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Volumn , Issue , 2011, Pages 1-181

chirality in biological nanospaces: Reactions in active sites

Author keywords

[No Author keywords available]

Indexed keywords

CHIRALITY; EFFICIENCY; ELECTRONIC STRUCTURE; ENZYMES; MOLECULES; VAN DER WAALS FORCES;

EID: 84894146710     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Book
Times cited : (25)

References (414)
  • 1
    • 33845183463 scopus 로고
    • Chiral discrimination and phase transitions in Langmuir monolayers
    • Andelman, D. (1989). Chiral discrimination and phase transitions in Langmuir monolayers. J. Am. Chem. Soc., 111: 6536-6544.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 6536-6544
    • Andelman, D.1
  • 2
    • 0027892574 scopus 로고
    • Chiral discrimination in solutions and in Langmuir monolayers
    • Andelman, D. and Orland, H. (1993). Chiral discrimination in solutions and in Langmuir monolayers. J. Am. Chem. Soc., 115: 12322-12329.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12322-12329
    • Andelman, D.1    Orland, H.2
  • 3
    • 0035896024 scopus 로고    scopus 로고
    • ConSurf: An algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information
    • Armon, A., Graur, D., and Ben-Tal, N. (2001). ConSurf: An algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information. J. Mol. Biol., 307: 447-463.
    • (2001) J. Mol. Biol. , vol.307 , pp. 447-463
    • Armon, A.1    Graur, D.2    Ben-Tal, N.3
  • 4
    • 0001283767 scopus 로고
    • Stereochemistry and molecular recognition in two dimensions
    • Arnett, E.M., Harvey, N.G., and Rose, P.L. (1989). Stereochemistry and molecular recognition in two dimensions. Acc. Chem. Res., 22: 131-148.
    • (1989) Acc. Chem. Res. , vol.22 , pp. 131-148
    • Arnett, E.M.1    Harvey, N.G.2    Rose, P.L.3
  • 5
    • 0030788568 scopus 로고    scopus 로고
    • The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase
    • Arnez, J.G., Augustine, J.G., Moras, D., and Francklyn, C.S. (1997). The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase. Proc. Natl. Acad. Sci. (USA), 94: 7144-7149.
    • (1997) Proc. Natl. Acad. Sci. (USA) , vol.94 , pp. 7144-7149
    • Arnez, J.G.1    Augustine, J.G.2    Moras, D.3    Francklyn, C.S.4
  • 6
    • 0029958175 scopus 로고    scopus 로고
    • Mirror symmetry breaking at the molecular level
    • Avetisov, V. and Goldanskii, V. (1996). Mirror symmetry breaking at the molecular level. Proc. Natl. Acad. Sci. (USA), 93: 11435-11442.
    • (1996) Proc. Natl. Acad. Sci. (USA) , vol.93 , pp. 11435-11442
    • Avetisov, V.1    Goldanskii, V.2
  • 7
    • 3843108983 scopus 로고    scopus 로고
    • Mimicking enzymatic transaminations: Attempts to understand and develop a catalytic asymmetric approach to chiral a-amino acids
    • Bachman, S., Knudsen, K.R., and Jørgensen, K.A. (2004). Mimicking enzymatic transaminations: Attempts to understand and develop a catalytic asymmetric approach to chiral a-amino acids. Org. Biomol. Chem., 2: 2044-2049.
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 2044-2049
    • Bachman, S.1    Knudsen, K.R.2    Jørgensen, K.A.3
  • 9
    • 0027668216 scopus 로고
    • Catalysis: Design versus selection
    • Benner S. (1993). Catalysis: Design versus selection. Science, 261: 1402-1403.
    • (1993) Science , vol.261 , pp. 1402-1403
    • Benner, S.1
  • 14
    • 0001101731 scopus 로고
    • On the rotation of plane of polarisation of electric waves by a twisted structure
    • Bose, J.C. (1898). On the rotation of plane of polarisation of electric waves by a twisted structure. Proc. Roy Soc. Lond. A, 63: 146-152.
    • (1898) Proc. Roy Soc. Lond. A , vol.63 , pp. 146-152
    • Bose, J.C.1
  • 15
    • 0016912106 scopus 로고
    • Some pertinent aspects of mechanism as determined with small molecules
    • Bruice, T.C. (1976). Some pertinent aspects of mechanism as determined with small molecules. Annu. Rev. Biochem., 45: 331-374.
    • (1976) Annu. Rev. Biochem. , vol.45 , pp. 331-374
    • Bruice, T.C.1
  • 17
    • 5744237833 scopus 로고    scopus 로고
    • Chirality in NMR spectroscopy
    • Buckingham, A.D. (2004). Chirality in NMR spectroscopy. Chem. Phys. Lett., 398: 1-5.
    • (2004) Chem. Phys. Lett. , vol.398 , pp. 1-5
    • Buckingham, A.D.1
  • 19
    • 0025820796 scopus 로고
    • Effect of D-amino acids on Escherichia coli strains with impaired penicillin-binding proteins
    • Caparros, M., Torrecuadrada, J.L.M., and de Pedro, M.A. (1991). Effect of D-amino acids on Escherichia coli strains with impaired penicillin-binding proteins. Res. Microbiol., 142: 345-350.
    • (1991) Res. Microbiol. , vol.142 , pp. 345-350
    • Caparros, M.1    Torrecuadrada, J.L.M.2    de Pedro, M.A.3
  • 20
    • 0026795665 scopus 로고
    • Effect of D-amino acids on structure and synthesis of peptidoglycan in Escherichia coli
    • Caparros, M., Pisabarro, A.G., and de Pedro, M.A. (1992). Effect of D-amino acids on structure and synthesis of peptidoglycan in Escherichia coli. J. Bacteriol., 174: 5549-5559.
    • (1992) J. Bacteriol. , vol.174 , pp. 5549-5559
    • Caparros, M.1    Pisabarro, A.G.2    de Pedro, M.A.3
  • 21
    • 9944250036 scopus 로고    scopus 로고
    • Structural aspects of non-ribosomal peptide biosynthesis
    • Challis, G.L. and Naismith, J.H. (2004). Structural aspects of non-ribosomal peptide biosynthesis. Curr. Opin. Str. Biol., 14: 748-756.
    • (2004) Curr. Opin. Str. Biol. , vol.14 , pp. 748-756
    • Challis, G.L.1    Naismith, J.H.2
  • 22
    • 0014864291 scopus 로고
    • Molecular events in the growth inhibition of bacillus subtilis by D-tyrosine
    • Champney, W.S. and Jensen, R.A. (1970). Molecular events in the growth inhibition of bacillus subtilis by D-tyrosine. J. Bacteriol., 104: 107-116.
    • (1970) J. Bacteriol. , vol.104 , pp. 107-116
    • Champney, W.S.1    Jensen, R.A.2
  • 23
    • 4544230537 scopus 로고    scopus 로고
    • Distinguishing structural and functional restraints in evolution in order to identify interaction sites
    • Chelliah, V., Chen, L., Blundell, T.L., and Lovell, S.C. (2004). Distinguishing structural and functional restraints in evolution in order to identify interaction sites. J. Mol. Biol., 342: 1487-1504.
    • (2004) J. Mol. Biol. , vol.342 , pp. 1487-1504
    • Chelliah, V.1    Chen, L.2    Blundell, T.L.3    Lovell, S.C.4
  • 24
    • 27144551715 scopus 로고    scopus 로고
    • Improvement in protein functional site prediction by distinguishing structural and functional constraints on protein family evolution using computational design
    • Cheng, G., Qian, B., Samudrala, R., and Baker, D. (2005). Improvement in protein functional site prediction by distinguishing structural and functional constraints on protein family evolution using computational design. Nucleic Acids Res., 33: 5861-5867.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 5861-5867
    • Cheng, G.1    Qian, B.2    Samudrala, R.3    Baker, D.4
  • 26
    • 0015624304 scopus 로고
    • Metabolism of D-serine in Escherichia coli K-12: Mechanism of growth inhibition
    • Cosloy, S.D. and McFall, E. (1973). Metabolism of D-serine in Escherichia coli K-12: Mechanism of growth inhibition. J. Bacteriol., 114: 685-694.
    • (1973) J. Bacteriol. , vol.114 , pp. 685-694
    • Cosloy, S.D.1    McFall, E.2
  • 27
    • 0001190759 scopus 로고
    • The interaction of optically active molecules, Proc
    • Craig, D.P., Power, E.A., and Thirunamachandran, T. (1971). The interaction of optically active molecules, Proc. R. Soc. Lond. A, 322: 165-179.
    • (1971) R. Soc. Lond. A , vol.322 , pp. 165-179
    • Craig, D.P.1    Power, E.A.2    Thirunamachandran, T.3
  • 28
    • 1842857771 scopus 로고    scopus 로고
    • Asymmetry in the shapes of folded and denatured states of protein
    • Dima, R.I. and Thirumalai, D. (2004). Asymmetry in the shapes of folded and denatured states of protein. J. Phys. Chem. B, 108: 6564-6570.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 6564-6570
    • Dima, R.I.1    Thirumalai, D.2
  • 29
    • 25144474487 scopus 로고    scopus 로고
    • Chiral induction in quinoline-derived oligoamide foldamers: Assignment of helical handedness and role of steric effects
    • Dolain, C., Jiang, H., Léger, J.M., Guionneau, P., and Huc, I. (2005). Chiral induction in quinoline-derived oligoamide foldamers: Assignment of helical handedness and role of steric effects. J. Am. Chem. Soc., 127: 12943-12951.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 12943-12951
    • Dolain, C.1    Jiang, H.2    Léger, J.M.3    Guionneau, P.4    Huc, I.5
  • 30
    • 0035965145 scopus 로고    scopus 로고
    • Prediction of functionally important residues based solely on the computed energetics of protein structure
    • Elcock, A.H. (2001). Prediction of functionally important residues based solely on the computed energetics of protein structure. J. Mol. Biol., 312: 885-896.
    • (2001) J. Mol. Biol. , vol.312 , pp. 885-896
    • Elcock, A.H.1
  • 31
    • 65149103555 scopus 로고    scopus 로고
    • Optical activity in an artificial chiral media: A terahertz time-domain investigation of Karl F
    • Elezzabi, A.Y. and Sederberg, S. (2009). Optical activity in an artificial chiral media: A terahertz time-domain investigation of Karl F. Lindman's 1920 pioneering experiment. Opt. Express, 17: 6600-6612.
    • (2009) Lindman's 1920 pioneering experiment. Opt. Express , vol.17 , pp. 6600-6612
    • Elezzabi, A.Y.1    Sederberg, S.2
  • 35
    • 0032839957 scopus 로고    scopus 로고
    • Chemistry, nutrition, and microbiology of D-amino acids
    • Friedman, M. (1999). Chemistry, nutrition, and microbiology of D-amino acids. J. Agric. Food Chem., 47: 3457-3479.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 3457-3479
    • Friedman, M.1
  • 36
    • 12044259093 scopus 로고
    • Fluid and solid fibers made of lipid molecular bilayers
    • Fuhrhop, J.H. and Helfrich, W. (1993). Fluid and solid fibers made of lipid molecular bilayers. Chem. Rev., 93: 1565-1582.
    • (1993) Chem. Rev. , vol.93 , pp. 1565-1582
    • Fuhrhop, J.H.1    Helfrich, W.2
  • 37
    • 0035997506 scopus 로고    scopus 로고
    • D-amino acids in living higher organisms
    • Fuji, N. (2002). D-amino acids in living higher organisms. Orig. Life Evol. Biosph., 32: 103-127.
    • (2002) Orig. Life Evol. Biosph. , vol.32 , pp. 103-127
    • Fuji, N.1
  • 39
    • 0000592694 scopus 로고
    • Relationships between enzymatic catalysis and active site structure revealed by applications of site-directed mutagenesis
    • Gerlt, J.A. (1987). Relationships between enzymatic catalysis and active site structure revealed by applications of site-directed mutagenesis. Chem. Rev., 87: 1079-1105.
    • (1987) Chem. Rev. , vol.87 , pp. 1079-1105
    • Gerlt, J.A.1
  • 41
    • 1942512277 scopus 로고    scopus 로고
    • Chirality of catalysts for stereospecific polymerizations.
    • in Green, M., Nolte, R.J.M., and Meijer, E.W. (eds), (series eds). New York: Wiley Interscience, John Wiley & Sons
    • Guerra, G., Cavallo, L., and Corradini, P. (2003). Chirality of catalysts for stereospecific polymerizations. in Green, M., Nolte, R.J.M., and Meijer, E.W. (eds), Materials Chirality: Volume 24 of Topics in Stereochemistry Series, and Denmark, S. E., Siegel, J. (series eds). New York: Wiley Interscience, John Wiley & Sons, 1-69.
    • (2003) Materials Chirality: Volume 24 of Topics in Stereochemistry Series, and Denmark, S. E., Siegel, J. , pp. 1-69
    • Guerra, G.1    Cavallo, L.2    Corradini, P.3
  • 42
    • 0041195591 scopus 로고    scopus 로고
    • Chiralitydependent two-photon absorption probabilities and circular dichroic line strengths: Theory, calculation and measurement
    • Gunde, K.E., Gary, W., Burdicka, G.W., and Richardson, S. (1996). Chiralitydependent two-photon absorption probabilities and circular dichroic line strengths: Theory, calculation and measurement. Chem. Phys., 208: 195-219.
    • (1996) Chem. Phys. , vol.208 , pp. 195-219
    • Gunde, K.E.1    Gary, W.2    Burdicka, G.W.3    Richardson, S.4
  • 43
    • 0042674397 scopus 로고    scopus 로고
    • Using a neural network and spatial clustering to predict the location of active sites in enzymes
    • Gutteridge, A., Bartlett, G.J., and Thornton, J.M. (2003). Using a neural network and spatial clustering to predict the location of active sites in enzymes. J. Mol. Biol., 330: 719-734.
    • (2003) J. Mol. Biol. , vol.330 , pp. 719-734
    • Gutteridge, A.1    Bartlett, G.J.2    Thornton, J.M.3
  • 44
    • 0027177971 scopus 로고
    • Metal ion-dependent modulation of the dynamics of a designed protein
    • Handel, T., Williams, S., and DeGrado W. (1993). Metal ion-dependent modulation of the dynamics of a designed protein. Science, 261: 879-885.
    • (1993) Science , vol.261 , pp. 879-885
    • Handel, T.1    Williams, S.2    DeGrado, W.3
  • 46
    • 0008731726 scopus 로고
    • The exciton chirality method and its application to configurational and conformational studies of natural products
    • Harada, N. and Nakanishi, K. (1972). The exciton chirality method and its application to configurational and conformational studies of natural products. Acc. Chem. Res., 5: 257-263.
    • (1972) Acc. Chem. Res. , vol.5 , pp. 257-263
    • Harada, N.1    Nakanishi, K.2
  • 47
    • 0019496855 scopus 로고
    • Cysteine and growth inhibition of Escherichia coli: Threonine deaminase as the target enzyme
    • Harris, C.L. (1981). Cysteine and growth inhibition of Escherichia coli: Threonine deaminase as the target enzyme. J. Bacteriol., 145: 1031-1035.
    • (1981) J. Bacteriol. , vol.145 , pp. 1031-1035
    • Harris, C.L.1
  • 48
    • 0025190781 scopus 로고
    • The handedness of the universe
    • Hegstrom, R. and Kondepudi, D.K. (1990). The handedness of the universe. Sci. Am., 262: 108-115.
    • (1990) Sci. Am. , vol.262 , pp. 108-115
    • Hegstrom, R.1    Kondepudi, D.K.2
  • 49
    • 0038814072 scopus 로고    scopus 로고
    • Mutations in distant residues moderately increase the enantioselectivity of Pseudomonas fluorescens esterase towards methyl 3-bromo-2-methylpropanoate and ethyl 3-phenylbutyrate
    • Horsman, G.P., Liu, A.M.F., Henke, E., Bornscheuer, U.T., and Kazlauskas, R.J. (2003). Mutations in distant residues moderately increase the enantioselectivity of Pseudomonas fluorescens esterase towards methyl 3-bromo-2-methylpropanoate and ethyl 3-phenylbutyrate. Chem. Eur. J., 9: 1933-1939.
    • (2003) Chem. Eur. J. , vol.9 , pp. 1933-1939
    • Horsman, G.P.1    Liu, A.M.F.2    Henke, E.3    Bornscheuer, U.T.4    Kazlauskas, R.J.5
  • 53
    • 0942298051 scopus 로고    scopus 로고
    • Switching of chiral induction in helical aromatic oligoamides using solid state-solution state equilibrium
    • Jiang, H., Dolain, C., Léger, J.M., Gornitzka, H., and Huc, I. (2004). Switching of chiral induction in helical aromatic oligoamides using solid state-solution state equilibrium. J. Am. Chem. Soc., 126: 1034-1035.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1034-1035
    • Jiang, H.1    Dolain, C.2    Léger, J.M.3    Gornitzka, H.4    Huc, I.5
  • 54
    • 1042264059 scopus 로고    scopus 로고
    • Searching for functional sites in protein structures
    • Jones, S. and Thornton, J.M. (2004). Searching for functional sites in protein structures. Curr. Opin. Chem. Biol., 8: 3-7.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 3-7
    • Jones, S.1    Thornton, J.M.2
  • 55
    • 0002622819 scopus 로고    scopus 로고
    • Prospects for understanding the origin of the RNA world.
    • In Gesteland, R.F., Cech, T.R., Atkins, J.F. (eds). 2nd ed., Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Joyce, G.F. and Orgel, L.E. (1999). Prospects for understanding the origin of the RNA world. In Gesteland, R.F., Cech, T.R., Atkins, J.F. (eds). The RNA World, 2nd ed., Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 49-77.
    • (1999) The RNA World , pp. 49-77
    • Joyce, G.F.1    Orgel, L.E.2
  • 56
    • 23444436172 scopus 로고
    • Protein design by binary patterning of polar and nonpolar amino acids
    • Kamtekar, S., Schiffer, J., Xiong, H., Babik, J., and Hecht, M. (1993). Protein design by binary patterning of polar and nonpolar amino acids. Science, 262: 1680-1685.
    • (1993) Science , vol.262 , pp. 1680-1685
    • Kamtekar, S.1    Schiffer, J.2    Xiong, H.3    Babik, J.4    Hecht, M.5
  • 58
    • 0000814596 scopus 로고
    • Recent developments in the study of monolayers at the airwater interface
    • Knobler, C.M. (1990). Recent developments in the study of monolayers at the airwater interface. Adv. Chem. Phys., 77: 397-425.
    • (1990) Adv. Chem. Phys. , vol.77 , pp. 397-425
    • Knobler, C.M.1
  • 59
    • 0034968510 scopus 로고    scopus 로고
    • Chiral asymmetry in spiral galaxies
    • Kondepudi, D.K. and Durand, D.J. (2001). Chiral asymmetry in spiral galaxies? Chirality, 13: 351-356.
    • (2001) Chirality , vol.13 , pp. 351-356
    • Kondepudi, D.K.1    Durand, D.J.2
  • 60
    • 0037195144 scopus 로고    scopus 로고
    • A simple physical model for binding energy hot spots in protein-protein complexes
    • Kortemme, T. and Baker, D. (2002). A simple physical model for binding energy hot spots in protein-protein complexes. Proc. Natl. Acad. Sci. (USA), 99: 14116-14121.
    • (2002) Proc. Natl. Acad. Sci. (USA) , vol.99 , pp. 14116-14121
    • Kortemme, T.1    Baker, D.2
  • 61
    • 0031006967 scopus 로고    scopus 로고
    • D-amino acids in animal peptides
    • Kreil, G. (1997). D-amino acids in animal peptides. Annu. Rev. Biochem., 66: 337-345.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 337-345
    • Kreil, G.1
  • 62
    • 0001835708 scopus 로고
    • Chiral discriminations- an extended transition monopole model
    • Kuroda, R., Mason S.F., Rodger, C.D., and Seal R.H. (1981). Chiral discriminations- an extended transition monopole model. Mol. Phys., 42: 33-50.
    • (1981) Mol. Phys. , vol.42 , pp. 33-50
    • Kuroda, R.1    Mason, S.F.2    Rodger, C.D.3    Seal, R.H.4
  • 63
    • 25344479745 scopus 로고
    • A stereochemical basis for chiral discrimination: The extended transition monopole model
    • Kuroda, R., Mason S.F., Rodger, C.D., and Seal, R.H. (1978). A stereochemical basis for chiral discrimination: The extended transition monopole model. Chem. Phys. Lett., 57: 1-4.
