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Volumn 2, Issue 1, 2014, Pages 128-153

Dynamic new world: Refining our view of protein structure, function and evolution

Author keywords

Evolution; Function; Intrinsically disordered; Promiscuity; Protein dynamism; Structure

Indexed keywords


EID: 84983346463     PISSN: None     EISSN: 22277382     Source Type: Journal    
DOI: 10.3390/proteomes2010128     Document Type: Review
Times cited : (19)

References (165)
  • 7
    • 70349503591 scopus 로고    scopus 로고
    • Biophysics of Parkinsons Disease: Structure and Aggregation of-Synuclein
    • Uversky, V.N.; Eliezer, D. Biophysics of Parkinsons Disease: Structure and Aggregation of-Synuclein. Curr. Protein Pept. Sci. 2009, 10, 483-499
    • (2009) Curr. Protein Pept. Sci , vol.10 , pp. 483-499
    • Uversky, V.N.1    Eliezer, D.2
  • 8
    • 67650385638 scopus 로고    scopus 로고
    • Protein disorder in the human diseasome: Unfoldomics of human genetic diseases
    • Midic, U.; Oldfield, C.J.; Dunker, A.K.; Obradovic, Z.; Uversky, V.N. Protein disorder in the human diseasome: Unfoldomics of human genetic diseases. BMC Genomics 2009, 10, S12
    • (2009) BMC Genomics , vol.10 , pp. S12
    • Midic, U.1    Oldfield, C.J.2    Dunker, A.K.3    Obradovic, Z.4    Uversky, V.N.5
  • 9
    • 0141858715 scopus 로고    scopus 로고
    • The specificity of cross-reactivity: Promiscuous antibody binding involves specific hydrogen bonds rather than nonspecific hydrophobic stickiness
    • James, L.C.; Tawfik, D.S. The specificity of cross-reactivity: Promiscuous antibody binding involves specific hydrogen bonds rather than nonspecific hydrophobic stickiness. Protein Sci. 2003, 12, 2183-2193
    • (2003) Protein Sci , vol.12 , pp. 2183-2193
    • James, L.C.1    Tawfik, D.S.2
  • 10
    • 78649986101 scopus 로고    scopus 로고
    • From 'fluctuation fit' to 'conformational selection': Evolution, rediscovery, and integration of a concept
    • Vértessy, B.G.; Orosz, F. From 'fluctuation fit' to 'conformational selection': Evolution, rediscovery, and integration of a concept. Bioessays 2011, 33, 30-34
    • (2011) Bioessays , vol.33 , pp. 30-34
    • Vértessy, B.G.1    Orosz, F.2
  • 12
    • 33947445379 scopus 로고
    • A theory of the structure and process of formation of antibodies*
    • Pauling, L. A theory of the structure and process of formation of antibodies*. J. Am. Chem. Soc. 1940, 62, 2643-2657
    • (1940) J. Am. Chem. Soc , vol.62 , pp. 2643-2657
    • Pauling, L.1
  • 13
    • 0033117461 scopus 로고    scopus 로고
    • Catalytic promiscuity and the evolution of new enzymatic activities
    • O'Brien, P.J.; Herschlag, D. Catalytic promiscuity and the evolution of new enzymatic activities. Chem. Biol. 1999, 6, R91-R105
    • (1999) Chem. Biol , vol.6 , pp. R91-R105
    • O'Brien, P.J.1    Herschlag, D.2
  • 14
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V.N. Natively unfolded proteins: A point where biology waits for physics. Protein Sci. 2002, 11, 739-756
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 15
    • 68749093787 scopus 로고    scopus 로고
    • Predicting intrinsic disorder in proteins: An overview
    • He, B.; Wang, K.; Liu, Y.; Xue, B.; Uversky, V.N.; Dunker, A.K. Predicting intrinsic disorder in proteins: An overview. Cell Res. 2009, 19, 929-949
    • (2009) Cell Res , vol.19 , pp. 929-949
    • He, B.1    Wang, K.2    Liu, Y.3    Xue, B.4    Uversky, V.N.5    Dunker, A.K.6
  • 16
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution-A 60-year-old hypothesis revisited
    • James, L.C.; Tawfik, D.S. Conformational diversity and protein evolution-A 60-year-old hypothesis revisited. Trends Biochem. Sci. 2003, 28, 361-368
    • (2003) Trends Biochem. Sci , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 17
    • 64849101493 scopus 로고    scopus 로고
    • Protein dynamism and evolvability
    • Tokuriki, N.; Tawfik, D.S. Protein dynamism and evolvability. Science 2009, 324, 203-207
    • (2009) Science , vol.324 , pp. 203-207
    • Tokuriki, N.1    Tawfik, D.S.2
  • 18
    • 82655175850 scopus 로고    scopus 로고
    • The relationship between proteome size, structural disorder and organism complexity
    • Schad, E.; Tompa, P.; Hegyi, H. The relationship between proteome size, structural disorder and organism complexity. Genome Biol. 2011, 12, R120
    • (2011) Genome Biol , vol.12 , pp. R120
    • Schad, E.1    Tompa, P.2    Hegyi, H.3
  • 19
    • 0037396292 scopus 로고    scopus 로고
    • Enzymes with extra talents: Moonlighting functions and catalytic promiscuity
    • Copley, S.D. Enzymes with extra talents: Moonlighting functions and catalytic promiscuity. Curr. Opin. Chem. Biol. 2003, 7, 265-272
    • (2003) Curr. Opin. Chem. Biol , vol.7 , pp. 265-272
    • Copley, S.D.1
  • 20
  • 23
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: Introducing the D2 concept
    • Uversky, V.N.; Oldfield, C.J.; Dunker, A.K. Intrinsically disordered proteins in human diseases: Introducing the D2 concept. Annu. Rev. Biophys. 2008, 37, 215-246
    • (2008) Annu. Rev. Biophys , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 24
    • 79958741408 scopus 로고    scopus 로고
    • Intrinsically disordered proteins from A to Z
    • Uversky, V.N. Intrinsically disordered proteins from A to Z. Int. J. Biochem. Cell Biol. 2011, 43, 1090-1103
    • (2011) Int. J. Biochem. Cell Biol , vol.43 , pp. 1090-1103
    • Uversky, V.N.1
  • 25
    • 67650287695 scopus 로고    scopus 로고
    • In the light of directed evolution: Pathways of adaptive protein evolution
    • Bloom, J.D.; Arnold, F.H. In the light of directed evolution: Pathways of adaptive protein evolution. Proc. Natl. Acad. Sci. USA 2009, 106, 9995-10000
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 9995-10000
    • Bloom, J.D.1    Arnold, F.H.2
  • 27
    • 76549252207 scopus 로고
    • The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain
