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Volumn 2013, Issue 2, 2013, Pages

Her2 activation mechanism reflects evolutionary preservation of asymmetric ectodomain dimers in the human EGFR family

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPIDERMAL GROWTH FACTOR RECEPTOR; ERBB2 PROTEIN, HUMAN;

EID: 84880633751     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.00708     Document Type: Article
Times cited : (67)

References (45)
  • 1
    • 70249141245 scopus 로고    scopus 로고
    • ErbB2 resembles an autoinhibited invertebrate epidermal growth factor receptor
    • doi: 10.1038/nature08297
    • Alvarado D, Klein DE, Lemmon MA. 2009. ErbB2 resembles an autoinhibited invertebrate epidermal growth factor receptor. Nature 461:287-91. doi: 10.1038/nature08297.
    • (2009) Nature , vol.461 , pp. 287-291
    • Alvarado, D.1    Klein, D.E.2    Lemmon, M.A.3
  • 2
    • 77955627615 scopus 로고    scopus 로고
    • Structural basis for negative cooperativity in growth factor binding to an EGF receptor
    • doi: 10.1016/j.cell.2010.07.015
    • Alvarado D, Klein DE, Lemmon MA. 2010. Structural basis for negative cooperativity in growth factor binding to an EGF receptor. Cell 142:568-79. doi: 10.1016/j.cell.2010.07.015.
    • (2010) Cell , vol.142 , pp. 568-579
    • Alvarado, D.1    Klein, D.E.2    Lemmon, M.A.3
  • 3
    • 84873292211 scopus 로고    scopus 로고
    • Architecture and membrane interactions of the EGF receptor
    • doi: 10.1016/j.cell.2012.12.030
    • Arkhipov A, Shan Y, Das R, Endres NF, Eastwood MP, Wemmer DE, et al. 2013. Architecture and membrane interactions of the EGF receptor. Cell 152:557-69. doi: 10.1016/j.cell.2012.12.030.
    • (2013) Cell , vol.152 , pp. 557-569
    • Arkhipov, A.1    Shan, Y.2    Das, R.3    Endres, N.F.4    Eastwood, M.P.5    Wemmer, D.E.6
  • 4
    • 67649472398 scopus 로고    scopus 로고
    • Novel anticancer targets: Revisiting ERBB2 and discovering ERBB3
    • doi: 10.1038/nrc2656
    • Baselga J, Swain SM. 2009. Novel anticancer targets: revisiting ERBB2 and discovering ERBB3. Nat Rev Cancer 9:463-75. doi: 10.1038/nrc2656.
    • (2009) Nat Rev Cancer , vol.9 , pp. 463-475
    • Baselga, J.1    Swain, S.M.2
  • 6
    • 62849095162 scopus 로고    scopus 로고
    • Variants of the antibody herceptin that interact with HER2 and VEGF at the antigen binding site
    • doi: 10.1126/ science.1165480
    • Bostrom J, Yu SF, Kan D, Appleton BA, Lee CV, Billeci K, et al. 2009. Variants of the antibody herceptin that interact with HER2 and VEGF at the antigen binding site. Science 323:1610-4. doi: 10.1126/ science.1165480.
    • (2009) Science , vol.323 , pp. 1610-1614
    • Bostrom, J.1    Yu, S.F.2    Kan, D.3    Appleton, B.A.4    Lee, C.V.5    Billeci, K.6
  • 7
    • 0037162799 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER3 reveals an interdomain tether
    • doi: 10.1126/science.1074611
    • Cho H-S, Leahy DJ. 2002. Structure of the extracellular region of HER3 reveals an interdomain tether. Science 297:1330-3. doi: 10.1126/science.1074611.
    • (2002) Science , vol.297 , pp. 1330-1333
    • Cho, H.-S.1    Leahy, D.J.2
  • 8
    • 0037434791 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab
    • doi: 10.1038/nature01392
    • Cho H-S, Mason K, Ramyar KX, Stanley AM, Gabelli SB, Denney DW, et al. 2003. Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab. Nature 421:756-60. doi: 10.1038/nature01392.
    • (2003) Nature , vol.421 , pp. 756-760
    • Cho, H.-S.1    Mason, K.2    Ramyar, K.X.3    Stanley, A.M.4    Gabelli, S.B.5    Denney, D.W.6
  • 9
    • 77950460037 scopus 로고    scopus 로고
    • Spatial control of EGF receptor activation by reversible dimerization on living cells
    • doi: 10.1038/nature08827
    • Chung I, Akita R, Vandlen R, Toomre D, Schlessinger J, Mellman I. 2010. Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 464:783-7. doi: 10.1038/nature08827.
