메뉴 건너뛰기




Volumn 40, Issue 11, 2012, Pages 2295-2306

Structural systems biology and multiscale signaling models

Author keywords

Molecular resolution; Multiscale modeling; Signaling networks; Structural biology; Systems biology

Indexed keywords

MOLECULAR RESOLUTION; MULTI-SCALE MODELING; SIGNALING NETWORKS; STRUCTURAL BIOLOGY; SYSTEMS BIOLOGY;

EID: 84868374977     PISSN: 00906964     EISSN: 15739686     Source Type: Journal    
DOI: 10.1007/s10439-012-0576-6     Document Type: Article
Times cited : (8)

References (62)
  • 1
    • 78049436709 scopus 로고    scopus 로고
    • Minimal mesoscale model for protein-mediated vesiculation in clathrin-dependent endocytosis
    • Agrawal, N. J., J. Nukpezah, and R. Radhakrishnan. Minimal mesoscale model for protein-mediated vesiculation in clathrin-dependent endocytosis. PLoS Comput. Biol. 6(9):e1000926, 2010.
    • (2010) PLoS Comput. Biol. , vol.6 , Issue.9
    • Agrawal, N.J.1    Nukpezah, J.2    Radhakrishnan, R.3
  • 2
    • 36749088906 scopus 로고    scopus 로고
    • Determining the architectures of macromolecular assemblies
    • Alber, F., et al. Determining the architectures of macromolecular assemblies. Nature 450(7170):683-701, 2007.
    • (2007) Nature , vol.450 , Issue.7170 , pp. 683-701
    • Alber, F.1
  • 3
    • 33644550021 scopus 로고    scopus 로고
    • Structural systems biology: Modelling protein interactions
    • Aloy, P., and R. B. Russell. Structural systems biology: modelling protein interactions. Nat. Rev. Mol. Cell Biol. 7(3):188-197, 2006.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , Issue.3 , pp. 188-197
    • Aloy, P.1    Russell, R.B.2
  • 4
    • 77950595062 scopus 로고    scopus 로고
    • Multiscale simulation of protein mediated membrane remodeling
    • Ayton, G. S., and G. A. Voth. Multiscale simulation of protein mediated membrane remodeling. Semin. Cell Dev. Biol. 21(4):357-362, 2010.
    • (2010) Semin. Cell Dev. Biol. , vol.21 , Issue.4 , pp. 357-362
    • Ayton, G.S.1    Voth, G.A.2
  • 5
    • 78349258978 scopus 로고    scopus 로고
    • Multiscale computer simulation of the immature HIV-1 virion
    • Ayton, G. S., and G. A. Voth. Multiscale computer simulation of the immature HIV-1 virion. Biophys. J. 99(9):2757-2765, 2010.
    • (2010) Biophys. J. , vol.99 , Issue.9 , pp. 2757-2765
    • Ayton, G.S.1    Voth, G.A.2
  • 7
    • 0033555859 scopus 로고    scopus 로고
    • Emergent properties of biological networks
    • Bhalla, U. S., and R. Iyengar. Emergent properties of biological networks. Science 283:381-387, 1999.
    • (1999) Science , vol.283 , pp. 381-387
    • Bhalla, U.S.1    Iyengar, R.2
  • 8
    • 36248988538 scopus 로고    scopus 로고
    • Ligand-dependent responses of the ErbB signaling network: Experimental and modeling analyses
    • Birtwistle, M. R., et al. Ligand-dependent responses of the ErbB signaling network: experimental and modeling analyses. Mol. Syst. Biol. 3:144, 2007.
    • (2007) Mol. Syst. Biol. , vol.3 , pp. 144
    • Birtwistle, M.R.1
  • 9
    • 33747886526 scopus 로고    scopus 로고
    • Emerging roles of pseudokinases
    • Boudeau, J., et al. Emerging roles of pseudokinases. Trends Cell Biol. 16(9):443-452, 2006.
    • (2006) Trends Cell Biol , vol.16 , Issue.9 , pp. 443-452
    • Boudeau, J.1
  • 10
    • 1842431537 scopus 로고    scopus 로고
    • Comparative study of several algorithms for flexible ligand docking
    • Bursulaya, B. D., et al. Comparative study of several algorithms for flexible ligand docking. J. Comput. Aided Mol. Des. 17(11):755-763, 2003.
