메뉴 건너뛰기




Volumn 4, Issue , 2008, Pages 3-21

Chapter 1 Structural Perspectives on Protein Evolution

Author keywords

Designability; Evolutionary determinants; Evolvability; Fitness density; Molecular evolution; Protein structure

Indexed keywords


EID: 54849410447     PISSN: 15741400     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1574-1400(08)00001-7     Document Type: Chapter
Times cited : (9)

References (91)
  • 1
    • 76549154030 scopus 로고
    • Biology, molecular and organismic
    • Dobzhansky T. Biology, molecular and organismic. Am. Zool. 4 (1964) 443-452
    • (1964) Am. Zool. , vol.4 , pp. 443-452
    • Dobzhansky, T.1
  • 2
    • 33646375934 scopus 로고    scopus 로고
    • The causes of protein evolutionary rate variation
    • McInerney J.O. The causes of protein evolutionary rate variation. Trends Ecol. Evol. 21 5 (2006) 230-232
    • (2006) Trends Ecol. Evol. , vol.21 , Issue.5 , pp. 230-232
    • McInerney, J.O.1
  • 3
    • 1942452749 scopus 로고    scopus 로고
    • Proof and evolutionary analysis of ancient genome duplication in the yeast Saccharomyces cerevisiae
    • Kellis M., Birren B.W., and Lander E.S. Proof and evolutionary analysis of ancient genome duplication in the yeast Saccharomyces cerevisiae. Nature 428 6983 (2004) 617-624
    • (2004) Nature , vol.428 , Issue.6983 , pp. 617-624
    • Kellis, M.1    Birren, B.W.2    Lander, E.S.3
  • 4
    • 0036720020 scopus 로고    scopus 로고
    • The Ka/Ks ratio: Diagnosing the form of sequence evolution
    • Hurst L.D. The Ka/Ks ratio: Diagnosing the form of sequence evolution. Trends Genet. 18 9 (2002) 486
    • (2002) Trends Genet. , vol.18 , Issue.9 , pp. 486
    • Hurst, L.D.1
  • 5
    • 33646182934 scopus 로고    scopus 로고
    • An integrated view of protein evolution
    • Pal C., Papp B., and Lercher M.J. An integrated view of protein evolution. Nat. Rev. Genet. 7 5 (2006) 337-348
    • (2006) Nat. Rev. Genet. , vol.7 , Issue.5 , pp. 337-348
    • Pal, C.1    Papp, B.2    Lercher, M.J.3
  • 6
    • 33746237576 scopus 로고    scopus 로고
    • The quest for the universals of protein evolution
    • Rocha E.P. The quest for the universals of protein evolution. Trends Genet. 22 8 (2006) 412-416
    • (2006) Trends Genet. , vol.22 , Issue.8 , pp. 412-416
    • Rocha, E.P.1
  • 7
    • 33748143748 scopus 로고    scopus 로고
    • Structural determinants of the rate of protein evolution in yeast
    • Bloom J.D., et al. Structural determinants of the rate of protein evolution in yeast. Mol. Biol. Evol. 23 9 (2006) 1751-1761
    • (2006) Mol. Biol. Evol. , vol.23 , Issue.9 , pp. 1751-1761
    • Bloom, J.D.1
  • 8
    • 34548357121 scopus 로고    scopus 로고
    • Assessing the determinants of evolutionary rates in the presence of noise
    • Plotkin J.B., and Fraser H.B. Assessing the determinants of evolutionary rates in the presence of noise. Mol. Biol. Evol. 24 5 (2007) 1113-1121
    • (2007) Mol. Biol. Evol. , vol.24 , Issue.5 , pp. 1113-1121
    • Plotkin, J.B.1    Fraser, H.B.2
  • 9
    • 1242284655 scopus 로고    scopus 로고
    • An analysis of determinants of amino acids substitution rates in bacterial proteins
    • Rocha E.P., and Danchin A. An analysis of determinants of amino acids substitution rates in bacterial proteins. Mol. Biol. Evol. 21 1 (2004) 108-116
    • (2004) Mol. Biol. Evol. , vol.21 , Issue.1 , pp. 108-116
    • Rocha, E.P.1    Danchin, A.2
  • 10
    • 0041817645 scopus 로고    scopus 로고
    • Translational selection and yeast proteome evolution