    • (2010) Nature , vol.464 , pp. 783-787
    • Chung, I.1    Akita, R.2    Vandlen, R.3    Toomre, D.4    Schlessinger, J.5    Mellman, I.6
  • 10
    • 0037429779 scopus 로고    scopus 로고
    • The deaf and the dumb: The biology of ErbB-2 and ErbB-3
    • doi: 10.1016/S0014-4827(02)00101-5
    • Citri A, Skaria KB, Yarden Y. 2003. The deaf and the dumb: the biology of ErbB-2 and ErbB-3. Exp Cell Res 284:54-65. doi: 10.1016/S0014-4827(02)00101-5.
    • (2003) Exp Cell Res , vol.284 , pp. 54-65
    • Citri, A.1    Skaria, K.B.2    Yarden, Y.3
  • 11
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: Towards the systems level
    • doi: 10.1038/nrm1962
    • Citri A, Yarden Y. 2006. EGF-ERBB signalling: towards the systems level. Nat Rev Mol Cell Biol 7:505-16. doi: 10.1038/nrm1962.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 12
    • 23844471971 scopus 로고    scopus 로고
    • Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface
    • doi: 10.1128/MCB.25.17.7734-7742.2005
    • Dawson JP, Berger MB, Lin CC, Schlessinger J, Lemmon MA, Ferguson KM. 2005. Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface. Mol Cell Biol 25:7734-42. doi: 10.1128/MCB.25.17.7734-7742.2005.
    • (2005) Mol Cell Biol , vol.25 , pp. 7734-7742
    • Dawson, J.P.1    Berger, M.B.2    Lin, C.C.3    Schlessinger, J.4    Lemmon, M.A.5    Ferguson, K.M.6
  • 13
    • 84873280409 scopus 로고    scopus 로고
    • Conformational coupling across the plasma membrane in activation of the EGF receptor
    • doi: 10.1016/j.cell.2012.12.032
    • Endres NF, Das R, Smith A, Arkhipov A, Kovacs E, Huang Y, et al. 2013. Conformational coupling across the plasma membrane in activation of the EGF receptor. Cell 152:543-56. doi: 10.1016/j.cell.2012.12.032.
    • (2013) Cell , vol.152 , pp. 543-556
    • Endres, N.F.1    Das, R.2    Smith, A.3    Arkhipov, A.4    Kovacs, E.5    Huang, Y.6
  • 14
    • 84860390423 scopus 로고    scopus 로고
    • Regulation of the catalytic activity of the EGF receptor
    • doi: 10.1016/j.sbi.2011.07.007
    • Endres NF, Engel K, Das R, Kovacs E, Kuriyan J. 2011. Regulation of the catalytic activity of the EGF receptor. Curr Opin Struct Biol 27:777-84. doi: 10.1016/j.sbi.2011.07.007.
    • (2011) Curr Opin Struct Biol , vol.27 , pp. 777-784
    • Endres, N.F.1    Engel, K.2    Das, R.3    Kovacs, E.4    Kuriyan, J.5
  • 15
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization
    • doi: 10.1016/S1097-2765(03)00047-9
    • Ferguson KM, Berger MB, Mendrola JM, Cho HS, Leahy DJ, Lemmon MA. 2003. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol Cell 11:507-17. doi: 10.1016/ S1097-2765(03)00047-9.
    • (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
  • 16
    • 0034282556 scopus 로고    scopus 로고
    • Extracellular domains drive homo- but not hetero-dimerization of erbB receptors
    • doi: 10.1093/emboj/19.17.4632
    • Ferguson KM, Darling PJ, Mohan MJ, Macatee TL, Lemmon MA. 2000. Extracellular domains drive homo- but not hetero-dimerization of erbB receptors. EMBO J 19:4632-43. doi: 10.1093/emboj/19.17.4632.
    • (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
  • 17
    • 1842605531 scopus 로고    scopus 로고
    • Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex
    • doi: 10.1016/S1535- 6108(04)00083-2
    • Franklin MC, Carey KD, Vajdos FF, Leahy DJ, de Vos AM, Sliwkowski MX. 2004. Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex. Cancer Cell 5:317-28. doi: 10.1016/S1535- 6108(04)00083-2.