    • (1978) Chem. Phys. Lett. , vol.57 , pp. 1-4
    • Kuroda, R.1    Mason, S.F.2    Rodger, C.D.3    Seal, R.H.4
  • 64
    • 0035853280 scopus 로고    scopus 로고
    • Three-dimensional cluster analysis identifies interfaces and functional residue clusters in proteins
    • Landgraf, R., Xenarios, I., and Eisenberg, D. (2001). Three-dimensional cluster analysis identifies interfaces and functional residue clusters in proteins. J. Mol. Biol., 307: 1487-1502.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1487-1502
    • Landgraf, R.1    Xenarios, I.2    Eisenberg, D.3
  • 66
    • 0015228848 scopus 로고
    • Evidence for the difference between the odours of the optical isomers (+)- and (-)-carvone
    • Leitereg, T.J., Guadagni, D.G., Harris, J., Mon, T.R., and Teranishi, R. (1971). Evidence for the difference between the odours of the optical isomers (+)- and (-)-carvone. Nature, 230: 455-456.
    • (1971) Nature , vol.230 , pp. 455-456
    • Leitereg, T.J.1    Guadagni, D.G.2    Harris, J.3    Mon, T.R.4    Teranishi, R.5
  • 67
    • 0000351208 scopus 로고
    • Discriminating interactions between chiral molecules in the liquid phase: Effect on volumetric introduction properties
    • Leporl, L., Mengheri, M., and Mollica, V. (1983). Discriminating interactions between chiral molecules in the liquid phase: Effect on volumetric introduction properties. J. Phys. Chem., 87: 3520-3525.
    • (1983) J. Phys. Chem. , vol.87 , pp. 3520-3525
    • Leporl, L.1    Mengheri, M.2    Mollica, V.3
  • 68
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge, O., Bourne, H.R., and Cohen, F.E. (1996). An evolutionary trace method defines binding surfaces common to protein families. J. Mol. Biol., 257: 342-358.
    • (1996) J. Mol. Biol. , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 69
    • 0036300444 scopus 로고    scopus 로고
    • Structural clusters of evolutionary trace residues are statistically significant and common in proteins
    • Madabushi, S., Yao, H., Marsh, M., Kristensen, D.M., Philippi, A., Sowa, M.E., and Lichtarge, O. (2002). Structural clusters of evolutionary trace residues are statistically significant and common in proteins. J. Mol. Biol., 316: 139-154.
    • (2002) J. Mol. Biol. , vol.316 , pp. 139-154
    • Madabushi, S.1    Yao, H.2    Marsh, M.3    Kristensen, D.M.4    Philippi, A.5    Sowa, M.E.6    Lichtarge, O.7
  • 70
    • 9444278428 scopus 로고    scopus 로고
    • Modular peptide synthetases involved in nonribosomal peptide synthesis
    • Marahiel, M.A., Stachelhaus, T., and Mootz, H.D. (1997). Modular peptide synthetases involved in nonribosomal peptide synthesis. Chem. Rev., 97: 2651-2674.
    • (1997) Chem. Rev. , vol.97 , pp. 2651-2674
    • Marahiel, M.A.1    Stachelhaus, T.2    Mootz, H.D.3
  • 72
    • 0001446204 scopus 로고
    • Biomolecular homochirality
    • Mason, S. (1988). Biomolecular homochirality. Chem. Soc. Rev., 17: 347-359.
    • (1988) Chem. Soc. Rev. , vol.17 , pp. 347-359
    • Mason, S.1
  • 74
    • 0024780925 scopus 로고
    • The development of concepts of chiral discrimination
    • Mason, S.F. (1989). The development of concepts of chiral discrimination. Chirality, 1: 183-191.
    • (1989) Chirality , vol.1 , pp. 183-191
    • Mason, S.F.1
  • 75
    • 0001815609 scopus 로고
    • The electroweak origin of biomolecular handedness
    • Mason, S.F. and Tranter, G.E. (1985). The electroweak origin of biomolecular handedness. Proc. Roy. Soc. London A, 397: 45-65.
    • (1985) Proc. Roy. Soc. London A , vol.397 , pp. 45-65
    • Mason, S.F.1    Tranter, G.E.2
  • 76
    • 0344955341 scopus 로고
    • Structures and transitions in lipid monolayers at the air/ water interface
    • McConnell, H.M. (1991). Structures and transitions in lipid monolayers at the air/ water interface. Annu. Rev. Phys. Chem., 42: 171-195.
    • (1991) Annu. Rev. Phys. Chem. , vol.42 , pp. 171-195
    • McConnell, H.M.1
  • 77
    • 85059295957 scopus 로고
    • Jr. (ed). Mass Extinctions: Process and Evidence. London: Belhaven Press, 133
    • McGhee, G.R. (1989). In Donovan S.K. Jr. (ed). Mass Extinctions: Process and Evidence. London: Belhaven Press, 133.
    • (1989) In Donovan S.K
    • McGhee, G.R.1
  • 78
    • 0025579948 scopus 로고
    • Phospholipid and phospholipid-protein monolayers at the air/water interface
    • Möhwald, H. (1990). Phospholipid and phospholipid-protein monolayers at the air/water interface. Annu. Rev. Phys. Chem., 41: 441-476.
    • (1990) Annu. Rev. Phys. Chem. , vol.41 , pp. 441-476
    • Möhwald, H.1
  • 79
    • 18144403554 scopus 로고    scopus 로고
    • Improving enzyme properties: When are closer mutations better
    • Morley, K.L. and Kazlauskas, R.J. (2005). Improving enzyme properties: When are closer mutations better. Trends Biotechnol., 23: 231-237.
    • (2005) Trends Biotechnol. , vol.23 , pp. 231-237
    • Morley, K.L.1    Kazlauskas, R.J.2
  • 80
    • 85059294480 scopus 로고    scopus 로고
    • Recommendations of the Nomenclature Committee. International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes by the Reactions They Catalyze.
    • Retrieved 2006-03-14.
    • Moss, G.P. Recommendations of the Nomenclature Committee. International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes by the Reactions They Catalyze. http://www. chem.qmul.ac.uk/iubmb/enzyme/. Retrieved 2006-03-14.
    • Moss, G.P.1
  • 81
    • 0038339629 scopus 로고    scopus 로고
    • Molecular origin of the recognition of chiral odorant by chiral lipid: Interaction of dipalmitoyl phosphatidyl choline and carvone
    • Nandi, N. (2003). Molecular origin of the recognition of chiral odorant by chiral lipid: Interaction of dipalmitoyl phosphatidyl choline and carvone. J. Phys. Chem. A, 107: 4588-4591.
    • (2003) J. Phys. Chem. A , vol.107 , pp. 4588-4591
    • Nandi, N.1
  • 82
    • 0942279303 scopus 로고    scopus 로고
    • Role of secondary level chiral structure in the process of molecular recognition of ligand: Study of model helical peptide
    • Nandi, N. (2004). Role of secondary level chiral structure in the process of molecular recognition of ligand: Study of model helical peptide. J. Phys. Chem. B., 108: 789-797.
    • (2004) J. Phys. Chem. B. , vol.108 , pp. 789-797
    • Nandi, N.1
  • 83
    • 70350173558 scopus 로고    scopus 로고
    • Chiral discrimination in the confined environment of biological nanospace: Reactions and interactions involving amino acids and peptides
    • Nandi, N. (2009). Chiral discrimination in the confined environment of biological nanospace: Reactions and interactions involving amino acids and peptides. Int. Rev. Phys. Chem., 28: 111-167.
    • (2009) Int. Rev. Phys. Chem. , vol.28 , pp. 111-167
    • Nandi, N.1
  • 84
    • 0029912599 scopus 로고    scopus 로고
    • Molecular origin of the intrinsic bending force for helical morphology observed in chiral amphiphilic assemblies: Concentration and size dependence
    • Nandi, N. and Bagchi, B. (1996). Molecular origin of the intrinsic bending force for helical morphology observed in chiral amphiphilic assemblies: Concentration and size dependence. J. Am. Chem. Soc., 118: 11208-11216.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11208-11216
    • Nandi, N.1    Bagchi, B.2
  • 85
    • 0031076037 scopus 로고    scopus 로고
    • Prediction of the senses of helical amphiphilic assemblies from effective intermolecular pair potential: Studies on chiral monolayers and bilayers
    • Nandi, N. and Bagchi, B. (1997). Prediction of the senses of helical amphiphilic assemblies from effective intermolecular pair potential: Studies on chiral monolayers and bilayers. J. Phys. Chem. A., 101: 1343-1351.
    • (1997) J. Phys. Chem. A. , vol.101 , pp. 1343-1351
    • Nandi, N.1    Bagchi, B.2
  • 86
    • 0001930365 scopus 로고    scopus 로고
    • Microscopic study of chiral interactions in Langmuir monolayer: Monolayers of N-palmitoyl aspartic acid and N-stearoyl serine methyl ester.
    • Nandi, N. and Vollhardt, D. (2000). Microscopic study of chiral interactions in Langmuir monolayer: Monolayers of N-palmitoyl aspartic acid and N-stearoyl serine methyl ester. Colloids Surf. A, 183-185: 67-83.
    • (2000) Colloids Surf. A , vol.183-185 , pp. 67-83
    • Nandi, N.1    Vollhardt, D.2
  • 87
    • 0037015733 scopus 로고    scopus 로고
    • Molecular origin of the chiral interaction in biomimetic systems: Dipalmitoylphosphatidylcholine Langmuir monolayer
    • Nandi, N. and Vollhardt, D. (2002a). Molecular origin of the chiral interaction in biomimetic systems: Dipalmitoylphosphatidylcholine Langmuir monolayer. J. Phys. Chem. B., 106: 10144-10149.
    • (2002) J. Phys. Chem. B. , vol.106 , pp. 10144-10149
    • Nandi, N.1    Vollhardt, D.2
  • 88
    • 0037127937 scopus 로고    scopus 로고
    • Prediction of the handedness of the chiral domains of amphiphilic monolayers: Monolayers of amino acid amphiphiles.
    • Nandi, N. and Vollhardt, D. (2002b). Prediction of the handedness of the chiral domains of amphiphilic monolayers: Monolayers of amino acid amphiphiles. Colloids Surf. A., 198-200: 207-221.
    • (2002) Colloids Surf. A. , vol.198-200 , pp. 207-221
    • Nandi, N.1    Vollhardt, D.2
  • 89
    • 0037452009 scopus 로고    scopus 로고
    • Chiral discrimination effects in Langmuir monolayers: Monolayers of palmitoyl aspartic acid, n-stearoyl serine methyl ester, and n-tetradecyl-?,d dihydroxypentanoic acid amide
    • Nandi, N. and Vollhardt, D. (2003a). Chiral discrimination effects in Langmuir monolayers: Monolayers of palmitoyl aspartic acid, n-stearoyl serine methyl ester, and n-tetradecyl-?,d dihydroxypentanoic acid amide. J. Phys. Chem. B, 107: 3464-3475.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 3464-3475
    • Nandi, N.1    Vollhardt, D.2
  • 90
    • 0037940017 scopus 로고    scopus 로고
    • Correlation between the microscopic and mesoscopic chirality in Langmuir monolayers
    • Nandi, N. and Vollhardt, D. (2003b). Correlation between the microscopic and mesoscopic chirality in Langmuir monolayers. Thin Solid Films, 433: 12-21.
    • (2003) Thin Solid Films , vol.433 , pp. 12-21
    • Nandi, N.1    Vollhardt, D.2
  • 91
    • 0242334618 scopus 로고    scopus 로고
    • Effect of molecular chirality on the morphology of biomimetic Langmuir monolayers
    • Nandi, N. and Vollhardt, D. (2003c). Effect of molecular chirality on the morphology of biomimetic Langmuir monolayers. Chem. Rev., 103: 4033-4075.
    • (2003) Chem. Rev. , vol.103 , pp. 4033-4075
    • Nandi, N.1    Vollhardt, D.2
  • 92
    • 34548563361 scopus 로고    scopus 로고
    • Chirality and molecular recognition in biomimetic organized films.
    • In Ariga, K. and Nalwa, H.S. (eds), Valencia, CA: American Scientific Publishers
    • Nandi, N. and Vollhardt, D. (2006). Chirality and molecular recognition in biomimetic organized films. In Ariga, K. and Nalwa, H.S. (eds), Bottoms up. Nanofabrication: Supramolecules, Self Assemblies and Organized Films. Valencia, CA: American Scientific Publishers, 5: 1-29.
    • (2006) Bottoms up. Nanofabrication: Supramolecules, Self Assemblies and Organized Films. , vol.5 , pp. 1-29
    • Nandi, N.1    Vollhardt, D.2
  • 93
    • 34447632663 scopus 로고    scopus 로고
    • Molecular interactions in amphiphilic assemblies: Theoretical perspective
    • Nandi, N. and Vollhardt, D. (2007). Molecular interactions in amphiphilic assemblies: Theoretical perspective. Acc. Chem. Res., 40: 351-360.
    • (2007) Acc. Chem. Res. , vol.40 , pp. 351-360
    • Nandi, N.1    Vollhardt, D.2
  • 94
    • 37249070303 scopus 로고    scopus 로고
    • Chiral discrimination and recognition in Langmuir monolayers
    • Nandi, N. and Vollhardt, D. (2008). Chiral discrimination and recognition in Langmuir monolayers. Curr. Opin. Colloid Surf., 13: 40-46.
    • (2008) Curr. Opin. Colloid Surf. , vol.13 , pp. 40-46
    • Nandi, N.1    Vollhardt, D.2
  • 95
    • 0036964862 scopus 로고    scopus 로고
    • Chiral interaction in enantiomeric and racemic dipalmitoyl phosphatidylcholine Langmuir monolayer
    • Nandi, N., Roy, R.K., Anupriya, Upadhaya, S., and Vollhardt, D. (2002). Chiral interaction in enantiomeric and racemic dipalmitoyl phosphatidylcholine Langmuir monolayer. J. Surf. Sci. Technol., 18: 51-66.
    • (2002) J. Surf. Sci. Technol. , vol.18 , pp. 51-66
    • Nandi, N.1    Roy, R.K.2    Anupriya Upadhaya, S.3    Vollhardt, D.4
  • 96
    • 51449112928 scopus 로고    scopus 로고
    • Chiral discrimination in stearoyl amine glycerol monolayers
    • Nandi, N., Thirumoorthy, K., and Vollhardt, D. (2008). Chiral discrimination in stearoyl amine glycerol monolayers. Langmuir, 24: 9489-9494.
    • (2008) Langmuir , vol.24 , pp. 9489-9494
    • Nandi, N.1    Thirumoorthy, K.2    Vollhardt, D.3
  • 97
    • 1642520779 scopus 로고    scopus 로고
    • Chiral discrimination effects in Langmuir monolayers of 1-O-hexadecyl glycerol
    • Nandi, N., Vollhardt, D., and Brezesinski, G. (2004). Chiral discrimination effects in Langmuir monolayers of 1-O-hexadecyl glycerol. J. Phys. Chem. B, 108: 327-335.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 327-335
    • Nandi, N.1    Vollhardt, D.2    Brezesinski, G.3
  • 98
    • 10144249620 scopus 로고    scopus 로고
    • Molecular pair potential of chiral amino acid amphiphile in Langmuir monolayers on the basis of an atomistic model
    • Nandi, N., Vollhardt, D., and Rudert, R. (2004). Molecular pair potential of chiral amino acid amphiphile in Langmuir monolayers on the basis of an atomistic model. Colloids Surf. A, 250: 279-287.
    • (2004) Colloids Surf. A , vol.250 , pp. 279-287
    • Nandi, N.1    Vollhardt, D.2    Rudert, R.3
  • 99
    • 14644390842 scopus 로고    scopus 로고
    • A survey of left-handed helices in protein structures
    • Novotny, M. and Kleywegt, G.J. (2005). A survey of left-handed helices in protein structures. J. Mol. Biol., 347: 231-241.
    • (2005) J. Mol. Biol. , vol.347 , pp. 231-241
    • Novotny, M.1    Kleywegt, G.J.2
  • 100
    • 0007601986 scopus 로고
    • Mutants of neurospora deficient in D-amino acid oxidase
    • Ohnishi, E., Macleod, H., and Horowitz, N.H. (1962). Mutants of neurospora deficient in D-amino acid oxidase. J. Biol. Chem., 237: 138-142.
    • (1962) J. Biol. Chem. , vol.237 , pp. 138-142
    • Ohnishi, E.1    Macleod, H.2    Horowitz, N.H.3
  • 101
    • 30044441152 scopus 로고    scopus 로고
    • Optically active polymers with chiral recognition ability.
    • In Green, M., Nolte, R.J.M., Meijer, E.W. (eds), (series eds). New York: Wiley Interscience, John Wiley & Sons
    • Okamoto, Y., Yashima, E., and Yamamoto, C. (2003). Optically active polymers with chiral recognition ability. In Green, M., Nolte, R.J.M., Meijer, E.W. (eds), Materials Chirality: Volume 24 of Topics in Stereochemistry Series, and Denmark, S.E., Siegel, J. (series eds). New York: Wiley Interscience, John Wiley & Sons, 157-207.
    • (2003) Materials Chirality: Volume 24 of Topics in Stereochemistry Series, and Denmark, S.E., Siegel, J. , pp. 157-207
    • Okamoto, Y.1    Yashima, E.2    Yamamoto, C.3
  • 102
    • 0035940421 scopus 로고    scopus 로고
    • Thematics: A simple computational predictor of enzyme function from structure
    • Ondrechen, M.J., Clifton, J.G., and Ringe, D. (2001). Thematics: A simple computational predictor of enzyme function from structure. Proc. Natl. Acad. Sci. (USA), 98: 12473-12478.
    • (2001) Proc. Natl. Acad. Sci. (USA) , vol.98 , pp. 12473-12478
    • Ondrechen, M.J.1    Clifton, J.G.2    Ringe, D.3
  • 103
    • 71849104042 scopus 로고    scopus 로고
    • Enzyme engineering for enantioselectivity: From trial-and-error to rational design
    • Otten, L.G., Hollmann, F., and Arends, I.W.C.E. (2010). Enzyme engineering for enantioselectivity: From trial-and-error to rational design? Trends Biotechnol., 28: 46-54.
    • (2010) Trends Biotechnol. , vol.28 , pp. 46-54
    • Otten, L.G.1    Hollmann, F.2    Arends, I.W.C.E.3
  • 104
    • 0033593453 scopus 로고    scopus 로고
    • Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of nonactive site residues
    • Oue, S., Okamoto, A., Yano, T., and Kagamiyama, H. (1999). Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of nonactive site residues. J. Biol. Chem., 274: 2344-2349.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2344-2349
    • Oue, S.1    Okamoto, A.2    Yano, T.3    Kagamiyama, H.4
  • 107
    • 0030047220 scopus 로고    scopus 로고
    • Functionalized proteinlike structures from conformationally defined synthetic combinatorial libraries
    • Pérez-Payá, E., Houghten, R.A., and Blondelle S.E. (1996). Functionalized proteinlike structures from conformationally defined synthetic combinatorial libraries. J. Biol. Chem., 271: 4120-4126.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4120-4126
    • Pérez-Payá, E.1    Houghten, R.A.2    Blondelle, S.E.3
  • 108
    • 0345864027 scopus 로고    scopus 로고
    • The catalytic site atlas: A resource of catalytic sites and residues identified in enzymes using structural data
    • Porter, C.T., Bartlett, G.J., and Thornton, J.M. (2004). The catalytic site atlas: A resource of catalytic sites and residues identified in enzymes using structural data. Nucleic Acids Res., 32: D129-D133.
    • (2004) Nucleic Acids Res. , vol.32 , pp. D129-D133
    • Porter, C.T.1    Bartlett, G.J.2    Thornton, J.M.3
  • 109
    • 4544365318 scopus 로고    scopus 로고
    • Chain conformation, crystal structures, and structural disorder in stereoregular polymers
    • In Green, M., Nolte, R.J.M., Meijer, E.W. (eds), (series eds). New York: Wiley Interscience, John Wiley & Sons
    • Rosa, C.D. (2003). Chain conformation, crystal structures, and structural disorder in stereoregular polymers. In Green, M., Nolte, R.J.M., Meijer, E.W. (eds), Materials Chirality: Volume 24 of Topics in Stereochemistry Series, and Denmark, S.E., Siegel, J. (series eds). New York: Wiley Interscience, John Wiley & Sons, 71-155.