    • Akashi H. Translational selection and yeast proteome evolution. Genetics 164 4 (2003) 1291-1303
    • (2003) Genetics , vol.164 , Issue.4 , pp. 1291-1303
    • Akashi, H.1
  • 11
    • 26444621352 scopus 로고    scopus 로고
    • Why highly expressed proteins evolve slowly
    • Drummond D.A., et al. Why highly expressed proteins evolve slowly. Proc. Natl. Acad. Sci. USA 102 40 (2005) 14338-14343
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.40 , pp. 14338-14343
    • Drummond, D.A.1
  • 12
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg A.L. Protein degradation and protection against misfolded or damaged proteins. Nature 426 6968 (2003) 895-899
    • (2003) Nature , vol.426 , Issue.6968 , pp. 895-899
    • Goldberg, A.L.1
  • 13
    • 0014937223 scopus 로고
    • Central dogma of molecular biology
    • Crick F. Central dogma of molecular biology. Nature 227 5258 (1970) 561-563
    • (1970) Nature , vol.227 , Issue.5258 , pp. 561-563
    • Crick, F.1
  • 14
    • 34347375915 scopus 로고    scopus 로고
    • The protein folding problem: When will it be solved?
    • Dill K.A., et al. The protein folding problem: When will it be solved?. Curr. Opin. Struct. Biol. 17 3 (2007) 342-346
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , Issue.3 , pp. 342-346
    • Dill, K.A.1
  • 15
    • 0030792253 scopus 로고    scopus 로고
    • SCOP: A structural classification of proteins database
    • Hubbard T.J., et al. SCOP: A structural classification of proteins database. Nucleic Acids Res. 25 1 (1997) 236-239
    • (1997) Nucleic Acids Res. , vol.25 , Issue.1 , pp. 236-239
    • Hubbard, T.J.1
  • 16
    • 0027122748 scopus 로고
    • Proteins. One thousand families for the molecular biologist
    • Chothia C. Proteins. One thousand families for the molecular biologist. Nature 357 6379 (1992) 543-544
    • (1992) Nature , vol.357 , Issue.6379 , pp. 543-544
    • Chothia, C.1
  • 17
    • 0011542799 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Bateman A., et al. The Pfam protein families database. Nucleic Acids Res. 30 1 (2002) 276-280
    • (2002) Nucleic Acids Res. , vol.30 , Issue.1 , pp. 276-280
    • Bateman, A.1
  • 18
    • 0035005949 scopus 로고    scopus 로고
    • The designability of protein structures
    • Helling R., et al. The designability of protein structures. J. Mol. Graph Model 19 1 (2001) 157-167
    • (2001) J. Mol. Graph Model , vol.19 , Issue.1 , pp. 157-167
    • Helling, R.1
  • 20
    • 14844325784 scopus 로고    scopus 로고
    • Robustness, evolvability, and neutrality
    • Wagner A. Robustness, evolvability, and neutrality. FEBS Lett. 579 8 (2005) 1772-1778
    • (2005) FEBS Lett. , vol.579 , Issue.8 , pp. 1772-1778
    • Wagner, A.1
  • 21
    • 0029654101 scopus 로고
    • DNA sequence evolution: The sounds of silence
    • Sharp P.M., et al. DNA sequence evolution: The sounds of silence. Philos. Trans. R. Soc. Lond. B Biol. Sci. 349 1329 (1995) 241-247
    • (1995) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.349 , Issue.1329 , pp. 241-247
    • Sharp, P.M.1
  • 22
    • 33646938731 scopus 로고    scopus 로고
    • Fold designability, distribution, and disease
    • Wong P., and Frishman D. Fold designability, distribution, and disease. PLoS Comput. Biol. 2 5 (2006) e40
    • (2006) PLoS Comput. Biol. , vol.2 , Issue.5
    • Wong, P.1    Frishman, D.2
  • 24
    • 0029772552 scopus 로고    scopus 로고
    • Emergence of preferred structures in a simple model of protein folding
    • Li H., et al. Emergence of preferred structures in a simple model of protein folding. Science 273 5275 (1996) 666-669
