메뉴 건너뛰기




Volumn 106, Issue 3, 2011, Pages 498-516

Basic statistical recipes for the emergence of biochemical discernment

Author keywords

Brillouin; Cooperativity; Entropy; Induced fit; Information; Life

Indexed keywords

ANIMAL; BIOCHEMISTRY; BIOMETRY; CHEMICAL MODEL; ENTROPY; EVOLUTION; HUMAN; METHODOLOGY; REVIEW; SYSTEMS BIOLOGY;

EID: 84860392685     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbiomolbio.2011.07.011     Document Type: Review
Times cited : (8)

References (87)
  • 1
    • 0026506720 scopus 로고
    • Transcription factor loading on the MMTV promoter: a bimodal mechanism for promoter activation
    • Archer T.K., Lefebvre P., Wolford R.G., Hager G.L. Transcription factor loading on the MMTV promoter: a bimodal mechanism for promoter activation. Science 1992, 255:1573-1576.
    • (1992) Science , vol.255 , pp. 1573-1576
    • Archer, T.K.1    Lefebvre, P.2    Wolford, R.G.3    Hager, G.L.4
  • 4
    • 46649103793 scopus 로고    scopus 로고
    • Relationship between thermodynamic driving force and one-way fluxes in reversible processes
    • Beard D.A., Qian H. Relationship between thermodynamic driving force and one-way fluxes in reversible processes. PLoS One 2007, 2:e144.
    • (2007) PLoS One , vol.2
    • Beard, D.A.1    Qian, H.2
  • 5
    • 9644270350 scopus 로고    scopus 로고
    • Nuclear factor 1 and octamer transcription factor 1 binding preset the chromatin structure of the mouse mammary tumor virus promoter for hormone induction
    • Belikov S., Holmqvist P.H., Astrand C., Wrange O. Nuclear factor 1 and octamer transcription factor 1 binding preset the chromatin structure of the mouse mammary tumor virus promoter for hormone induction. J. Biol. Chem. 2004, 279:49857-49867.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49857-49867
    • Belikov, S.1    Holmqvist, P.H.2    Astrand, C.3    Wrange, O.4
  • 6
    • 0030724751 scopus 로고    scopus 로고
    • Transcription factor NF-kB regulates inducible Oct-2 gene expression in precursor B lymphocytes
    • Bendall H.H., Schrerer D.C., Edson C.R., Ballard D.W., Oltz E.M. Transcription factor NF-kB regulates inducible Oct-2 gene expression in precursor B lymphocytes. J. Biol. Chem. 1997, 272:28826-28828.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28826-28828
    • Bendall, H.H.1    Schrerer, D.C.2    Edson, C.R.3    Ballard, D.W.4    Oltz, E.M.5
  • 7
    • 0033855774 scopus 로고    scopus 로고
    • Fluctuations and quality of control in biological cells: zero-order ultrasensitivity reinvestigated
    • Berg O.G., Paulsson J., Ehrenberg M. Fluctuations and quality of control in biological cells: zero-order ultrasensitivity reinvestigated. Biophys. J. 2000, 79:1228-1236.
    • (2000) Biophys. J. , vol.79 , pp. 1228-1236
    • Berg, O.G.1    Paulsson, J.2    Ehrenberg, M.3
  • 9
    • 0036607524 scopus 로고    scopus 로고
    • Modeling DNA sequence-based cis-regulatory gene networks
    • Bolouri H., Davidson E.H. Modeling DNA sequence-based cis-regulatory gene networks. Dev. Biol. 2002, 246:2-13.
    • (2002) Dev. Biol. , vol.246 , pp. 2-13
    • Bolouri, H.1    Davidson, E.H.2
  • 12
    • 67349284051 scopus 로고    scopus 로고
    • Non-genetic heterogeneity - A mutation-independent driving force for the somatic evolution of tumours
    • Brock A., Chang H., Huang S. Non-genetic heterogeneity - A mutation-independent driving force for the somatic evolution of tumours. Nat. Rev. Genet. 2009, 10:336-342.
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 336-342
    • Brock, A.1    Chang, H.2    Huang, S.3
  • 13
    • 67149138163 scopus 로고    scopus 로고
    • Protein sequestration generates a flexible ultrasensitive response in a genetic network
    • Buchler N.E., Cross F.R. Protein sequestration generates a flexible ultrasensitive response in a genetic network. Mol. Syst. Biol. 2009, 5:272.
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 272
    • Buchler, N.E.1    Cross, F.R.2
  • 16
    • 0030995542 scopus 로고    scopus 로고
    • Nucleosome-mediated synergism between transcription factors on the mouse mammary tumor virus promoter
