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Volumn 10, Issue 2, 2009, Pages 133-145

Protein domains as information processing units

Author keywords

Communication; Computational methods; Domains; Information theory; Protein structure; Sequence versus structure; Signal transduction; Thermodynamic coupling

Indexed keywords

CHAPERONIN; PDZ PROTEIN; PROTEIN SH2;

EID: 65649103710     PISSN: 13892037     EISSN: None     Source Type: Journal    
DOI: 10.2174/138920309787847626     Document Type: Review
Times cited : (3)

References (64)
  • 1
    • 0029037739 scopus 로고    scopus 로고
    • Bray, D. Protein molecules as computational elements in living cells. (1995) Nature, 376, 307-312.
    • Bray, D. Protein molecules as computational elements in living cells. (1995) Nature, 376, 307-312.
  • 2
    • 0141957253 scopus 로고    scopus 로고
    • Pawson, T. Organization of cell-regulatory systems through modular-protein-interaction domains. (2003) Philos. Transact. A Math. Phys. Eng. Sci., 361, 1251-1262.
    • Pawson, T. Organization of cell-regulatory systems through modular-protein-interaction domains. (2003) Philos. Transact. A Math. Phys. Eng. Sci., 361, 1251-1262.
  • 3
    • 0742305866 scopus 로고    scopus 로고
    • Barabasi, A.L. and Oltvai, Z.N. Network biology: understanding the cell's functional organization. (2004) Nat. Rev. Genet., 5, 101-113.
    • Barabasi, A.L. and Oltvai, Z.N. Network biology: understanding the cell's functional organization. (2004) Nat. Rev. Genet., 5, 101-113.
  • 4
    • 2942544498 scopus 로고    scopus 로고
    • Bork, P., Jensen, L.J., von Mering, C., Ramani, A.K., Lee, I. and Marcotte, E.M. Protein interaction networks from yeast to human. ( 2004) Curr. Opin. Struct. Biol., 14, 292-299.
    • Bork, P., Jensen, L.J., von Mering, C., Ramani, A.K., Lee, I. and Marcotte, E.M. Protein interaction networks from yeast to human. ( 2004) Curr. Opin. Struct. Biol., 14, 292-299.
  • 5
    • 25144498379 scopus 로고    scopus 로고
    • Stelzl, U., Worm, U., Lalowski, M., Haenig, C., Brembeck, F.H., Goehler, H., Stroedicke, M., Zenkner, M., Schoenherr, A., Koeppen, S., Timm, J., Mintzlaff, S., Abraham, C., Bock, N., Kietzmann, S., Goedde, A., Toksoz, E., Droege, A., Krobitsch, S., Korn, B., Birchmeier, W., Lehrach, H. and Wanker, E.E. A human protein-protein interaction network: a resource for annotating the proteome. (2005) Cell, 122, 957-968.
    • Stelzl, U., Worm, U., Lalowski, M., Haenig, C., Brembeck, F.H., Goehler, H., Stroedicke, M., Zenkner, M., Schoenherr, A., Koeppen, S., Timm, J., Mintzlaff, S., Abraham, C., Bock, N., Kietzmann, S., Goedde, A., Toksoz, E., Droege, A., Krobitsch, S., Korn, B., Birchmeier, W., Lehrach, H. and Wanker, E.E. A human protein-protein interaction network: a resource for annotating the proteome. (2005) Cell, 122, 957-968.
  • 6
    • 33750351769 scopus 로고    scopus 로고
    • Janes, K.A. and Yaffe, M.B. Data-driven modelling of signal-transduction networks. (2006) Nat. Rev. Mol. Cell Biol., 7, 820-828.
    • Janes, K.A. and Yaffe, M.B. Data-driven modelling of signal-transduction networks. (2006) Nat. Rev. Mol. Cell Biol., 7, 820-828.
  • 7
    • 37849020261 scopus 로고    scopus 로고
    • Albert, R. Network inference, analysis, and modeling in systems biology. (2007) Plant Cell, 19, 3327-3338.