    • (1996) Science , vol.273 , Issue.5275 , pp. 666-669
    • Li, H.1
  • 26
    • 0030030533 scopus 로고    scopus 로고
    • Smoothness within ruggedness: The role of neutrality in adaptation
    • Huynen M.A., Stadler P.F., and Fontana W. Smoothness within ruggedness: The role of neutrality in adaptation. Proc. Natl. Acad. Sci. USA 93 1 (1996) 397-401
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , Issue.1 , pp. 397-401
    • Huynen, M.A.1    Stadler, P.F.2    Fontana, W.3
  • 27
    • 0035930008 scopus 로고    scopus 로고
    • The topology of the possible: Formal spaces underlying patterns of evolutionary change
    • Stadler B.M., et al. The topology of the possible: Formal spaces underlying patterns of evolutionary change. J. Theor. Biol. 213 2 (2001) 241-274
    • (2001) J. Theor. Biol. , vol.213 , Issue.2 , pp. 241-274
    • Stadler, B.M.1
  • 28
    • 0032556237 scopus 로고    scopus 로고
    • Shaping space: The possible and the attainable in RNA genotype-phenotype mapping
    • Fontana W., and Schuster P. Shaping space: The possible and the attainable in RNA genotype-phenotype mapping. J. Theor. Biol. 194 4 (1998) 491-515
    • (1998) J. Theor. Biol. , vol.194 , Issue.4 , pp. 491-515
    • Fontana, W.1    Schuster, P.2
  • 29
    • 0028196714 scopus 로고
    • From sequences to shapes and back: A case study in RNA secondary structures
    • Schuster P., et al. From sequences to shapes and back: A case study in RNA secondary structures. Proc. Biol. Sci. 255 1344 (1994) 279-284
    • (1994) Proc. Biol. Sci. , vol.255 , Issue.1344 , pp. 279-284
    • Schuster, P.1
  • 30
    • 39149116322 scopus 로고    scopus 로고
    • The quest to understand protein folding
    • Itzhaki L., and Wolynes P. The quest to understand protein folding. Curr. Opin. Struct. Biol. 18 1 (2008) 1-3
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , Issue.1 , pp. 1-3
    • Itzhaki, L.1    Wolynes, P.2
  • 31
    • 0028929556 scopus 로고
    • Principles of protein folding-A perspective from simple exact models
    • Dill K.A., et al. Principles of protein folding-A perspective from simple exact models. Protein Sci. 4 4 (1995) 561-602
    • (1995) Protein Sci. , vol.4 , Issue.4 , pp. 561-602
    • Dill, K.A.1
  • 32
    • 0031059496 scopus 로고    scopus 로고
    • Theoretical studies of protein-folding thermodynamics and kinetics
    • Shakhnovich E.I. Theoretical studies of protein-folding thermodynamics and kinetics. Curr. Opin. Struct. Biol. 7 1 (1997) 29-40
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , Issue.1 , pp. 29-40
    • Shakhnovich, E.I.1
  • 33
    • 1842839788 scopus 로고    scopus 로고
    • Simulating protein evolution in sequence and structure space
    • Xia Y., and Levitt M. Simulating protein evolution in sequence and structure space. Curr. Opin. Struct. Biol. 14 2 (2004) 202-207
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , Issue.2 , pp. 202-207
    • Xia, Y.1    Levitt, M.2
  • 34
    • 0029883960 scopus 로고    scopus 로고
    • From structure to sequence and back again
    • Hinds D.A., and Levitt M. From structure to sequence and back again. J. Mol. Biol. 258 1 (1996) 201-209
    • (1996) J. Mol. Biol. , vol.258 , Issue.1 , pp. 201-209
    • Hinds, D.A.1    Levitt, M.2
  • 35
    • 0029063717 scopus 로고
    • The complexity and accuracy of discrete state models of protein structure
    • Park B.H., and Levitt M. The complexity and accuracy of discrete state models of protein structure. J. Mol. Biol. 249 2 (1995) 493-507
