
    • Transmembrane signaling by the aspartate receptor: Engineered disulfides reveal static regions of the subunit interface
    • Chervitz, S. A., C. M. Lin, and J. J. Falke. 1995. Transmembrane signaling by the aspartate receptor: engineered disulfides reveal static regions of the subunit interface. Biochemistry 34:9722-9733.
    • (1995) Biochemistry , vol.34 , pp. 9722-9733
    • Chervitz, S.A.1    Lin, C.M.2    Falke, J.J.3
  • 15
    • 0023848318 scopus 로고
    • Demonstration of epidermal growth factor-induced receptor dimerization in living cells using a chemical covalent cross-linking agent
    • Cochet, C., O. Kashles, E. M. Chambaz, I. Borello, C. R. King, and J. Schlessinger. 1988. Demonstration of epidermal growth factor-induced receptor dimerization in living cells using a chemical covalent cross-linking agent. J. Biol. Chem. 263:3290-3295.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3290-3295
    • Cochet, C.1    Kashles, O.2    Chambaz, E.M.3    Borello, I.4    King, C.R.5    Schlessinger, J.6
  • 16
    • 0025272940 scopus 로고
    • Alpha-helical coiled-coils and bundles: How to design an alpha-helical protein
    • Cohen, C., and D. A. D. Parry. 1990. Alpha-helical coiled-coils and bundles: how to design an alpha-helical protein. Proteins 7:1-15.
    • (1990) Proteins , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 18
    • 0030794283 scopus 로고    scopus 로고
    • Distinct tyrosine autophosphorylation sites negatively and positively modulate Neu-mediated transformation
    • Dankort, D. L., Z. Wang, V. Blackmore, M. F. Moran, and W. J. Muller. 1997. Distinct tyrosine autophosphorylation sites negatively and positively modulate Neu-mediated transformation. Mol. Cell. Biol. 17:5410-5425.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5410-5425
    • Dankort, D.L.1    Wang, Z.2    Blackmore, V.3    Moran, M.F.4    Muller, W.J.5
  • 19
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • De Vos, A. M., M. Ultsch, and A. A. Kossiakoff. 1992. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255:306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 20
    • 0028290891 scopus 로고
    • The neu-oncogene: Signal transduction pathways, transformation mechanisms and evolving therapies
    • Dougall, W. C., X. Qian, N. C. Peterson, M. J. Miller, A. Samanta, and M. I. Greene. 1994. The neu-oncogene: signal transduction pathways, transformation mechanisms and evolving therapies. Oncogene 9:2109-2123.
    • (1994) Oncogene , vol.9 , pp. 2109-2123
    • Dougall, W.C.1    Qian, X.2    Peterson, N.C.3    Miller, M.J.4    Samanta, A.5    Greene, M.I.6
  • 22
    • 0021680507 scopus 로고
    • Monoclonal antibodies recognize a cell-surface antigen associated with an activated cellular oncogene
    • Drebin, J. A., D. F. Stern, V. C. Link, R. A. Weinberg, and M. I. Greene. 1984. Monoclonal antibodies recognize a cell-surface antigen associated with an activated cellular oncogene. Nature 312:545-548.
    • (1984) Nature , vol.312 , pp. 545-548
    • Drebin, J.A.1    Stern, D.F.2    Link, V.C.3    Weinberg, R.A.4    Greene, M.I.5
  • 23
    • 0031214550 scopus 로고    scopus 로고
    • Molecular modeling of c-erbB2 receptor dimerization: Coiled-coil structure of wild and oncogenic transmembrane domains - Stabilization by interhelical hydrogen bonds in the oncogenic form
    • Garnier, N., D. Genest, J. P. Duneau, and M. Genest. 1997. Molecular modeling of c-erbB2 receptor dimerization: coiled-coil structure of wild and oncogenic transmembrane domains - stabilization by interhelical hydrogen bonds in the oncogenic form. Biopoly 42:157-168.
    • (1997) Biopoly , vol.42 , pp. 157-168
    • Garnier, N.1    Genest, D.2    Duneau, J.P.3    Genest, M.4
  • 25
    • 0021742462 scopus 로고
    • Conversion of a secretory protein into a transmembrane protein results in its transport to the Golgi complex but not the cell surface
    • Guan, J.-L., and J. K. Rose. 1984. Conversion of a secretory protein into a transmembrane protein results in its transport to the Golgi complex but not the cell surface. Cell 37:779-787.