    • (2003) Materials Chirality: Volume 24 of Topics in Stereochemistry Series, and Denmark, S.E., Siegel, J. , pp. 71-155
    • Rosa, C.D.1
  • 110
    • 0016426264 scopus 로고
    • Positive selection of general amino acid permease mutants in Saccharomyces cerevisiae
    • Rytka, J. (1975). Positive selection of general amino acid permease mutants in Saccharomyces cerevisiae. J. Bacteriol., 121: 562-570.
    • (1975) J. Bacteriol. , vol.121 , pp. 562-570
    • Rytka, J.1
  • 112
    • 33744479600 scopus 로고    scopus 로고
    • Chirality in the RNA world and beyond
    • Sandars, P.G.H. (2005). Chirality in the RNA world and beyond. Int. J. Astrobiology, 4: 49-61.
    • (2005) Int. J. Astrobiology , vol.4 , pp. 49-61
    • Sandars, P.G.H.1
  • 113
    • 0031583033 scopus 로고    scopus 로고
    • Information content of individual genetic sequences
    • Schneider, T.D. (1997). Information content of individual genetic sequences. J. Theor. Biol., 189: 427-441.
    • (1997) J. Theor. Biol. , vol.189 , pp. 427-441
    • Schneider, T.D.1
  • 114
    • 1642370200 scopus 로고
    • Lipid tubules: A paradigm for molecularly engineered structures
    • Schnur, J.M. (1993). Lipid tubules: A paradigm for molecularly engineered structures. Science, 262: 1669-1676.
    • (1993) Science , vol.262 , pp. 1669-1676
    • Schnur, J.M.1
  • 115
    • 0035797725 scopus 로고    scopus 로고
    • Theory of self-assembled tubules and helical ribbons
    • Selinger, J.V., Spector, M.S., and Schnur, J.M. (2001). Theory of self-assembled tubules and helical ribbons. J. Phys. Chem. B., 105: 7157-7169.
    • (2001) J. Phys. Chem. B. , vol.105 , pp. 7157-7169
    • Selinger, J.V.1    Spector, M.S.2    Schnur, J.M.3
  • 116
    • 0014667672 scopus 로고
    • Sweet taste of D and L-sugars and amino-acids and the steric nature of their chemo-receptor site
    • Shallenberger, R.S., Acree, T.E., and Lee, C.Y. (1969). Sweet taste of D and L-sugars and amino-acids and the steric nature of their chemo-receptor site. Nature, 221: 555-556.
    • (1969) Nature , vol.221 , pp. 555-556
    • Shallenberger, R.S.1    Acree, T.E.2    Lee, C.Y.3
  • 117
    • 0029559848 scopus 로고
    • Asymmetric autocatalysis and amplification of enantiomeric excess of a chiral molecule
    • Soai, K., Shibata, T., Morioka, H., and Choji, K. (1995). Asymmetric autocatalysis and amplification of enantiomeric excess of a chiral molecule. Nature, 378: 767-768.
    • (1995) Nature , vol.378 , pp. 767-768
    • Soai, K.1    Shibata, T.2    Morioka, H.3    Choji, K.4
  • 118
    • 0034673983 scopus 로고    scopus 로고
    • Mutational analysis of the epimerization domain in the initiation module PheATE of gramicidin S synthetase
    • Stachelhaus, T. and Walsh, C.T. (2000). Mutational analysis of the epimerization domain in the initiation module PheATE of gramicidin S synthetase. Biochemistry, 39: 5775-5787.
    • (2000) Biochemistry , vol.39 , pp. 5775-5787
    • Stachelhaus, T.1    Walsh, C.T.2
  • 119
    • 65249108138 scopus 로고    scopus 로고
    • Absolute configuration of actinophyllic acid as determined through chiroptical data
    • Taniguchi, T., Martin, C.L., Monde, K., Nakanishi, K., Berova, N., and Overman, L.E. (2009). Absolute configuration of actinophyllic acid as determined through chiroptical data. J. Nat. Prod., 72: 430-432.
    • (2009) J. Nat. Prod. , vol.72 , pp. 430-432
    • Taniguchi, T.1    Martin, C.L.2    Monde, K.3    Nakanishi, K.4    Berova, N.5    Overman, L.E.6
  • 120
    • 0036005636 scopus 로고    scopus 로고
    • Understanding nature's strategies for enzyme-catalyzed racemization and epimerization
    • Tanner, M.E. (2002). Understanding nature's strategies for enzyme-catalyzed racemization and epimerization. Acc. Chem. Res., 35: 237-246.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 237-246
    • Tanner, M.E.1
  • 122
    • 0022591495 scopus 로고
    • The classification of amino acid conservation
    • Taylor, W.R. (1986). The classification of amino acid conservation. J. Theor. Biol., 119: 205-218.
    • (1986) J. Theor. Biol. , vol.119 , pp. 205-218
    • Taylor, W.R.1
  • 123
    • 25844439576 scopus 로고    scopus 로고
    • The correlation between the molecular chirality of the sugar ring on the mesoscopic aggregate morphology in RNA and DNA mimetic systems
    • Thirumoorthy, K. and Nandi, N. (2005). The correlation between the molecular chirality of the sugar ring on the mesoscopic aggregate morphology in RNA and DNA mimetic systems. Chem. Phys. Lett., 414: 336-430.
    • (2005) Chem. Phys. Lett. , vol.414 , pp. 336-430
    • Thirumoorthy, K.1    Nandi, N.2
  • 124
    • 33744477096 scopus 로고    scopus 로고
    • Comparison of the intermolecular energy surfaces of amino acids: Orientation-dependent chiral discrimination
    • Thirumoorthy, K. and Nandi, N. (2006). Comparison of the intermolecular energy surfaces of amino acids: Orientation-dependent chiral discrimination. J. Phys. Chem. B, 110: 8840-8849.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 8840-8849
    • Thirumoorthy, K.1    Nandi, N.2
  • 125
    • 33745453591 scopus 로고    scopus 로고
    • Prediction of the handedness of the domains of monolayers of D-N-palmitoyl aspartic acid: Integrated molecular orbital and molecular mechanics based calculation.
    • Thirumoorthy, K., Nandi, N., and Vollhardt, D. (2006). Prediction of the handedness of the domains of monolayers of D-N-palmitoyl aspartic acid: Integrated molecular orbital and molecular mechanics based calculation. Colloids Surf. A, 282-283: 222-226.
    • (2006) Colloids Surf. A , vol.282-283 , pp. 222-226
    • Thirumoorthy, K.1    Nandi, N.2    Vollhardt, D.3
  • 126
    • 0035815113 scopus 로고    scopus 로고
    • Evolution of function in protein superfamilies from a structural perspective
    • Todd, A.E., Orengo, C.A., and Thornton, J.M. (2001). Evolution of function in protein superfamilies from a structural perspective. J. Mol. Biol., 307: 1113-1143.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1113-1143
    • Todd, A.E.1    Orengo, C.A.2    Thornton, J.M.3
  • 127
    • 14744305761 scopus 로고    scopus 로고
    • Using a library of structural templates to recognize catalytic sites and explore their evolution in homologous families
    • Torrance, J.W., Bartlett, G.J., Porter, C.T., and Thornton, J.M. (2005). Using a library of structural templates to recognize catalytic sites and explore their evolution in homologous families. J. Mol. Biol., 347: 565-581.
    • (2005) J. Mol. Biol. , vol.347 , pp. 565-581
    • Torrance, J.W.1    Bartlett, G.J.2    Porter, C.T.3    Thornton, J.M.4
  • 129
    • 0021741805 scopus 로고
    • Penicillin-insensitive incorporation of D-amino acids into cell wall peptidoglycan influences the amount of bound lipoprotein in Escherichia coli
    • Tsuruoka, T., Tamura, A., Miyata, A., Takei, T., Iwamatsu, K., Inouye, S., and Matsuhashi, M. (1984). Penicillin-insensitive incorporation of D-amino acids into cell wall peptidoglycan influences the amount of bound lipoprotein in Escherichia coli. J. Bacteriol., 160: 889-894.
    • (1984) J. Bacteriol. , vol.160 , pp. 889-894
    • Tsuruoka, T.1    Tamura, A.2    Miyata, A.3    Takei, T.4    Iwamatsu, K.5    Inouye, S.6    Matsuhashi, M.7
  • 130
    • 0002744133 scopus 로고    scopus 로고
    • Morphology and phase behavior of monolayers
    • Vollhardt, D. (1996). Morphology and phase behavior of monolayers. Adv. Colloid Interface Sci., 64: 143-171.
    • (1996) Adv. Colloid Interface Sci. , vol.64 , pp. 143-171
    • Vollhardt, D.1
  • 132
    • 0024531901 scopus 로고
    • Facilitated target location in biological system
    • von Hippel P.H. and Berg, O.G. (1989). Facilitated target location in biological system. J. Biol. Chem., 264: 675-678.
    • (1989) J. Biol. Chem. , vol.264 , pp. 675-678
    • von Hippel, P.H.1    Berg, O.G.2
  • 133
    • 21444449871 scopus 로고    scopus 로고
    • FSSA: A novel method for identifying functional signatures from structural alignments
    • Wang, K. and Samudrala, R. (2005). FSSA: A novel method for identifying functional signatures from structural alignments. Bioinformatics, 21: 2969-2977.
    • (2005) Bioinformatics , vol.21 , pp. 2969-2977
    • Wang, K.1    Samudrala, R.2
  • 134
    • 0000230329 scopus 로고
    • Energetics of enzyme catalysis
    • Warshel, A. (1978). Energetics of enzyme catalysis. Proc. Natl. Acad. Sci. (USA), 75: 5250-5254.
    • (1978) Proc. Natl. Acad. Sci. (USA) , vol.75 , pp. 5250-5254
    • Warshel, A.1
  • 136
    • 0003450992 scopus 로고
    • Enzyme nomenclature 1992: Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes.
    • San Diego: Published for the International Union of Biochemistry and Molecular Biology by Academic Press.
    • Webb, Edwin C. (1992). Enzyme nomenclature 1992: Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes. San Diego: Published for the International Union of Biochemistry and Molecular Biology by Academic Press. ISBN 0-12-227164-5. http://www.chem.qmul. ac.uk/iubmb/enzyme/.
    • (1992)
    • Webb Edwin, C.1
  • 138
    • 0033564943 scopus 로고    scopus 로고
    • Interchange of catalytic activity within the 2-enoyl-coenzyme A hydratase/isomerase superfamily based on a common active site template
    • Xiang, H., Luo, L., Taylor, K.L., and Dunaway-Mariano, D. (1999). Interchange of catalytic activity within the 2-enoyl-coenzyme A hydratase/isomerase superfamily based on a common active site template. Biochemistry, 38: 7638-7652.
    • (1999) Biochemistry , vol.38 , pp. 7638-7652
    • Xiang, H.1    Luo, L.2    Taylor, K.L.3    Dunaway-Mariano, D.4
  • 139
    • 2542470615 scopus 로고    scopus 로고
    • The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release
    • Youngman, E.M., Brunelle, J.L., Kochaniak, A.B., and Green, R. (2004). The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release. Cell, 117: 589-599.
    • (2004) Cell , vol.117 , pp. 589-599
    • Youngman, E.M.1    Brunelle, J.L.2    Kochaniak, A.B.3    Green, R.4
  • 140
    • 0024208742 scopus 로고
    • The roles of active site hydrogen bonding in cytochrome P-450cam as revealed by site-directed mutagenesis
    • Atkins, W.M. and Sligar, S.G. (1988). The roles of active site hydrogen bonding in cytochrome P-450cam as revealed by site-directed mutagenesis. J. Biol. Chem., 263: 18842-18849.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18842-18849
    • Atkins, W.M.1    Sligar, S.G.2
  • 141
    • 0024566973 scopus 로고
    • Molecular recognition in cytochrome P-450: Alteration of regioselective alkane hydroxylation via protein engineering
    • Atkins, W.M. and Sligar, S.G. (1989). Molecular recognition in cytochrome P-450: Alteration of regioselective alkane hydroxylation via protein engineering. J. Am. Chem. Soc., 111: 2715-2717.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 2715-2717
    • Atkins, W.M.1    Sligar, S.G.2
  • 142
    • 2542586375 scopus 로고    scopus 로고
    • The stereoselectivity and catalytic properties of Xanthobacter autotrophicus 2-[(R)-2-Hydroxypropylthio]ethanesulfonate dehydrogenase are controlled by interactions between C-Terminal Arginine residues and the sulfonate of coenzyme M. Biochemistry
    • Clark, D.D., Boyd, J.M., and Ensign, S.A. (2004). The stereoselectivity and catalytic properties of Xanthobacter autotrophicus 2-[(R)-2-Hydroxypropylthio]ethanesulfonate dehydrogenase are controlled by interactions between C-Terminal Arginine residues and the sulfonate of coenzyme M. Biochemistry, 43: 6763-6771.
    • (2004) , vol.43 , pp. 6763-6771
    • Clark, D.D.1    Boyd, J.M.2    Ensign, S.A.3
  • 143
    • 0029999399 scopus 로고    scopus 로고
    • Influence of amino acid residue 374 of cytochrome P-450 2D6 (CYP2D6) on the regio- and enantio-selective metabolism of metoprolol
    • Ellis, S.W., Rowland, K., Ackland, M.J., Rekka, E., Simula, A.P., Lennard, M.S., Wolf, C.R., and Tucker, G.T. (1996). Influence of amino acid residue 374 of cytochrome P-450 2D6 (CYP2D6) on the regio- and enantio-selective metabolism of metoprolol. Biochem. J., 316: 647-654.
    • (1996) Biochem. J. , vol.316 , pp. 647-654
    • Ellis, S.W.1    Rowland, K.2    Ackland, M.J.3    Rekka, E.4    Simula, A.P.5    Lennard, M.S.6    Wolf, C.R.7    Tucker, G.T.8
  • 145
    • 0024457966 scopus 로고
    • Site-directed mutageneses of rat liver cytochrome P-450d: Catalytic activities toward benzphetamine and 7-ethoxycoumarin
    • Furuya, H., Shimizu,T., Hirano, K., Hatano, M., Fujii-Kuriyama, Y., Raag, R., and Poulos, T.L. (1989). Site-directed mutageneses of rat liver cytochrome P-450d: Catalytic activities toward benzphetamine and 7-ethoxycoumarin. Biochemistry, 28: 6848-6857.
    • (1989) Biochemistry , vol.28 , pp. 6848-6857
    • Furuya, H.1    Shimizu, T.2    Hirano, K.3    Hatano, M.4    Fujii-Kuriyama, Y.5    Raag, R.6    Poulos, T.L.7
  • 146
    • 0000589432 scopus 로고
    • Catalytic mechanism of cytochrome P-450: Evidence for a distal charge relay
    • Gerber, N.C. and Sligar, S.G. (1992). Catalytic mechanism of cytochrome P-450: Evidence for a distal charge relay. J. Am. Chem. Soc., 114: 8742-8743.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 8742-8743
    • Gerber, N.C.1    Sligar, S.G.2
  • 147
    • 0026542989 scopus 로고
    • Substrate recognition sites in cytochrome P450 family 2 (CYPB) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
    • Gotoh, O. (1992). Substrate recognition sites in cytochrome P450 family 2 (CYPB) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. J. Biol. Chem., 267: 83-90.
    • (1992) J. Biol. Chem. , vol.267 , pp. 83-90
    • Gotoh, O.1
  • 148
    • 0025955439 scopus 로고
    • Structure-function relationships of human aromatase cytochrome P-450 using molecular modeling and site-directed mutagenesis
    • Graham-Lorence, S., Khalil, M.W., Lorence, M. C., Mendelson, C.R., and Simpson, E.R. (1991). Structure-function relationships of human aromatase cytochrome P-450 using molecular modeling and site-directed mutagenesis. J. Biol. Chem., 266: 11939-11946.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11939-11946
    • Graham-Lorence, S.1    Khalil, M.W.2    Lorence, M.C.3    Mendelson, C.R.4    Simpson, E.R.5
  • 149
    • 0026562457 scopus 로고
    • Site-directed mutagenesis of cytochrome P450s CYP2A1 and CYP2A2: Influence of the distal helix on the kinetics of testosterone hydroxylation
    • Hanioka, N., Gonzalez, F.J., Lindberg, N.A., Liu, G., Gelboin, H.V., and Korzekwa, K.R. (1992). Site-directed mutagenesis of cytochrome P450s CYP2A1 and CYP2A2: Influence of the distal helix on the kinetics of testosterone hydroxylation. Biochemistry, 31: 3364-3370.
    • (1992) Biochemistry , vol.31 , pp. 3364-3370
    • Hanioka, N.1    Gonzalez, F.J.2    Lindberg, N.A.3    Liu, G.4    Gelboin, H.V.5    Korzekwa, K.R.6
  • 150
    • 0033485933 scopus 로고    scopus 로고
    • Structural forms of phenprocoumon and warfarin that are metabolized at the active site of CYP2C91
    • He, M., Korzekwa, K.R., Jones, J.P., Rettie, A.E., and Trager, W.F. (1999). Structural forms of phenprocoumon and warfarin that are metabolized at the active site of CYP2C91. Arch. Biochem. Biophys., 372: 16-28.
    • (1999) Arch. Biochem. Biophys. , vol.372 , pp. 16-28
    • He, M.1    Korzekwa, K.R.2    Jones, J.P.3    Rettie, A.E.4    Trager, W.F.5
  • 152
    • 0001541099 scopus 로고
    • Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: A possible role of the hydroxy amino acid in oxygen activation
    • Imai, M., Shimada, H., Watanabe, Y., Matsushima-Hibiya, Y., Makino, R., Koga, H., Horiuchi, T., and Ishimura, Y. (1989). Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: A possible role of the hydroxy amino acid in oxygen activation. Proc. Natl. Acad. Sci. (USA), 86: 7823-7827.
    • (1989) Proc. Natl. Acad. Sci. (USA) , vol.86 , pp. 7823-7827
    • Imai, M.1    Shimada, H.2    Watanabe, Y.3    Matsushima-Hibiya, Y.4    Makino, R.5    Koga, H.6    Horiuchi, T.7    Ishimura, Y.8
  • 153
    • 0024520452 scopus 로고
    • Point mutations at threonine-301 modify substrate specificity of rabbit liver microsomal cytochromes P-450 (laurate (ω-1)-hydroxylase and testosterone 16a-hydroxylase)
    • Imai, Y. and Nakamura, M. (1989). Point mutations at threonine-301 modify substrate specificity of rabbit liver microsomal cytochromes P-450 (laurate (ω-1)-hydroxylase and testosterone 16a-hydroxylase). Biochem. Biophys. Res. Commun., 158: 717-722.
    • (1989) Biochem. Biophys. Res. Commun. , vol.158 , pp. 717-722
    • Imai, Y.1    Nakamura, M.2
  • 154
    • 0026594706 scopus 로고
    • Role of Glu318 at the putative distal site in the catalytic function of cytochrome P450d
    • Ishigooka, M., Shimizu, T., Hiroya, K., and Hatano, M. (1992). Role of Glu318 at the putative distal site in the catalytic function of cytochrome P450d. Biochemistry, 31: 1528-1531.
    • (1992) Biochemistry , vol.31 , pp. 1528-1531
    • Ishigooka, M.1    Shimizu, T.2    Hiroya, K.3    Hatano, M.4
  • 155
    • 0025868688 scopus 로고
    • Alteration of high and low spin equilibrium by a single mutation of amino acid 209 in mouse cytochromes P450
    • Iwasaki, M., Juvonen, R., Lindberg, R., and Negishi, M. (1991). Alteration of high and low spin equilibrium by a single mutation of amino acid 209 in mouse cytochromes P450. J. Biol. Chem., 266: 3380-3382.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3380-3382
    • Iwasaki, M.1    Juvonen, R.2    Lindberg, R.3    Negishi, M.4
  • 156
    • 0027400926 scopus 로고
    • Chiral recognition at cytochrome P450 1A2 active site: Effects of mutations at the putative distal site on the bindings of asymmetrical axial ligands
    • Krainev, A.G., Shimizu, T., Ishigooka, M., Hiroya, K., and Hatano, M. (1993). Chiral recognition at cytochrome P450 1A2 active site: Effects of mutations at the putative distal site on the bindings of asymmetrical axial ligands. Biochemistry, 32: 1951-1957.
    • (1993) Biochemistry , vol.32 , pp. 1951-1957
    • Krainev, A.G.1    Shimizu, T.2    Ishigooka, M.3    Hiroya, K.4    Hatano, M.5
  • 157
    • 33746223991 scopus 로고    scopus 로고
    • Structural basis for stereoselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases
    • Krishnakumar, A.M., Nocek, B.P., Clark, D.D., Ensign, S.A., and Peters, J.W. (2006). Structural basis for stereoselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases. Biochemistry, 45: 8831-8840.