    • (1995) J. Mol. Biol. , vol.249 , Issue.2 , pp. 493-507
    • Park, B.H.1    Levitt, M.2
  • 36
    • 0034984144 scopus 로고    scopus 로고
    • Protein folding theory: From lattice to all-atom models
    • Mirny L., and Shakhnovich E. Protein folding theory: From lattice to all-atom models. Ann. Rev. Biophys. Biomol. Struct. 30 (2001) 361-396
    • (2001) Ann. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 361-396
    • Mirny, L.1    Shakhnovich, E.2
  • 37
    • 0036678845 scopus 로고    scopus 로고
    • Roles of mutation and recombination in the evolution of protein thermodynamics
    • Xia Y., and Levitt M. Roles of mutation and recombination in the evolution of protein thermodynamics. Proc. Natl. Acad. Sci. USA 99 16 (2002) 10382-10387
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.16 , pp. 10382-10387
    • Xia, Y.1    Levitt, M.2
  • 38
    • 1442324641 scopus 로고    scopus 로고
    • Funnel-like organization in sequence space determines the distributions of protein stability and folding rate preferred by evolution
    • Xia Y., and Levitt M. Funnel-like organization in sequence space determines the distributions of protein stability and folding rate preferred by evolution. Proteins 55 1 (2004) 107-114
    • (2004) Proteins , vol.55 , Issue.1 , pp. 107-114
    • Xia, Y.1    Levitt, M.2
  • 41
    • 36348992094 scopus 로고    scopus 로고
    • Robustness and evolvability: A paradox resolved
    • Wagner A. Robustness and evolvability: A paradox resolved. Proc. Biol. Sci. 275 1630 (2008) 91-100
    • (2008) Proc. Biol. Sci. , vol.275 , Issue.1630 , pp. 91-100
    • Wagner, A.1
  • 42
    • 33845487715 scopus 로고    scopus 로고
    • Balancing robustness and evolvability
    • Lenski R.E., Barrick J.E., and Ofria C. Balancing robustness and evolvability. PLoS Biol. 4 12 (2006) e428
    • (2006) PLoS Biol. , vol.4 , Issue.12
    • Lenski, R.E.1    Barrick, J.E.2    Ofria, C.3
  • 43
    • 33645811495 scopus 로고    scopus 로고
    • Protein stability promotes evolvability
    • Bloom J.D., et al. Protein stability promotes evolvability. Proc. Natl. Acad. Sci. USA 103 15 (2006) 5869-5874
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.15 , pp. 5869-5874
    • Bloom, J.D.1
  • 44
    • 1842835981 scopus 로고    scopus 로고
    • Stability and the evolvability of function in a model protein
    • Bloom J.D., et al. Stability and the evolvability of function in a model protein. Biophys. J. 86 5 (2004) 2758-2764
    • (2004) Biophys. J. , vol.86 , Issue.5 , pp. 2758-2764
    • Bloom, J.D.1
  • 45
    • 4143091655 scopus 로고    scopus 로고
    • Evolvability is a selectable trait
    • Earl D.J., and Deem M.W. Evolvability is a selectable trait. Proc. Natl. Acad. Sci. USA 101 32 (2004) 11531-11536
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.32 , pp. 11531-11536
    • Earl, D.J.1    Deem, M.W.2
  • 47
    • 0031933143 scopus 로고    scopus 로고
    • Determining the structures of large proteins and protein complexes by NMR
    • Clore G.M., and Gronenborn A.M. Determining the structures of large proteins and protein complexes by NMR. Trends Biotechnol. 16 1 (1998) 22-34
    • (1998) Trends Biotechnol. , vol.16 , Issue.1 , pp. 22-34
    • Clore, G.M.1    Gronenborn, A.M.2
  • 48
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein F.C., et al. The Protein Data Bank: A computer-based archival file for macromolecular structures. J. Mol. Biol. 112 3 (1977) 535-542
    • (1977) J. Mol. Biol. , vol.112 , Issue.3 , pp. 535-542
    • Bernstein, F.C.1