    • (1984) Cell , vol.37 , pp. 779-787
    • Guan, J.-L.1    Rose, J.K.2
  • 26
    • 0026472124 scopus 로고
    • Expression of the neu protooncogene in the mammary epithelium of transgenic mice induces metastatic disease
    • Guy, C. T., M. A. Webster, M. Schaller, T. J. Parsons, R. D. Cardiff, and W. J. Muller. 1992. Expression of the neu protooncogene in the mammary epithelium of transgenic mice induces metastatic disease. Proc. Natl. Acad. Sci. USA 89:10578-10582.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10578-10582
    • Guy, C.T.1    Webster, M.A.2    Schaller, M.3    Parsons, T.J.4    Cardiff, R.D.5    Muller, W.J.6
  • 27
    • 0030183048 scopus 로고    scopus 로고
    • Ligand-induced dimerization of growth factor receptors: Variations on the theme
    • Heldin, C.-H., and A. Ostman. 1996. Ligand-induced dimerization of growth factor receptors: variations on the theme. Cytokine Growth Factor Rev. 7: 33-40.
    • (1996) Cytokine Growth Factor Rev. , vol.7 , pp. 33-40
    • Heldin, C.-H.1    Ostman, A.2
  • 28
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin, C. H. 1995. Dimerization of cell surface receptors in signal transduction. Cell 80:213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 29
    • 0028670125 scopus 로고
    • The biology of erbB-2/neu/HER-2 and its role in cancer
    • Hynes, N. E., and D. F. Stern. 1994. The biology of erbB-2/neu/HER-2 and its role in cancer. Biochim. Biophys. Acta Rev. Cancer 1198:165-184.
    • (1994) Biochim. Biophys. Acta Rev. Cancer , vol.1198 , pp. 165-184
    • Hynes, N.E.1    Stern, D.F.2
  • 30
    • 0023919982 scopus 로고
    • Identification of multiple novel polypeptide substrates of the v-src, v-yes, v-fps, v-ros, and v-erb-B oncogenic tyrosine protein kinases utilizing antisera against phosphotyrosine
    • Kamps, M. P., and B. M. Sefton. 1988. Identification of multiple novel polypeptide substrates of the v-src, v-yes, v-fps, v-ros, and v-erb-B oncogenic tyrosine protein kinases utilizing antisera against phosphotyrosine. Oncogene 2:305-315.
    • (1988) Oncogene , vol.2 , pp. 305-315
    • Kamps, M.P.1    Sefton, B.M.2
  • 31
    • 0024395587 scopus 로고
    • Synergistic interaction of p185 c-neu and the EGF receptor leads to transformation of rodent fibroblasts
    • Kokai, Y., J. N. Meyers, T. Wada, V. I. Brown, C. M. LeVea, J. G. Davis, K. Dobashi, and M. I. Greene. 1989. Synergistic interaction of p185 c-neu and the EGF receptor leads to transformation of rodent fibroblasts. Cell 58:287-292.
    • (1989) Cell , vol.58 , pp. 287-292
    • Kokai, Y.1    Meyers, J.N.2    Wada, T.3    Brown, V.I.4    Levea, C.M.5    Davis, J.G.6    Dobashi, K.7    Greene, M.I.8
  • 33
    • 0000963997 scopus 로고
    • Helix-helix interactions inside lipid bilayers
    • Lemmon, M. A., and D. M. Engelman. 1992. Helix-helix interactions inside lipid bilayers. Curr. Opin. Struct. Biol. 2:511-518.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 511-518
    • Lemmon, M.A.1    Engelman, D.M.2
  • 35
    • 0027203585 scopus 로고
    • Specific short transmembrane sequences can inhibit transformation by the mutant neu growth factor receptor in vitro and in vivo
    • Lofts, F. J., H. C. Hurst, M. J. E. Sternberg, and W. J. Gullick. 1993. Specific short transmembrane sequences can inhibit transformation by the mutant neu growth factor receptor in vitro and in vivo. Oncogene 8:2813-2820.
    • (1993) Oncogene , vol.8 , pp. 2813-2820
    • Lofts, F.J.1    Hurst, H.C.2    Sternberg, M.J.E.3    Gullick, W.J.4
  • 36
    • 0025872118 scopus 로고
    • Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli
    • Lynch, B. A., and D. E. Koshland. 1991. Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli. Proc. Natl. Acad. Sci. USA 88:10402-10406.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10402-10406
    • Lynch, B.A.1    Koshland, D.E.2
  • 37
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K. R., J. H. Prestegard, and D. M. Engelman. 1997. A transmembrane helix dimer: structure and implications. Science 276:131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 38
    • 0022641294 scopus 로고
    • A human oncogene formed by the fusion of truncated tropomyosin and protein-tyrosine kinase sequences
    • Martin-Zanca, D., S. H. Hughes, and M. Barbacid. 1986. A human oncogene formed by the fusion of truncated tropomyosin and protein-tyrosine kinase sequences. Nature 319:743-748.