    • (2006) Biochemistry , vol.45 , pp. 8831-8840
    • Krishnakumar, A.M.1    Nocek, B.P.2    Clark, D.D.3    Ensign, S.A.4    Peters, J.W.5
  • 159
    • 59249100026 scopus 로고    scopus 로고
    • Probing stereoselectivity and pro-chirality of hydride transfer during short-chain alcohol dehydrogenase activity: A combined quantitative 2H NMR and computational approach.
    • Kwiecien, R.A., Ayadi, F., Nemmaoui, Y., Silvestre, V., Zhang, B.L., and Robins, R.J. (2009). Probing stereoselectivity and pro-chirality of hydride transfer during short-chain alcohol dehydrogenase activity: A combined quantitative 2H NMR and computational approach. Arch. Biochem. Biophys., 482: 42-51.
    • (2009) Arch. Biochem. Biophys. , vol.482 , pp. 42-51
    • Kwiecien, R.A.1    Ayadi, F.2    Nemmaoui, Y.3    Silvestre, V.4    Zhang, B.L.5    Robins, R.J.6
  • 160
    • 0024832753 scopus 로고
    • A conserved residue of cytochrome P-450 is involved in heme-oxygen stability and activation.
    • Martinis, S.A., Atkins, W.M., Stayton, P.S., and Sligar, S.G. (1989). A conserved residue of cytochrome P-450 is involved in heme-oxygen stability and activation. J. Am. Chem. Soc., 111: 9252-9253.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 9252-9253
    • Martinis, S.A.1    Atkins, W.M.2    Stayton, P.S.3    Sligar, S.G.4
  • 161
    • 67349134721 scopus 로고    scopus 로고
    • A comparative analysis of binding sites between mouse CYP2C38 and CYP2C39 based on homology modeling, molecular dynamics simulation and docking studies
    • Meng, X.-Yu, Zheng, Q.C., and Zhang, H.-X. (2009). A comparative analysis of binding sites between mouse CYP2C38 and CYP2C39 based on homology modeling, molecular dynamics simulation and docking studies. Biochim. Biophys. Acta., 1794: 1066-1072.
    • (2009) Biochim. Biophys. Acta. , vol.1794 , pp. 1066-1072
    • Meng X.-Yu Zheng, Q.C.1    Zhang, H.-X.2
  • 162
    • 4644275807 scopus 로고    scopus 로고
    • Mechanism of oxidation reactions catalyzed by cytochrome p450 enzymes
    • Meunier, B., de Visser, S.P., and Shaik, S. (2004). Mechanism of oxidation reactions catalyzed by cytochrome p450 enzymes. Chem. Rev., 104: 3947-3980.
    • (2004) Chem. Rev. , vol.104 , pp. 3947-3980
    • Meunier, B.1    de Visser, S.P.2    Shaik, S.3
  • 163
    • 0032581360 scopus 로고    scopus 로고
    • Chiral recognition at the heme active site of nitric oxide synthase is markedly enhanced by L-arginine and 5,6,7,8-tetrahydrobiopterin
    • Nakano, K., Sagami, I., Daff, S., and Shimizu, T. (1998). Chiral recognition at the heme active site of nitric oxide synthase is markedly enhanced by L-arginine and 5,6,7,8-tetrahydrobiopterin. Biochem. Biophys. Res. Commun., 248: 767-772.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 767-772
    • Nakano, K.1    Sagami, I.2    Daff, S.3    Shimizu, T.4
  • 165
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P450cam
    • Poulos, T.L., Finzel, B.C., and Howard, A.J. (1987). High-resolution crystal structure of cytochrome P450cam. J. Mol. Biol., 195: 687-700.
    • (1987) J. Mol. Biol. , vol.195 , pp. 687-700
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 166
    • 0022273620 scopus 로고
    • The 2.6Å crystal structure of Pseudomonas putida cytochrome P-450
    • Poulos, T.L., Finzel, B.C., Gunsalus, I.C., Wagner, G.C., and Kraut, J. (1985). The 2.6Å crystal structure of Pseudomonas putida cytochrome P-450. J. Biol. Chem., 260: 16122-16130.
    • (1985) J. Biol. Chem. , vol.260 , pp. 16122-16130
    • Poulos, T.L.1    Finzel, B.C.2    Gunsalus, I.C.3    Wagner, G.C.4    Kraut, J.5
  • 167
    • 0026352457 scopus 로고
    • Crystal structure of the cytochrome P-450cam active site mutant Thr252Ala
    • Raag, R., Martinis, S.A., Sligar, S.G., and Poulos, T.L. (1991). Crystal structure of the cytochrome P-450cam active site mutant Thr252Ala. Biochemistry, 30: 11420-11429.
    • (1991) Biochemistry , vol.30 , pp. 11420-11429
    • Raag, R.1    Martinis, S.A.2    Sligar, S.G.3    Poulos, T.L.4
  • 168
    • 34248596797 scopus 로고    scopus 로고
    • Control of oxygenation in lipoxygenase and cyclooxygenase catalysis
    • Schneider, C., Pratt, D.A., Porter, N.A., and Brash, A.R. (2007). Control of oxygenation in lipoxygenase and cyclooxygenase catalysis. Chem. Biol., 14: 473-488.
    • (2007) Chem. Biol. , vol.14 , pp. 473-488
    • Schneider, C.1    Pratt, D.A.2    Porter, N.A.3    Brash, A.R.4
  • 169
    • 3543038251 scopus 로고    scopus 로고
    • Active-site characteristics of CYP2C19 and CYP2C9 probed with hydantoin and barbiturate inhibitors
    • Suzuki, H., Kneller, M.B., Rock, D.A. Jones, J.P., Trager, W.F., and Rettiea, A.E. (2004). Active-site characteristics of CYP2C19 and CYP2C9 probed with hydantoin and barbiturate inhibitors. Arch. Biochem. Biophys., 429: 1-15.
    • (2004) Arch. Biochem. Biophys. , vol.429 , pp. 1-15
    • Suzuki, H.1    Kneller, M.B.2    Rock, D.A.3    Jones, J.P.4    Trager, W.F.5    Rettiea, A.E.6
  • 171
    • 0042265520 scopus 로고    scopus 로고
    • Crystal structure of human cytochrome P450 2C9 with bound warfarin
    • Williams, P.A., Cosme, J., Ward, A., Angove, H.C., Vinkovic, D.M., and Jhoti, H. (2003). Crystal structure of human cytochrome P450 2C9 with bound warfarin. Nature, 424: 464-468.
    • (2003) Nature , vol.424 , pp. 464-468
    • Williams, P.A.1    Cosme, J.2    Ward, A.3    Angove, H.C.4    Vinkovic, D.M.5    Jhoti, H.6
  • 172
    • 0026558679 scopus 로고
    • Site-directed mutagenesis study of human placental aromatase
    • Zhou, D., Korzekwa, K.R., Poulos, T., and Chen, S. (1992). Site-directed mutagenesis study of human placental aromatase. J Biol. Chem., 267: 762-768.
    • (1992) J Biol. Chem. , vol.267 , pp. 762-768
    • Zhou, D.1    Korzekwa, K.R.2    Poulos, T.3    Chen, S.4
  • 173
    • 0025874005 scopus 로고
    • Site-specific incorporation of nonnatural residues during in vitro protein biosynthesis with semisynthetic aminoacyl-tRNAs
    • Bain, J.D., Diala, E.S., Glabe, C.G., Wacker, D.A., Lyttle, M.H., Dix, T.A., and Chamberlin, A.R. (1991). Site-specific incorporation of nonnatural residues during in vitro protein biosynthesis with semisynthetic aminoacyl-tRNAs. Biochemistry, 30: 5411-5421.
    • (1991) Biochemistry , vol.30 , pp. 5411-5421
    • Bain, J.D.1    Diala, E.S.2    Glabe, C.G.3    Wacker, D.A.4    Lyttle, M.H.5    Dix, T.A.6    Chamberlin, A.R.7
  • 175
    • 0019873831 scopus 로고
    • Stereochemical control of ribosomal peptidyltransferase reaction: Role of amino acid sidechain orientation of acceptor substrate
    • Bhuta, A., Quiggle, K., Ott, T., Ringer, D., and Chladek, S. (1981). Stereochemical control of ribosomal peptidyltransferase reaction: Role of amino acid sidechain orientation of acceptor substrate. Biochemistry, 20: 8-15.
    • (1981) Biochemistry , vol.20 , pp. 8-15
    • Bhuta, A.1    Quiggle, K.2    Ott, T.3    Ringer, D.4    Chladek, S.5
  • 176
    • 0025731583 scopus 로고
    • Structure and function of telomeres
    • Blackburn, E.H. (1991). Structure and function of telomeres. Nature, 350: 569-573.
    • (1991) Nature , vol.350 , pp. 569-573
    • Blackburn, E.H.1
  • 178
    • 0014219470 scopus 로고
    • D-Tyrosyl RNA: Formation, hydrolysis and utilization for protein synthesis
    • Calendar, R. and Berg, P. (1967). D-Tyrosyl RNA: Formation, hydrolysis and utilization for protein synthesis. J. Mol. Biol., 26: 39-54.
    • (1967) J. Mol. Biol. , vol.26 , pp. 39-54
    • Calendar, R.1    Berg, P.2
  • 179
    • 0037069377 scopus 로고    scopus 로고
    • Catalysis of amide synthesis by RNA phosphodiester and hydroxyl groups
    • Chamberlin, S.I. Merino, E.J., and Weeks, K.M. (2002). Catalysis of amide synthesis by RNA phosphodiester and hydroxyl groups. Proc. Natl. Acad. Sci. (USA)., 99: 14688-14693.
    • (2002) Proc. Natl. Acad. Sci. (USA). , vol.99 , pp. 14688-14693
    • Chamberlin, S.I.1    Merino, E.J.2    Weeks, K.M.3
  • 182
    • 0038547955 scopus 로고    scopus 로고
    • Enhanced D-amino acid incorporation into protein by modified ribosomes
    • Dedkova, L.M., Fahmi, N.E., Golovine, S.Y., and Hecht, S.M. (2003). Enhanced D-amino acid incorporation into protein by modified ribosomes. J. Am. Chem. Soc., 125: 6616-6617.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6616-6617
    • Dedkova, L.M.1    Fahmi, N.E.2    Golovine, S.Y.3    Hecht, S.M.4
  • 184
    • 0029094279 scopus 로고
    • Stereospecificity of human DNA polymerases alpha, beta, gamma, delta and epsilon, HIV reverse transcriptase, HSV-1 DNA polymerase, calf thymus terminal transferase and Escherichia coli DNA polymerase I in recognizing D- and L-thymidine 59-triphosphate as substrate
    • Focher, F., Maga, G., Bendiscioli, A., Capobianco, M., Colonna, F., Garbesi, A., and Spadari, S. (1995). Stereospecificity of human DNA polymerases alpha, beta, gamma, delta and epsilon, HIV reverse transcriptase, HSV-1 DNA polymerase, calf thymus terminal transferase and Escherichia coli DNA polymerase I in recognizing D- and L-thymidine 59-triphosphate as substrate. Nucleic Acids Res., 23: 2840-2847.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2840-2847
    • Focher, F.1    Maga, G.2    Bendiscioli, A.3    Capobianco, M.4    Colonna, F.5    Garbesi, A.6    Spadari, S.7
  • 185
    • 0034190019 scopus 로고    scopus 로고
    • Structures, vibrational absorption and vibrational circular dichroism spectra of L-alanine in aqueous solution: A density functional theory and RHF study
    • Friman, K., Bohr, H., Jalkanen, K.J., and Suhai, S. (2000). Structures, vibrational absorption and vibrational circular dichroism spectra of L-alanine in aqueous solution: A density functional theory and RHF study. Chem. Phys., 255: 165-194.
    • (2000) Chem. Phys. , vol.255 , pp. 165-194
    • Friman, K.1    Bohr, H.2    Jalkanen, K.J.3    Suhai, S.4
  • 186
    • 0038626673 scopus 로고    scopus 로고
    • Revision C.02, Wallingford, CT: Gaussian, Inc
    • Frisch, M.J. et al. (2004). Gaussian 03, Revision C.02, Wallingford, CT: Gaussian, Inc.
    • (2004) Gaussian 03
    • Frisch, M.J.1
  • 189
    • 0025279931 scopus 로고
    • Telomeres shorten during ageing of human fibroblasts
    • Harley, C.B., Futcher, A.B., and Greider, C.W. (1990). Telomeres shorten during ageing of human fibroblasts. Nature, 345: 458-460.
    • (1990) Nature , vol.345 , pp. 458-460
    • Harley, C.B.1    Futcher, A.B.2    Greider, C.W.3
  • 191
    • 20644440861 scopus 로고
    • Participation of isomeric tRNA's in the partial reactions of protein biosynthesis
    • Hecht, S.M. (1977). Participation of isomeric tRNA's in the partial reactions of protein biosynthesis. Tetrahedron, 33: 1671-1696.
    • (1977) Tetrahedron , vol.33 , pp. 1671-1696
    • Hecht, S.M.1
  • 192
    • 0008178378 scopus 로고
    • Probing the synthetic capabilities of a center of biochemical catalysis
    • Hecht, S.M. (1992). Probing the synthetic capabilities of a center of biochemical catalysis. Acc. Chem. Res., 25: 545-552.
    • (1992) Acc. Chem. Res. , vol.25 , pp. 545-552
    • Hecht, S.M.1
  • 193
    • 0024293249 scopus 로고
    • Ribosomal binding and dipeptide formation by misacylated tRNAPhe's
    • Heckler, T.G., Roesser, J.R., Xu, C., Chang, P.I., and Hecht, S. (1988). Ribosomal binding and dipeptide formation by misacylated tRNAPhe's, Biochemistry, 27: 7254-7262.
    • (1988) Biochemistry , vol.27 , pp. 7254-7262
    • Heckler, T.G.1    Roesser, J.R.2    Xu, C.3    Chang, P.I.4    Hecht, S.5
  • 194
    • 0020584812 scopus 로고
    • Dipeptide formation with misacylated tRNAPhes
    • Heckler, T.G., Zama, Y., Naka, T., and Hecht, S. (1983). Dipeptide formation with misacylated tRNAPhes. J. Biol. Chem., 258: 4492-4495.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4492-4495
    • Heckler, T.G.1    Zama, Y.2    Naka, T.3    Hecht, S.4
  • 197
    • 0035313507 scopus 로고    scopus 로고
    • A comparison of aqueous solvent models used in the calculation of the Raman and ROA spectra of L-alanine
    • Jalkanen, K.J., Nieminen, R.M., Friman, K., Bohr, J., Bohr, H., Wade, R.C., Tajkhorshid, E., and Suhai, S. (2001). A comparison of aqueous solvent models used in the calculation of the Raman and ROA spectra of L-alanine. Chem. Phys., 265: 125-151.
    • (2001) Chem. Phys. , vol.265 , pp. 125-151
    • Jalkanen, K.J.1    Nieminen, R.M.2    Friman, K.3    Bohr, J.4    Bohr, H.5    Wade, R.C.6    Tajkhorshid, E.7    Suhai, S.8
  • 199
    • 0033482851 scopus 로고    scopus 로고
    • L-Alanyl-L-alanine in the zwitterionic state: Structures determined in the presence of explicit water molecules and with continuum models using density functional theory
    • Knapp-Mohammady, M., Jalkanen, K.J., Nardi, F., Wade, R.C., and Suhai, S. (1999). L-Alanyl-L-alanine in the zwitterionic state: Structures determined in the presence of explicit water molecules and with continuum models using density functional theory. Chem. Phys., 240: 63-77.
    • (1999) Chem. Phys. , vol.240 , pp. 63-77
    • Knapp-Mohammady, M.1    Jalkanen, K.J.2    Nardi, F.3    Wade, R.C.4    Suhai, S.5
  • 200
    • 0033557321 scopus 로고    scopus 로고
    • Molecular basis for the enantioselectivity of HIV-1 reverse transcriptase: Role of the 3'-hydroxyl group of the L-(ß)-ribose in chiral discrimination between D- and L-enantiomers of deoxy- and dideoxy-nucleoside triphosphate analogs
    • Maga, G., Amacker, M., Hübscher, U., Gosselin, G., Imbach, J.-L., Mathé, C., Faraj, A., Sommadossi, J.-P., and Spadari, S. (1999). Molecular basis for the enantioselectivity of HIV-1 reverse transcriptase: Role of the 3'-hydroxyl group of the L-(ß)-ribose in chiral discrimination between D- and L-enantiomers of deoxy- and dideoxy-nucleoside triphosphate analogs. Nucleic Acids Res., 27: 972-978.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 972-978
    • Maga, G.1    Amacker, M.2    Hübscher, U.3    Gosselin, G.4    Imbach, J.-L.5    Mathé, C.6    Faraj, A.7    Sommadossi, J.-P.8    Spadari, S.9
  • 202
    • 0014219393 scopus 로고
    • Ribosome-catalysed reaction of puromycin with a formylmethionine-containing oligonucleotide
    • Monro, R.E. and Marcker, K.A. (1967). Ribosome-catalysed reaction of puromycin with a formylmethionine-containing oligonucleotide. J. Mol. Biol., 25: 347-350.
    • (1967) J. Mol. Biol. , vol.25 , pp. 347-350
    • Monro, R.E.1    Marcker, K.A.2
  • 203
    • 0014360492 scopus 로고
    • Ribosome catalyzed peptidyl transfer: Substrate specificity at the P-site
    • Monro, R.E., Cerna, J., and Marcker, K.A. (1968). Ribosome catalyzed peptidyl transfer: Substrate specificity at the P-site. Proc. Natl. Acad. Sci. (USA), 61: 1042-1049.
    • (1968) Proc. Natl. Acad. Sci. (USA) , vol.61 , pp. 1042-1049
    • Monro, R.E.1    Cerna, J.2    Marcker, K.A.3
  • 204
    • 0024325562 scopus 로고
    • The human telomere terminal transferase enzyme is a ribonucleoprotein that synthesizes TTAGGG repeats
    • Morin, G.B. (1989). The human telomere terminal transferase enzyme is a ribonucleoprotein that synthesizes TTAGGG repeats. Cell, 59: 521-529.
    • (1989) Cell , vol.59 , pp. 521-529
    • Morin, G.B.1
  • 205
    • 0942279303 scopus 로고    scopus 로고
    • Role of secondary level chiral structure in the process of molecular recognition of ligand: Study of model helical peptide
    • Nandi, N. (2004). Role of secondary level chiral structure in the process of molecular recognition of ligand: Study of model helical peptide. J. Phys. Chem. B., 108: 789-797.
    • (2004) J. Phys. Chem. B. , vol.108 , pp. 789-797
    • Nandi, N.1
  • 206
    • 0000603264 scopus 로고
    • Puromycine inhibition of protein synthesis: Incorporation of puromycin into peptide chains
    • Nathans, D. (1964). Puromycine inhibition of protein synthesis: Incorporation of puromycin into peptide chains. Proc. Natl. Acad. Sci. (USA), 51: 585-592.
    • (1964) Proc. Natl. Acad. Sci. (USA) , vol.51 , pp. 585-592
    • Nathans, D.1
  • 207
    • 0001412985 scopus 로고
    • Structural requirements for puromycin inhibition of protein synthesis
    • Nathans, D. and Neidle, A. (1963). Structural requirements for puromycin inhibition of protein synthesis. Nature (Lond.), 197: 1076-1077.
    • (1963) Nature (Lond.) , vol.197 , pp. 1076-1077
    • Nathans, D.1    Neidle, A.2
  • 208
    • 0009758179 scopus 로고
    • Evaluation of the density functional approximation on the computation of hydrogen bond interactions
    • Novoa, J.J. and Sosa, C. (1995). Evaluation of the density functional approximation on the computation of hydrogen bond interactions. J. Phys. Chem., 99: 15837-15845.
    • (1995) J. Phys. Chem. , vol.99 , pp. 15837-15845
    • Novoa, J.J.1    Sosa, C.2
  • 209
    • 0032080678 scopus 로고    scopus 로고
    • Telomerase from human leukemia cells: Properties and its interaction with deoxynucleoside analogues
    • Pai, R.B., Pai, S.B., Kukhanova, M., Dutschman, G.E., Guo, X., and Cheng, Y. -C. (1998). Telomerase from human leukemia cells: Properties and its interaction with deoxynucleoside analogues. Cancer Res., 58: 1909-1913.