    • Pauling, L.; Corey, R.B.; Branson, H.R. The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain. Proc. Natl. Acad. Sci. USA 1951, 37, 205-211
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 29
    • 0141817701 scopus 로고    scopus 로고
    • The discovery of the α-helix and β-sheet, the principal structural features of proteins
    • Eisenberg, D. The discovery of the α-helix and β-sheet, the principal structural features of proteins. Proc. Natl. Acad. Sci. USA 2003, 100, 11207-11210
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11207-11210
    • Eisenberg, D.1
  • 30
    • 85054282241 scopus 로고    scopus 로고
    • [27] adhered to basic but still relatively new chemical principles such as planarity of the amide bond within each amino acid and linear hydrogen bonding rules (notions that were omitted in a previously failed attempt a year earlier by luminaries Bragg, Kendrew, and Perutz [28])
    • Pauling et al. [27] adhered to basic but still relatively new chemical principles such as planarity of the amide bond within each amino acid and linear hydrogen bonding rules (notions that were omitted in a previously failed attempt a year earlier by luminaries Bragg, Kendrew, and Perutz [28])
    • Pauling1
  • 31
    • 0001266102 scopus 로고
    • A three-dimensional model of the myoglobin molecule obtained by X-ray analysis
    • Kendrew, J.C.; Bodo, G.; Dintzis, H.M.; Parrish, R.G.; Wyckoff, H.; Phillips, D.C. A three-dimensional model of the myoglobin molecule obtained by X-ray analysis. Nature 1958, 181, 662-666
    • (1958) Nature , vol.181 , pp. 662-666
    • Kendrew, J.C.1    Bodo, G.2    Dintzis, H.M.3    Parrish, R.G.4    Wyckoff, H.5    Phillips, D.C.6
  • 32
    • 0000893108 scopus 로고
    • Studies on the reduction and re-formation of protein disulfide bonds
    • Anfinsen, C.B.; Haber, E. Studies on the reduction and re-formation of protein disulfide bonds. J. Biol. Chem. 1961, 236, 1361-1363
    • (1961) J. Biol. Chem , vol.236 , pp. 1361-1363
    • Anfinsen, C.B.1    Haber, E.2
  • 33
    • 84892166712 scopus 로고
    • Einfluss der configuration auf die wirkung der enzyme
    • Fischer, E. Einfluss der configuration auf die wirkung der enzyme. Ber. Dt. Chem. Ges. 1894, 27, 2985-2993
    • (1894) Ber. Dt. Chem. Ges , vol.27 , pp. 2985-2993
    • Fischer, E.1
  • 35
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland, D., Jr. Application of a theory of enzyme specificity to protein synthesis. Proc. Natl. Acad. Sci. USA 1958, 44, 98-104
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland, D.1
  • 38
    • 1342302339 scopus 로고    scopus 로고
    • Conformational changes associated with protein-protein interactions
    • Goh, C.S.; Milburn, D.; Gerstein, M. Conformational changes associated with protein-protein interactions. Curr. Opin. Struct. Biol. 2004, 14, 104-109
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 104-109
    • Goh, C.S.1    Milburn, D.2    Gerstein, M.3
  • 39
    • 85054261852 scopus 로고    scopus 로고
    • Kendrew's structure [31] predated the Protein Databank [36]; however, Watson and Kendrew eventually deposited into the PDB a refined version of the original structure in 1973; PDB ID: 1MBN
    • Kendrew's structure [31] predated the Protein Databank [36]; however, Watson and Kendrew eventually deposited into the PDB a refined version of the original structure in 1973; PDB ID: 1MBN
  • 40
    • 85054230579 scopus 로고    scopus 로고
    • For example, the first decade of structure deposition in the PDB-the 1970's-witnessed only one of 92 deposited protein chains (PDB ID 1CHG, chain A) that displayed a substantial number of residues (>5%) with missing backbone coordinates
    • For example, the first decade of structure deposition in the PDB-the 1970's-witnessed only one of 92 deposited protein chains (PDB ID 1CHG, chain A) that displayed a substantial number of residues (>5%) with missing backbone coordinates
  • 41
    • 33751206245 scopus 로고    scopus 로고
    • Widening the protein crystallization bottleneck
    • Doerr, A. Widening the protein crystallization bottleneck. Nat. Methods 2006, 3, 961
    • (2006) Nat. Methods , vol.3 , pp. 961
    • Doerr, A.1
  • 44
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • Karplus, M.; McCammon, J.A. Molecular dynamics simulations of biomolecules. Nat. Struct. Biol. 2002, 9, 646-652
    • (2002) Nat. Struct. Biol , vol.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 48
    • 84941522332 scopus 로고
    • Chemische untersuchung des präzipitates aus Hämoglobin und anti-Hämoglobin-serum und bemerkungen über die natur der antikörper
    • Breinl, F.; Haurowitz, F. Chemische untersuchung des präzipitates aus Hämoglobin und anti-Hämoglobin-serum und bemerkungen über die natur der antikörper. Hoppe-Seyler's Z. Physiol. Chem. 1930, 192, 45-57
    • (1930) Hoppe-Seyler's Z. Physiol. Chem , vol.192 , pp. 45-57
    • Breinl, F.1    Haurowitz, F.2
  • 49
    • 34250573136 scopus 로고
    • Some intracellular aspects of life and disease
    • Alexander, J. Some intracellular aspects of life and disease. Protoplasma 1932, 14, 296-306
    • (1932) Protoplasma , vol.14 , pp. 296-306
    • Alexander, J.1
  • 50
    • 0004441746 scopus 로고
    • A hypothetical mechanism of antibody formation
    • Mudd, S. A hypothetical mechanism of antibody formation. J. Immunol. 1932, 23, 423-427
    • (1932) J. Immunol , vol.23 , pp. 423-427
    • Mudd, S.1
  • 51
    • 0018172628 scopus 로고
    • Internal motion in globular proteins
    • Wüthrich, K.; Wagner, G. Internal motion in globular proteins. Trends Biochem. Sci. 1978, 3, 227-230
    • (1978) Trends Biochem. Sci , vol.3 , pp. 227-230
    • Wüthrich, K.1    Wagner, G.2
  • 54
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P.E.; Dyson, H.J. Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm. J. Mol. Biol. 1999, 293, 321-331
    • (1999) J. Mol. Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 56
  • 57
    • 0141861067 scopus 로고    scopus 로고
    • Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: Which way to go?