    • (2003) J. Comput. Aided Mol. Des. , vol.17 , Issue.11 , pp. 755-763
    • Bursulaya, B.D.1
  • 11
    • 0034663658 scopus 로고    scopus 로고
    • Scoring dockied conformations generated by rigid body protein-protein docking
    • Camacho, J. C., et al. Scoring dockied conformations generated by rigid body protein-protein docking. Proteins 40:525-537, 2000.
    • (2000) Proteins , vol.40 , pp. 525-537
    • Camacho, J.C.1
  • 12
    • 79960302607 scopus 로고    scopus 로고
    • Simulated self-assembly of the HIV-1 capsid: Protein shape and native contacts are sufficient for two-dimensional lattice formation
    • Chen, B., and R. Tycko. Simulated self-assembly of the HIV-1 capsid: protein shape and native contacts are sufficient for two-dimensional lattice formation. Biophys. J. 100(12):3035-3044, 2011.
    • (2011) Biophys. J. , vol.100 , Issue.12 , pp. 3035-3044
    • Chen, B.1    Tycko, R.2
  • 13
    • 77951454595 scopus 로고    scopus 로고
    • A multiscale model for virus capsid dynamics
    • Chen, C., R. Saxena, and G. W. Wei. A multiscale model for virus capsid dynamics. Int. J. Biomed. Imaging 2010: 308627, 2010.
    • (2010) Int. J. Biomed. Imaging , vol.2010 , pp. 308627
    • Chen, C.1    Saxena, R.2    Wei, G.W.3
  • 14
    • 33244483907 scopus 로고    scopus 로고
    • Evaluating molecular-docking methods for pose prediction and enrichment factors
    • Chen, H. M., et al. Evaluating molecular-docking methods for pose prediction and enrichment factors. J. Chem. Inf. Model. 46(1):401-415, 2006.
    • (2006) J. Chem. Inf. Model. , vol.46 , Issue.1 , pp. 401-415
    • Chen, H.M.1
  • 15
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: Towards the systems level
    • Citri, A., and Y. Yarden. EGF-ERBB signalling: towards the systems level. Nat. Rev. Mol. Cell Biol. 7(7):505-516, 2006.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , Issue.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 16
    • 34249075147 scopus 로고    scopus 로고
    • MET amplification leads to gefitinib resistance in lung cancer by activating ERBB3 signaling
    • Engelman, J. A., et al. MET amplification leads to gefitinib resistance in lung cancer by activating ERBB3 signaling. Science 316(5827):1039-1043, 2007.
    • (2007) Science , vol.316 , Issue.5827 , pp. 1039-1043
    • Engelman, J.A.1
  • 17
    • 84859962733 scopus 로고    scopus 로고
    • Structure-function mapping of a heptameric module in the nuclear pore complex
    • Fernandez-Martinez, J., et al. Structure-function mapping of a heptameric module in the nuclear pore complex. J. Cell Biol. 196:419-434, 2012.
    • (2012) J. Cell Biol. , vol.196 , pp. 419-434
    • Fernandez-Martinez, J.1
  • 18
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: Generation and refinement of homology-based protein structure models
    • Fiser, A., and A. Sali. Modeller: generation and refinement of homology-based protein structure models. Methods Enzymol. 374:461-491, 2003.
    • (2003) Methods Enzymol. , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 19
    • 51649116700 scopus 로고    scopus 로고
    • Intrinsic bending and structural rearrangement of tubulin dimer: Molecular dynamics simulations and coarse-grained analysis
    • Gebremichael, Y., J. W. Chu, and G. A. Voth. Intrinsic bending and structural rearrangement of tubulin dimer: molecular dynamics simulations and coarse-grained analysis. Biophys. J. 95(5):2487-2499, 2008.
    • (2008) Biophys. J. , vol.95 , Issue.5 , pp. 2487-2499
    • Gebremichael, Y.1    Chu, J.W.2    Voth, G.A.3
  • 20
    • 77949366471 scopus 로고    scopus 로고
    • Coarse-grained protein - Protein stiffnesses and dynamics from all-atom simulations
    • Hicks, S. D., and C. L. Henley. Coarse-grained protein - protein stiffnesses and dynamics from all-atom simulations. Phys. Rev. E 81(31):030903, 2010.