    • (1998) Cancer Res. , vol.58 , pp. 1909-1913
    • Pai, R.B.1    Pai, S.B.2    Kukhanova, M.3    Dutschman, G.E.4    Guo, X.5    Cheng, Y.-C.6
  • 210
    • 23944434896 scopus 로고    scopus 로고
    • Accurate interaction energies for argon, krypton, and benzene dimers from perturbation theory based on the Kohn- Sham model
    • Podeszwa, R. and Szalewicz, K. (2005). Accurate interaction energies for argon, krypton, and benzene dimers from perturbation theory based on the Kohn- Sham model. Chem. Phys. Lett., 412: 488-493.
    • (2005) Chem. Phys. Lett. , vol.412 , pp. 488-493
    • Podeszwa, R.1    Szalewicz, K.2
  • 211
    • 0019876111 scopus 로고
    • Donor site of ribosomal peptidyltransferase: Investigation of substrate specificity using 2' (3')-O-(N-Acylaminoacyl) dinucleoside phosphates as models of the 3' terminus of N-acylaminoacyl transfer ribonucleic acid
    • Quiggle, K., Kumar, G., Ott, T.W., Ryu, E.K., and Chladek, S. (1981). Donor site of ribosomal peptidyltransferase: Investigation of substrate specificity using 2' (3')-O-(N-Acylaminoacyl) dinucleoside phosphates as models of the 3' terminus of N-acylaminoacyl transfer ribonucleic acid. Biochemistry, 20: 3480-3485.
    • (1981) Biochemistry , vol.20 , pp. 3480-3485
    • Quiggle, K.1    Kumar, G.2    Ott, T.W.3    Ryu, E.K.4    Chladek, S.5
  • 212
    • 21044455301 scopus 로고    scopus 로고
    • Ten remarks on peptide bond formation on the ribosome
    • Rodnina, M.V., Beringer, M., and Bieling, P. (2005). Ten remarks on peptide bond formation on the ribosome. Biochem. Soc. Trans., 33: 493-498.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 493-498
    • Rodnina, M.V.1    Beringer, M.2    Bieling, P.3
  • 213
    • 0024403732 scopus 로고
    • Preparation of misacylated aminoacyl-tRNAPhe's useful as probes of the ribosomal acceptor site
    • Roesser, J.R., Xu, C., Payne, R.C. Surratt, C.K., and Hecht, S. (1989). Preparation of misacylated aminoacyl-tRNAPhe's useful as probes of the ribosomal acceptor site. Biochemistry, 28: 5185-5195.
    • (1989) Biochemistry , vol.28 , pp. 5185-5195
    • Roesser, J.R.1    Xu, C.2    Payne, R.C.3    Surratt, C.K.4    Hecht, S.5
  • 214
    • 27644557445 scopus 로고    scopus 로고
    • Structural insights into the roles of water and the 2'-hydroxyl of the P site tRNA in the peptidyl transferase reaction
    • Schmeing, T.M., Huang, K.S., Kitchen, D.E., Strobel, S.A., and Steitz, T.A. (2005). Structural insights into the roles of water and the 2'-hydroxyl of the P site tRNA in the peptidyl transferase reaction. Mol. Cell., 20: 437-448.
    • (2005) Mol. Cell. , vol.20 , pp. 437-448
    • Schmeing, T.M.1    Huang, K.S.2    Kitchen, D.E.3    Strobel, S.A.4    Steitz, T.A.5
  • 215
    • 70449234472 scopus 로고
    • Purification and properties of tyrosine-activating enzyme of hog pancreas
    • Schweet, R.S. and Allen, E. (1958). Purification and properties of tyrosine-activating enzyme of hog pancreas. J. Biol. Chem., 233: 1104-1108.
    • (1958) J. Biol. Chem. , vol.233 , pp. 1104-1108
    • Schweet, R.S.1    Allen, E.2
  • 216
    • 23944472625 scopus 로고    scopus 로고
    • What are the roles of substrate-assisted catalysis and proximity effects in peptide bond formation by the ribosome
    • Sharma, P.K., Xiang, Y., Kato, M., and Warshel, A. (2005). What are the roles of substrate-assisted catalysis and proximity effects in peptide bond formation by the ribosome? Biochemistry, 44: 11307-11310.
    • (2005) Biochemistry , vol.44 , pp. 11307-11310
    • Sharma, P.K.1    Xiang, Y.2    Kato, M.3    Warshel, A.4
  • 218
    • 0031822118 scopus 로고    scopus 로고
    • Molecular basis for the antiviral and anticancer activities of unnatural L-beta-nucleosides
    • Spadari S., Maga G., Verri, A., and Focher, F. (1998). Molecular basis for the antiviral and anticancer activities of unnatural L-beta-nucleosides. Expert Opin. Investig. Drugs., 8: 1285-1300.
    • (1998) Expert Opin. Investig. Drugs. , vol.8 , pp. 1285-1300
    • Spadari, S.1    Maga, G.2    Verri, A.3    Focher, F.4
  • 219
    • 0018624914 scopus 로고
    • The -C-C-A end of tRNA and its role in protein biosynthesis
    • Sprinzl, M. and Cramer, F. (1979). The -C-C-A end of tRNA and its role in protein biosynthesis. Prog. Nucleic Acid Res. Mol. Biol., 22: 1-69.
    • (1979) Prog. Nucleic Acid Res. Mol. Biol. , vol.22 , pp. 1-69
    • Sprinzl, M.1    Cramer, F.2
  • 220
    • 0037668349 scopus 로고    scopus 로고
    • The puromycin route to assess stereo- and regiochemical constraints on peptide bond formation in eukaryotic ribosomes
    • Starck, S.R., Qi, X., Olsen, B.N., and Roberts, R.W. (2003). The puromycin route to assess stereo- and regiochemical constraints on peptide bond formation in eukaryotic ribosomes. J. Am. Chem. Soc., 125: 8090-8091.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8090-8091
    • Starck, S.R.1    Qi, X.2    Olsen, B.N.3    Roberts, R.W.4
  • 221
    • 0001152446 scopus 로고    scopus 로고
    • Structure and vibrational spectra of the zwitterion L-alanine in the presence of explicit water molecules: A density functional analysis
    • Tajkhorshid, E., Jalkanen, K.J., and Suhai, S. (1998). Structure and vibrational spectra of the zwitterion L-alanine in the presence of explicit water molecules: A density functional analysis. J. Phys. Chem., 102: 5899-5913.
    • (1998) J. Phys. Chem. , vol.102 , pp. 5899-5913
    • Tajkhorshid, E.1    Jalkanen, K.J.2    Suhai, S.3
  • 222
    • 0034072173 scopus 로고    scopus 로고
    • Interaction of deoxyguanosine nucleotide analogs with human telomerase
    • Tendian, S.W. and Parker, W.B. (2000). Interaction of deoxyguanosine nucleotide analogs with human telomerase. Mol. Pharmacol., 57: 695-699.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 695-699
    • Tendian, S.W.1    Parker, W.B.2
  • 223
    • 33744477096 scopus 로고    scopus 로고
    • Comparison of the intermolecular energy surfaces of amino acids: Orientation-dependent chiral discrimination
    • Thirumoorthy, K. and Nandi, N. (2006). Comparison of the intermolecular energy surfaces of amino acids: Orientation-dependent chiral discrimination. J. Phys. Chem. B., 110: 8840-8849.
    • (2006) J. Phys. Chem. B. , vol.110 , pp. 8840-8849
    • Thirumoorthy, K.1    Nandi, N.2
  • 224
    • 34548561996 scopus 로고    scopus 로고
    • Homochiral preference in peptide synthesis in ribosome: Role of amino terminal, peptidyl terminal and U2620
    • Thirumoorthy, K. and Nandi, N. (2007a). Homochiral preference in peptide synthesis in ribosome: Role of amino terminal, peptidyl terminal and U2620. J. Phys. Chem. B, 111: 9999-10004.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 9999-10004
    • Thirumoorthy, K.1    Nandi, N.2
  • 225
    • 34547661986 scopus 로고    scopus 로고
    • Water catalyzed peptide bond formation in L-alanine dipeptide: The role of weak hydrogen bonding
    • Thirumoorthy, K. and Nandi, N. (2007b). Water catalyzed peptide bond formation in L-alanine dipeptide: The role of weak hydrogen bonding. J. Mol. Str. (Theo Chem), 818: 107-118.
    • (2007) J. Mol. Str. (Theo Chem) , vol.818 , pp. 107-118
    • Thirumoorthy, K.1    Nandi, N.2
  • 226
    • 49349097901 scopus 로고    scopus 로고
    • Role of chirality of the sugar ring in the ribosomal peptide synthesis
    • Thirumoorthy, K. and Nandi, N. (2008). Role of chirality of the sugar ring in the ribosomal peptide synthesis. J. Phys. Chem. B., 112: 9187-9195.
    • (2008) J. Phys. Chem. B. , vol.112 , pp. 9187-9195
    • Thirumoorthy, K.1    Nandi, N.2
  • 227
    • 24644461086 scopus 로고    scopus 로고
    • Mechanism of peptide bond synthesis on the ribosome
    • Trobro, S. and Åqvist, J. (2005). Mechanism of peptide bond synthesis on the ribosome. Proc. Natl. Acad. Sci. (USA), 102: 12395-12400.
    • (2005) Proc. Natl. Acad. Sci. (USA) , vol.102 , pp. 12395-12400
    • Trobro, S.1    Åqvist, J.2
  • 229
    • 33846616455 scopus 로고    scopus 로고
    • Exploring the mechanism of protein synthesis with modified substrates and novel intermediate mimics
    • Weinger, J.S. and Strobel, S. (2007). Exploring the mechanism of protein synthesis with modified substrates and novel intermediate mimics. Blood Cells Mol. Dis., 38: 110-116.
    • (2007) Blood Cells Mol. Dis. , vol.38 , pp. 110-116
    • Weinger, J.S.1    Strobel, S.2
  • 231
    • 0035134013 scopus 로고    scopus 로고
    • Using Kohn-Sham orbitals in symmetry- adapted perturbation theory to investigate intermolecular interactions
    • Williams, H.L. and Chabalowski, C.F. (2001). Using Kohn-Sham orbitals in symmetry- adapted perturbation theory to investigate intermolecular interactions. J. Phys. Chem. A., 105: 646-659.
    • (2001) J. Phys. Chem. A. , vol.105 , pp. 646-659
    • Williams, H.L.1    Chabalowski, C.F.2
  • 232
    • 0028207542 scopus 로고
    • Chiral discrimination of enantiomeric 2'-deoxythymidine 5'-triphosphate by HIV-1 reverse transcriptase and eukaryotic DNA polymerases
    • Yamaguchi T., Iwanami N., Shudo, K., and Saneyoshi, M. (1994). Chiral discrimination of enantiomeric 2'-deoxythymidine 5'-triphosphate by HIV-1 reverse transcriptase and eukaryotic DNA polymerases. Biochem. Biophys. Res. Commun., 200: 1023-1027.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 1023-1027
    • Yamaguchi, T.1    Iwanami, N.2    Shudo, K.3    Saneyoshi, M.4
  • 234
    • 0019875775 scopus 로고
    • Discrimination between D- and L-tyrosyl transfer ribonucleic acids in peptide chain elongation
    • Yamane, T., Miller, L., and Hopfield, J.J. (1981). Discrimination between D- and L-tyrosyl transfer ribonucleic acids in peptide chain elongation. Biochemistry, 20: 7059-7064.
    • (1981) Biochemistry , vol.20 , pp. 7059-7064
    • Yamane, T.1    Miller, L.2    Hopfield, J.J.3
  • 235
    • 2542470615 scopus 로고    scopus 로고
    • The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release
    • Youngman, E.M., Brunelle, J.L., Kochaniak, A.B., and Green, R. (2004). The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release. Cell, 117: 589-599.
    • (2004) Cell , vol.117 , pp. 589-599
    • Youngman, E.M.1    Brunelle, J.L.2    Kochaniak, A.B.3    Green, R.4
  • 237
    • 28944452159 scopus 로고    scopus 로고
    • Structures and properties of cytosine-BX3 (X=F, Cl) complexes: An investigation with DFT and MP2 methods
    • Zhang, S.G. and Yang, P. (2005). Structures and properties of cytosine-BX3 (X=F, Cl) complexes: An investigation with DFT and MP2 methods. J. Mol. Struc. (Theo Chem), 757: 77-86.
    • (2005) J. Mol. Struc. (Theo Chem) , vol.757 , pp. 77-86
    • Zhang, S.G.1    Yang, P.2
  • 238
    • 0032103824 scopus 로고    scopus 로고
    • Rhizomucor miehei lipase as the catalyst in the resolution of chiral compounds: An overview
    • Alcántara, A.R., de Fuentes, I.E., and Sinisterra, J.V. (1998). Rhizomucor miehei lipase as the catalyst in the resolution of chiral compounds: An overview. Chem. Phys. Lipids, 93: 169-184.
    • (1998) Chem. Phys. Lipids , vol.93 , pp. 169-184
    • Alcántara, A.R.1    de Fuentes, I.E.2    Sinisterra, J.V.3
  • 239
    • 0032031614 scopus 로고    scopus 로고
    • Epoxide hydrolases: New tools for the synthesis of fine organic chemicals
    • Archelas, A. and Furstoss, R. (1998). Epoxide hydrolases: New tools for the synthesis of fine organic chemicals. Trends Biotechnol., 16: 108-116.
    • (1998) Trends Biotechnol. , vol.16 , pp. 108-116
    • Archelas, A.1    Furstoss, R.2
  • 240
    • 0030869888 scopus 로고    scopus 로고
    • Epoxide hydrolases as asymmetric catalysts
    • Archer, I.V.J. (1997). Epoxide hydrolases as asymmetric catalysts. Tetrahedron, 53: 15617-15662.
    • (1997) Tetrahedron , vol.53 , pp. 15617-15662
    • Archer, I.V.J.1
  • 241
    • 0032849109 scopus 로고    scopus 로고
    • Detoxification of environmental mutagens and carcinogens: Structure, mechanism and evolution of liver epoxide hydrolase
    • Argiriadi, M.A., Morisseau, C., Hammock, B.D., and Christianson, D.W. (1999). Detoxification of environmental mutagens and carcinogens: Structure, mechanism and evolution of liver epoxide hydrolase. Proc. Natl. Acad. Sci. (USA), 96: 10637-10642.
    • (1999) Proc. Natl. Acad. Sci. (USA) , vol.96 , pp. 10637-10642
    • Argiriadi, M.A.1    Morisseau, C.2    Hammock, B.D.3    Christianson, D.W.4
  • 245
    • 0031556926 scopus 로고    scopus 로고
    • Covalent inhibition of digestive lipases: An in vitro study
    • Gargouri, Y., Ransac, S. and Verger, R. (1997). Covalent inhibition of digestive lipases: An in vitro study. Biochim. Biophys. Acta., 1344: 6-37.
    • (1997) Biochim. Biophys. Acta. , vol.1344 , pp. 6-37
    • Gargouri, Y.1    Ransac, S.2    Verger, R.3
  • 248
    • 0028103723 scopus 로고
    • Two conformational states of Candida rugosa lipase
    • Grochulski, P., Li, Y., Schrag, J.D. and Cygler, M. (1994). Two conformational states of Candida rugosa lipase. Protein Sci., 3: 82-91.
    • (1994) Protein Sci. , vol.3 , pp. 82-91
    • Grochulski, P.1    Li, Y.2    Schrag, J.D.3    Cygler, M.4
  • 249
    • 33751280486 scopus 로고    scopus 로고
    • Insights into the reaction mechanism of soluble epoxide hydrolase from theoretical active site mutants
    • Hopmann, K.H. and Himo, F. (2006). Insights into the reaction mechanism of soluble epoxide hydrolase from theoretical active site mutants. J. Phys. Chem. B., 110: 21299-21310.
    • (2006) J. Phys. Chem. B. , vol.110 , pp. 21299-21310
    • Hopmann, K.H.1    Himo, F.2
  • 251
    • 0032102831 scopus 로고    scopus 로고
    • Structural investigations of the regio- and enantioselectivity of lipases
    • Lang, D.A. and Dijkstra, B.W. (1998). Structural investigations of the regio- and enantioselectivity of lipases. Chem. Phys. Lipids, 93: 115-122.
    • (1998) Chem. Phys. Lipids , vol.93 , pp. 115-122
    • Lang, D.A.1    Dijkstra, B.W.2
  • 252
    • 0034829750 scopus 로고    scopus 로고
    • A theoretical examination of the acid-catalyzed and noncatalyzed ring-opening reaction of an oxirane by nucleophilic addition of acetate. Implications to epoxide hydrolases.
    • Lau, E.Y., Newby, Z.E., and Bruice, T.C. (2001). A theoretical examination of the acid-catalyzed and noncatalyzed ring-opening reaction of an oxirane by nucleophilic addition of acetate. Implications to epoxide hydrolases. J. Am. Chem. Soc., 123: 3350-3357.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3350-3357
    • Lau, E.Y.1    Newby, Z.E.2    Bruice, T.C.3
  • 253
    • 0032512591 scopus 로고    scopus 로고
    • Enantioselectivity of a recombinant epoxide hydrolase from Agrobacterium radiobacter
    • Lutje Spelberg, J.H., Rink, R., Kellogg, R.M., and Janssen, D.B. (1998). Enantioselectivity of a recombinant epoxide hydrolase from Agrobacterium radiobacter. Tetrahedron: Asymmetry, 9: 459-482.
    • (1998) Tetrahedron: Asymmetry , vol.9 , pp. 459-482
    • Lutje Spelberg, J.H.1    Rink, R.2    Kellogg, R.M.3    Janssen, D.B.4
  • 255
    • 0942279303 scopus 로고    scopus 로고
    • Role of secondary level chiral structure in the process of molecular recognition of ligand: Study of model helical peptide
    • Nandi, N. (2004). Role of secondary level chiral structure in the process of molecular recognition of ligand: Study of model helical peptide. J. Phys. Chem. B., 108: 789-797.
    • (2004) J. Phys. Chem. B. , vol.108 , pp. 789-797
    • Nandi, N.1
  • 256
    • 70350173558 scopus 로고    scopus 로고
    • Chiral discrimination in the confined environment of biological nanospace: Reactions and interactions involving amino acids and peptides
    • Nandi, N. (2009). Chiral discrimination in the confined environment of biological nanospace: Reactions and interactions involving amino acids and peptides. Int. Rev. Phys. Chem., 28: 111-167.
    • (2009) Int. Rev. Phys. Chem. , vol.28 , pp. 111-167
    • Nandi, N.1
  • 257
    • 0033591361 scopus 로고    scopus 로고
    • The x-ray structure of epoxide hydrolase from Agrobacterium radiobacter AD1: An enzyme to detoxify harmful epoxides
    • Nardini, M., Ridder, I.S., Rozeboom, H.J., Kalk, K.H., Rink, R., Janssen, D.B., and Dijkstra, B.W. (1999). The x-ray structure of epoxide hydrolase from Agrobacterium radiobacter AD1: An enzyme to detoxify harmful epoxides. J. Biol. Chem., 274: 14579-14586.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14579-14586
    • Nardini, M.1    Ridder, I.S.2    Rozeboom, H.J.3    Kalk, K.H.4    Rink, R.5    Janssen, D.B.6    Dijkstra, B.W.7
  • 258
    • 14644429730 scopus 로고    scopus 로고
    • Epoxide hydrolases: Their roles and interactions with lipid metabolism
    • Newman, J.W., Morisseau, C., and Hammock, B.D. (2005). Epoxide hydrolases: Their roles and interactions with lipid metabolism. Prog Lipid Res. 44: 1-51.
    • (2005) Prog Lipid Res. , vol.44 , pp. 1-51
    • Newman, J.W.1    Morisseau, C.2    Hammock, B.D.3
  • 259
    • 0032558964 scopus 로고    scopus 로고
    • Kinetic mechanism of the enantioselective conversion of styrene oxide by epoxide hydrolase from Agrobacterium radiobacter AD1
    • Rink, R. and Janssen, D.B. (1998). Kinetic mechanism of the enantioselective conversion of styrene oxide by epoxide hydrolase from Agrobacterium radiobacter AD1. Biochemistry, 37: 18119-18127.