    • Uversky, V.N. Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: Which way to go? Cell. Mol. Life Sci. 2003, 60, 1852-1871
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 1852-1871
    • Uversky, V.N.1
  • 58
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink, A.L. Natively unfolded proteins. Curr. Opin. Struct. Biol. 2005, 15, 35-41
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 59
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H.J.; Wright, P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 2005, 6, 197-208
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 64
    • 0034669882 scopus 로고    scopus 로고
    • Why are 'natively unfolded' proteins unstructured under physiologic conditions
    • Uversky, V.N.; Gillespie, J.R.; Fink, A.L. Why are 'natively unfolded' proteins unstructured under physiologic conditions? Proteins 2000, 41, 415-427
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 66
    • 77950957385 scopus 로고    scopus 로고
    • Bioinformatical approaches to characterize intrinsically disordered/unstructured proteins
    • Dosztnyi, Z.; Mszros, B.; Simon, I. Bioinformatical approaches to characterize intrinsically disordered/unstructured proteins. Brief. Bioinform. 2010, 11, 225-243
    • (2010) Brief. Bioinform , vol.11 , pp. 225-243
    • Dosztnyi, Z.1    Mszros, B.2    Simon, I.3
  • 67
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa, P. The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett. 2005, 579, 3346-3354
    • (2005) FEBS Lett , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 68
    • 67650045816 scopus 로고    scopus 로고
    • Limitations of induced folding in molecular recognition by intrinsically disordered proteins
    • Hazy, E.; Tompa, P. Limitations of induced folding in molecular recognition by intrinsically disordered proteins. ChemPhysChem 2009, 10, 1415-1419
    • (2009) ChemPhysChem , vol.10 , pp. 1415-1419
    • Hazy, E.1    Tompa, P.2
  • 69
    • 79957878205 scopus 로고    scopus 로고
    • Proteins without 3D structure: Definition, detection and beyond
    • Orosz, F.; Ovádi, J. Proteins without 3D structure: Definition, detection and beyond. Bioinformatics 2011, 27, 1449-1454
    • (2011) Bioinformatics , vol.27 , pp. 1449-1454
    • Orosz, F.1    Ovádi, J.2
  • 71
    • 79958044914 scopus 로고    scopus 로고
    • Unstructural biology coming of age
    • Tompa, P. Unstructural biology coming of age. Curr. Opin. Struct. Biol. 2011, 21, 419-425
    • (2011) Curr. Opin. Struct. Biol , vol.21 , pp. 419-425
    • Tompa, P.1
  • 72
  • 73
    • 0000613310 scopus 로고
    • Zinc fingers: A novel protein motif for nucleic acid recognition
    • Klug, A.; Rhodes, D. Zinc fingers: A novel protein motif for nucleic acid recognition. Trends Biochem. Sci. 1987, 12, 464-469
    • (1987) Trends Biochem. Sci , vol.12 , pp. 464-469
    • Klug, A.1    Rhodes, D.2
  • 74
    • 0035253047 scopus 로고    scopus 로고
    • Zinc finger proteins: New insights into structural and functional diversity
    • Laity, J.H.; Lee, B.M.; Wright, P.E. Zinc finger proteins: New insights into structural and functional diversity. Curr. Opin. Struct. Biol. 2001, 11, 39-46
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 39-46
    • Laity, J.H.1    Lee, B.M.2    Wright, P.E.3
  • 75
    • 33644748247 scopus 로고    scopus 로고
    • Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination
    • Liu, Y.; Liao, J.; Zhu, B.;Wang, E.; Ding, J. Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination. Biochem. J. 2006, 394, 399-407
    • (2006) Biochem. J , vol.394 , pp. 399-407
    • Liu, Y.1    Liao, J.2    Zhu, B.3    Wang, E.4    Ding, J.5
  • 79
    • 46649120886 scopus 로고    scopus 로고
    • Crystal structure of yeast hexokinase PI in complex with glucose: A classical 'induced fit' example revised
    • Kuser, P.; Cupri, F.; Bleicher, L.; Polikarpov, I. Crystal structure of yeast hexokinase PI in complex with glucose: A classical 'induced fit' example revised. Proteins: Struct. Funct. Bioinform. 2008, 72, 731-740
    • (2008) Proteins: Struct. Funct. Bioinform , vol.72 , pp. 731-740
    • Kuser, P.1    Cupri, F.2    Bleicher, L.3    Polikarpov, I.4
  • 80
    • 0025340754 scopus 로고
    • Induced-fit movements in adenylate kinases
    • Schulz, G.E.; Müller, C.W.; Diederichs, K. Induced-fit movements in adenylate kinases. J. Mol. Biol. 1990, 213, 627-630
    • (1990) J. Mol. Biol , vol.213 , pp. 627-630
    • Schulz, G.E.1    Müller, C.W.2    Diederichs, K.3
  • 81
    • 84868090870 scopus 로고    scopus 로고
    • Ubiquitin dynamics in complexes reveal molecular recognition mechanisms beyond induced fit and conformational selection
    • Peters, J.H.; de Groot, B.L. Ubiquitin dynamics in complexes reveal molecular recognition mechanisms beyond induced fit and conformational selection. PLoS Comput. Biol. 2012, 8, e1002704
    • (2012) PLoS Comput. Biol , vol.8
    • Peters, J.H.1    de Groot, B.L.2
  • 82
    • 34250001164 scopus 로고    scopus 로고
    • Binding induced conformational changes of proteins correlate with their intrinsic fluctuations: A case study of antibodies