    • Albert, R. Network inference, analysis, and modeling in systems biology. (2007) Plant Cell, 19, 3327-3338.
  • 8
    • 33745986047 scopus 로고    scopus 로고
    • Andrews, S.S. and Arkin, A.P. Simulating cell biology. (2006) Curr. Biol., 16, R523-527.
    • Andrews, S.S. and Arkin, A.P. Simulating cell biology. (2006) Curr. Biol., 16, R523-527.
  • 9
    • 0028895654 scopus 로고    scopus 로고
    • Cohen, G.B., Ren, R. and Baltimore, D. Modular binding domains in signal transduction proteins. (1995) Cell, 80, 237-248.
    • Cohen, G.B., Ren, R. and Baltimore, D. Modular binding domains in signal transduction proteins. (1995) Cell, 80, 237-248.
  • 10
    • 0030950608 scopus 로고    scopus 로고
    • Kuriyan, J. and Cowburn, D. Modular peptide recognition domains in eukaryotic signaling. (1997) Annu. Rev. Biophys. Biomol. Struct., 26, 259-288.
    • Kuriyan, J. and Cowburn, D. Modular peptide recognition domains in eukaryotic signaling. (1997) Annu. Rev. Biophys. Biomol. Struct., 26, 259-288.
  • 11
    • 24944446722 scopus 로고    scopus 로고
    • Cesareni, G, Gimona, M, Sudo, M. and Yaffe, M, Eds, Wiley VCH
    • Cesareni, G., Gimona, M., Sudo, M. and Yaffe, M. (Eds.): Modular protein domains (2004). Wiley VCH.
    • (2004) Modular protein domains
  • 12
    • 15044350197 scopus 로고    scopus 로고
    • Bornberg-Bauer, E., Beaussart, F., Kummerfeld, S.K., Teichmann, S.A. and Weiner, J. 3rd. The evolution of domain arrangements in proteins and interaction networks. (2005) Cell. Mol. Life Sci., 62, 435-445.
    • Bornberg-Bauer, E., Beaussart, F., Kummerfeld, S.K., Teichmann, S.A. and Weiner, J. 3rd. The evolution of domain arrangements in proteins and interaction networks. (2005) Cell. Mol. Life Sci., 62, 435-445.
  • 13
    • 0037155199 scopus 로고    scopus 로고
    • Hung, A.Y. and Sheng, M. PDZ domains: structural modules for protein complex assembly. (2002) J. Biol. Chem., 277, 5699-5702.
    • Hung, A.Y. and Sheng, M. PDZ domains: structural modules for protein complex assembly. (2002) J. Biol. Chem., 277, 5699-5702.
  • 14
    • 0037503653 scopus 로고    scopus 로고
    • van Ham, M. and Hendriks, W. PDZ domains-glue and guide. (2003) Mol. Biol. Rep., 30, 69-82.
    • van Ham, M. and Hendriks, W. PDZ domains-glue and guide. (2003) Mol. Biol. Rep., 30, 69-82.
  • 15
    • 13244284809 scopus 로고    scopus 로고
    • Pawson, T. and Schlessingert, J. SH2 and SH3 domains. (1993) Curr. Biol., 3, 434-442.
    • Pawson, T. and Schlessingert, J. SH2 and SH3 domains. (1993) Curr. Biol., 3, 434-442.
  • 16
    • 0013033597 scopus 로고    scopus 로고
    • The structure and function of proline recognition domains. (2003)
    • Zarrinpar, A., Bhattacharyya, R.P. and Lim, W.A. The structure and function of proline recognition domains. (2003) Science STKE, 2003, RE8.
    • (2003) Science STKE
    • Zarrinpar, A.1    Bhattacharyya, R.P.2    Lim, W.A.3
  • 17
    • 0036417094 scopus 로고    scopus 로고
    • Bradshaw, J.M. and Waksman, G. Molecular recognition by SH2 domains. ( 2002) Adv. Protein Chem., 61, 161-210.
    • Bradshaw, J.M. and Waksman, G. Molecular recognition by SH2 domains. ( 2002) Adv. Protein Chem., 61, 161-210.