  • 49
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul S.F., et al. Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res. 25 17 (1997) 3389-3402
    • (1997) Nucleic Acids Res. , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1
  • 50
    • 85021467943 scopus 로고
    • Structure and function of haemoglobin II. Some relations between polypeptide chain configuration and amino acid sequence
    • Perutz M.F., Kendrew J.C., and Watson H.C. Structure and function of haemoglobin II. Some relations between polypeptide chain configuration and amino acid sequence. J. Mol. Biol. 13 (1965) 669-678
    • (1965) J. Mol. Biol. , vol.13 , pp. 669-678
    • Perutz, M.F.1    Kendrew, J.C.2    Watson, H.C.3
  • 51
    • 34047204789 scopus 로고    scopus 로고
    • Proportion of solvent-exposed amino acids in a protein and rate of protein evolution
    • Lin Y.S., et al. Proportion of solvent-exposed amino acids in a protein and rate of protein evolution. Mol. Biol. Evol. 24 4 (2007) 1005-1011
    • (2007) Mol. Biol. Evol. , vol.24 , Issue.4 , pp. 1005-1011
    • Lin, Y.S.1
  • 52
    • 34547153905 scopus 로고    scopus 로고
    • The selection of acceptable protein mutations
    • Sasidharan R., and Chothia C. The selection of acceptable protein mutations. Proc. Natl. Acad. Sci. USA 104 24 (2007) 10080-10085
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.24 , pp. 10080-10085
    • Sasidharan, R.1    Chothia, C.2
  • 53
    • 33749559644 scopus 로고    scopus 로고
    • Systematically assessing the influence of 3-dimensional structural context on the molecular evolution of mammalian proteomes
    • Choi S.S., Vallender E.J., and Lahn B.T. Systematically assessing the influence of 3-dimensional structural context on the molecular evolution of mammalian proteomes. Mol. Biol. Evol. 23 11 (2006) 2131-2133
    • (2006) Mol. Biol. Evol. , vol.23 , Issue.11 , pp. 2131-2133
    • Choi, S.S.1    Vallender, E.J.2    Lahn, B.T.3
  • 54
    • 0017227120 scopus 로고
    • Evolutionary processes and evolutionary noise at the molecular level. I. Functional density in proteins
    • Zuckerkandl E. Evolutionary processes and evolutionary noise at the molecular level. I. Functional density in proteins. J. Mol. Evol. 7 3 (1976) 167-183
    • (1976) J. Mol. Evol. , vol.7 , Issue.3 , pp. 167-183
    • Zuckerkandl, E.1
  • 55
    • 0041673352 scopus 로고    scopus 로고
    • Structural determinant of protein designability
    • England J.L., and Shakhnovich E.I. Structural determinant of protein designability. Phys. Rev. Lett. 90 21 (2003) 218101
    • (2003) Phys. Rev. Lett. , vol.90 , Issue.21 , pp. 218101
    • England, J.L.1    Shakhnovich, E.I.2
  • 56
    • 33748562538 scopus 로고    scopus 로고
    • Evolutionary constraints on yeast protein size
    • Warringer J., and Blomberg A. Evolutionary constraints on yeast protein size. BMC Evol. Biol. 6 (2006) 61
    • (2006) BMC Evol. Biol. , vol.6 , pp. 61
    • Warringer, J.1    Blomberg, A.2
  • 58
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff S., and Henikoff J.G. Amino acid substitution matrices from protein blocks. Proc. Natl. Acad. Sci. USA 89 22 (1992) 10915-10919
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , Issue.22 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 59
    • 0022180868 scopus 로고
    • Amino acid composition and the evolutionary rates of protein-coding genes
    • Graur D. Amino acid composition and the evolutionary rates of protein-coding genes. J. Mol. Evol. 22 1 (1985) 53-62