    • Keskin, O. Binding induced conformational changes of proteins correlate with their intrinsic fluctuations: A case study of antibodies. BMC Struct. Biol. 2007, 7, e31
    • (2007) BMC Struct. Biol , vol.7
    • Keskin, O.1
  • 83
    • 0037154116 scopus 로고    scopus 로고
    • Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1)
    • Bienkiewicz, E.A.; Adkins, J.N.; Lumb, K.J. Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1). Biochemistry 2002, 41, 752-759
    • (2002) Biochemistry , vol.41 , pp. 752-759
    • Bienkiewicz, E.A.1    Adkins, J.N.2    Lumb, K.J.3
  • 84
    • 0037627721 scopus 로고    scopus 로고
    • Simulating disorder-order transitions in molecular recognition of unstructured proteins: Where folding meets binding
    • Verkhivker, G.M.; Bouzida, D.; Gehlhaar, D.K.; Rejto, P.A.; Freer, S.T.; Rose, P.W. Simulating disorder-order transitions in molecular recognition of unstructured proteins: Where folding meets binding. Proc. Natl. Acad. Sci. USA 2003, 100, 5148-5153
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5148-5153
    • Verkhivker, G.M.1    Bouzida, D.2    Gehlhaar, D.K.3    Rejto, P.A.4    Freer, S.T.5    Rose, P.W.6
  • 88
    • 84859494186 scopus 로고    scopus 로고
    • Fuzzy complexes: A more stochastic view of protein function
    • Fuxreiter, M.; Tompa, P. Fuzzy complexes: A more stochastic view of protein function. Adv. Exp. Med. Biol. 2012, 725, 1-14
    • (2012) Adv. Exp. Med. Biol , vol.725 , pp. 1-14
    • Fuxreiter, M.1    Tompa, P.2
  • 89
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions
    • Tompa, P.; Fuxreiter, M. Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions. Trends Biochem. Sci. 2008, 33, 2-8
    • (2008) Trends Biochem. Sci , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 90
    • 0037470496 scopus 로고    scopus 로고
    • Antibody multispecificity mediated by conformational diversity
    • James, L.C.; Roversi, P.; Tawfik, D.S. Antibody multispecificity mediated by conformational diversity. Science 2003, 299, 1362-1367
    • (2003) Science , vol.299 , pp. 1362-1367
    • James, L.C.1    Roversi, P.2    Tawfik, D.S.3
  • 91
    • 77957228360 scopus 로고
    • Chapter Remarks on the Dynamic Aspects of Enzyme Structure (in Russian): Nauka, Moscow
    • Straub, F.B.; Szabolcsi, G. Molecular Biology: Problems and Perspectives; Chapter Remarks on the Dynamic Aspects of Enzyme Structure (in Russian): Nauka, Moscow, 1964; pp. 182-187
    • (1964) Molecular Biology: Problems and Perspectives , pp. 182-187
    • Straub, F.B.1    Szabolcsi, G.2
  • 93
    • 44949167588 scopus 로고    scopus 로고
    • Entropic contributions and the influence of the hydrophobic environment in promiscuous protein-protein association
    • Chang, C.E.A.; McLaughlin, W.A.; Baron, R.; Wang, W.; McCammon, J.A. Entropic contributions and the influence of the hydrophobic environment in promiscuous protein-protein association. Proc. Natl. Acad. Sci. USA 2008, 105, 7456-7461
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7456-7461
    • Chang, C.E.A.1    McLaughlin, W.A.2    Baron, R.3    Wang, W.4    McCammon, J.A.5
  • 94
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme promiscuity: A mechanistic and evolutionary perspective
    • Khersonsky, O.; Tawfik, D.S. Enzyme promiscuity: A mechanistic and evolutionary perspective. Annu. Rev. Biochem. 2010, 79, 471-505
    • (2010) Annu. Rev. Biochem , vol.79 , pp. 471-505
    • Khersonsky, O.1    Tawfik, D.S.2
  • 95
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker, B.A.; Portman, J.J.; Wolynes, P.G. Speeding molecular recognition by using the folding funnel: The fly-casting mechanism. Proc. Natl. Acad. Sci. USA 2000, 97, 8868-8873
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 96
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • Sugase, K.; Dyson, H.J.; Wright, P.E. Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 2007, 447, 1021-1025
    • (2007) Nature , vol.447 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 97
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • Fuxreiter, M.; Simon, I.; Friedrich, P.; Tompa, P. Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. J. Mol. Biol. 2004, 338, 1015-1026
    • (2004) J. Mol. Biol , vol.338 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 99
    • 70350012289 scopus 로고    scopus 로고
    • Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: A critical assessment of the 'fly-casting' mechanism
    • Huang, Y.; Liu, Z. Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: A critical assessment of the 'fly-casting' mechanism. J. Mol. Biol. 2009, 393, 1143-1159
    • (2009) J. Mol. Biol , vol.393 , pp. 1143-1159
    • Huang, Y.1    Liu, Z.2
  • 100
    • 77949587817 scopus 로고    scopus 로고
    • From induced fit to conformational selection: A continuum of binding mechanism controlled by the timescale of conformational transitions
    • Zhou, H.X. From induced fit to conformational selection: A continuum of binding mechanism controlled by the timescale of conformational transitions. Biophys. J. 2010, 98, L15-L17