    • (2010) Phys. Rev. e , vol.81 , Issue.31 , pp. 030903
    • Hicks, S.D.1    Henley, C.L.2
  • 21
    • 77951876275 scopus 로고    scopus 로고
    • Spatio-temporal modeling of signaling protein recruitment to EGFR
    • Hsieh, M. Y., et al. Spatio-temporal modeling of signaling protein recruitment to EGFR. BMC Syst. Biol. 4:57, 2010.
    • (2010) BMC Syst. Biol. , vol.4 , pp. 57
    • Hsieh, M.Y.1
  • 22
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse, M., and J. Kuriyan. The conformational plasticity of protein kinases. Cell 109:275-282, 2002.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 23
  • 24
    • 18744371588 scopus 로고    scopus 로고
    • Molecular dynamics and protein function
    • Karplus, M., and J. Kuriyan. Molecular dynamics and protein function. Proc. Natl. Acad. Sci. USA 102(19): 6679-6685, 2005.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.19 , pp. 6679-6685
    • Karplus, M.1    Kuriyan, J.2
  • 25
    • 33644524741 scopus 로고    scopus 로고
    • Cell-signalling dynamics in time and space
    • Kholodenko, B. N. Cell-signalling dynamics in time and space. Nat. Rev. Mol. Cell Biol. 7(3):165-176, 2006.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , Issue.3 , pp. 165-176
    • Kholodenko, B.N.1
  • 26
    • 0034572830 scopus 로고    scopus 로고
    • Three ways to make a vesicle
    • Kirchhausen, T. Three ways to make a vesicle. Nat. Rev. Mol. Cell Biol. 1(3):187-198, 2000.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , Issue.3 , pp. 187-198
    • Kirchhausen, T.1
  • 27
    • 0037449766 scopus 로고    scopus 로고
    • STAT5b, a mediator of synergism between c-Src and the epidermal growth factor receptor
    • Kloth, M. T., et al. STAT5b, a mediator of synergism between c-Src and the epidermal growth factor receptor. J. Biol. Chem. 278:1671-1679, 2003.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1671-1679
    • Kloth, M.T.1
  • 28
    • 34249650622 scopus 로고    scopus 로고
    • A multiscale computational approach to dissect early events in the Erb family receptor mediated activation, differential signaling, and relevance to oncogenic transformations
    • Liu, Y., et al. A multiscale computational approach to dissect early events in the Erb family receptor mediated activation, differential signaling, and relevance to oncogenic transformations. Ann. Biomed. Eng. 35(6):1012-1025, 2007.
    • (2007) Ann. Biomed. Eng. , vol.35 , Issue.6 , pp. 1012-1025
    • Liu, Y.1
  • 29
    • 2342471392 scopus 로고    scopus 로고
    • Activating mutations in the epidermal growth factor receptor underlying responsiveness of nonsmall-cell lung cancer to gefitinib
    • Lynch, T. J., et al. Activating mutations in the epidermal growth factor receptor underlying responsiveness of nonsmall-cell lung cancer to gefitinib. N. Engl. J. Med. 350(21): 2129-2139, 2004.
    • (2004) N. Engl. J. Med. , vol.350 , Issue.21 , pp. 2129-2139
    • Lynch, T.J.1
  • 30
    • 0030598848 scopus 로고    scopus 로고
    • Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
    • Mohammadi, M., J. Schlessinger, and S. R. Hubbard. Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell 86(4): 577-587, 1996.
    • (1996) Cell , vol.86 , Issue.4 , pp. 577-587
    • Mohammadi, M.1    Schlessinger, J.2    Hubbard, S.R.3
  • 31
    • 0030945871 scopus 로고    scopus 로고
    • Structures of tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors
    • Mohammadi, M., et al. Structures of tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors. Science 276:955-960, 1997.
    • (1997) Science , vol.276 , pp. 955-960
    • Mohammadi, M.1
  • 32
    • 0032531929 scopus 로고    scopus 로고
    • Crystal structure of an angiogenesis inhibitor bound to the FGF receptor tyrosine kinase domain
    • Mohammadi, M., et al. Crystal structure of an angiogenesis inhibitor bound to the FGF receptor tyrosine kinase domain. EMBO J. 17:5896-5904, 1998.
    • (1998) EMBO J , vol.17 , pp. 5896-5904
    • Mohammadi, M.1
  • 33
    • 54549102284 scopus 로고    scopus 로고
    • Derailed endocytosis: An emerging feature of cancer
    • Mosesson, Y., G. B. Mills, and Y. Yarden. Derailed endocytosis: an emerging feature of cancer. Nat. Rev. Cancer 8(11):835-850, 2008.