  • 18
    • 0842346438 scopus 로고    scopus 로고
    • Pawson, T. Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. (2004) Cell, 116, 191-203.
    • Pawson, T. Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. (2004) Cell, 116, 191-203.
  • 19
    • 0030781598 scopus 로고    scopus 로고
    • Rotin, D. WW (WWP) domains: from structure to function. (1998) Curr. Top. Microbiol. Immunol., 228, 115-133.
    • Rotin, D. WW (WWP) domains: from structure to function. (1998) Curr. Top. Microbiol. Immunol., 228, 115-133.
  • 20
    • 30344454668 scopus 로고    scopus 로고
    • Sudol, M., Recinos, C.C., Abraczinskas, J., Humbert, J. and Farooq, A. WW or WoW: the WW domains in a union of bliss. (2005) IUBMB Life, 57, 773-778.
    • Sudol, M., Recinos, C.C., Abraczinskas, J., Humbert, J. and Farooq, A. WW or WoW: the WW domains in a union of bliss. (2005) IUBMB Life, 57, 773-778.
  • 21
    • 33745185987 scopus 로고    scopus 로고
    • Liu, B.A., Jablonowski, K., Raina, M., Arce, M., Pawson, T. and Nash, P.D. The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling. (2006) Mol. Cell, 22, 851-868.
    • Liu, B.A., Jablonowski, K., Raina, M., Arce, M., Pawson, T. and Nash, P.D. The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling. (2006) Mol. Cell, 22, 851-868.
  • 22
    • 0036468436 scopus 로고    scopus 로고
    • Lim, W.A. The modular logic of signaling proteins: building allosteric switches from simple binding domains. (2002) Curr. Opin. Struct. Biol., 12, 61-68.
    • Lim, W.A. The modular logic of signaling proteins: building allosteric switches from simple binding domains. (2002) Curr. Opin. Struct. Biol., 12, 61-68.
  • 23
    • 0042821546 scopus 로고    scopus 로고
    • Seeliger, M.A., Breward, S.E., Friedler, A., Schon, O. and Itzhaki, L.S. Cooperative organization in a macromolecular complex. (2003) Nat. Struct. Biol., 10, 718-724.
    • Seeliger, M.A., Breward, S.E., Friedler, A., Schon, O. and Itzhaki, L.S. Cooperative organization in a macromolecular complex. (2003) Nat. Struct. Biol., 10, 718-724.
  • 24
    • 6344219895 scopus 로고    scopus 로고
    • Gunasekaran, K., Ma, B. and Nussinov, R. Is allostery an intrinsic property of all dynamic proteins? (2004) Proteins, 57, 433-443.
    • Gunasekaran, K., Ma, B. and Nussinov, R. Is allostery an intrinsic property of all dynamic proteins? (2004) Proteins, 57, 433-443.
  • 25
    • 32344434479 scopus 로고    scopus 로고
    • Swain, J.F. and Gierasch, L.M. The changing landscape of protein allostery. (2006) Curr. Opin. Struct. Biol., 16, 102-108.
    • Swain, J.F. and Gierasch, L.M. The changing landscape of protein allostery. (2006) Curr. Opin. Struct. Biol., 16, 102-108.
  • 26
    • 0015528157 scopus 로고    scopus 로고
    • Weber, G. Ligand binding and internal equilibria in proteins. (1972) Biochemistry, 11, 864-878.
    • Weber, G. Ligand binding and internal equilibria in proteins. (1972) Biochemistry, 11, 864-878.
  • 27
    • 0033621118 scopus 로고    scopus 로고
    • Freire, E. The propagation of binding interactions to remote sites in proteins: analysis of the binding of the monoclonal antibody D1.3 to lysozyme. (1999) Proc. Natl. Acad. Sci. USA, 96, 10118-10122.
    • Freire, E. The propagation of binding interactions to remote sites in proteins: analysis of the binding of the monoclonal antibody D1.3 to lysozyme. (1999) Proc. Natl. Acad. Sci. USA, 96, 10118-10122.