    • (1985) J. Mol. Evol. , vol.22 , Issue.1 , pp. 53-62
    • Graur, D.1
  • 60
    • 0034079112 scopus 로고    scopus 로고
    • Selective constraints, amino acid composition, and the rate of protein evolution
    • Tourasse N.J., and Li W.H. Selective constraints, amino acid composition, and the rate of protein evolution. Mol. Biol. Evol. 17 4 (2000) 656-664
    • (2000) Mol. Biol. Evol. , vol.17 , Issue.4 , pp. 656-664
    • Tourasse, N.J.1    Li, W.H.2
  • 61
    • 0036017388 scopus 로고    scopus 로고
    • Evolutionary rate heterogeneity in proteins with long disordered regions
    • Brown C.J., et al. Evolutionary rate heterogeneity in proteins with long disordered regions. J. Mol. Evol. 55 1 (2002) 104-110
    • (2002) J. Mol. Evol. , vol.55 , Issue.1 , pp. 104-110
    • Brown, C.J.1
  • 62
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright P.E., and Dyson H.J. Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm. J. Mol. Biol. 293 2 (1999) 321-331
    • (1999) J. Mol. Biol. , vol.293 , Issue.2 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 64
    • 22244450719 scopus 로고    scopus 로고
    • Protein families and their evolution-A structural perspective
    • Orengo C.A., and Thornton J.M. Protein families and their evolution-A structural perspective. Ann. Rev. Biochem. 74 (2005) 867-900
    • (2005) Ann. Rev. Biochem. , vol.74 , pp. 867-900
    • Orengo, C.A.1    Thornton, J.M.2
  • 65
    • 0035783055 scopus 로고    scopus 로고
    • On the evolution of protein folds: Are similar motifs in different protein folds the result of convergence, insertion, or relics of an ancient peptide world?
    • Lupas A.N., Ponting C.P., and Russell R.B. On the evolution of protein folds: Are similar motifs in different protein folds the result of convergence, insertion, or relics of an ancient peptide world?. J. Struct. Biol. 134 2-3 (2001) 191-203
    • (2001) J. Struct. Biol. , vol.134 , Issue.2-3 , pp. 191-203
    • Lupas, A.N.1    Ponting, C.P.2    Russell, R.B.3
  • 66
    • 0030777303 scopus 로고    scopus 로고
    • CATH-A hierarchic classification of protein domain structures
    • Orengo C.A., et al. CATH-A hierarchic classification of protein domain structures. Structure 5 8 (1997) 1093-1108
    • (1997) Structure , vol.5 , Issue.8 , pp. 1093-1108
    • Orengo, C.A.1
  • 67
    • 0037841804 scopus 로고    scopus 로고
    • Evolution of the protein repertoire
    • Chothia C., et al. Evolution of the protein repertoire. Science 300 5626 (2003) 1701-1703
    • (2003) Science , vol.300 , Issue.5626 , pp. 1701-1703
    • Chothia, C.1
  • 68
    • 26844454995 scopus 로고    scopus 로고
    • Domain rearrangements in protein evolution
    • Bjorklund A.K., et al. Domain rearrangements in protein evolution. J. Mol. Biol. 353 4 (2005) 911-923
    • (2005) J. Mol. Biol. , vol.353 , Issue.4 , pp. 911-923
    • Bjorklund, A.K.1
  • 69
    • 0032545151 scopus 로고    scopus 로고
    • Estimating the number of protein folds
    • Zhang C., and DeLisi C. Estimating the number of protein folds. J. Mol. Biol. 284 5 (1998) 1301-1305
    • (1998) J. Mol. Biol. , vol.284 , Issue.5 , pp. 1301-1305
    • Zhang, C.1    DeLisi, C.2
  • 70
    • 0037195119 scopus 로고    scopus 로고
    • Expanding protein universe and its origin from the biological Big Bang
    • Dokholyan N.V., Shakhnovich B., and Shakhnovich E.I. Expanding protein universe and its origin from the biological Big Bang. Proc. Natl. Acad. Sci. USA 99 22 (2002) 14132-14136
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.22 , pp. 14132-14136