    • (2008) Nat. Rev. Cancer , vol.8 , Issue.11 , pp. 835-850
    • Mosesson, Y.1    Mills, G.B.2    Yarden, Y.3
  • 34
    • 33947287270 scopus 로고    scopus 로고
    • Epidermal growth factor receptor mutants from human lung cancers exhibit enhanced catalytic activity and increased sensitivity to gefitinib
    • Mulloy, R., et al. Epidermal growth factor receptor mutants from human lung cancers exhibit enhanced catalytic activity and increased sensitivity to gefitinib. Cancer Res. 67(5):2325-2330, 2007.
    • (2007) Cancer Res , vol.67 , Issue.5 , pp. 2325-2330
    • Mulloy, R.1
  • 35
    • 0037076002 scopus 로고    scopus 로고
    • Molecular ticket to enter cells
    • Oved, S., and Y. Yarden. Molecular ticket to enter cells. Nature 416:133-136, 2002.
    • (2002) Nature , vol.416 , pp. 133-136
    • Oved, S.1    Yarden, Y.2
  • 36
    • 2342624080 scopus 로고    scopus 로고
    • EGFR mutations in lung, cancer: Correlation with clinical response to gefitinib therapy
    • Paez, J. G., et al. EGFR mutations in lung, cancer: correlation with clinical response to gefitinib therapy. Science 304(5676):1497-1500, 2004.
    • (2004) Science , vol.304 , Issue.5676 , pp. 1497-1500
    • Paez, J.G.1
  • 37
    • 73349084983 scopus 로고    scopus 로고
    • Combining an elastic network with a coarse-grained molecular force field: Structure, dynamics, and intermolecular recognition
    • Periole, X., et al. Combining an elastic network with a coarse-grained molecular force field: structure, dynamics, and intermolecular recognition. J. Chem. Theory Comput. 5(9):2531-2543, 2009.
    • (2009) J. Chem. Theory Comput. , vol.5 , Issue.9 , pp. 2531-2543
    • Periole, X.1
  • 38
    • 45349107336 scopus 로고    scopus 로고
    • Role of network branching in eliciting differential short-term signaling responses in the hyper-sensitive epidermal growth factor receptor mutants implicated in lung cancer
    • Purvis, J., V. Ilango, and R. Radhakrishnan. Role of network branching in eliciting differential short-term signaling responses in the hyper-sensitive epidermal growth factor receptor mutants implicated in lung cancer. Biotechnol. Prog. 24(3):540-553, 2008.
    • (2008) Biotechnol. Prog. , vol.24 , Issue.3 , pp. 540-553
    • Purvis, J.1    Ilango, V.2    Radhakrishnan, R.3
  • 39
    • 79953703252 scopus 로고    scopus 로고
    • Efficacy of tyrosine kinase inhibitors in the mutants of the epidermal growth factor receptor: A multiscale molecularsystems model for phosphorylation and inhibition
    • Stuttgart: IRB Verlag
    • Purvis, J., et al. Efficacy of tyrosine kinase inhibitors in the mutants of the epidermal growth factor receptor: a multiscale molecular/systems model for phosphorylation and inhibition. In: Proceedings of the Foundations in Systems Biology II. Stuttgart: IRB Verlag, 2007, pp. 289-294.
    • (2007) Proceedings of the Foundations in Systems Biology II , pp. 289-294
    • Purvis, J.1
  • 40
    • 79961142425 scopus 로고    scopus 로고
    • Systems biology and physical biology of clathrin-mediated endocytosis
    • Ramanan, V., et al. Systems biology and physical biology of clathrin-mediated endocytosis. Integr. Biol. 3(8):803-815, 2011.
    • (2011) Integr. Biol. , vol.3 , Issue.8 , pp. 803-815
    • Ramanan, V.1
  • 41
    • 84861770615 scopus 로고    scopus 로고
    • Coarse-graining of multiprotein assemblies
    • Saunders, M. G., and G. A. Voth. Coarse-graining of multiprotein assemblies. Curr. Opin. Struct. Biol. 22:144-150, 2012.