  • 28
    • 33847718707 scopus 로고    scopus 로고
    • Pawson, T. Dynamic control of signaling by modular adaptor proteins. ( 2007) Curr. Opin. Cell Biol., 19, 112-116.
    • Pawson, T. Dynamic control of signaling by modular adaptor proteins. ( 2007) Curr. Opin. Cell Biol., 19, 112-116.
  • 29
    • 84988043558 scopus 로고    scopus 로고
    • Hatada, M.H., Lu, X., Laird, E.R., Green, J., Morgenstern, J.P., Lou, M., Marr, C.S., Phillips, T.B., Ram, M.K., Theriault, K. and et al. Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor. (1995) Nature, 377, 32-38.
    • Hatada, M.H., Lu, X., Laird, E.R., Green, J., Morgenstern, J.P., Lou, M., Marr, C.S., Phillips, T.B., Ram, M.K., Theriault, K. and et al. Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor. (1995) Nature, 377, 32-38.
  • 30
    • 1642276423 scopus 로고    scopus 로고
    • Peterson, F.C., Penkert, R.R., Volkman, B.F. and Prehoda, K.E. Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIBPDZ transition. (2004) Mol. Cell, 13, 665-676.
    • Peterson, F.C., Penkert, R.R., Volkman, B.F. and Prehoda, K.E. Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIBPDZ transition. (2004) Mol. Cell, 13, 665-676.
  • 31
    • 0033536602 scopus 로고    scopus 로고
    • Lockless, S.W. and Ranganathan, R. Evolutionarily conserved pathways of energetic connectivity in protein families. (1999) Science, 286, 295-299.
    • Lockless, S.W. and Ranganathan, R. Evolutionarily conserved pathways of energetic connectivity in protein families. (1999) Science, 286, 295-299.
  • 32
    • 0037219686 scopus 로고    scopus 로고
    • Suel, G.M., Lockless, S.W., Wall, M.A. and Ranganathan, R. Evolutionarily conserved networks of residues mediate allosteric communication in proteins. (2003) Nat. Struct. Biol., 10, 59-69.
    • Suel, G.M., Lockless, S.W., Wall, M.A. and Ranganathan, R. Evolutionarily conserved networks of residues mediate allosteric communication in proteins. (2003) Nat. Struct. Biol., 10, 59-69.
  • 34
    • 13844296720 scopus 로고    scopus 로고
    • Rousseau, F. and Schymkowitz, J. A systems biology perspective on protein structural dynamics and signal transduction. (2005) Curr. Opin. Struct. Biol., 15, 23-30.
    • Rousseau, F. and Schymkowitz, J. A systems biology perspective on protein structural dynamics and signal transduction. (2005) Curr. Opin. Struct. Biol., 15, 23-30.
  • 35
    • 0028455053 scopus 로고    scopus 로고
    • Schlitter, J., Engels, M. and Kruger, P. Targeted molecular dynamics: a new approach for searching pathways of conformational transitions. ( 1994) J. Mol. Graph., 12, 84-89.
    • Schlitter, J., Engels, M. and Kruger, P. Targeted molecular dynamics: a new approach for searching pathways of conformational transitions. ( 1994) J. Mol. Graph., 12, 84-89.
  • 36
    • 0034665864 scopus 로고    scopus 로고
    • Ma, J., Sigler, P.B., Xu, Z. and Karplus, M. A dynamic model for the allosteric mechanism of GroEL. (2000) J Mol Biol, 302, 303-313.
    • Ma, J., Sigler, P.B., Xu, Z. and Karplus, M. A dynamic model for the allosteric mechanism of GroEL. (2000) J Mol Biol, 302, 303-313.
  • 37
    • 33746652529 scopus 로고    scopus 로고
    • Best, R.B., Lindorff-Larsen, K., DePristo, M.A. and Vendruscolo, M. Relation between native ensembles and experimental structures of proteins. (2006) Proc. Natl. Acad. Sci. USA, 103, 10901-10906.