    • (2010) Biophys. J , vol.98 , pp. L15-L17
    • Zhou, H.X.1
  • 101
    • 77957231785 scopus 로고    scopus 로고
    • Induced fit, conformational selection and independent dynamic segments: An extended view of binding events
    • Csermely, P.; Palotai, R.; Nussinov, R. Induced fit, conformational selection and independent dynamic segments: An extended view of binding events. Trends Biochem. Sci. 2010, 35, 539-546
    • (2010) Trends Biochem. Sci , vol.35 , pp. 539-546
    • Csermely, P.1    Palotai, R.2    Nussinov, R.3
  • 102
    • 84862274751 scopus 로고    scopus 로고
    • Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly
    • Fermani, S.; Trivelli, X.; Sparla, F.; Thumiger, A.; Calvaresi, M.; Marri, L.; Falini, G.; Zerbetto, F.; Trost, P. Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly. J. Biol. Chem. 2012, 287, 21372-21383
    • (2012) J. Biol. Chem , vol.287 , pp. 21372-21383
    • Fermani, S.1    Trivelli, X.2    Sparla, F.3    Thumiger, A.4    Calvaresi, M.5    Marri, L.6    Falini, G.7    Zerbetto, F.8    Trost, P.9
  • 103
    • 84885065793 scopus 로고    scopus 로고
    • Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein
    • Wang, Y.; Chu, X.; Longhi, S.; Roche, P.; Han, W.; Wang, E.; Wang, J. Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein. Proc. Natl. Acad. Sci. USA 2013, 110, E3743-E3752
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. E3743-E3752
    • Wang, Y.1    Chu, X.2    Longhi, S.3    Roche, P.4    Han, W.5    Wang, E.6    Wang, J.7
  • 104
    • 82655180384 scopus 로고    scopus 로고
    • Fuzziness: Linking regulation to protein dynamics
    • Fuxreiter, M. Fuzziness: Linking regulation to protein dynamics. Mol. Biosyst. 2012, 8, 168-177
    • (2012) Mol. Biosyst , vol.8 , pp. 168-177
    • Fuxreiter, M.1
  • 105
    • 32444442870 scopus 로고    scopus 로고
    • The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway
    • Bhattacharyya, R.P.; Remnyi, A.; Good, M.C.; Bashor, C.J.; Falick, A.M.; Lim, W.A. The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway. Science 2006, 311, 822-826
    • (2006) Science , vol.311 , pp. 822-826
    • Bhattacharyya, R.P.1    Remnyi, A.2    Good, M.C.3    Bashor, C.J.4    Falick, A.M.5    Lim, W.A.6
  • 106
    • 59849106371 scopus 로고    scopus 로고
    • Protein promiscuity and its implications for biotechnology
    • Nobeli, I.; Favia, A.D.; Thornton, J.M. Protein promiscuity and its implications for biotechnology. Nat. Biotechnol. 2009, 27, 157-167
    • (2009) Nat. Biotechnol , vol.27 , pp. 157-167
    • Nobeli, I.1    Favia, A.D.2    Thornton, J.M.3
  • 107
    • 85054239375 scopus 로고    scopus 로고
    • s findings, a protein with high net charge magnitude (R) could remain folded if it were countered by high hydrophobicity (H; on a Kyte-Doolittle scale normalized to range between 0 and 1[64]); accordingly, the remarkable boundary line on the H-R landscape that distinguishes folding vs. disordered proteins was reported [64] to be: hRi = 2:785hHi-1:151
    • From Uversky et al.'s findings, a protein with high net charge magnitude (R) could remain folded if it were countered by high hydrophobicity (H; on a Kyte-Doolittle scale normalized to range between 0 and 1[64]); accordingly, the remarkable boundary line on the H-R landscape that distinguishes folding vs. disordered proteins was reported [64] to be: hRi = 2:785hHi-1:151
  • 109
    • 33645691679 scopus 로고    scopus 로고
    • Evolution of hormone-receptor complexity by molecular exploitation
    • Bridgham, J.T.; Carroll, S.M.; Thornton, J.W. Evolution of hormone-receptor complexity by molecular exploitation. Science 2006, 312, 97-101
    • (2006) Science , vol.312 , pp. 97-101
    • Bridgham, J.T.1    Carroll, S.M.2    Thornton, J.W.3
  • 110
    • 33645668076 scopus 로고    scopus 로고
    • Reducible complexity
    • Adami, C. Reducible complexity. Science 2006, 312, 61-63
    • (2006) Science , vol.312 , pp. 61-63
    • Adami, C.1
  • 111
    • 31944447797 scopus 로고    scopus 로고
    • Transcriptional regulators a la carte: Engineering new effector specificities in bacterial regulatory proteins
    • Galvão, T.C.; de Lorenzo, V. Transcriptional regulators a la carte: Engineering new effector specificities in bacterial regulatory proteins. Curr. Opin. Biotechnol. 2006, 17, 34-42
    • (2006) Curr. Opin. Biotechnol , vol.17 , pp. 34-42
    • Galvão, T.C.1    de Lorenzo, V.2
  • 112
    • 0001895697 scopus 로고
    • Evolutionary divergence and convergence in proteins
    • Zuckerkandl, E.; Pauling, L. Evolutionary divergence and convergence in proteins. Evol. Genes Proteins 1965, 97, 97-166
    • (1965) Evol. Genes Proteins , vol.97 , pp. 97-166
    • Zuckerkandl, E.1    Pauling, L.2
  • 114
    • 0001753988 scopus 로고
    • Primary structure and evolution of cytochrome C
    • Marigoliash, E. Primary structure and evolution of cytochrome C. Proc. Natl. Acad. Sci. USA 1963, 50, 672-679
    • (1963) Proc. Natl. Acad. Sci. USA , vol.50 , pp. 672-679
    • Marigoliash, E.1
  • 115
    • 0013776758 scopus 로고