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 144-150
    • Saunders, M.G.1    Voth, G.A.2
  • 42
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell 103:211-225, 2000.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 43
    • 33746905531 scopus 로고    scopus 로고
    • Phosphotyrosine interactome of the ErbB-receptor kinase family
    • Schulze, W. X., L. Deng, and M. Mann. Phosphotyrosine interactome of the ErbB-receptor kinase family. Mol. Syst. Biol. 1:E1-E13, 2005.
    • (2005) Mol. Syst. Biol. , vol.1
    • Schulze, W.X.1    Deng, L.2    Mann, M.3
  • 44
    • 77952338791 scopus 로고    scopus 로고
    • ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation
    • Shi, F., et al. ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation. Proc. Natl. Acad. Sci. USA 107:7692-7697, 2010.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 7692-7697
    • Shi, F.1
  • 45
    • 56349159166 scopus 로고    scopus 로고
    • Molecular systems biology of ErbB1 signaling: Bridging the gap through multiscale modeling and high-performance computing
    • Shih, A. J., J. Purvis, and R. Radhakrishnan. Molecular systems biology of ErbB1 signaling: bridging the gap through multiscale modeling and high-performance computing. Mol. BioSyst. 4(12):1151-1159, 2008.
    • (2008) Mol. BioSyst. , vol.4 , Issue.12 , pp. 1151-1159
    • Shih, A.J.1    Purvis, J.2    Radhakrishnan, R.3
  • 46
    • 79953684580 scopus 로고    scopus 로고
    • Analysis of somatic mutations in cancer: Molecular mechanisms of activation in the ErbB family of receptor tyrosine kinases
    • Shih, A. J., S. E. Telesco, and R. Radhakrishnan. Analysis of somatic mutations in cancer: molecular mechanisms of activation in the ErbB family of receptor tyrosine kinases. Cancers 3(1):1195-1231, 2011.
    • (2011) Cancers , vol.3 , Issue.1 , pp. 1195-1231
    • Shih, A.J.1    Telesco, S.E.2    Radhakrishnan, R.3
  • 47
    • 79953686030 scopus 로고    scopus 로고
    • The role for molecular modeling in multiscale cancer models
    • edited by T. S. Deisboeck, and G. Stamatakos. Boca Raton: Chapman & Hall/CRC
    • Shih, A., et al. The role for molecular modeling in multiscale cancer models. In: Multiscale Cancer Modeling of Cancer. Mathematical and Computational Biology Series, edited by T. S. Deisboeck, and G. Stamatakos. Boca Raton: Chapman & Hall/CRC, 2010, pp. 31-43.
    • (2010) Multiscale Cancer Modeling of Cancer. Mathematical and Computational Biology Series , pp. 31-43
    • Shih, A.1
  • 48
    • 79953726111 scopus 로고    scopus 로고
    • Molecular dynamics analysis of conserved hydrophobic and hydrophilic bond interaction networks in ErbB family kinases
    • Shih, A., et al. Molecular dynamics analysis of conserved hydrophobic and hydrophilic bond interaction networks in ErbB family kinases. Biochem. J. 436:241-251, 2011.
    • (2011) Biochem. J. , vol.436 , pp. 241-251
    • Shih, A.1
  • 49
    • 0029889579 scopus 로고    scopus 로고
    • Epidermal growth factor receptor interaction with clathrin adaptors is mediated by the Tyr974-containing internalization motif
    • Sorkin, A., et al. Epidermal growth factor receptor interaction with clathrin adaptors is mediated by the Tyr974-containing internalization motif. J. Biol. Chem. 271(23): 13377-13384, 1996.
    • (1996) J. Biol. Chem. , vol.271 , Issue.23 , pp. 13377-13384
    • Sorkin, A.1
  • 50
    • 0035945611 scopus 로고    scopus 로고
    • Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle
    • Stark, H., et al. Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle. Nature 409(6819):539-542, 2001.
    • (2001) Nature , vol.409 , Issue.6819 , pp. 539-542
    • Stark, H.1
  • 51
    • 66149108395 scopus 로고    scopus 로고
    • Molecular dynamics simulations reveal that Tyr-317 phosphorylation reduces Shc binding affinity for phosphotyrosyl residues of epidermal
    • Suenaga, A., et al. Molecular dynamics simulations reveal that Tyr-317 phosphorylation reduces Shc binding affinity for phosphotyrosyl residues of epidermal. Growth Factor Recept. 96(6):2278-2288, 2009.