    • Best, R.B., Lindorff-Larsen, K., DePristo, M.A. and Vendruscolo, M. Relation between native ensembles and experimental structures of proteins. (2006) Proc. Natl. Acad. Sci. USA, 103, 10901-10906.
  • 38
    • 3042846748 scopus 로고    scopus 로고
    • Best, R.B. and Vendruscolo, M. Determination of protein structures consistent with NMR order parameters. (2004) J. Am. Chem. Soc., 126, 8090-8091.
    • Best, R.B. and Vendruscolo, M. Determination of protein structures consistent with NMR order parameters. (2004) J. Am. Chem. Soc., 126, 8090-8091.
  • 39
    • 22444450449 scopus 로고    scopus 로고
    • Ota, N. and Agard, D.A. Intramolecular signaling pathways revealed by modeling anisotropic thermal diffusion. (2005) J. Mol. Biol., 351, 345-354.
    • Ota, N. and Agard, D.A. Intramolecular signaling pathways revealed by modeling anisotropic thermal diffusion. (2005) J. Mol. Biol., 351, 345-354.
  • 40
    • 0030580089 scopus 로고    scopus 로고
    • Hilser, V.J. and Freire, E. Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. (1996) J. Mol. Biol., 262, 756-772.
    • Hilser, V.J. and Freire, E. Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. (1996) J. Mol. Biol., 262, 756-772.
  • 41
    • 0034710950 scopus 로고    scopus 로고
    • Pan, H., Lee, J.C. and Hilser, V.J. Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble. (2000) Proc. Natl. Acad. Sci. USA, 97, 12020-12025.
    • Pan, H., Lee, J.C. and Hilser, V.J. Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble. (2000) Proc. Natl. Acad. Sci. USA, 97, 12020-12025.
  • 42
    • 0000355428 scopus 로고    scopus 로고
    • Go, N. and Taketomi, H. Respective roles of short- and long-range interactions in protein folding. (1978) Proc. Natl. Acad. Sci. USA, 75, 559-563.
    • Go, N. and Taketomi, H. Respective roles of short- and long-range interactions in protein folding. (1978) Proc. Natl. Acad. Sci. USA, 75, 559-563.
  • 43
    • 0032544060 scopus 로고    scopus 로고
    • Hilser, V.J., Dowdy, D., Oas, T.G. and Freire, E. The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble. (1998) Proc Natl Acad Sci USA, 95, 9903-9908.
    • Hilser, V.J., Dowdy, D., Oas, T.G. and Freire, E. The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble. (1998) Proc Natl Acad Sci USA, 95, 9903-9908.
  • 44
    • 0033642945 scopus 로고    scopus 로고
    • Luque, I. and Freire, E. Structural stability of binding sites: consequences for binding affinity and allosteric effects. (2000) Proteins, Suppl, 63-71.
    • Luque, I. and Freire, E. Structural stability of binding sites: consequences for binding affinity and allosteric effects. (2000) Proteins, Suppl, 63-71.
  • 45
    • 23144436398 scopus 로고    scopus 로고
    • Schymkowitz, J., Borg, J., Stricher, F., Nys, R., Rousseau, F. and Serrano, L. The FoldX web server: an online force field. (2005) Nucleic Acids Res., 33, W382-388.
    • Schymkowitz, J., Borg, J., Stricher, F., Nys, R., Rousseau, F. and Serrano, L. The FoldX web server: an online force field. (2005) Nucleic Acids Res., 33, W382-388.
  • 46
    • 22544450150 scopus 로고    scopus 로고
    • Schymkowitz, J.W., Rousseau, F., Martins, I.C., Ferkinghoff-Borg, J., Stricher, F. and Serrano, L. Prediction of water and metal binding sites and their affinities by using the Fold-X force field. (2005) Proc. Natl. Acad. Sci. USA, 102, 10147-10152.
    • Schymkowitz, J.W., Rousseau, F., Martins, I.C., Ferkinghoff-Borg, J., Stricher, F. and Serrano, L. Prediction of water and metal binding sites and their affinities by using the Fold-X force field. (2005) Proc. Natl. Acad. Sci. USA, 102, 10147-10152.