    • Chávez S., Beato M. Nucleosome-mediated synergism between transcription factors on the mouse mammary tumor virus promoter. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:2885-2890.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2885-2890
    • Chávez, S.1    Beato, M.2
  • 17
    • 0034696445 scopus 로고    scopus 로고
    • How to make a biological switch
    • Cherry J.L., Adler F.R. How to make a biological switch. J.Theor. Biol. 2000, 203:117-133.
    • (2000) J.Theor. Biol. , vol.203 , pp. 117-133
    • Cherry, J.L.1    Adler, F.R.2
  • 19
  • 20
    • 48249134043 scopus 로고    scopus 로고
    • Evolution of evolvability in gene regulatory networks
    • Crombach A., Hogeweg P. Evolution of evolvability in gene regulatory networks. PLoS Comput. Biol. 2008, 4:e1000112.
    • (2008) PLoS Comput. Biol. , vol.4
    • Crombach, A.1    Hogeweg, P.2
  • 21
    • 78650061153 scopus 로고    scopus 로고
    • Transgenerational epigenetic inheritance: more questions than answers
    • Daxinger L., Whitelaw E. Transgenerational epigenetic inheritance: more questions than answers. Genome Res. 2010, 20:1623-1628.
    • (2010) Genome Res. , vol.20 , pp. 1623-1628
    • Daxinger, L.1    Whitelaw, E.2
  • 22
    • 33746659395 scopus 로고    scopus 로고
    • Multiple phosphorylation sites confer reproducibility of the rod's single-photon response
    • Doan T., Mendez A., Detwiler P.B., Chen J., Rieke F. Multiple phosphorylation sites confer reproducibility of the rod's single-photon response. Science 2006, 313:530-533.
    • (2006) Science , vol.313 , pp. 530-533
    • Doan, T.1    Mendez, A.2    Detwiler, P.B.3    Chen, J.4    Rieke, F.5
  • 24
    • 0030793885 scopus 로고    scopus 로고
    • Binding of NF1 to the MMTV promoter in nucleosomes: influence of rotational phasing, translational positioning and histone H1
    • Eisfeld K., Candau R., Truss M., Beato M. Binding of NF1 to the MMTV promoter in nucleosomes: influence of rotational phasing, translational positioning and histone H1. Nucl. Acids Res. 1997, 25:3733-3742.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3733-3742
    • Eisfeld, K.1    Candau, R.2    Truss, M.3    Beato, M.4
  • 25
    • 77956520011 scopus 로고    scopus 로고
    • Functional roles for noise in genetic circuits
    • Eldar A., Elowitz M.B. Functional roles for noise in genetic circuits. Nature 2010, 467:167-173.
    • (2010) Nature , vol.467 , pp. 167-173
    • Eldar, A.1    Elowitz, M.B.2
  • 26
    • 0001485928 scopus 로고
    • Entropy in an expanding universe
    • Frautschi S. Entropy in an expanding universe. Science 1982, 217:593-599.
    • (1982) Science , vol.217 , pp. 593-599
    • Frautschi, S.1
  • 27
    • 0032492846 scopus 로고    scopus 로고
    • Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex
    • Fryer C.J., Archer T.K. Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex. Nature 1998, 393:88-91.
    • (1998) Nature , vol.393 , pp. 88-91
    • Fryer, C.J.1    Archer, T.K.2
  • 28
    • 36849148382 scopus 로고
    • Origin of life: the RNA world
    • Gilbert W. Origin of life: the RNA world. Nature 1986, 319:618-628.
    • (1986) Nature , vol.319 , pp. 618-628
    • Gilbert, W.1
  • 29
    • 0001424903 scopus 로고
    • An amplified sensitivity arising from covalent modification in biological systems
    • Goldbeter A., Koshland D.E. An amplified sensitivity arising from covalent modification in biological systems. Proc. Natl. Acad. Sci. U. S. A. 1981.
    • (1981) Proc. Natl. Acad. Sci. U. S. A.
    • Goldbeter, A.1    Koshland, D.E.2
  • 31
    • 69549120472 scopus 로고    scopus 로고
    • Conformational selection or induced fit: a flux description of reaction mechanism
    • Hammes G.G., Chang Y.C., Oas T.G. Conformational selection or induced fit: a flux description of reaction mechanism. Proc. Natl. Acad. Sci. USA 2009, 106:13737-13741.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13737-13741
    • Hammes, G.G.1    Chang, Y.C.2    Oas, T.G.3
  • 33
    • 34247281521 scopus 로고    scopus 로고
    • Chromatin-dependent cooperativity between site-specific transcription factors in vivo
    • Hebbar P.B., Archer T.K. Chromatin-dependent cooperativity between site-specific transcription factors in vivo. J. Biol. Chem. 2007, 282:8284-8291.
    • (2007) J. Biol. Chem. , vol.282 , pp. 8284-8291