    • (2004) Cancer Cell , vol.5 , pp. 317-328
    • Franklin, M.C.1    Carey, K.D.2    Vajdos, F.F.3    Leahy, D.J.4    de Vos, A.M.5    Sliwkowski, M.X.6
  • 18
    • 18644370411 scopus 로고    scopus 로고
    • Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor α
    • doi: 10.1016/S0092-8674(02)00940-6
    • Garrett TP, McKern NM, Lou M, Elleman TC, Adams TE, Lovrecz GO, et al. 2002. Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor α. Cell 110:763-73. doi: 10.1016/S0092-8674(02)00940-6.
    • (2002) Cell , vol.110 , pp. 763-773
    • Garrett, T.P.1    McKern, N.M.2    Lou, M.3    Elleman, T.C.4    Adams, T.E.5    Lovrecz, G.O.6
  • 19
    • 0037291226 scopus 로고    scopus 로고
    • The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors
    • doi: 10.1016/S0092-8674(02)00940-6
    • Garrett TPJ, McKern NM, Lou MZ, Elleman TC, Adams TE, Lovrecz GO, et al. 2003. The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors. Mol Cell 11:495-05. doi: 10.1016/S0092-8674(02)00940-6.
    • (2003) Mol Cell , vol.11 , pp. 495-505
    • Garrett, T.P.J.1    McKern, N.M.2    Lou, M.Z.3    Elleman, T.C.4    Adams, T.E.5    Lovrecz, G.O.6
  • 20
    • 0030944455 scopus 로고    scopus 로고
    • ErbB-2, the preferred heterodimerization partner of all erbb receptors, is a mediator of lateral signaling
    • doi: 10.1093/emboj/16.7.1647
    • Graus-Porta D, Beerli RR, Daly JM, Hynes NE. 1997. ErbB-2, the preferred heterodimerization partner of all erbb receptors, is a mediator of lateral signaling. EMBO J 16:1647-55. doi: 10.1093/emboj/16.7.1647.
    • (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
    • 0028802638 scopus 로고
    • Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3
    • doi: 10.1074/jbc.270.41.24604
    • Horan T, Wen J, Arakawa T, Liu N, Brankow D, Hu S, et al. 1995. Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3. J Biol Chem 270:24604-8. doi: 10.1074/jbc.270.41.24604.
    • (1995) J Biol Chem , vol.270 , pp. 24604-24608
    • Horan, T.1    Wen, J.2    Arakawa, T.3    Liu, N.4    Brankow, D.5    Hu, S.6
  • 22
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • doi: 10.1016/ 0263-7855(96)00018-5
    • Humphrey W, Dalke A, Schulten K. 1996. VMD: visual molecular dynamics. J Mol Graph 14:33-8. doi: 10.1016/ 0263-7855(96)00018-5.
    • (1996) J Mol Graph , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 23
    • 18344390418 scopus 로고    scopus 로고
    • Erbb receptors and cancer: The complexity of targeted inhibitors
    • doi: 10.1038/nrc1667
    • Hynes NE, Lane HA. 2005. Erbb receptors and cancer: the complexity of targeted inhibitors. Nat Rev Cancer 5:341-54. doi: 10.1038/nrc1667.
    • (2005) Nat Rev Cancer , vol.5 , pp. 341-354
    • Hynes, N.E.1    Lane, H.A.2
  • 25
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • doi: 10.1021/bi952626l
    • Jorgensen WL, Chandrasekhar J, Madura JD, Impey RW, Klein ML. 1983. Comparison of simple potential functions for simulating liquid water. J Chem Phys 79:926-35. doi: 10.1021/bi952626l.
    • (1983) J Chem Phys , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3    Impey, R.W.4    Klein, M.L.5
  • 26
    • 0035871686 scopus 로고    scopus 로고
    • A fast SHAKE algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations
    • doi: 10.1002/ 1096-987X(20010415)22:5<501::AID-JCC1021>3.0.CO;2-V
    • Kräutler V, van Gunsteren WF, Hünenberger PH. 2001. A fast SHAKE algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations. J Comput Chem 22:501-8. doi: 10.1002/ 1096-987X(20010415)22:5<501::AID-JCC1021>3.0.CO;2-V.
    • (2001) J Comput Chem , vol.22 , pp. 501-508
    • Kräutler, V.1    van Gunsteren, W.F.2    Hünenberger, P.H.3
  • 27
    • 62649159075 scopus 로고    scopus 로고
    • Ligand-induced ErbB receptor dimerization
    • doi: 10.1016/j. yexcr.2008.10.024
    • Lemmon MA. 2009. Ligand-induced ErbB receptor dimerization. Exp Cell Res 315:638-48. doi: 10.1016/j. yexcr.2008.10.024.