  • 47
    • 84940644968 scopus 로고    scopus 로고
    • Shannon, C.E. A mathematical theory of communication. (1948) Bell System Technical Journal, 27, 379-423.
    • Shannon, C.E. A mathematical theory of communication. (1948) Bell System Technical Journal, 27, 379-423.
  • 48
    • 0021173703 scopus 로고    scopus 로고
    • Stone, J.C., Atkinson, T., Smith, M. and Pawson, T. Identification of functional regions in the transforming protein of Fujinami sarcoma virus by in-phase insertion mutagenesis. (1984) Cell, 37, 549-558.
    • Stone, J.C., Atkinson, T., Smith, M. and Pawson, T. Identification of functional regions in the transforming protein of Fujinami sarcoma virus by in-phase insertion mutagenesis. (1984) Cell, 37, 549-558.
  • 49
    • 0022977712 scopus 로고    scopus 로고
    • Sadowski, I., Stone, J.C. and Pawson, T. A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps. ( 1986) Mol. Cell Biol., 6, 4396-4408.
    • Sadowski, I., Stone, J.C. and Pawson, T. A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps. ( 1986) Mol. Cell Biol., 6, 4396-4408.
  • 50
    • 0037693805 scopus 로고    scopus 로고
    • Campbell, S.J. and Jackson, R.M. Diversity in the SH2 domain family phosphotyrosyl peptide binding site. (2003) Protein Eng., 16, 217-227.
    • Campbell, S.J. and Jackson, R.M. Diversity in the SH2 domain family phosphotyrosyl peptide binding site. (2003) Protein Eng., 16, 217-227.
  • 51
    • 38549146894 scopus 로고    scopus 로고
    • Finn, R.D., Tate, J., Mistry, J., Coggill, P.C., Sammut, S.J., Hotz, H.R., Ceric, G., Forslund, K., Eddy, S.R., Sonnhammer, E.L. and Bateman, A. The Pfam protein families database. (2008) Nucleic Acids Res., 36, D281-288.
    • Finn, R.D., Tate, J., Mistry, J., Coggill, P.C., Sammut, S.J., Hotz, H.R., Ceric, G., Forslund, K., Eddy, S.R., Sonnhammer, E.L. and Bateman, A. The Pfam protein families database. (2008) Nucleic Acids Res., 36, D281-288.
  • 52
    • 0030925920 scopus 로고    scopus 로고
    • Sonnhammer, E.L., Eddy, S.R. and Durbin, R. Pfam: a comprehensive database of protein domain families based on seed alignments. (1997) Proteins, 28, 405-420.
    • Sonnhammer, E.L., Eddy, S.R. and Durbin, R. Pfam: a comprehensive database of protein domain families based on seed alignments. (1997) Proteins, 28, 405-420.
  • 53
    • 0033990087 scopus 로고    scopus 로고
    • Aiyar, A. The use of CLUSTAL W and CLUSTAL X for multiple sequence alignment. (2000) Methods Mol. Biol., 132, 221-241.
    • Aiyar, A. The use of CLUSTAL W and CLUSTAL X for multiple sequence alignment. (2000) Methods Mol. Biol., 132, 221-241.
  • 54
    • 36448991500 scopus 로고    scopus 로고
    • Larkin, M.A, Blackshields, G, Brown, N.P, Chenna, R, McGettigan, P.A, McWilliam, H, Valentin, F, Wallace, I.M, Wilm, A, Lopez, R, Thompson, J.D, Gibson, T.J. and Higgins, D.G. Clustal W and Clustal X version 2.0, 2007 Bioinformatics, 23, 2947-2948
    • Larkin, M.A., Blackshields, G., Brown, N.P., Chenna, R., McGettigan, P.A., McWilliam, H., Valentin, F., Wallace, I.M., Wilm, A., Lopez, R., Thompson, J.D., Gibson, T.J. and Higgins, D.G. Clustal W and Clustal X version 2.0. (2007) Bioinformatics, 23, 2947-2948.