    • Molecules as documents of evolutionary history
    • Zuckerkandl, E.; Pauling, L. Molecules as documents of evolutionary history. J. Theor. Biol. 1965, 8, 357-366
    • (1965) J. Theor. Biol , vol.8 , pp. 357-366
    • Zuckerkandl, E.1    Pauling, L.2
  • 116
    • 0037373563 scopus 로고    scopus 로고
    • The modern molecular clock
    • Bromham, L.; Penny, D. The modern molecular clock. Nat. Rev. Genet. 2003, 4, 216-224
    • (2003) Nat. Rev. Genet , vol.4 , pp. 216-224
    • Bromham, L.1    Penny, D.2
  • 117
    • 0024356362 scopus 로고
    • The neutral theory of molecular evolution and the world view of the neutralists
    • Kimura, M. The neutral theory of molecular evolution and the world view of the neutralists. Genome 1989, 31, 24-31
    • (1989) Genome , vol.31 , pp. 24-31
    • Kimura, M.1
  • 118
    • 0014421064 scopus 로고
    • Evolutionary rate at the molecular level
    • Kimura, M. Evolutionary rate at the molecular level. Nature 1968, 217, 624-626
    • (1968) Nature , vol.217 , pp. 624-626
    • Kimura, M.1
  • 119
    • 0014680905 scopus 로고
    • Non-Darwinian evolution
    • King, J.L.; Jukes, T.H. Non-Darwinian evolution. Science 1969, 164, 788-798
    • (1969) Science , vol.164 , pp. 788-798
    • King, J.L.1    Jukes, T.H.2
  • 120
    • 17744413756 scopus 로고
    • Model of effectively neutral mutations in which selective constraint is incorporated
    • Kimura, M. Model of effectively neutral mutations in which selective constraint is incorporated. Proc. Natl. Acad. Sci. USA 1979, 76, 3440-3444
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 3440-3444
    • Kimura, M.1
  • 121
    • 0015722319 scopus 로고
    • Slightly deleterious mutant substitutions in evolution
    • Ohta, T. Slightly deleterious mutant substitutions in evolution. Nature 1973, 246, 96-98
    • (1973) Nature , vol.246 , pp. 96-98
    • Ohta, T.1
  • 122
    • 0016087667 scopus 로고
    • On some principles governing molecular evolution
    • Kimura, M.; Ota, T. On some principles governing molecular evolution. Proc. Natl. Acad. Sci. USA 1974, 71, 2848-2852
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 2848-2852
    • Kimura, M.1    Ota, T.2
  • 123
    • 0342947190 scopus 로고
    • Possibility of extensive neutral evolution under stabilizing selection with special reference to nonrandom usage of synonymous codons
    • Kimura, M. Possibility of extensive neutral evolution under stabilizing selection with special reference to nonrandom usage of synonymous codons. Proc. Natl. Acad. Sci. USA 1981, 78, 5773-5777
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 5773-5777
    • Kimura, M.1
  • 124
    • 0001654122 scopus 로고    scopus 로고
    • Development of Neutral and Nearly Neutral Theories
    • Ohta, T.; Gillespie, J.H. Development of Neutral and Nearly Neutral Theories. Theor. Popul. Biol. 1996, 49, 128-142
    • (1996) Theor. Popul. Biol , vol.49 , pp. 128-142
    • Ohta, T.1    Gillespie, J.H.2
  • 125
    • 33846515095 scopus 로고    scopus 로고
    • Thermodynamics of neutral protein evolution
    • Bloom, J.D.; Raval, A.; Wilke, C.O. Thermodynamics of neutral protein evolution. Genetics 2007, 175, 255-266
    • (2007) Genetics , vol.175 , pp. 255-266
    • Bloom, J.D.1    Raval, A.2    Wilke, C.O.3
  • 126
    • 0021715830 scopus 로고
    • The molecular clock may be an episodic clock
    • Gillespie, J.H. The molecular clock may be an episodic clock. Proc. Natl. Acad. Sci. USA 1984, 81, 8009-8013
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 8009-8013
    • Gillespie, J.H.1
  • 127
    • 39749124074 scopus 로고
    • The status of the neutral theory: The neutral theory of molecular evolution
    • Gillespie, J.H. The status of the neutral theory: The neutral theory of molecular evolution. Science 1984, 224, 732-733
    • (1984) Science , vol.224 , pp. 732-733
    • Gillespie, J.H.1
  • 128
    • 0022641120 scopus 로고
    • Natural selection and the molecular clock
    • Gillespie, J.H. Natural selection and the molecular clock. Mol. Biol. Evol. 1986, 3, 138-155
    • (1986) Mol. Biol. Evol , vol.3 , pp. 138-155
    • Gillespie, J.H.1
  • 129
    • 79960555958 scopus 로고    scopus 로고
    • Proteome-wide evidence for enhanced positive Darwinian selection within intrinsically disordered regions in proteins
    • Nilsson, J.; Grahn, M.; Wright, A.P.H. Proteome-wide evidence for enhanced positive Darwinian selection within intrinsically disordered regions in proteins. Genome Biol. 2011, 12, R65
    • (2011) Genome Biol , vol.12 , pp. R65
    • Nilsson, J.1    Grahn, M.2    Wright, A.P.H.3
  • 131
    • 84993865850 scopus 로고
    • Mode of allozyme evolution: Increased genetic distance associated with speciation events
    • Mindell, D.; Sites, J.; Graur, D. Mode of allozyme evolution: Increased genetic distance associated with speciation events. J. Evol. Biol. 1990, 3, 125-131
    • (1990) J. Evol. Biol , vol.3 , pp. 125-131
    • Mindell, D.1    Sites, J.2    Graur, D.3
  • 132
    • 84989486097 scopus 로고
    • Assessing The Relationship Between Speciation And Evolutionary Change
