메뉴 건너뛰기




Volumn 395, Issue 4, 2010, Pages 834-843

The Dominance of Symmetry in the Evolution of Homo-oligomeric Proteins

Author keywords

association energy; evolutionary drift; evolutionary selection; point group symmetry; surface contact

Indexed keywords

PROTEIN X;

EID: 73649087910     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.10.044     Document Type: Article
Times cited : (25)

References (26)
  • 1
    • 0004158366 scopus 로고
    • Princeton University Press, Princeton, NJ
    • Weyl H. Symmetry (1952), Princeton University Press, Princeton, NJ
    • (1952) Symmetry
    • Weyl, H.1
  • 2
    • 10544220028 scopus 로고
    • Über quantenmechanische Resonanzanziehung und über das Problem der Immunitätsreaktionen (Quantum-mechanical resonance attraction and immune reactions)
    • Jordan P. Über quantenmechanische Resonanzanziehung und über das Problem der Immunitätsreaktionen (Quantum-mechanical resonance attraction and immune reactions). Z. Phys. 113 (1939) 431-438
    • (1939) Z. Phys. , vol.113 , pp. 431-438
    • Jordan, P.1
  • 3
    • 0001971367 scopus 로고
    • The nature of the intermolecular forces operative in biological processes
    • Pauling L., and Delbrück M. The nature of the intermolecular forces operative in biological processes. Science 92 (1940) 77-79
    • (1940) Science , vol.92 , pp. 77-79
    • Pauling, L.1    Delbrück, M.2
  • 4
    • 85025312372 scopus 로고
    • Structure and function of haemoglobin
    • Perutz M.F. Structure and function of haemoglobin. J. Mol. Biol. 13 (1965) 646-668
    • (1965) J. Mol. Biol. , vol.13 , pp. 646-668
    • Perutz, M.F.1
  • 5
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: a plausible model
    • Monod J., Wyman J., and Changeaux J.-P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12 (1965) 88-118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeaux, J.-P.3
  • 7
  • 11
    • 46249083761 scopus 로고    scopus 로고
    • Assembly reflects evolution of protein complexes
    • Levy E.D., Erba E.B., Robinson C.V., and Teichmann S.A. Assembly reflects evolution of protein complexes. Nature 453 (2008) 1262-1265
    • (2008) Nature , vol.453 , pp. 1262-1265
    • Levy, E.D.1    Erba, E.B.2    Robinson, C.V.3    Teichmann, S.A.4
  • 13
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • Chothia C., and Janin J. Principles of protein-protein recognition. Nature 256 (1975) 705-708
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia, C.1    Janin, J.2
  • 14
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S., and Thornton J.M. Principles of protein-protein interactions. Proc. Natl Acad. Sci. USA 93 (1996) 13-20
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 15
    • 0029919190 scopus 로고    scopus 로고
    • Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading
    • Miyazawa S., and Jernigan R.L. Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading. J. Mol. Biol. 256 (1996) 623-644
    • (1996) J. Mol. Biol. , vol.256 , pp. 623-644
    • Miyazawa, S.1    Jernigan, R.L.2
  • 16
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein-protein interfaces: a statistical analysis of the hydrophobic effect
    • Tsai C.-J., Lin S.L., Wolfson H.J., and Nussinov R. Studies of protein-protein interfaces: a statistical analysis of the hydrophobic effect. Protein Sci. 6 (1997) 53-64
    • (1997) Protein Sci. , vol.6 , pp. 53-64
    • Tsai, C.-J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 17
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L., Chothia C., and Janin J. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285 (1999) 2177-2198
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 18
    • 0037229456 scopus 로고    scopus 로고
    • Analysing six types of protein-protein interfaces
    • Ofran Y., and Rost B. Analysing six types of protein-protein interfaces. J. Mol. Biol. 325 (2003) 377-387
    • (2003) J. Mol. Biol. , vol.325 , pp. 377-387
    • Ofran, Y.1    Rost, B.2
  • 19
    • 1042275583 scopus 로고    scopus 로고
    • A dissection of specific and non-specific protein-protein interfaces
    • Bahadur R.P., Chakrabarti P., Rodier F., and Janin J. A dissection of specific and non-specific protein-protein interfaces. J. Mol. Biol. 336 (2004) 943-955
    • (2004) J. Mol. Biol. , vol.336 , pp. 943-955
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 20
    • 0035956861 scopus 로고    scopus 로고
    • Nanohedra: using symmetry to design self assembling protein cages, layers, crystals, and filaments
    • Padilla J.E., Colovos C., and Yeates T.O. Nanohedra: using symmetry to design self assembling protein cages, layers, crystals, and filaments. Proc. Natl Acad. Sci. USA 98 (2001) 2217-2221
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 2217-2221
    • Padilla, J.E.1    Colovos, C.2    Yeates, T.O.3
  • 23
    • 33845875196 scopus 로고    scopus 로고
    • Relating three-dimensional structures to protein networks provides evolutionary insights
    • Kim P.M., Lu L.J., and Gerstein M.B. Relating three-dimensional structures to protein networks provides evolutionary insights. Science 314 (2006) 1938-1941
    • (2006) Science , vol.314 , pp. 1938-1941
    • Kim, P.M.1    Lu, L.J.2    Gerstein, M.B.3
  • 24
    • 0031450906 scopus 로고    scopus 로고
    • Structure, catalysis and supramolecular assembly of adenylate kinase from maize
    • Wild K., Grafmüller R., Wagner E., and Schulz G.E. Structure, catalysis and supramolecular assembly of adenylate kinase from maize. Eur. J. Biochem. 250 (1997) 326-331
    • (1997) Eur. J. Biochem. , vol.250 , pp. 326-331
    • Wild, K.1    Grafmüller, R.2    Wagner, E.3    Schulz, G.E.4
  • 25
    • 27344449197 scopus 로고    scopus 로고
    • Progress in modeling of protein structures and interactions
    • Schueler-Furman O., Wang C., Bradley P., Misura K., and Baker D. Progress in modeling of protein structures and interactions. Science 310 (2005) 638-642
    • (2005) Science , vol.310 , pp. 638-642
    • Schueler-Furman, O.1    Wang, C.2    Bradley, P.3    Misura, K.4    Baker, D.5
  • 26
    • 0015217634 scopus 로고
    • The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions
    • Nozaki Y., and Tanford C. The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. J. Biol. Chem. 246 (1971) 2211-2217
    • (1971) J. Biol. Chem. , vol.246 , pp. 2211-2217
    • Nozaki, Y.1    Tanford, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.