    • (2009) Exp Cell Res , vol.315 , pp. 638-648
    • Lemmon, M.A.1
  • 28
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • doi: 10.1016/j. cell.2010.06.011
    • Lemmon MA, Schlessinger J. 2010. Cell signaling by receptor tyrosine kinases. Cell 141:1117-34. doi: 10.1016/j. cell.2010.06.011.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 29
    • 17444403242 scopus 로고    scopus 로고
    • Structural basis for inhibition of the epidermal growth factor receptor by cetuximab
    • doi: 10.1016/j.ccr.2005.03.003
    • Li S, Schmitz KR, Jeffrey PD, Wiltzius JJW, Kussie P, Ferguson KM. 2005. Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. Cancer Cell 7:301-11. doi: 10.1016/j.ccr.2005.03.003.
    • (2005) Cancer Cell , vol.7 , pp. 301-311
    • Li, S.1    Schmitz, K.R.2    Jeffrey, P.D.3    Wiltzius, J.J.W.4    Kussie, P.5    Ferguson, K.M.6
  • 31
    • 78649548465 scopus 로고    scopus 로고
    • Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor
    • doi: 10.1128/MCB.00742-10
    • Lu CF, Mi LZ, Grey MJ, Zhu JQ, Graef E, Yokoyama S, et al. 2010. Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor. Mol Cell Biol 30:5432-43. doi: 10.1128/MCB.00742-10.
    • (2010) Mol Cell Biol , vol.30 , pp. 5432-5443
    • Lu, C.F.1    Mi, L.Z.2    Grey, M.J.3    Zhu, J.Q.4    Graef, E.5    Yokoyama, S.6
  • 32
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • doi: 10.1021/jp973084f
    • MacKerell AD, Bashford D, Bellott M, Dunbrack RL, Evanseck JD, Field MJ, et al. 1998. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem B 102:3586-616. doi: 10.1021/jp973084f.
    • (1998) J Phys Chem B , vol.102 , pp. 3586-3616
    • Mackerell, A.D.1    Bashford, D.2    Bellott, M.3    Dunbrack, R.L.4    Evanseck, J.D.5    Field, M.J.6
  • 33
    • 78049239930 scopus 로고    scopus 로고
    • Distribution of resting and ligand-bound ErbB1 and ErbB2 receptor tyrosine kinases in living cells using number and brightness analysis
    • doi: 10.1073/pnas.1002642107
    • Nagy P, Claus J, Jovin TM, Arndt-Jovin DJ. 2010. Distribution of resting and ligand-bound ErbB1 and ErbB2 receptor tyrosine kinases in living cells using number and brightness analysis. Proc Natl Acad Sci USA 107:16524-9. doi: 10.1073/pnas.1002642107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 16524-16529
    • Nagy, P.1    Claus, J.2    Jovin, T.M.3    Arndt-Jovin, D.J.4
  • 34
    • 18644386251 scopus 로고    scopus 로고
    • Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains
    • doi: 10.1016/ S0092-8674(02)00963-7
    • Ogiso H, Ishitani R, Nureki O, Fukai S, Yamanaka M, Kim JH, et al. 2002. Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. Cell 110:775-87. doi: 10.1016/ S0092-8674(02)00963-7.
    • (2002) Cell , vol.110 , pp. 775-787
    • Ogiso, H.1    Ishitani, R.2    Nureki, O.3    Fukai, S.4    Yamanaka, M.5    Kim, J.H.6
  • 35
    • 79959720287 scopus 로고    scopus 로고
    • How robust are protein folding simulations with respect to force field parameterization?
    • doi: 10.1016/j.bpj.2011.03.051
    • Piana S, Lindorf-Larsen K, Shaw DE. 2011. How robust are protein folding simulations with respect to force field parameterization? Biophys J 100:L47-9. doi: 10.1016/j.bpj.2011.03.051.
    • (2011) Biophys J , vol.100
    • Piana, S.1    Lindorf-Larsen, K.2    Shaw, D.E.3
  • 36
    • 34250216633 scopus 로고    scopus 로고
    • Mutational activation of ErbB family receptor tyrosine kinases: Insights into mechanisms of signal transduction and tumorigenesis
    • doi: 10.1002/bies.20582
    • Riese DJ II, Gallo RM, Settleman J. 2007. Mutational activation of ErbB family receptor tyrosine kinases: insights into mechanisms of signal transduction and tumorigenesis. Bioessays 29:558-65. doi: 10.1002/bies.20582.