  • 55
    • 85142198235 scopus 로고    scopus 로고
    • Dekker, J.P., Fodor, A., Aldrich, R.W. and Yellen, G. A perturbation- based method for calculating explicit likelihood of evolutionary co-variance in multiple sequence alignments. (2004) Bioinformatics, 20, 1565-1572.
    • Dekker, J.P., Fodor, A., Aldrich, R.W. and Yellen, G. A perturbation- based method for calculating explicit likelihood of evolutionary co-variance in multiple sequence alignments. (2004) Bioinformatics, 20, 1565-1572.
  • 57
    • 11944266539 scopus 로고    scopus 로고
    • Jaynes, E.T. Information Theory and Statistical Mechanics. (1957) Phys. Rev., 106, 520-630.
    • Jaynes, E.T. Information Theory and Statistical Mechanics. (1957) Phys. Rev., 106, 520-630.
  • 58
    • 2442498470 scopus 로고    scopus 로고
    • Fodor, A.A. and Aldrich, R.W. On evolutionary conservation of thermodynamic coupling in proteins. (2004) J. Biol. Chem., 279, 19046-19050.
    • Fodor, A.A. and Aldrich, R.W. On evolutionary conservation of thermodynamic coupling in proteins. (2004) J. Biol. Chem., 279, 19046-19050.
  • 59
    • 0031572835 scopus 로고    scopus 로고
    • Mulhern, T.D., Shaw, G.L., Morton, C.J., Day, A.J. and Campbell, I.D. The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity. (1997) Structure, 5, 1313-1323.
    • Mulhern, T.D., Shaw, G.L., Morton, C.J., Day, A.J. and Campbell, I.D. The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity. (1997) Structure, 5, 1313-1323.
  • 60
    • 0035815288 scopus 로고    scopus 로고
    • Young, M.A., Gonfloni, S., Superti-Furga, G., Roux, B. and Kuriyan, J. Dynamic coupling between the SH2 and SH3 domains of c- Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation. ( 2001) Cell, 105, 115-126.
    • Young, M.A., Gonfloni, S., Superti-Furga, G., Roux, B. and Kuriyan, J. Dynamic coupling between the SH2 and SH3 domains of c- Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation. ( 2001) Cell, 105, 115-126.
  • 61
    • 85142121312 scopus 로고    scopus 로고
    • Steuer, R., Kurths, J., Daub, C.O., Weise, J. and Selbig, J. The mutual information: detecting and evaluating dependencies between variables. (2002) Bioinformatics, 18 Suppl 2, S231-240.
    • Steuer, R., Kurths, J., Daub, C.O., Weise, J. and Selbig, J. The mutual information: detecting and evaluating dependencies between variables. (2002) Bioinformatics, 18 Suppl 2, S231-240.
  • 62
    • 33746911627 scopus 로고    scopus 로고
    • Clarkson, M.W., Gilmore, S.A., Edgell, M.H. and Lee, A.L. Dynamic coupling and allosteric behavior in a nonallosteric protein. (2006) Biochemistry, 45, 7693-7699.
    • Clarkson, M.W., Gilmore, S.A., Edgell, M.H. and Lee, A.L. Dynamic coupling and allosteric behavior in a nonallosteric protein. (2006) Biochemistry, 45, 7693-7699.
  • 63
    • 0242268469 scopus 로고    scopus 로고
    • Miyashita, O., Onuchic, J.N. and Wolynes, P.G. Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins. (2003) Proc. Natl. Acad. Sci. USA, 100, 12570-12575.
    • Miyashita, O., Onuchic, J.N. and Wolynes, P.G. Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins. (2003) Proc. Natl. Acad. Sci. USA, 100, 12570-12575.
  • 64
    • 33644841721 scopus 로고    scopus 로고
    • Gimona, M. Protein linguistics - a grammar for modular protein assembly? (2006) Nat. Rev. Mol. Cell Biol., 7, 68-73.
    • Gimona, M. Protein linguistics - a grammar for modular protein assembly? (2006) Nat. Rev. Mol. Cell Biol., 7, 68-73.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.