    • Mindell, D.P.; Sites, J.W., Jr.; Graur, D. Assessing The Relationship Between Speciation And Evolutionary Change. Cladistics 1990, 6, 393-398
    • (1990) Cladistics , vol.6 , pp. 393-398
    • Mindell, D.P.1    Sites, J.W.2    Graur, D.3
  • 133
    • 0034998592 scopus 로고    scopus 로고
    • Evolutionary rates and species diversity in flowering plants
    • Barraclough, T.G.; Savolainen, V. Evolutionary rates and species diversity in flowering plants. Evolution 2001, 55, 677-683
    • (2001) Evolution , vol.55 , pp. 677-683
    • Barraclough, T.G.1    Savolainen, V.2
  • 135
    • 79955558282 scopus 로고    scopus 로고
    • Reply to Englund: Molecular evolution and diversification-Counting species is better than counting nodes when the phylogeny is unknown
    • Lanfear, R.; Bromham, L.; Ho, S.Y.W. Reply to Englund: Molecular evolution and diversification-Counting species is better than counting nodes when the phylogeny is unknown. Proc. Natl. Acad. Sci. USA 2011, 108, E85-E86
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. E85-E86
    • Lanfear, R.1    Bromham, L.2    Ho, S.Y.W.3
  • 136
    • 78650048171 scopus 로고    scopus 로고
    • Evolutionary rates of mitochondrial genomes correspond to diversification rates and to contemporary species richness in birds and reptiles
    • Eo, S.H.; DeWoody, J.A. Evolutionary rates of mitochondrial genomes correspond to diversification rates and to contemporary species richness in birds and reptiles. Proc. Biol. Sci. 2010, 277, 3587-3592
    • (2010) Proc. Biol. Sci , vol.277 , pp. 3587-3592
    • Eo, S.H.1    DeWoody, J.A.2
  • 138
    • 44349161622 scopus 로고    scopus 로고
    • Intense neutral drifts yield robust and evolvable consensus proteins
    • Bershtein, S.; Goldin, K.; Tawfik, D.S. Intense neutral drifts yield robust and evolvable consensus proteins. J. Mol. Biol. 2008, 379, 1029-1044
    • (2008) J. Mol. Biol , vol.379 , pp. 1029-1044
    • Bershtein, S.1    Goldin, K.2    Tawfik, D.S.3
  • 139
    • 34447559360 scopus 로고    scopus 로고
    • Neutral genetic drift can alter promiscuous protein functions, potentially aiding functional evolution
    • Bloom, J.D.; Romero, P.A.; Lu, Z.; Arnold, F.H. Neutral genetic drift can alter promiscuous protein functions, potentially aiding functional evolution. Biol. Direct 2007, 2, e17
    • (2007) Biol. Direct , vol.2
    • Bloom, J.D.1    Romero, P.A.2    Lu, Z.3    Arnold, F.H.4
  • 140
    • 0004006491 scopus 로고    scopus 로고
    • Harvard University Press: Cambridge, MA, USA, 1998; Translated by Cobb, M
    • Morange, M. History of Molecular Biology; Harvard University Press: Cambridge, MA, USA, 1998; Translated by Cobb, M
    • History of Molecular Biology
    • Morange, M.1
  • 141
    • 33745323376 scopus 로고    scopus 로고
    • Trends in antibody sequence changes during the somatic hypermutation process
    • Clark, L.A.; Ganesan, S.; Papp, S.; van Vlijmen, H.W.T. Trends in antibody sequence changes during the somatic hypermutation process. J. Immunol. 2006, 177, 333-340
    • (2006) J. Immunol , vol.177 , pp. 333-340
    • Clark, L.A.1    Ganesan, S.2    Papp, S.3    van Vlijmen, H.W.T.4
  • 142
    • 39049145798 scopus 로고    scopus 로고
    • Immunoglobulin somatic hypermutation
    • Teng, G.; Papavasiliou, F.N. Immunoglobulin somatic hypermutation. Annu. Rev. Genet. 2007, 41, 107-120
    • (2007) Annu. Rev. Genet , vol.41 , pp. 107-120
    • Teng, G.1    Papavasiliou, F.N.2
  • 144
    • 34547460183 scopus 로고    scopus 로고
    • Molecular evolution of affinity and flexibility in the immune system
    • Thorpe, I.F.; Brooks, C.L., III. Molecular evolution of affinity and flexibility in the immune system. Proc. Natl. Acad. Sci. USA 2007, 104, 8821-8826
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8821-8826
    • Thorpe, I.F.1    Brooks, C.L.2
  • 145
    • 0017272554 scopus 로고
    • Enzyme recruitment in evolution of new function
    • Jensen, R.A. Enzyme recruitment in evolution of new function. Annu. Rev. Microbiol. 1976, 30, 409-425
    • (1976) Annu. Rev. Microbiol , vol.30 , pp. 409-425
    • Jensen, R.A.1
  • 146
    • 0015980083 scopus 로고
    • On earlier states of the biochemical system
    • Yčas, M. On earlier states of the biochemical system. J. Theor. Biol. 1974, 44, 145-160
    • (1974) J. Theor. Biol , vol.44 , pp. 145-160
    • Yčas, M.1
  • 147
    • 0029919942 scopus 로고    scopus 로고
    • Evolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases
    • Jensen, R.A.; Gu, W. Evolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases. J. Bacteriol. 1996, 178, 2161-2171
    • (1996) J. Bacteriol , vol.178 , pp. 2161-2171
    • Jensen, R.A.1    Gu, W.2
  • 149
    • 84960296241 scopus 로고    scopus 로고
    • Mechanisms of protein evolution and their application to protein engineering
    • Toone, E.J., Ed.; Wiley: Hoboken, NJ, USA
    • Glasner, M.E.; Gerlt, J.A.; Babbitt, P.C. Mechanisms of protein evolution and their application to protein engineering. In Advances in Enzymology and Related Areas of Molecular Biology, Volume 75; Toone, E.J., Ed.; Wiley: Hoboken, NJ, USA, 2007; pp. 193-239