    • (1986) Nature , vol.319 , pp. 743-748
    • Martin-Zanca, D.1    Hughes, S.H.2    Barbacid, M.3
  • 39
    • 0022766181 scopus 로고
    • Human c-ros-1 gene homologous to the v-ros sequence of UR2 sarcoma virus encodes for a transmembrane receptor-like molecule
    • Matsushime, H., L.-H. Wang, and M. Shibuya. 1986. Human c-ros-1 gene homologous to the v-ros sequence of UR2 sarcoma virus encodes for a transmembrane receptor-like molecule. Mol. Cell. Biol. 6:3000-3004.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3000-3004
    • Matsushime, H.1    Wang, L.-H.2    Shibuya, M.3
  • 41
    • 0031936410 scopus 로고    scopus 로고
    • Specificity within the EGF/ErbB receptor family signaling network
    • Riese, D. J., II, and D. F. Stern. 1998. Specificity within the EGF/ErbB receptor family signaling network. Bioessays 20:41-48.
    • (1998) Bioessays , vol.20 , pp. 41-48
    • Riese II, D.J.1    Stern, D.F.2
  • 42
    • 0024278357 scopus 로고
    • Hydropathy of polar amino acid side-chains is markedly reduced by flanking peptide bonds
    • Roseman, M. A. 1988. Hydropathy of polar amino acid side-chains is markedly reduced by flanking peptide bonds. Mol. Biol. 200:513-522.
    • (1988) Mol. Biol. , vol.200 , pp. 513-522
    • Roseman, M.A.1
  • 43
    • 0023686033 scopus 로고
    • Signal transduction by allosteric receptor oligomerization
    • Schlessinger, J. 1988. Signal transduction by allosteric receptor oligomerization. Trends Biochem. Sci. 13:443-447.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 443-447
    • Schlessinger, J.1
  • 44
    • 0027986757 scopus 로고
    • Novel activating mutations in the neu proto-oncogene involved in induction of mammary tumors
    • Siegel, P. M., D. L. Dankort, W. R. Hardy, and W. J. Muller. 1994. Novel activating mutations in the neu proto-oncogene involved in induction of mammary tumors. Mol. Cell. Biol. 14:7068-7077.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7068-7077
    • Siegel, P.M.1    Dankort, D.L.2    Hardy, W.R.3    Muller, W.J.4
  • 45
    • 0029838204 scopus 로고    scopus 로고
    • Mutations affecting conserved cysteine residues within the extracellular domain of Neu promote receptor dimerization and activation
    • Siegel, P. M., and W. J. Muller. 1996. Mutations affecting conserved cysteine residues within the extracellular domain of Neu promote receptor dimerization and activation. Proc. Natl. Acad. Sci. USA 93:8878-8883.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8878-8883
    • Siegel, P.M.1    Muller, W.J.2
  • 46
    • 0029881315 scopus 로고    scopus 로고
    • Strong hydrogen bonding interactions involving a buried glutamic acid in the transmembrane sequence of the neu/erbB-2 receptor
    • Smith, S. O., C. S. Smith, and B. J. Bormann. 1996. Strong hydrogen bonding interactions involving a buried glutamic acid in the transmembrane sequence of the neu/erbB-2 receptor. Nat. Struct. Biol. 3:252-258.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 252-258
    • Smith, S.O.1    Smith, C.S.2    Bormann, B.J.3
  • 47
    • 0028307058 scopus 로고
    • Stabilization of an active dimeric form of the epidermal growth factor receptor by introduction of an inter-receptor disulfide bond
    • Sorokin, A., M. A. Lemmon, A. Ullrich, and J. Schlessinger. 1994. Stabilization of an active dimeric form of the epidermal growth factor receptor by introduction of an inter-receptor disulfide bond. J. Biol. Chem. 269:9752-9759.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9752-9759
    • Sorokin, A.1    Lemmon, M.A.2    Ullrich, A.3    Schlessinger, J.4
  • 48
    • 0022588291 scopus 로고
    • P185, a product of the neu proto-oncogene, is a receptorlike protein associated with tyrosine kinase activity
    • Stern, D. F., P. A. Heffernan, and R. A. Weinberg. 1986. p185, a product of the neu proto-oncogene, is a receptorlike protein associated with tyrosine kinase activity. Mol. Cell. Biol. 6:1729-1740.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 1729-1740
    • Stern, D.F.1    Heffernan, P.A.2    Weinberg, R.A.3
  • 49
    • 0343550659 scopus 로고
    • neu: A potential model for receptor interactions
    • neu: a potential model for receptor interactions. EMBO J. 7: 995-1001.