    • Dokholyan, N.V.1    Shakhnovich, B.2    Shakhnovich, E.I.3
  • 71
    • 0015847566 scopus 로고
    • Mutation and evolution at the molecular level
    • Kimura M., and Ota T. Mutation and evolution at the molecular level. Genetics 73 Suppl 73 (1973) 19-35
    • (1973) Genetics , vol.73 , Issue.SUPPL. 73 , pp. 19-35
    • Kimura, M.1    Ota, T.2
  • 72
    • 0015162882 scopus 로고
    • The structures of cytochrome c and the rates of molecular evolution
    • Dickerson R.E. The structures of cytochrome c and the rates of molecular evolution. J. Mol. Evol. 1 1 (1971) 26-45
    • (1971) J. Mol. Evol. , vol.1 , Issue.1 , pp. 26-45
    • Dickerson, R.E.1
  • 73
    • 0035178383 scopus 로고    scopus 로고
    • Protein-protein interfaces: Analysis of amino acid conservation in homodimers
    • Valdar W.S., and Thornton J.M. Protein-protein interfaces: Analysis of amino acid conservation in homodimers. Proteins 42 1 (2001) 108-124
    • (2001) Proteins , vol.42 , Issue.1 , pp. 108-124
    • Valdar, W.S.1    Thornton, J.M.2
  • 74
    • 0016197604 scopus 로고
    • Amino acid difference formula to help explain protein evolution
    • Grantham R. Amino acid difference formula to help explain protein evolution. Science 185 4154 (1974) 862-864
    • (1974) Science , vol.185 , Issue.4154 , pp. 862-864
    • Grantham, R.1
  • 75
    • 0346733329 scopus 로고    scopus 로고
    • Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?
    • Caffrey D.R., et al. Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?. Protein Sci. 13 1 (2004) 190-202
    • (2004) Protein Sci. , vol.13 , Issue.1 , pp. 190-202
    • Caffrey, D.R.1
  • 76
    • 23344451687 scopus 로고    scopus 로고
    • Structure, function, and evolution of transient and obligate protein-protein interactions
    • Mintseris J., and Weng Z. Structure, function, and evolution of transient and obligate protein-protein interactions. Proc. Natl. Acad. Sci. USA 102 31 (2005) 10930-10935
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.31 , pp. 10930-10935
    • Mintseris, J.1    Weng, Z.2
  • 77
    • 27944493925 scopus 로고    scopus 로고
    • Scale-free networks in cell biology
    • Albert R. Scale-free networks in cell biology. J. Cell. Sci. 118 Pt 21 (2005) 4947-4957
    • (2005) J. Cell. Sci. , vol.118 , Issue.PART 21 , pp. 4947-4957
    • Albert, R.1
  • 78
    • 0842291785 scopus 로고    scopus 로고
    • No simple dependence between protein evolution rate and the number of protein-protein interactions: Only the most prolific interactors tend to evolve slowly
    • Jordan I.K., Wolf Y.I., and Koonin E.V. No simple dependence between protein evolution rate and the number of protein-protein interactions: Only the most prolific interactors tend to evolve slowly. BMC Evol. Biol. 3 (2003) 1
    • (2003) BMC Evol. Biol. , vol.3 , pp. 1
    • Jordan, I.K.1    Wolf, Y.I.2    Koonin, E.V.3
  • 79
    • 3042848952 scopus 로고    scopus 로고
    • Evidence for dynamically organized modularity in the yeast protein-protein interaction network
    • Han J.D., et al. Evidence for dynamically organized modularity in the yeast protein-protein interaction network. Nature 430 6995 (2004) 88-93
    • (2004) Nature , vol.430 , Issue.6995 , pp. 88-93
    • Han, J.D.1
  • 80
    • 33644550021 scopus 로고    scopus 로고
    • Structural systems biology: Modelling protein interactions
    • Aloy P., and Russell R.B. Structural systems biology: Modelling protein interactions. Nat. Rev. Mol. Cell. Biol. 7 3 (2006) 188-197
    • (2006) Nat. Rev. Mol. Cell. Biol. , vol.7 , Issue.3 , pp. 188-197