    • (2007) In Advances in Enzymology and Related Areas of Molecular Biology , vol.75 , pp. 193-239
    • Glasner, M.E.1    Gerlt, J.A.2    Babbitt, P.C.3
  • 150
    • 37049243502 scopus 로고
    • A production of amino acids under possible primitive earth conditions
    • Miller, S.L. A production of amino acids under possible primitive earth conditions. Science 1953, 117, 528-529
    • (1953) Science , vol.117 , pp. 528-529
    • Miller, S.L.1
  • 151
    • 0014208557 scopus 로고
    • Peptide synthesis from hydrogen cyanide and water
    • Matthews, C.N.; Moser, R.E. Peptide synthesis from hydrogen cyanide and water. Nature 1967, 215, 1230-1234
    • (1967) Nature , vol.215 , pp. 1230-1234
    • Matthews, C.N.1    Moser, R.E.2
  • 152
    • 0024972533 scopus 로고
    • Pre-biotic organic matter from comets and asteroids
    • Anders, E. Pre-biotic organic matter from comets and asteroids. Nature 1989, 342, 255-257
    • (1989) Nature , vol.342 , pp. 255-257
    • Anders, E.1
  • 153
    • 0025573932 scopus 로고
    • Comet dust as a source of amino acids at the Cretaceous/Tertiary boundary
    • Zahnle, K.; Grinspoon, D. Comet dust as a source of amino acids at the Cretaceous/Tertiary boundary. Nature 1990, 348, 157-160
    • (1990) Nature , vol.348 , pp. 157-160
    • Zahnle, K.1    Grinspoon, D.2
  • 154
    • 46749146237 scopus 로고    scopus 로고
    • Detection of cometary amines in samples returned by Stardust
    • Glavin, D.; Dworkin, J.; Sandford, S. Detection of cometary amines in samples returned by Stardust. Meteorit. Planet. Sci. 2008, 43, 399-413
    • (2008) Meteorit. Planet. Sci , vol.43 , pp. 399-413
    • Glavin, D.1    Dworkin, J.2    Sandford, S.3
  • 155
    • 34249713769 scopus 로고    scopus 로고
    • On the chemistry and evolution of the pioneer organism
    • Wachtershauser, G. On the chemistry and evolution of the pioneer organism. Chem. Biodivers. 2007, 4, 584-602
    • (2007) Chem. Biodivers , vol.4 , pp. 584-602
    • Wachtershauser, G.1
  • 156
    • 26944440035 scopus 로고    scopus 로고
    • Catalytically increased prebiotic peptide formation: Ditryptophan, dilysine, and diserine
    • Plankensteiner, K.; Reiner, H.; Rode, B.M. Catalytically increased prebiotic peptide formation: Ditryptophan, dilysine, and diserine. Orig. Life Evol. Biosph. 2005, 35, 411-419
    • (2005) Orig. Life Evol. Biosph , vol.35 , pp. 411-419
    • Plankensteiner, K.1    Reiner, H.2    Rode, B.M.3
  • 157
    • 5044231756 scopus 로고    scopus 로고
    • Carbonyl sulfide-mediated prebiotic formation of peptides
    • Leman, L.; Orgel, L.; Ghadiri, M.R. Carbonyl sulfide-mediated prebiotic formation of peptides. Science 2004, 306, 283-286
    • (2004) Science , vol.306 , pp. 283-286
    • Leman, L.1    Orgel, L.2    Ghadiri, M.R.3
  • 160
    • 84879833434 scopus 로고    scopus 로고
    • Two regimes of protein evolution and their unique dependencies on sequence composition
    • Mannige, R.V. Two regimes of protein evolution and their unique dependencies on sequence composition. Phys. Rev. E 2013, 87, e062714
    • (2013) Phys. Rev. E , vol.87
    • Mannige, R.V.1
  • 161
    • 84872029834 scopus 로고    scopus 로고
    • A universal trend among proteomes indicates an oily last common ancestor
    • Mannige, R.V.; Brooks, C.L., III; Shakhnovich, E.I. A universal trend among proteomes indicates an oily last common ancestor. PLoS Comput. Biol. 2012, 8, e1002839
    • (2012) PLoS Comput. Biol , vol.8
    • Mannige, R.V.1    Brooks, C.L.2    Shakhnovich, E.I.3
  • 162
    • 84856708599 scopus 로고    scopus 로고
    • Intrinsic disorder: Signaling via highly specific but short-lived association
    • Zhou, H.X. Intrinsic disorder: Signaling via highly specific but short-lived association. Trends Biochem. Sci. 2012, 37, 43-48
    • (2012) Trends Biochem. Sci , vol.37 , pp. 43-48
    • Zhou, H.X.1
  • 163
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • Dunker, A.K.; Cortese, M.S.; Romero, P.; Iakoucheva, L.M.; Uversky, V.N. Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J. 2005, 272, 5129-5148
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 164
    • 33645214608 scopus 로고    scopus 로고
    • Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks
    • Patil, A.; Nakamura, H. Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks. FEBS Lett. 2006, 580, 2041-2045
    • (2006) FEBS Lett , vol.580 , pp. 2041-2045
    • Patil, A.1    Nakamura, H.2
  • 165
    • 60949085866 scopus 로고    scopus 로고
    • Evolutionary constraints on hub and non-hub proteins in human protein interaction network: Insight from protein connectivity and intrinsic disorder
    • Manna, B.; Bhattacharya, T.; Kahali, B.; Ghosh, T.C. Evolutionary constraints on hub and non-hub proteins in human protein interaction network: Insight from protein connectivity and intrinsic disorder. Gene 2009, 434, 50-55
    • (2009) Gene , vol.434 , pp. 50-55
    • Manna, B.1    Bhattacharya, T.2    Kahali, B.3    Ghosh, T.C.4


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