    • (1988) EMBO J. , vol.7 , pp. 995-1001
    • Stern, D.F.1    Kamps, M.P.2
  • 51
    • 0024976405 scopus 로고
    • Neu receptor dimerization
    • Sternberg, M. J. E., and W. J. Gullick. 1989. Neu receptor dimerization. Nature 339:587.
    • (1989) Nature , vol.339 , pp. 587
    • Sternberg, M.J.E.1    Gullick, W.J.2
  • 52
    • 3543042713 scopus 로고
    • Ret transforming gene encodes a fusion protein homologous to tyrosine kinases
    • Takahshi, M., and G. M. Cooper. 1987. ret transforming gene encodes a fusion protein homologous to tyrosine kinases. J. Biol. Chem. 263:3400-3447.
    • (1987) J. Biol. Chem. , vol.263 , pp. 3400-3447
    • Takahshi, M.1    Cooper, G.M.2
  • 54
    • 0028332086 scopus 로고
    • Activation and inhibition of erythropoietin receptor function: Role of receptor dimerization
    • Watowich, S. S., D. J. Hilton, and H. P. Lodish. 1994. Activation and inhibition of erythropoietin receptor function: role of receptor dimerization. Mol. Cell. Biol. 14:3535-3549.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3535-3549
    • Watowich, S.S.1    Hilton, D.J.2    Lodish, H.P.3
  • 55
    • 0024505028 scopus 로고
    • A point mutation in the neu oncogene mimics ligand induction of receptor aggregation
    • Weiner, D. B., J. Liu, J. A. Cohen, W. V. Williams, and M. I. Greene. 1989. A point mutation in the neu oncogene mimics ligand induction of receptor aggregation. Nature 339:230-231.
    • (1989) Nature , vol.339 , pp. 230-231
    • Weiner, D.B.1    Liu, J.2    Cohen, J.A.3    Williams, W.V.4    Greene, M.I.5
  • 56
    • 0030782410 scopus 로고    scopus 로고
    • Crystal structure at 1.7Å resolution of VEGF in complex with domain 2 of the Flt-1 receptor
    • Wiesmann, C., G. Fuh, H. W. Christinger, C. Eigenbrot, J. A. Wells, and A. M. deVos. 1997. Crystal structure at 1.7Å resolution of VEGF in complex with domain 2 of the Flt-1 receptor. Cell 91:695-704.
    • (1997) Cell , vol.91 , pp. 695-704
    • Wiesmann, C.1    Fuh, G.2    Christinger, H.W.3    Eigenbrot, C.4    Wells, J.A.5    Devos, A.M.6
  • 58
    • 0025317659 scopus 로고
    • Agonistic antibodies stimulate the kinase encoded by the neu protooncogene in living cells but the oncogenic mutant is constitutively active
    • Yarden, Y. 1990. Agonistic antibodies stimulate the kinase encoded by the neu protooncogene in living cells but the oncogenic mutant is constitutively active. Proc. Natl. Acad. Sci. USA 87:2569-2573.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2569-2573
    • Yarden, Y.1
  • 59
    • 0023100261 scopus 로고
    • Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor
    • Yarden, Y., and J. Schlessinger. 1987. Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor. Biochemistry 26:1443-1451.
    • (1987) Biochemistry , vol.26 , pp. 1443-1451
    • Yarden, Y.1    Schlessinger, J.2
  • 60
    • 0023156382 scopus 로고
    • Self- Phosphorylation of epidermal growth factor receptor: Evidence for a model of intermolecular allosteric activation
    • Yarden, Y., and J. Schlessinger. 1987. Self- phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activation. Biochemistry 26:1434-1442.
    • (1987) Biochemistry , vol.26 , pp. 1434-1442
    • Yarden, Y.1    Schlessinger, J.2
  • 61
    • 0025996871 scopus 로고
    • Proline in α-helix: Stability and conformation studied by dynamics stimulation
    • Yun, R. H., A. Anderson, and J. Hermans. 1991. Proline in α-helix: stability and conformation studied by dynamics stimulation. Proteins 10:219-228.
    • (1991) Proteins , vol.10 , pp. 219-228
    • Yun, R.H.1    Anderson, A.2    Hermans, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.