    • Aloy, P.1    Russell, R.B.2
  • 81
    • 33845875196 scopus 로고    scopus 로고
    • Relating three-dimensional structures to protein networks provides evolutionary insights
    • Kim P.M., et al. Relating three-dimensional structures to protein networks provides evolutionary insights. Science 314 5807 (2006) 1938-1941
    • (2006) Science , vol.314 , Issue.5807 , pp. 1938-1941
    • Kim, P.M.1
  • 82
    • 0037177560 scopus 로고    scopus 로고
    • Evolutionary rate in the protein interaction network
    • Fraser H.B., et al. Evolutionary rate in the protein interaction network. Science 296 5568 (2002) 750-752
    • (2002) Science , vol.296 , Issue.5568 , pp. 750-752
    • Fraser, H.B.1
  • 83
    • 50649096663 scopus 로고    scopus 로고
    • Analyzing protein interaction networks using structural information
    • Kiel C., Beltrao P., and Serrano L. Analyzing protein interaction networks using structural information. Ann. Rev. Biochem. (2008)
    • (2008) Ann. Rev. Biochem. , pp. 0
    • Kiel, C.1    Beltrao, P.2    Serrano, L.3
  • 84
    • 0036799752 scopus 로고    scopus 로고
    • Inferring domain-domain interactions from protein-protein interactions
    • Deng M., et al. Inferring domain-domain interactions from protein-protein interactions. Genome Res. 12 10 (2002) 1540-1548
    • (2002) Genome Res. , vol.12 , Issue.10 , pp. 1540-1548
    • Deng, M.1
  • 85
    • 34248576303 scopus 로고    scopus 로고
    • Functional evaluation of domain-domain interactions and human protein interaction networks
    • Schlicker A., et al. Functional evaluation of domain-domain interactions and human protein interaction networks. Bioinformatics 23 7 (2007) 859-865
    • (2007) Bioinformatics , vol.23 , Issue.7 , pp. 859-865
    • Schlicker, A.1
  • 86
    • 34548780821 scopus 로고    scopus 로고
    • Prediction of Ras-effector interactions using position energy matrices
    • Kiel C., and Serrano L. Prediction of Ras-effector interactions using position energy matrices. Bioinformatics 23 17 (2007) 2226-2230
    • (2007) Bioinformatics , vol.23 , Issue.17 , pp. 2226-2230
    • Kiel, C.1    Serrano, L.2
  • 87
    • 33748074139 scopus 로고    scopus 로고
    • Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes
    • Haynes C., et al. Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes. PLoS Comput. Biol. 2 8 (2006) e100
    • (2006) PLoS Comput. Biol. , vol.2 , Issue.8
    • Haynes, C.1
  • 88
    • 41149119083 scopus 로고    scopus 로고
    • The role of disorder in interaction networks: A structural analysis
    • Kim P.M., et al. The role of disorder in interaction networks: A structural analysis. Mol. Syst. Biol. 4 (2008) 179
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 179
    • Kim, P.M.1
  • 89
    • 0038157152 scopus 로고    scopus 로고
    • Dosage sensitivity and the evolution of gene families in yeast
    • Papp B., Pal C., and Hurst L.D. Dosage sensitivity and the evolution of gene families in yeast. Nature 424 6945 (2003) 194-197
    • (2003) Nature , vol.424 , Issue.6945 , pp. 194-197
    • Papp, B.1    Pal, C.2    Hurst, L.D.3
  • 90
    • 0035782661 scopus 로고    scopus 로고
    • Review: protein design-Where we were, where we are, where we're going
    • Pokala N., and Handel T.M. Review: protein design-Where we were, where we are, where we're going. J. Struct. Biol. 134 2-3 (2001) 269-281
    • (2001) J. Struct. Biol. , vol.134 , Issue.2-3 , pp. 269-281
    • Pokala, N.1    Handel, T.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.