    • (2007) Bioessays , vol.29 , pp. 558-565
    • Riese, D.J.I.I.1    Gallo, R.M.2    Settleman, J.3
  • 37
    • 0020659319 scopus 로고
    • Biological role of epidermal growth factor-receptor clustering. Investigation with monoclonal anti-receptor antibodies
    • Schreiber AB, Libermann TA, Lax I, Yarden Y, Schlessinger J. 1983. Biological role of epidermal growth factor-receptor clustering. Investigation with monoclonal anti-receptor antibodies. J Biol Chem 258:846-53.
    • (1983) J Biol Chem , vol.258 , pp. 846-853
    • Schreiber, A.B.1    Libermann, T.A.2    Lax, I.3    Yarden, Y.4    Schlessinger, J.5
  • 38
    • 22944460220 scopus 로고    scopus 로고
    • Gaussian split Ewald: A fast Ewald mesh method for molecular simulation
    • doi: 10.1063/1.1839571
    • Shan Y, Klepeis JL, Eastwood MP, Dror RO, Shaw DE. 2005. Gaussian split Ewald: a fast Ewald mesh method for molecular simulation. J Chem Phys 122:54101-13. doi: 10.1063/1.1839571.
    • (2005) J Chem Phys , vol.122 , pp. 54101-54213
    • Shan, Y.1    Klepeis, J.L.2    Eastwood, M.P.3    Dror, R.O.4    Shaw, D.E.5
  • 40
    • 0033947243 scopus 로고    scopus 로고
    • Evolutionary analysis of the ErbB receptor and ligand families
    • doi: 10.1007/s002390010043
    • Stein RA, Staros JV. 2000. Evolutionary analysis of the ErbB receptor and ligand families. J Mol Evol 50:397-412. doi: 10.1007/s002390010043.
    • (2000) J Mol Evol , vol.50 , pp. 397-412
    • Stein, R.A.1    Staros, J.V.2
  • 41
    • 33646650705 scopus 로고
    • Reversible multiple time scale molecular dynamics
    • doi: 10.1063/1.463137
    • Tuckerman M, Berne BJ, Martyna GJ. 1992. Reversible multiple time scale molecular dynamics. J Chem Phys 97:1990-2001. doi: 10.1063/1.463137.
    • (1992) J Chem Phys , vol.97 , pp. 1990-2001
    • Tuckerman, M.1    Berne, B.J.2    Martyna, G.J.3
  • 42
    • 79958071305 scopus 로고    scopus 로고
    • Human epidermal growth factor receptor (EGFR) aligned on the plasma membrane adopts key features of Drosophila EGFR asymmetry
    • doi: 10.1128/MCB.01431-10
    • Tynan CJ, Roberts SK, Rolfe DJ, Clarke DT, Loeffler HH, Kastner J, et al. 2011. Human epidermal growth factor receptor (EGFR) aligned on the plasma membrane adopts key features of Drosophila EGFR asymmetry. Mol Cell Biol 31:2241-52. doi: 10.1128/MCB.01431-10.
    • (2011) Mol Cell Biol , vol.31 , pp. 2241-2252
    • Tynan, C.J.1    Roberts, S.K.2    Rolfe, D.J.3    Clarke, D.T.4    Loeffler, H.H.5    Kastner, J.6
  • 43
    • 0019332971 scopus 로고
    • Identification of phosphotyrosine as a product of epidermal growth factor-activated protein kinase in A-431 cell membranes
    • Ushiro H, Cohen S. 1980. Identification of phosphotyrosine as a product of epidermal growth factor-activated protein kinase in A-431 cell membranes. J Biol Chem 255:8363-5.
    • (1980) J Biol Chem , vol.255 , pp. 8363-8365
    • Ushiro, H.1    Cohen, S.2
  • 44
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • doi: 10.1016/j.cell.2006.05.013
    • Zhang X, Gureasko J, Shen K, Cole PA, Kuriyan J. 2006. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125:1137-49. doi: 10.1016/j.cell.2006.05.013.
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 45
    • 79952937376 scopus 로고    scopus 로고
    • Polymorphism of the epidermal growth factor receptor extracellular ligand binding domain: The dimer interface depends on domain stabilization
    • doi: 10.1021/bi101843s
    • Zhang Z, Wriggers W. 2011. Polymorphism of the epidermal growth factor receptor extracellular ligand binding domain: the dimer interface depends on domain stabilization. Biochemistry 50:2144-56. doi: 10.1021/bi101843s.
    • (2011) Biochemistry , vol.50 , pp. 2144-2156
    • Zhang, Z.1    Wriggers, W.2


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