    • (1998) Biochemistry , vol.37 , pp. 18119-18127
    • Rink, R.1    Janssen, D.B.2
  • 260
    • 1942517067 scopus 로고    scopus 로고
    • Reaction mechanism of soluble epoxide hydrolase: Insights from molecular dynamics simulations
    • Schiøtt, B. and Bruice, T.C. (2002). Reaction mechanism of soluble epoxide hydrolase: Insights from molecular dynamics simulations. J. Am. Chem. Soc., 124: 14558-14570.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 14558-14570
    • Schiøtt, B.1    Bruice, T.C.2
  • 261
    • 0029911205 scopus 로고    scopus 로고
    • The catalytic mechanism of microsomal epoxide hydrolase involves reversible formation and rate-limiting hydrolysis of the alkyl-enzyme intermediate
    • Tzeng, H.-F., Laughlin, L.T., Lin, S., and Armstrong, R.M. (1996). The catalytic mechanism of microsomal epoxide hydrolase involves reversible formation and rate-limiting hydrolysis of the alkyl-enzyme intermediate. J. Am. Chem. Soc., 118: 9436-9437.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9436-9437
    • Tzeng, H.-F.1    Laughlin, L.T.2    Lin, S.3    Armstrong, R.M.4
  • 262
    • 0019501742 scopus 로고
    • Stereochemistry in the oxidative metabolism of styrene by hepatic microsomes
    • Watabe, T., Ozawe, N., and Hiratsuka, A. (1981). Stereochemistry in the oxidative metabolism of styrene by hepatic microsomes. Biochem. Pharmacol., 30: 1695-1698.
    • (1981) Biochem. Pharmacol. , vol.30 , pp. 1695-1698
    • Watabe, T.1    Ozawe, N.2    Hiratsuka, A.3
  • 263
    • 0026694205 scopus 로고
    • Enantio- and regioselectivity in the epoxide hydrolase catalyzed ring opening of simple aliphatic oxiranes: Part I: Monoalkyl substituted oxiranes
    • Wistuba, D. and Schurig, V. (1992). Enantio- and regioselectivity in the epoxide hydrolase catalyzed ring opening of simple aliphatic oxiranes: Part I: Monoalkyl substituted oxiranes. Chirality, 4: 178-184.
    • (1992) Chirality , vol.4 , pp. 178-184
    • Wistuba, D.1    Schurig, V.2
  • 264
    • 0026647474 scopus 로고
    • Enantio- and regioselectivity in the epoxide hydrolase catalyzed ring opening of simple aliphatic oxiranes: Part II: Dialkyl and trialkylsubstituted oxiranes
    • Wistuba, D., Träger, O. and Schurig, V. (1992). Enantio- and regioselectivity in the epoxide hydrolase catalyzed ring opening of simple aliphatic oxiranes: Part II: Dialkyl and trialkylsubstituted oxiranes. Chirality, 4: 185-192.
    • (1992) Chirality , vol.4 , pp. 185-192
    • Wistuba, D.1    Träger, O.2    Schurig, V.3
  • 265
    • 33645739748 scopus 로고    scopus 로고
    • Oxidoreductases and hydroxynitrilase lyases: Complementary enzymatic technologies for chiral alcohols
    • Daußmann, T., Rosen, T.C., and Dünkelmann, P. (2006). Oxidoreductases and hydroxynitrilase lyases: Complementary enzymatic technologies for chiral alcohols. Eng. Life Sci., 6: 125-129.
    • (2006) Eng. Life Sci. , vol.6 , pp. 125-129
    • Daußmann, T.1    Rosen, T.C.2    Dünkelmann, P.3
  • 266
    • 33947124469 scopus 로고    scopus 로고
    • Structural determinants of the enantioselectivity of the hydroxynitrile lyase from Hevea brasiliensis
    • Gartler, G., Kratky, C., and Gruber, K. (2007). Structural determinants of the enantioselectivity of the hydroxynitrile lyase from Hevea brasiliensis. J. Biotechnol., 129: 87-97.
    • (2007) J. Biotechnol. , vol.129 , pp. 87-97
    • Gartler, G.1    Kratky, C.2    Gruber, K.3
  • 267
    • 0034213036 scopus 로고    scopus 로고
    • The synthesis of chiral cyanohydrins by oxynitrilases
    • Griengl, H., Schwab, H., and Fechter, M. (2000). The synthesis of chiral cyanohydrins by oxynitrilases. Trends Biotechnol., 18: 252-256.
    • (2000) Trends Biotechnol. , vol.18 , pp. 252-256
    • Griengl, H.1    Schwab, H.2    Fechter, M.3
  • 268
    • 0001516109 scopus 로고
    • Enzyme-effected asymmetric syntheses
    • Rosenthaler, L. (1908). Enzyme-effected asymmetric syntheses. Biochem. Z., 14: 238-253.
    • (1908) Biochem. Z. , vol.14 , pp. 238-253
    • Rosenthaler, L.1
  • 270
    • 0030586027 scopus 로고    scopus 로고
    • Mechanism of cyanogenesis: The crystal structure of hydroxynitrile lyase from Hevea brasiliensis
    • Wagner, U.G., Hasslacher, M., Griengl, H., Schwab, H., and Kratky, C. (1996). Mechanism of cyanogenesis: The crystal structure of hydroxynitrile lyase from Hevea brasiliensis. Structure, 4: 811-822.
    • (1996) Structure , vol.4 , pp. 811-822
    • Wagner, U.G.1    Hasslacher, M.2    Griengl, H.3    Schwab, H.4    Kratky, C.5
  • 271
    • 0029955020 scopus 로고    scopus 로고
    • Identification of potential active-site residues in the hydroxynitrile lyase from Manihot esculenta
    • Wajant, H. and Pfizenmaier, K. (1996). Identification of potential active-site residues in the hydroxynitrile lyase from Manihot esculenta. J. Biol. Chem., 271: 25830-25834.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25830-25834
    • Wajant, H.1    Pfizenmaier, K.2
  • 272
    • 0030934790 scopus 로고    scopus 로고
    • Crystal structure analysis of the activation of histidine by Thermus thermophilus Histidyl-tRNA Synthetase
    • Åberg, A., Yaremchuk, A., Tukalo, M., Rasmussen, B., and Cusack, S. (1997). Crystal structure analysis of the activation of histidine by Thermus thermophilus Histidyl-tRNA Synthetase. Biochemistry, 36: 3084-3094.
    • (1997) Biochemistry , vol.36 , pp. 3084-3094
    • Åberg, A.1    Yaremchuk, A.2    Tukalo, M.3    Rasmussen, B.4    Cusack, S.5
  • 273
    • 0032488817 scopus 로고    scopus 로고
    • Specific amino acid recognition by aspartyl-tRNA synthetase studied by free energy simulations
    • Archontis, G., Simonson, T., Moras, D., and Karplus, M. (1998). Specific amino acid recognition by aspartyl-tRNA synthetase studied by free energy simulations. J. Mol. Biol., 275: 823-846.
    • (1998) J. Mol. Biol. , vol.275 , pp. 823-846
    • Archontis, G.1    Simonson, T.2    Moras, D.3    Karplus, M.4
  • 274
    • 0033548581 scopus 로고    scopus 로고
    • Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine
    • Arnez, J.G., Dock-Bregeon, A., and Moras, D. (1999). Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine. J. Mol. Biol., 286: 1449-1459.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1449-1459
    • Arnez, J.G.1    Dock-Bregeon, A.2    Moras, D.3
  • 275
    • 0030788568 scopus 로고    scopus 로고
    • The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase
    • Arnez, J.G., Augstine, J.G., Moras, D., and Francklyn, C.S. (1997). The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase. Proc. Natl. Acad. Sci. (USA), 94: 7144-7149.
    • (1997) Proc. Natl. Acad. Sci. (USA) , vol.94 , pp. 7144-7149
    • Arnez, J.G.1    Augstine, J.G.2    Moras, D.3    Francklyn, C.S.4
  • 276
    • 0029127816 scopus 로고
    • Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate
    • Arnez, J.G., Harris, D.C., Mitschler, A., Rees, B., Francklyn, C.S., and Moras, D. (1995). Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate. EMBO J., 14: 4143-4155.
    • (1995) EMBO J. , vol.14 , pp. 4143-4155
    • Arnez, J.G.1    Harris, D.C.2    Mitschler, A.3    Rees, B.4    Francklyn, C.S.5    Moras, D.6
  • 277
    • 0000370391 scopus 로고    scopus 로고
    • The topology of multidimensional potential energy surfaces: Theory and application to peptide structure and kinetics
    • Becker, O.M. and Karplus, M. (1997). The topology of multidimensional potential energy surfaces: Theory and application to peptide structure and kinetics. J. Chem. Phys., 106: 1495-1517.
    • (1997) J. Chem. Phys. , vol.106 , pp. 1495-1517
    • Becker, O.M.1    Karplus, M.2
  • 279
    • 0034332436 scopus 로고    scopus 로고
    • tRNA aminoacylation by arginyltRNA synthetase: Induced conformations during substrates binding
    • Benedicte, D., Moras, D., and Cavarelli, J. (2000). tRNA aminoacylation by arginyltRNA synthetase: Induced conformations during substrates binding. EMBO J., 19: 5599-5610.
    • (2000) EMBO J. , vol.19 , pp. 5599-5610
    • Benedicte, D.1    Moras, D.2    Cavarelli, J.3
  • 281
    • 0000026965 scopus 로고
    • The enzymic synthesis of amino acyl derivatives of ribonucleic acid
    • Bergmann, F., Berg P., and Dieckmann, M. (1961). The enzymic synthesis of amino acyl derivatives of ribonucleic acid. J. Biol. Chem., 236: 1735-1740.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1735-1740
    • Bergmann, F.1    Berg, P.2    Dieckmann, M.3
  • 282
    • 0028105601 scopus 로고
    • The 2.9 Å crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNASer.
    • Biou, V., Yaremchuk, A., Tukalo, M., and Cusack, S. (1994). The 2.9 Å crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNASer. Science, 263: 1404-1410.
    • (1994) Science , vol.263 , pp. 1404-1410
    • Biou, V.1    Yaremchuk, A.2    Tukalo, M.3    Cusack, S.4
  • 283
    • 0014219470 scopus 로고
    • D-tyrosyl RNA: Formation, hydrolysis and utilization for protein synthesis
    • Calendar, R. and Berg, P. (1967). D-tyrosyl RNA: Formation, hydrolysis and utilization for protein synthesis. J. Mol. Biol., 26: 39-54.
    • (1967) J. Mol. Biol. , vol.26 , pp. 39-54
    • Calendar, R.1    Berg, P.2
  • 284
    • 0013906161 scopus 로고
    • The catalytic properties of tyrosyl ribonucleic acid synthetases from Escherichia coli and Bacillus subtilis
    • Calendar, R. and Berg, P. (1966). The catalytic properties of tyrosyl ribonucleic acid synthetases from Escherichia coli and Bacillus subtilis. Biochemistry, 5: 1690-1695.
    • (1966) Biochemistry , vol.5 , pp. 1690-1695
    • Calendar, R.1    Berg, P.2
  • 285
    • 0032530309 scopus 로고    scopus 로고
    • L-arginine recognition by yeast arginyl tRNA synthetase
    • Cavarelli, J., Delagoutte, B., Eriani, G., Gangloff, J., and Moras, D. (1998). L-arginine recognition by yeast arginyl tRNA synthetase. EMBO J., 17: 5438-5448.
    • (1998) EMBO J. , vol.17 , pp. 5438-5448
    • Cavarelli, J.1    Delagoutte, B.2    Eriani, G.3    Gangloff, J.4    Moras, D.5
  • 287
    • 0032525301 scopus 로고    scopus 로고
    • The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: The mechanism of discrimination between asparagines and aspartic acid
    • Colominas, C., Seignovert, L., Härtlein, M., Grotli, M., Cusack, S., and Leberman, R. (1998). The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: The mechanism of discrimination between asparagines and aspartic acid. EMBO J., 17: 2947-2960.
    • (1998) EMBO J. , vol.17 , pp. 2947-2960
    • Colominas, C.1    Seignovert, L.2    Härtlein, M.3    Grotli, M.4    Cusack, S.5    Leberman, R.6
  • 288
    • 0034657687 scopus 로고    scopus 로고
    • The 2Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue
    • Cusack, S., Yaremchuk, A., and Tukalo, M. (2000). The 2Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue. EMBO J., 19: 2351-2361.
    • (2000) EMBO J. , vol.19 , pp. 2351-2361
    • Cusack, S.1    Yaremchuk, A.2    Tukalo, M.3
  • 289
    • 0013314162 scopus 로고
    • The isolation of a tryptophanactivating enzyme from pancreas
    • Davie, E., Konigsberger V., and Lipman, F. (1956). The isolation of a tryptophanactivating enzyme from pancreas. Arch. Biochem. Biophys., 65: 21-38.
    • (1956) Arch. Biochem. Biophys. , vol.65 , pp. 21-38
    • Davie, E.1    Konigsberger, V.2    Lipman, F.3
  • 290
    • 0034713835 scopus 로고    scopus 로고
    • Active site of lysyl-tRNA synthetase: Structural studies of the adenylation reaction
    • Desogus, G., Todone, F., Brick P., and Onesti, S. (2000). Active site of lysyl-tRNA synthetase: Structural studies of the adenylation reaction. Biochemistry, 39: 8418-8425.
    • (2000) Biochemistry , vol.39 , pp. 8418-8425
    • Desogus, G.1    Todone, F.2    Brick, P.3    Onesti, S.4
  • 291
    • 72749118568 scopus 로고    scopus 로고
    • Molecular understanding of the influence of chirality and interaction in soft systems: From biomimetics to biosystems, a retrospection
    • Dutta Banik, S. and Nandi, N. (2009a). Molecular understanding of the influence of chirality and interaction in soft systems: From biomimetics to biosystems, a retrospection. J. Surf. Sci. Technol., 25: 1-18.
    • (2009) J. Surf. Sci. Technol. , vol.25 , pp. 1-18
    • Dutta Banik, S.1    Nandi, N.2
  • 292
    • 70350202541 scopus 로고    scopus 로고
    • Orientation and distance dependent chiral discrimination in the first step of the aminoacylation reaction: Integrated molecular orbital and semi-empirical method (ONIOM) based calculation
    • Dutta Banik, S. and Nandi, N. (2009b). Orientation and distance dependent chiral discrimination in the first step of the aminoacylation reaction: Integrated molecular orbital and semi-empirical method (ONIOM) based calculation. Coll. Surf. B: Biointerfaces, 74: 468-476.
    • (2009) Coll. Surf. B: Biointerfaces , vol.74 , pp. 468-476
    • Dutta Banik, S.1    Nandi, N.2
  • 293
    • 77649169683 scopus 로고    scopus 로고
    • Aminoacylation reaction in the histidyltRNA synthetase: Fidelity mechanism of the activation step
    • Dutta Banik, S. and Nandi, N. (2010). Aminoacylation reaction in the histidyltRNA synthetase: Fidelity mechanism of the activation step. J. Phys. Chem. B., 114: 2301-2311.
    • (2010) J. Phys. Chem. B. , vol.114 , pp. 2301-2311
    • Dutta Banik, S.1    Nandi, N.2
  • 294
    • 79960191170 scopus 로고    scopus 로고
    • Influence of the conserved active sites residues of Histidyl tRNA synthetase on the mechanism of aminoacylation reaction
    • in press
    • Dutta Banik, S. and Nandi, N. (2011). Influence of the conserved active sites residues of Histidyl tRNA synthetase on the mechanism of aminoacylation reaction. Biophys. Chem. (in press).
    • (2011) Biophys. Chem.
    • Dutta Banik, S.1    Nandi, N.2
  • 295
    • 0033571581 scopus 로고    scopus 로고
    • Synthesis of aspartyl-tRNAAsp in Escherichia coli: A snapshot of the second step
    • Eiler, S., Dock-Bregeon, A.C., Moulinier, L., Thierry, J.C., and Moras, D. (1999). Synthesis of aspartyl-tRNAAsp in Escherichia coli: A snapshot of the second step. EMBO J., 18: 6532-6541.
    • (1999) EMBO J. , vol.18 , pp. 6532-6541
    • Eiler, S.1    Dock-Bregeon, A.C.2    Moulinier, L.3    Thierry, J.C.4    Moras, D.5
  • 297
    • 0343016029 scopus 로고
    • Kirkwood, T.B.L. Rosenberg, R.F. Galas, D.J. (eds), Chapman & Hall, New York
    • Fersht, A.R. (1986). Accuracy in Molecular Processes, Kirkwood, T.B.L. Rosenberg, R.F. Galas, D.J. (eds), Chapman & Hall, New York, 69-82.
    • (1986) Accuracy in Molecular Processes , pp. 69-82
    • Fersht, A.R.1
  • 298
    • 0023657031 scopus 로고
    • Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis
    • Fersht, A.R. (1987). Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis. Biochemistry, 26: 8031-8037.
    • (1987) Biochemistry , vol.26 , pp. 8031-8037
    • Fersht, A.R.1
  • 299
    • 38649136232 scopus 로고    scopus 로고
    • Methods for kinetic and thermodynamic analysis of aminoacyl tRNA synthetases
    • Francklyn, C.S., First, E.A., Perona, J.J., and Hou, Y. (2008). Methods for kinetic and thermodynamic analysis of aminoacyl tRNA synthetases. Methods, 44: 100-118.
    • (2008) Methods , vol.44 , pp. 100-118
    • Francklyn, C.S.1    First, E.A.2    Perona, J.J.3    Hou, Y.4
  • 300
    • 0023868490 scopus 로고
    • Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: A mobile loop envelopes the transition state in an induced-fit mechanism
    • Fersht, A.R., Knill-Jones, J.W., Bedouelle H., and Winter, G. (1988). Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: A mobile loop envelopes the transition state in an induced-fit mechanism. Biochemistry, 27: 1581-1587.
    • (1988) Biochemistry , vol.27 , pp. 1581-1587
    • Fersht, A.R.1    Knill-Jones, J.W.2    Bedouelle, H.3    Winter, G.4
  • 302
    • 0034703763 scopus 로고    scopus 로고
    • Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNAVal and valyl-tRNA synthetase
    • Fukai, S., Nureki, O., Sekine, S., Atsushi Shimada, Tao, J., Vassylyev, D.G., and Yokoyama, S. (2000). Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNAVal and valyl-tRNA synthetase. Cell, 103: 793-803.
    • (2000) Cell , vol.103 , pp. 793-803
    • Fukai, S.1    Nureki, O.2    Sekine, S.3    Atsushi Shimada Tao, J.4    Vassylyev, D.G.5    Yokoyama, S.6
  • 303
    • 0008178378 scopus 로고
    • Probing the synthetic capabilities of a center of biochemical catalysis
    • Hecht, S. (1992). Probing the synthetic capabilities of a center of biochemical catalysis. Acc. Chem. Res., 25: 545-552.
    • (1992) Acc. Chem. Res. , vol.25 , pp. 545-552
    • Hecht, S.1
  • 304
    • 0000359208 scopus 로고
    • Kinetic proofreading: A new mechanism for reducing errors in biosynthetic processes requiring high specificity
    • Hopfield, J.J. (1974). Kinetic proofreading: A new mechanism for reducing errors in biosynthetic processes requiring high specificity. Proc. Natl. Acad. Sci. (USA), 71: 4135-4139.
    • (1974) Proc. Natl. Acad. Sci. (USA) , vol.71 , pp. 4135-4139
    • Hopfield, J.J.1
  • 306
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba, M. and Söll, D. (2000). Aminoacyl-tRNA synthesis. Annu. Rev. Biochem., 69: 617-650.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 617-650
    • Ibba, M.1    Söll, D.2
  • 308
    • 0010835929 scopus 로고
    • Nonexistence of dianionic pentacovalent intermediates in an ab initio study of the base-catalyzed hydrolysis of ethylene phosphate
    • Lim, C. and Karplus, M. (1990). Nonexistence of dianionic pentacovalent intermediates in an ab initio study of the base-catalyzed hydrolysis of ethylene phosphate. J. Am. Chem. Soc., 112: 5872-5873.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 5872-5873
    • Lim, C.1    Karplus, M.2
  • 309
    • 0035861676 scopus 로고    scopus 로고
    • Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase
    • Nakama, T., Nureki, O., and Yokoyama, S. (2001). Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase. J Biol. Chem., 276: 47387-47393.
    • (2001) J Biol. Chem. , vol.276 , pp. 47387-47393
    • Nakama, T.1    Nureki, O.2    Yokoyama, S.3
  • 310
    • 27744575743 scopus 로고    scopus 로고
    • Study of chiral recognition of model peptides and odorants: Carvone and camphor
    • Nandi N. (2005). Study of chiral recognition of model peptides and odorants: Carvone and camphor. Curr. Sci., 88: 1929-1937.