    • (2009) Growth Factor Recept. , vol.96 , Issue.6 , pp. 2278-2288
    • Suenaga, A.1
  • 52
    • 33745024278 scopus 로고    scopus 로고
    • Symmetry, form, and shape: Guiding principles for robustness in macromolecular machines
    • Tama, F., and C. L. Brooks. Symmetry, form, and shape: guiding principles for robustness in macromolecular machines. Annu. Rev. Biophys. Biomol. Struct. 35:115-133, 2006.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 115-133
    • Tama, F.1    Brooks, C.L.2
  • 53
    • 77956278138 scopus 로고    scopus 로고
    • A coarse-grained molecular model for actin-myosin simulation
    • Taylor, W. R., and Z. Katsimitsoulia. A coarse-grained molecular model for actin-myosin simulation. J. Mol. Graph. Model. 29(2):266-279, 2010.
    • (2010) J. Mol. Graph. Model. , vol.29 , Issue.2 , pp. 266-279
    • Taylor, W.R.1    Katsimitsoulia, Z.2
  • 54
    • 66149084032 scopus 로고    scopus 로고
    • Atomistic insights into regulatory mechanisms of the HER2 tyrosine kinase domain: A molecular dynamics study
    • Telesco, S. E., and R. Radhakrishnan. Atomistic insights into regulatory mechanisms of the HER2 tyrosine kinase domain: a molecular dynamics study. Biophys. J. 96(6): 2321-2334, 2009.
    • (2009) Biophys. J. , vol.96 , Issue.6 , pp. 2321-2334
    • Telesco, S.E.1    Radhakrishnan, R.2
  • 55
    • 79956076840 scopus 로고    scopus 로고
    • Investigating molecular mechanisms of activation and mutation of the HER2 receptor tyrosine kinase through computational modeling and simulation
    • Telesco, S. E., A. Shih, Y. Liu, and R. Radhakrishnan. Investigating molecular mechanisms of activation and mutation of the HER2 receptor tyrosine kinase through computational modeling and simulation. Cancer Research Journal 4(4):1-35, 2011.
    • (2011) Cancer Research Journal , vol.4 , Issue.4 , pp. 1-35
    • Telesco, S.E.1    Shih, A.2    Liu, Y.3    Radhakrishnan, R.4
  • 56
    • 79956098237 scopus 로고    scopus 로고
    • A multiscale modeling approach to investigate molecular mechanisms of pseudokinase activation and drug resistance in the HER3/ErbB3 receptor tyrosine kinase signaling network
    • Telesco, S. E., et al. A multiscale modeling approach to investigate molecular mechanisms of pseudokinase activation and drug resistance in the HER3/ErbB3 receptor tyrosine kinase signaling network. Mol. BioSyst. 7(6): 2066-2080, 2011.
    • (2011) Mol. BioSyst. , vol.7 , Issue.6 , pp. 2066-2080
    • Telesco, S.E.1
  • 58
    • 7244239706 scopus 로고    scopus 로고
    • Multiscale modeling in computation
    • E, W., and B. Engquist. Multiscale modeling in computation. Notices AMS 50(9):1062-1070, 2003.
    • (2003) Notices AMS , vol.50 , Issue.9 , pp. 1062-1070
    • Engquist, B.1
  • 59
    • 0037367420 scopus 로고    scopus 로고
    • Heterogeneous multiscale method: A general methodology for multiscale modeling
    • E, W., B. Engquist, and Z. Y. Huang. Heterogeneous multiscale method: a general methodology for multiscale modeling. Phys. Rev. B 67(9):092101, 2003.
    • (2003) Phys. Rev. B , vol.67 , Issue.9 , pp. 092101
    • Engquist, E.W.B.1    Huang, Z.Y.2
  • 60
    • 5044227742 scopus 로고    scopus 로고
    • The evolution of molecular biology into systems biology
    • Westerhoff, H. V., and B. O. Palsson. The evolution of molecular biology into systems biology. Nat. Biotechnol. 22(10):1249-1252, 2004.
    • (2004) Nat. Biotechnol. , vol.22 , Issue.10 , pp. 1249-1252
    • Westerhoff, H.V.1    Palsson, B.O.2
  • 62
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang, X., et al. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125(6):1137-1149, 2006.
    • (2006) Cell , vol.125 , Issue.6 , pp. 1137-1149
    • Zhang, X.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.