    • (2005) Curr. Sci. , vol.88 , pp. 1929-1937
    • Nandi, N.1
  • 311
    • 0038339629 scopus 로고    scopus 로고
    • Molecular origin of the recognition of chiral odorant by chiral lipid: Interaction of dipalmitoyl phosphatidyl choline and carvone
    • Nandi, N. (2003). Molecular origin of the recognition of chiral odorant by chiral lipid: Interaction of dipalmitoyl phosphatidyl choline and carvone. J. Phys. Chem. A., 107: 4588-4591.
    • (2003) J. Phys. Chem. A. , vol.107 , pp. 4588-4591
    • Nandi, N.1
  • 312
    • 70350173558 scopus 로고    scopus 로고
    • Chiral discrimination in the confined environment of biological nanospace: Reactions and interactions involving amino acids and peptides
    • Nandi, N. (2009). Chiral discrimination in the confined environment of biological nanospace: Reactions and interactions involving amino acids and peptides. Int. Rev. Phys. Chem., 28: 111-167.
    • (2009) Int. Rev. Phys. Chem. , vol.28 , pp. 111-167
    • Nandi, N.1
  • 313
    • 0037013921 scopus 로고    scopus 로고
    • Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase
    • Newberry, K.J., Hou, Y.-M., and Perona, J.J. (2002). Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase. EMBO J., 21: 2778-2787.
    • (2002) EMBO J. , vol.21 , pp. 2778-2787
    • Newberry, K.J.1    Hou, Y.-M.2    Perona, J.J.3
  • 314
    • 0038946088 scopus 로고
    • Purification and properties of the aspartyl ribonucleic acid synthetase of Lactobacillus arabinosus
    • Norton, S., Ravel, J., Lee C., and Shive, W. (1963). Purification and properties of the aspartyl ribonucleic acid synthetase of Lactobacillus arabinosus. J. Biol. Chem., 238: 269-274.
    • (1963) J. Biol. Chem. , vol.238 , pp. 269-274
    • Norton, S.1    Ravel, J.2    Lee, C.3    Shive, W.4
  • 315
    • 0034710994 scopus 로고    scopus 로고
    • Structural studies of lysyl-tRNA synthetase: Conformational changes induced by substrate binding
    • Onesti, S., Desogus, G., Brevet, A., Chen, J., Plateau, P., Blanquet, S., and P. Brick, (2000). Structural studies of lysyl-tRNA synthetase: Conformational changes induced by substrate binding. Biochemistry, 39: 12853-12861.
    • (2000) Biochemistry , vol.39 , pp. 12853-12861
    • Onesti, S.1    Desogus, G.2    Brevet, A.3    Chen, J.4    Plateau, P.5    Blanquet, S.6    Brick, P.7
  • 316
    • 0027165755 scopus 로고
    • Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase
    • Perona, J.J., Rould, M.A., and Steitz, T.A. (1993). Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. Biochemistry, 32: 8758-8771.
    • (1993) Biochemistry , vol.32 , pp. 8758-8771
    • Perona, J.J.1    Rould, M.A.2    Steitz, T.A.3
  • 317
    • 0021119937 scopus 로고
    • Stereoselective aminoacylation of a dinucleoside monophosphate by the imidazolides of DL-alanine and N-(tertbutoxycarbonyl)- DL-alanine
    • Profy, A.T. and Usher, D.A. (1984). Stereoselective aminoacylation of a dinucleoside monophosphate by the imidazolides of DL-alanine and N-(tertbutoxycarbonyl)- DL-alanine. J. Mol. Evol., 20: 147-156.
    • (1984) J. Mol. Evol. , vol.20 , pp. 147-156
    • Profy, A.T.1    Usher, D.A.2
  • 318
    • 7944232372 scopus 로고    scopus 로고
    • Enantiospecific (+)- and (-)-germacrene D synthases, cloned from goldenrod, reveal a functionally active variant of the universal isoprenoid- biosynthesis aspartate-rich motif
    • Prosser, I., Altug, I.G., Phillips, A.L., König, W.A., Bouwmeester, H.J., and Beale, M.H. (2004). Enantiospecific (+)- and (-)-germacrene D synthases, cloned from goldenrod, reveal a functionally active variant of the universal isoprenoid- biosynthesis aspartate-rich motif. Archives Biochem. Biophys., 432: 136-144.
    • (2004) Archives Biochem. Biophys. , vol.432 , pp. 136-144
    • Prosser, I.1    Altug, I.G.2    Phillips, A.L.3    König, W.A.4    Bouwmeester, H.J.5    Beale, M.H.6
  • 319
    • 0033592311 scopus 로고    scopus 로고
    • Cooperative structural dynamics and a novel fidelity mechanism in histidyl-tRNA synthetases
    • Qiu, X., Janson, C.A., Blackburn, M.N., Chhohan, I.K., Hibbs, M., and Abdel-Meguid, S.S. (1999). Cooperative structural dynamics and a novel fidelity mechanism in histidyl-tRNA synthetases. Biochemistry, 38: 12296-12304.
    • (1999) Biochemistry , vol.38 , pp. 12296-12304
    • Qiu, X.1    Janson, C.A.2    Blackburn, M.N.3    Chhohan, I.K.4    Hibbs, M.5    Abdel-Meguid, S.S.6
  • 321
    • 0035226156 scopus 로고    scopus 로고
    • The fidelity of the translation of the genetic code
    • Sankaranarayanan R. and Moras, D. (2001). The fidelity of the translation of the genetic code. Acta Biochim. Polonica, 48: 323-335.
    • (2001) Acta Biochim. Polonica , vol.48 , pp. 323-335
    • Sankaranarayanan, R.1    Moras, D.2
  • 323
    • 0034693045 scopus 로고    scopus 로고
    • Metabolism of D-aminoacyltRNAs in Escherichia coli and Saccharomyces cerevisiae cells
    • Soutourina, J., Plateau P., and Blanquet, S. (2000). Metabolism of D-aminoacyltRNAs in Escherichia coli and Saccharomyces cerevisiae cells. J. Biol. Chem., 275: 32535-32542.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32535-32542
    • Soutourina, J.1    Plateau, P.2    Blanquet, S.3
  • 324
    • 0036123173 scopus 로고    scopus 로고
    • Receptor neuron discrimination of the germacrene D enantiomers in the moth Helicoverpa armigera
    • Stranden, M., Borg-Karlson, A.K., and Mustaparta, H. (2004). Receptor neuron discrimination of the germacrene D enantiomers in the moth Helicoverpa armigera. Chem. Senses., 27: 143-152.
    • (2004) Chem. Senses. , vol.27 , pp. 143-152
    • Stranden, M.1    Borg-Karlson, A.K.2    Mustaparta, H.3
  • 325
    • 4344578505 scopus 로고    scopus 로고
    • Chiral-selective aminoacylation of an RNA minihelix
    • Tamura, K. and Schimmel, P. (2004). Chiral-selective aminoacylation of an RNA minihelix. Science, 305: 1253.
    • (2004) Science , vol.305 , pp. 1253
    • Tamura, K.1    Schimmel, P.2
  • 326
    • 33748766632 scopus 로고    scopus 로고
    • Chiral-selective aminoacylation of an RNA minihelix: Mechanistic features and chiral suppression
    • Tamura, K. and Schimmel, P. (2006). Chiral-selective aminoacylation of an RNA minihelix: Mechanistic features and chiral suppression. Proc. Natl. Acad. Sci. (USA), 103: 13750-13752.
    • (2006) Proc. Natl. Acad. Sci. (USA) , vol.103 , pp. 13750-13752
    • Tamura, K.1    Schimmel, P.2
  • 327
    • 35648937527 scopus 로고    scopus 로고
    • Ammonium scanning in an enzyme active site the chiral specificity of aspartyl-tRNA synthetase
    • Thompson, D., Lazennec, C., Plateau P., and Simonson, T. (2007). Ammonium scanning in an enzyme active site the chiral specificity of aspartyl-tRNA synthetase. J. Biol. Chem., 282: 30856-30868.
    • (2007) J. Biol. Chem. , vol.282 , pp. 30856-30868
    • Thompson, D.1    Lazennec, C.2    Plateau, P.3    Simonson, T.4
  • 328
    • 0035815113 scopus 로고    scopus 로고
    • Evolution of function in protein superfamilies from a structural perspective
    • Todd, A.E., Orengo, C.A., and Thornton, J.M. (2001). Evolution of function in protein superfamilies from a structural perspective. J. Mol. Biol., 307: 1113-1143.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1113-1143
    • Todd, A.E.1    Orengo, C.A.2    Thornton, J.M.3
  • 329
    • 0032552138 scopus 로고    scopus 로고
    • Archetypal energy landscapes
    • Wales, D.J., Miller, M.A., and Walsh, T.R. (1998). Archetypal energy landscapes. Nature, 394: 758-760.
    • (1998) Nature , vol.394 , pp. 758-760
    • Wales, D.J.1    Miller, M.A.2    Walsh, T.R.3
  • 331
    • 0034692903 scopus 로고    scopus 로고
    • Stabilization of the transition state for the transfer of tyrosine to tRNATyr by tyrosyl-tRNA synthetase
    • Xin, Y., Li, W., and First, E.A. (2000). Stabilization of the transition state for the transfer of tyrosine to tRNATyr by tyrosyl-tRNA synthetase. J. Mol. Biol., 303: 299-310.
    • (2000) J. Mol. Biol. , vol.303 , pp. 299-310
    • Xin, Y.1    Li, W.2    First, E.A.3
  • 332
    • 0017394853 scopus 로고
    • Experimental evidence for kinetic proofreading in the aminoacylation of tRNA by synthetase
    • Yamane, T. and Hopfield, J.J. (1977). Experimental evidence for kinetic proofreading in the aminoacylation of tRNA by synthetase. Proc. Natl. Acad. Sci. (USA), 74: 2246-2250.
    • (1977) Proc. Natl. Acad. Sci. (USA) , vol.74 , pp. 2246-2250
    • Yamane, T.1    Hopfield, J.J.2
  • 333
    • 0000359208 scopus 로고
    • Kinetic proofreading: A new mechanism for reducing errors in biosynthetic processes requiring high specificity
    • Yamane, T., Miller, L., and Hopfield, J.J. (1974). Kinetic proofreading: A new mechanism for reducing errors in biosynthetic processes requiring high specificity. Proc. Natl. Acad. Sci. (USA), 71: 4135-4139.
    • (1974) Proc. Natl. Acad. Sci. (USA) , vol.71 , pp. 4135-4139
    • Yamane, T.1    Miller, L.2    Hopfield, J.J.3
  • 334
    • 0038867278 scopus 로고    scopus 로고
    • (-)-Germacrene D: Masking substance of attractants for the cerambycid beetle, Monochamus alternatus (Hope)
    • Yamasaki, T., Sato, M., and Sakoguchi, H. (1997). (-)-Germacrene D: Masking substance of attractants for the cerambycid beetle, Monochamus alternatus (Hope). Appl. Entomol. Zool., 32: 423-429.
    • (1997) Appl. Entomol. Zool. , vol.32 , pp. 423-429
    • Yamasaki, T.1    Sato, M.2    Sakoguchi, H.3
  • 335
    • 0037099498 scopus 로고    scopus 로고
    • Class I tyrosyltRNA synthetase has a class II mode of cognate tRNA recognition
    • Yaremchuk, A., Kriklivyi, I., Tukalo, M., and Cusack, S. (2002). Class I tyrosyltRNA synthetase has a class II mode of cognate tRNA recognition. EMBO J., 21: 3829-3840.
    • (2002) EMBO J. , vol.21 , pp. 3829-3840
    • Yaremchuk, A.1    Kriklivyi, I.2    Tukalo, M.3    Cusack, S.4
  • 336
    • 0035875882 scopus 로고    scopus 로고
    • A succession of substrate induced conformational changes ensures the amino acid specificity of Thermus thermophilus prolyl-tRNA synthetase: Comparison with histidyltRNA synthetase
    • Yaremchuk, A., Tukalo, M., Grotli, M., and Cusack, S. (2001). A succession of substrate induced conformational changes ensures the amino acid specificity of Thermus thermophilus prolyl-tRNA synthetase: Comparison with histidyltRNA synthetase. J. Mol. Biol., 309: 989-1002.
    • (2001) J. Mol. Biol. , vol.309 , pp. 989-1002
    • Yaremchuk, A.1    Tukalo, M.2    Grotli, M.3    Cusack, S.4
  • 338
    • 0001490606 scopus 로고    scopus 로고
    • Molecular recognition at air-water and related interfaces: Complementary hydrogen bonding and multisite interaction
    • Ariga, K. and Kunitake, T. (1998). Molecular recognition at air-water and related interfaces: Complementary hydrogen bonding and multisite interaction. Acc. Chem. Res., 31: 371-378.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 371-378
    • Ariga, K.1    Kunitake, T.2
  • 341
    • 33744754038 scopus 로고    scopus 로고
    • A paradigm shift in the field of molecular recognition at the air-water interface: From static to dynamic
    • Ariga, K., Nakanishi, T., and Hill, J.P. (2006). A paradigm shift in the field of molecular recognition at the air-water interface: From static to dynamic. Soft Matter, 2: 465-498.
    • (2006) Soft Matter , vol.2 , pp. 465-498
    • Ariga, K.1    Nakanishi, T.2    Hill, J.P.3
  • 342
    • 0030951462 scopus 로고    scopus 로고
    • Design of an active fragment of a class II aminoacyl tRNA synthetase and its significance for synthetase evolution
    • Augustine, J. and Francklyn, C. (1997). Design of an active fragment of a class II aminoacyl tRNA synthetase and its significance for synthetase evolution. Biochemistry, 36: 3473-3482.
    • (1997) Biochemistry , vol.36 , pp. 3473-3482
    • Augustine, J.1    Francklyn, C.2
  • 343
    • 0031029551 scopus 로고    scopus 로고
    • Protein design: The choice of de novo sequences
    • Beasley, J.R. and Hecht, M.H. (1997). Protein design: The choice of de novo sequences. J. Biol. Chem., 272: 2031-2034.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2031-2034
    • Beasley, J.R.1    Hecht, M.H.2
  • 344
    • 0027668216 scopus 로고
    • Catalysis: Design versus selection
    • Benner, S. (1993). Catalysis: Design versus selection. Science, 261: 1402-1403.
    • (1993) Science , vol.261 , pp. 1402-1403
    • Benner, S.1
  • 346
    • 0037523450 scopus 로고    scopus 로고
    • The discovery of catalytically active peptides through combinatorial chemistry
    • Berkessel, A. (2003). The discovery of catalytically active peptides through combinatorial chemistry. Curr. Opin. Chem. Biol., 7: 409-419.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 409-419
    • Berkessel, A.1
  • 347
    • 65349124747 scopus 로고    scopus 로고
    • Opportunities for enzyme engineering in natural product biosynthesis
    • Bernhardt, P. and O'Connor, S.E. (2009). Opportunities for enzyme engineering in natural product biosynthesis. Curr. Opin. Chem. Biol., 13: 35-42.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 35-42
    • Bernhardt, P.1    O'Connor, S.E.2
  • 348
    • 7444241366 scopus 로고    scopus 로고
    • De novo design of defined helical bundles in membrane environments
    • Bilgicer, B. and Kumar, K. (2004). De novo design of defined helical bundles in membrane environments. Proc. Natl. Acad. Sci. (USA), 101: 15324-15329.
    • (2004) Proc. Natl. Acad. Sci. (USA) , vol.101 , pp. 15324-15329
    • Bilgicer, B.1    Kumar, K.2
  • 349
    • 18844393705 scopus 로고    scopus 로고
    • An intein-based genetic selection allows the construction of a high-quality library of binary patterned de novo protein sequences
    • Bradley, L.H., Kleiner, R.E., Wang, A.F., Hecht, M.H., and Wood, D.W. (2005). An intein-based genetic selection allows the construction of a high-quality library of binary patterned de novo protein sequences. Protein Eng. Des. Sel., 18: 201-207.
    • (2005) Protein Eng. Des. Sel. , vol.18 , pp. 201-207
    • Bradley, L.H.1    Kleiner, R.E.2    Wang, A.F.3    Hecht, M.H.4    Wood, D.W.5
  • 351
    • 0034704217 scopus 로고    scopus 로고
    • The structural basis for the action of the antibiotics tetracycline, pactamycin and hygromycin B on the 30S ribosomal subunit
    • Brodersen, D.E., Clemons, W.M., Jr., Carter, A.P., Morgan-Warren, R.J., Wimberly, B.T., and Ramakrishnan, V. (2000). The structural basis for the action of the antibiotics tetracycline, pactamycin and hygromycin B on the 30S ribosomal subunit. Cell, 103: 1143-1154.
    • (2000) Cell , vol.103 , pp. 1143-1154
    • Brodersen, D.E.1    Clemons, W.M.2    Carter, A.P.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 352
    • 0141480046 scopus 로고    scopus 로고
    • Coarse-grained sequences for protein folding and design
    • Brown, S., Fawzi, N.J., and Head-Gordon, T. (2003). Coarse-grained sequences for protein folding and design. Proc. Natl. Acad. Sci. (USA), 100: 10712-10717.
    • (2003) Proc. Natl. Acad. Sci. (USA) , vol.100 , pp. 10712-10717
    • Brown, S.1    Fawzi, N.J.2    Head-Gordon, T.3
  • 354
    • 0034699519 scopus 로고    scopus 로고
    • Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
    • Carter, A.P., Clemons, W.M., Jr., Brodersen, D.E., Morgan-Warren, R.J., Wimberly, B.T., and Ramakrishnan, V. (2000). Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics. Nature, 407: 340-348.
    • (2000) Nature , vol.407 , pp. 340-348
    • Carter, A.P.1    Clemons, W.M.2    Brodersen, D.E.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 357
    • 0023868490 scopus 로고
    • Reconstruction by site-directed mutagenesis of the formation state for the activation of tyrosine by the tyrosyl-tRNA synthetase: A mobile loop envelopes the transition state in an induced fit mechanism
    • Fersht, A.R., Knill-Jones, J.W., Bedonelle, H., Winter, G. (1988). Reconstruction by site-directed mutagenesis of the formation state for the activation of tyrosine by the tyrosyl-tRNA synthetase: A mobile loop envelopes the transition state in an induced fit mechanism. Biochemstry, 27: 1581-1587.
    • (1988) Biochemstry , vol.27 , pp. 1581-1587
    • Fersht, A.R.1    Knill-Jones, J.W.2    Bedonelle, H.3    Winter, G.4
  • 358
    • 0025335121 scopus 로고
    • Design and synthesis of a peptide having chymotrypsin-like esterase activity
    • Hahn, K.W., Klis, W.A., and Stewart, J.M. (1990). Design and synthesis of a peptide having chymotrypsin-like esterase activity. Science, 248: 1544-1547.
    • (1990) Science , vol.248 , pp. 1544-1547
    • Hahn, K.W.1    Klis, W.A.2    Stewart, J.M.3
  • 359
    • 0027177971 scopus 로고
    • Metal ion-dependent modulation of the dynamics of a designed protein
    • Handel, T., Williams, S., and DeGrado, W. (1993). Metal ion-dependent modulation of the dynamics of a designed protein. Science, 261: 879-885.
    • (1993) Science , vol.261 , pp. 879-885
    • Handel, T.1    Williams, S.2    DeGrado, W.3
  • 360
    • 0030886443 scopus 로고    scopus 로고
    • Rational protein design: Combining theory and experiment
    • Hellinga, H.W. (1997). Rational protein design: Combining theory and experiment. Proc. Natl. Acad. Sci. (USA), 94: 10015-10017.
    • (1997) Proc. Natl. Acad. Sci. (USA) , vol.94 , pp. 10015-10017
    • Hellinga, H.W.1
  • 361
    • 1542364374 scopus 로고    scopus 로고
    • Metallothioneins: Zinc, cadmium, mercury, and copper thiolates and selenolates mimicking protein active site features- structural aspects and biological implications
    • Henkel, G. and Krebs, B. (2004). Metallothioneins: Zinc, cadmium, mercury, and copper thiolates and selenolates mimicking protein active site features- structural aspects and biological implications. Chem. Rev., 104: 801-824.
    • (2004) Chem. Rev. , vol.104 , pp. 801-824
    • Henkel, G.1    Krebs, B.2
  • 362
    • 20444495201 scopus 로고    scopus 로고
    • Drugs targeting the ribosome
    • Hermann, T. (2005). Drugs targeting the ribosome. Curr. Opin. Struct. Biol., 15: 355-366.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 355-366
    • Hermann, T.1
  • 364
    • 0038814072 scopus 로고    scopus 로고
    • Mutations in distant residues moderately increase the enantioselectivity of Pseudomonas fluorescens esterase towards methyl 3-bromo-2-methylpropanoate and ethyl 3-phenylbutyrate
    • Horsman, G.P., Liu, A.M.F., Henke, E., Bornscheuer, U.T., and Kazlauskas, R.J. (2003). Mutations in distant residues moderately increase the enantioselectivity of Pseudomonas fluorescens esterase towards methyl 3-bromo-2-methylpropanoate and ethyl 3-phenylbutyrate. Chem. Eur. J., 9: 1933-1939.
    • (2003) Chem. Eur. J. , vol.9 , pp. 1933-1939
    • Horsman, G.P.1    Liu, A.M.F.2    Henke, E.3    Bornscheuer, U.T.4    Kazlauskas, R.J.5
  • 365
  • 367
    • 0004425540 scopus 로고    scopus 로고
    • Quantum crystallography applied to crystalline maleic anhydride
    • Huang, L., Massa, L., and Karle, J. (1999). Quantum crystallography applied to crystalline maleic anhydride. Int. J. Quantum Chem., 73: 439-450.
    • (1999) Int. J. Quantum Chem. , vol.73 , pp. 439-450
    • Huang, L.1    Massa, L.2    Karle, J.3
  • 368
    • 0035327181 scopus 로고    scopus 로고
    • Quantum crystallography, a developing area of computational chemistry extending to macromolecules
    • Huang, L., Massa, L., and Karle, J. (2001). Quantum crystallography, a developing area of computational chemistry extending to macromolecules. J. Res.Dev., 45: 409-415.
    • (2001) J. Res.Dev. , vol.45 , pp. 409-415
    • Huang, L.1    Massa, L.2    Karle, J.3
  • 369
    • 24644518254 scopus 로고    scopus 로고
    • Kernel energy method illustrated with peptides
    • Huang, L., Massa, L., and Karle, J. (2005). Kernel energy method illustrated with peptides. Int. J. Quantum Chem., 103: 808-817.
    • (2005) Int. J. Quantum Chem. , vol.103 , pp. 808-817
    • Huang, L.1    Massa, L.2    Karle, J.3
  • 370
    • 31944451277 scopus 로고    scopus 로고
    • Kernel energy method: Basis functions and quantum methods
    • Huang, L., Massa, L., and Karle, J. (2006a). Kernel energy method: Basis functions and quantum methods. Int. J. Quantum Chem., 106: 447-457.
    • (2006) Int. J. Quantum Chem. , vol.106 , pp. 447-457
    • Huang, L.1    Massa, L.2    Karle, J.3
  • 371
    • 31944449774 scopus 로고    scopus 로고
    • The kernel energy method: Application to a tRNA
    • Huang, L., Massa, L., and Karle, J. (2006b). The kernel energy method: Application to a tRNA. Proc. Natl. Acad. Sci. (USA), 103: 1233-1237.
    • (2006) Proc. Natl. Acad. Sci. (USA) , vol.103 , pp. 1233-1237
    • Huang, L.1    Massa, L.2    Karle, J.3
  • 372
    • 34248353534 scopus 로고    scopus 로고
    • Drug target interaction energies by the kernel energy method in aminoglycoside drugs and ribosomal A site RNA targets
    • Huang, L., Massa, L., and Karle, J. (2007). Drug target interaction energies by the kernel energy method in aminoglycoside drugs and ribosomal A site RNA targets. Proc. Natl. Acad. Sci. (USA), 104: 4261-4266.
    • (2007) Proc. Natl. Acad. Sci. (USA) , vol.104 , pp. 4261-4266
    • Huang, L.1    Massa, L.2    Karle, J.3
  • 373
    • 3242706731 scopus 로고    scopus 로고
    • Combined spectroscopic/computational studies on Fe and Mn dependent superoxide dismutases: Insights into second- sphere tuning of active site properties
    • Jackson, T.A. and Brunold, T.C. (2004). Combined spectroscopic/computational studies on Fe and Mn dependent superoxide dismutases: Insights into second- sphere tuning of active site properties. Acc. Chem. Res., 37: 461-470.
    • (2004) Acc. Chem. Res. , vol.37 , pp. 461-470
    • Jackson, T.A.1    Brunold, T.C.2
  • 375
    • 23444436172 scopus 로고
    • Protein design by binary patterning of polar and nonpolar amino acids
    • Kamtekar, S., Schiffer, J.M., Xiong, H., Babik, J.M., and Hecht, M.H. (1993). Protein design by binary patterning of polar and nonpolar amino acids. Science, 262: 1680-1685.
    • (1993) Science , vol.262 , pp. 1680-1685
    • Kamtekar, S.1    Schiffer, J.M.2    Xiong, H.3    Babik, J.M.4    Hecht, M.H.5
  • 376
    • 33744522163 scopus 로고    scopus 로고
    • Nanorotors using asymmetric inorganic nanorods in an optical trap
    • Khan, M., Sood, A.K., Deepak, F.L., and Rao, C.N.R. (2006). Nanorotors using asymmetric inorganic nanorods in an optical trap. Nanotechnology, 17: S287.
    • (2006) Nanotechnology , vol.17
    • Khan, M.1    Sood, A.K.2    Deepak, F.L.3    Rao, C.N.R.4
  • 377
    • 33750430630 scopus 로고    scopus 로고
    • Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Abeta42 peptide
    • Kim, W. and Hecht, M.H. (2006). Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Abeta42 peptide. Proc. Natl. Acad. Sci. (USA), 103: 15824-15829.
    • (2006) Proc. Natl. Acad. Sci. (USA) , vol.103 , pp. 15824-15829
    • Kim, W.1    Hecht, M.H.2
  • 378
    • 0025335121 scopus 로고
    • Design and synthesis of a peptide having chymotrypsin- like esterase activity
    • Klis, W.A. and Stewart, J.M. (1990). Design and synthesis of a peptide having chymotrypsin- like esterase activity. Science, 248: 1544-1547.
    • (1990) Science , vol.248 , pp. 1544-1547
    • Klis, W.A.1    Stewart, J.M.2
  • 379
    • 0030231879 scopus 로고    scopus 로고
    • Molecular recognition by molecular monolayers, bilayers, and films.
    • Kunitake, T. (1996). Molecular recognition by molecular monolayers, bilayers, and films. Thin Solid Films, 284-285: 9-12.
    • (1996) Thin Solid Films , vol.284-285 , pp. 9-12
    • Kunitake, T.1
  • 380
    • 0027588112 scopus 로고
    • Enzymes in the synthesis of chiral drugs
    • Margolin, A.L. (1993). Enzymes in the synthesis of chiral drugs. Enzyme Microb. Technol., 15: 266-280.
    • (1993) Enzyme Microb. Technol. , vol.15 , pp. 266-280
    • Margolin, A.L.1
  • 382
    • 33751014543 scopus 로고    scopus 로고
    • Mechanical control of enantioselectivity of amino acid recognition by cholesterol-armed cyclen monolayer at the air-water interface
    • Michinobu, T., Shinoda, S., Nakanishi, T., Hill, J.P., Fuji, K., Player, T.N., Tsukube, H., and Ariga, K. (2006). Mechanical control of enantioselectivity of amino acid recognition by cholesterol-armed cyclen monolayer at the air-water interface. J. Am. Chem. Soc., 128: 14478-14479.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 14478-14479
    • Michinobu, T.1    Shinoda, S.2    Nakanishi, T.3    Hill, J.P.4    Fuji, K.5    Player, T.N.6    Tsukube, H.7    Ariga, K.8
  • 383
    • 18144403554 scopus 로고    scopus 로고
    • Improving enzyme properties: When are closer mutations better
    • Morley, K.L. and Kazlauskas, R.J. (2005). Improving enzyme properties: When are closer mutations better? Trends Biotech., 23: 231-237.
    • (2005) Trends Biotech. , vol.23 , pp. 231-237
    • Morley, K.L.1    Kazlauskas, R.J.2
  • 384
    • 0001338954 scopus 로고    scopus 로고
    • Simplified amino acid alphabets for protein fold recognition and implications for folding
    • Murphy, L.R., Wallqvist, A., and Levy, R.M. (2000). Simplified amino acid alphabets for protein fold recognition and implications for folding. Protein Eng. Des. Sel., 13: 149-152.
    • (2000) Protein Eng. Des. Sel. , vol.13 , pp. 149-152
    • Murphy, L.R.1    Wallqvist, A.2    Levy, R.M.3
  • 385
    • 0942279303 scopus 로고    scopus 로고
    • Role of secondary level chiral structure in the process of molecular recognition of ligand: Study of model helical peptide
    • Nandi, N. (2004). Role of secondary level chiral structure in the process of molecular recognition of ligand: Study of model helical peptide. J. Phys. Chem. B., 108: 789-797.
    • (2004) J. Phys. Chem. B. , vol.108 , pp. 789-797
    • Nandi, N.1
  • 386
    • 0033690126 scopus 로고    scopus 로고
    • Dielectric relaxation and solvation dynamics of water in complex chemical and biological systems
    • Nandi, N., Bhattacharyya, K., and Bagchi, B. (2000). Dielectric relaxation and solvation dynamics of water in complex chemical and biological systems. Chem. Rev., 100: 2013-2045.
    • (2000) Chem. Rev. , vol.100 , pp. 2013-2045
    • Nandi, N.1    Bhattacharyya, K.2    Bagchi, B.3
  • 387
    • 0030963838 scopus 로고    scopus 로고
    • Minimized protein structures: A little goes a long way
    • Nedwidek, M.N. and Hecht, M.H. (1997). Minimized protein structures: A little goes a long way. Proc. Natl. Acad. Sci. (USA), 94: 10010-10011.
    • (1997) Proc. Natl. Acad. Sci. (USA) , vol.94 , pp. 10010-10011
    • Nedwidek, M.N.1    Hecht, M.H.2
  • 389
    • 0034637574 scopus 로고    scopus 로고
    • Assignment of functional amino acids around the active site of human DNA topoisomerase II alpha
    • Okada, Y., Ito, Y., Kikuchi, A., Nimura, Y., Yoshida, S., and Suzuki, M. (2000). Assignment of functional amino acids around the active site of human DNA topoisomerase II alpha. J. Biol. Chem., 275: 24630-24638.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24630-24638
    • Okada, Y.1    Ito, Y.2    Kikuchi, A.3    Nimura, Y.4    Yoshida, S.5    Suzuki, M.6
  • 390
    • 71849104042 scopus 로고    scopus 로고
    • Enzyme engineering for enantioselectivity: From trial-and-error to rational design
    • Otten, L.G., Hollmann, F., and Arends, I.W.C.E. (2009). Enzyme engineering for enantioselectivity: From trial-and-error to rational design? Trends Biotech., 28: 46-54.
    • (2009) Trends Biotech. , vol.28 , pp. 46-54
    • Otten, L.G.1    Hollmann, F.2    Arends, I.W.C.E.3
  • 391
    • 0033593453 scopus 로고    scopus 로고
    • Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of nonactive site residues
    • Oue, S., Okamoto, A., Yano, T., and Kagamiyama, H. (1999). Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of nonactive site residues. J. Biol. Chem., 274: 2344-2349.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2344-2349
    • Oue, S.1    Okamoto, A.2    Yano, T.3    Kagamiyama, H.4
  • 392
    • 0030047220 scopus 로고    scopus 로고
    • Functionalized proteinlike structures from conformationally defined synthetic combinatorial libraries
    • Pérez-Payá, E., Houghten, R.A., and Blondelle, S.E. (1996). Functionalized proteinlike structures from conformationally defined synthetic combinatorial libraries. J. Biol. Chem., 271: 4120-4126.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4120-4126
    • Pérez-Payá, E.1    Houghten, R.A.2    Blondelle, S.E.3
  • 393
    • 0036933840 scopus 로고    scopus 로고
    • Identification of conserved residue patterns in small ß-barrel proteins
    • Qamra, R., Taneja, B., and Mande, S.C. (2002). Identification of conserved residue patterns in small ß-barrel proteins. Protein Eng. Des. Sel., 15: 967-977.
    • (2002) Protein Eng. Des. Sel. , vol.15 , pp. 967-977
    • Qamra, R.1    Taneja, B.2    Mande, S.C.3
  • 394
    • 49349091280 scopus 로고    scopus 로고
    • What we have learned from ribosome structures
    • Ramakrishnan, V. (2008). What we have learned from ribosome structures. Biochem. Soc. Trans., 36: 567-574.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 567-574
    • Ramakrishnan, V.1
  • 395
    • 33847182056 scopus 로고    scopus 로고
    • Synthesis and selection of de novo proteins that bind and impede cellular functions of an essential mycobacterial protein
    • Rao, A., Ram, G., Saini, A.K., Vohra, R., Kumar, K., Singh, Y., and Ranganathan, A. (2007). Synthesis and selection of de novo proteins that bind and impede cellular functions of an essential mycobacterial protein. Appl. Environ. Microbiol., 73: 1320-1331.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 1320-1331
    • Rao, A.1    Ram, G.2    Saini, A.K.3    Vohra, R.4    Kumar, K.5    Singh, Y.6    Ranganathan, A.7
  • 396
    • 0034730144 scopus 로고    scopus 로고
    • Novel folded protein domains generated by combinatorial shuffling of polypeptide segments
    • Riechmann, L. and Winter, G. (2000). Novel folded protein domains generated by combinatorial shuffling of polypeptide segments. Proc. Natl. Acad. Sci. (USA), 97: 10068-10073.
    • (2000) Proc. Natl. Acad. Sci. (USA) , vol.97 , pp. 10068-10073
    • Riechmann, L.1    Winter, G.2
  • 397
    • 33846524196 scopus 로고    scopus 로고
    • DNA and RNA induced enantioselectivity in chemical synthesis
    • Roelfes, G. (2007). DNA and RNA induced enantioselectivity in chemical synthesis. Mol. BioSyst., 3: 126-135.
    • (2007) Mol. BioSyst. , vol.3 , pp. 126-135
    • Roelfes, G.1
  • 399
    • 0000611517 scopus 로고    scopus 로고
    • Theoretical study of intermolecular interaction at the lipid-water interface.1. Quantum chemical analysis using a reaction field theory.
    • Sakurai, M., Tamagawa, H., Inous, Y., Ariga, K., and Kunitake, T. (1997a). Theoretical study of intermolecular interaction at the lipid-water interface.1. Quantum chemical analysis using a reaction field theory. J. Phys. Chem. B, 101: 4810-4816.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 4810-4816
    • Sakurai, M.1    Tamagawa, H.2    Inous, Y.3    Ariga, K.4    Kunitake, T.5
  • 400
    • 0000611517 scopus 로고    scopus 로고
    • Theoretical study of intermolecular interaction at the lipid-water interface. 2 Analysis based on the Poisson-Boltzmann equation
    • Sakurai, M., Tamagawa, H., Inous, Y., Ariga, K., and Kunitake, T. (1997b). Theoretical study of intermolecular interaction at the lipid-water interface. 2. Analysis based on the Poisson-Boltzmann equation. J. Phys. Chem. B, 101: 4817-4825.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 4817-4825
    • Sakurai, M.1    Tamagawa, H.2    Inous, Y.3    Ariga, K.4    Kunitake, T.5
  • 401
    • 0036900263 scopus 로고    scopus 로고
    • The production of fine chemicals by biotransformations
    • Straathof, A.J., Panke, S., and Schmid, A. (2002). The production of fine chemicals by biotransformations. Curr. Opin. Biotechnol., 13: 548-556.
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 548-556
    • Straathof, A.J.1    Panke, S.2    Schmid, A.3
  • 402
    • 0036005636 scopus 로고    scopus 로고
    • Understanding Nature's strategies for enzyme-catalyzed racemization and epimerization
    • Tanner, M.E. (2002). Understanding Nature's strategies for enzyme-catalyzed racemization and epimerization. Acc. Chem. Res. 35: 237-246.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 237-246
    • Tanner, M.E.1
  • 403
    • 38749138838 scopus 로고    scopus 로고
    • Molecular dynamics as a pattern recognition tool: An automated process detects peptides that preserve the 3D arrangement of trypsin's active site
    • Tatsis, V.A., Stavrakoudis, A., and Demetropoulos, I.N. (2008). Molecular dynamics as a pattern recognition tool: An automated process detects peptides that preserve the 3D arrangement of trypsin's active site. Biophys. Chem., 133: 36-44.
    • (2008) Biophys. Chem. , vol.133 , pp. 36-44
    • Tatsis, V.A.1    Stavrakoudis, A.2    Demetropoulos, I.N.3
  • 404
    • 47249163245 scopus 로고    scopus 로고
    • Exploiting nanospace for asymmetric catalysis: Confinement of immobilized, single-site chiral catalysts enhances enantioselectivity
    • Thomas, J.M. and Raja, R. (2008). Exploiting nanospace for asymmetric catalysis: Confinement of immobilized, single-site chiral catalysts enhances enantioselectivity. Acc. Chem. Res., 41: 708-720.
    • (2008) Acc. Chem. Res. , vol.41 , pp. 708-720
    • Thomas, J.M.1    Raja, R.2
  • 405
    • 0041430558 scopus 로고    scopus 로고
    • Controlling chirality
    • Turner, N.J. (2003). Controlling chirality. Curr. Opin. Biotechnol., 14: 401-406.
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 401-406
    • Turner, N.J.1
  • 407
    • 27844496157 scopus 로고    scopus 로고
    • An active enzyme constructed from a 9-amino acid alphabet
    • Walter, K.U., Vamvaca, K., and Hilvert, D. (2005). An active enzyme constructed from a 9-amino acid alphabet. J. Biol. Chem., 280: 37742-37746.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37742-37746
    • Walter, K.U.1    Vamvaca, K.2    Hilvert, D.3
  • 408
    • 0037022661 scopus 로고    scopus 로고
    • Rationally designed mutations convert de novo amyloid-like fibrils into monomeric beta-sheet proteins
    • Wang, W. and Hecht, M.H. (2002). Rationally designed mutations convert de novo amyloid-like fibrils into monomeric beta-sheet proteins. Proc. Natl. Acad. Sci. (USA), 99: 2760-2765.
    • (2002) Proc. Natl. Acad. Sci. (USA) , vol.99 , pp. 2760-2765
    • Wang, W.1    Hecht, M.H.2
  • 409
    • 0344392714 scopus 로고    scopus 로고
    • Solution structure of a de novo protein from a designed combinatorial library
    • Wei, Y., Kim, S., Fela, D., Baum, J., and Hecht, M.H. (2003). Solution structure of a de novo protein from a designed combinatorial library. Proc. Natl. Acad. Sci. (USA), 100: 13270-13273.
    • (2003) Proc. Natl. Acad. Sci. (USA) , vol.100 , pp. 13270-13273
    • Wei, Y.1    Kim, S.2    Fela, D.3    Baum, J.4    Hecht, M.H.5
  • 410
    • 0842270116 scopus 로고    scopus 로고
    • Enzyme-like proteins from an unselected library of designed amino acid sequences
    • Wei, Y. and Hecht, M.H. (2004). Enzyme-like proteins from an unselected library of designed amino acid sequences. Protein Eng. Des. Sel., 17: 67-75.
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 67-75
    • Wei, Y.1    Hecht, M.H.2
  • 412
    • 13844314290 scopus 로고    scopus 로고
    • Metalloporphyrines as active site analogues-lessons from enzymes and enzyme models
    • Woggon, W.-D. (2005). Metalloporphyrines as active site analogues-lessons from enzymes and enzyme models. Acc. Chem. Res., 38: 127-136.
    • (2005) Acc. Chem. Res. , vol.38 , pp. 127-136
    • Woggon, W.-D.1
  • 413
    • 0033564943 scopus 로고    scopus 로고
    • Interchange of catalytic activity within the 2-enoyl-coenzyme A hydratase/isomerase superfamily based on a common active site template
    • Xiang, H., Luo, L., Taylor, K.L., and Dunaway-Mariano, D. (1999). Interchange of catalytic activity within the 2-enoyl-coenzyme A hydratase/isomerase superfamily based on a common active site template. Biochemistry, 38: 7638-7652.
    • (1999) Biochemistry , vol.38 , pp. 7638-7652
    • Xiang, H.1    Luo, L.2    Taylor, K.L.3    Dunaway-Mariano, D.4
  • 414
    • 0037473526 scopus 로고    scopus 로고
    • Chiral molecular assemblies from a novel achiral amphiphilic 2-(heptadecyl) naphtha[2,3]imidazole through interfacial coordination
    • Yuan, J. and Liu, M. (2003). Chiral molecular assemblies from a novel achiral amphiphilic 2-(heptadecyl) naphtha[2,3]imidazole through interfacial coordination. J. Am. Chem. Soc., 125: 5051-5056.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5051-5056
    • Yuan, J.1    Liu, M.2


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