    • Hebbar, P.B.1    Archer, T.K.2
  • 34
    • 33745150728 scopus 로고    scopus 로고
    • Glucose-induced conformational changes in glucokinase mediate allosteric regulation: transient kinetic analysis
    • Heredia V.V., Thomson J., Nettleton D., Sun S. Glucose-induced conformational changes in glucokinase mediate allosteric regulation: transient kinetic analysis. Biochemistry 2006, 45:7553-7562.
    • (2006) Biochemistry , vol.45 , pp. 7553-7562
    • Heredia, V.V.1    Thomson, J.2    Nettleton, D.3    Sun, S.4
  • 35
    • 0000359208 scopus 로고
    • Kinetic proofreading: a new mechanism for reducing errors in biosynthetic processes requiring high specificity
    • Hopfield J.J. Kinetic proofreading: a new mechanism for reducing errors in biosynthetic processes requiring high specificity. Proc. Natl. Acad. Sci. USA 1974, 71:4135-4139.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4135-4139
    • Hopfield, J.J.1
  • 36
    • 0020118274 scopus 로고
    • Neural networks and physical systems with emergent collective computational abilities
    • Hopfield J.J. Neural networks and physical systems with emergent collective computational abilities. Proc. Natl. Acad. Sci. USA 1982, 79:2554-2558.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2554-2558
    • Hopfield, J.J.1
  • 37
    • 2442668310 scopus 로고
    • Genetic repression, allosteric inhibition, and cellular differentiation
    • Acad. Press. Inc., New York, M. Locke (Ed.)
    • Jacob F., Monod J. Genetic repression, allosteric inhibition, and cellular differentiation. Cytodifferential and Macromolecular Synthesis 1963, 30-64. Acad. Press. Inc., New York. M. Locke (Ed.).
    • (1963) Cytodifferential and Macromolecular Synthesis , pp. 30-64
    • Jacob, F.1    Monod, J.2
  • 38
    • 11944266539 scopus 로고
    • Information theory and statistical mechanics
    • Jaynes E.T. Information theory and statistical mechanics. Phys. Rev. 1957, 106:620-630.
    • (1957) Phys. Rev. , vol.106 , pp. 620-630
    • Jaynes, E.T.1
  • 39
    • 4444311806 scopus 로고    scopus 로고
    • A proposal for using the ensemble approach to understand genetic regulatory networks
    • Kauffman S. A proposal for using the ensemble approach to understand genetic regulatory networks. J. Theor. Biol. 2004, 230:581-590.
    • (2004) J. Theor. Biol. , vol.230 , pp. 581-590
    • Kauffman, S.1
  • 40
    • 67149134671 scopus 로고    scopus 로고
    • On the free energy that drove primordial anabolism
    • Kaufmann M. On the free energy that drove primordial anabolism. Int. J. Mol. Sci. 2009, 10:1853-1871.
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 1853-1871
    • Kaufmann, M.1
  • 41
    • 0027209703 scopus 로고
    • Transition modes in Ising networks: an approximate theory for macromolecular recognition
    • Keating S., Di Cera E. Transition modes in Ising networks: an approximate theory for macromolecular recognition. Biophys. J. 1993, 65:253-269.
    • (1993) Biophys. J. , vol.65 , pp. 253-269
    • Keating, S.1    Di Cera, E.2
  • 42
    • 58149198799 scopus 로고    scopus 로고
    • Variation in patterns of human meiotic recombination
    • Khil P.P., Camerini-Otero R.D. Variation in patterns of human meiotic recombination. Genome Dyn. 2009, 5:117-127.
    • (2009) Genome Dyn. , vol.5 , pp. 117-127
    • Khil, P.P.1    Camerini-Otero, R.D.2
  • 44
    • 33947472850 scopus 로고
    • A schematic method of deriving the rate laws for enzyme-catalyzed reactions
    • King E.L., Altman C. A schematic method of deriving the rate laws for enzyme-catalyzed reactions. J. Phys. Chem. B. 1956, 60:1375-1378.
    • (1956) J. Phys. Chem. B. , vol.60 , pp. 1375-1378
    • King, E.L.1    Altman, C.2
  • 45
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland D.E. Application of a theory of enzyme specificity to protein synthesis. Proc. Natl. Acad. Sci. U.S.A 1958, 44:98-104.
    • (1958) Proc. Natl. Acad. Sci. U.S.A , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 46
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland D.E., Nemethy G., Filmer D. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 1966, 5:365-385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland, D.E.1    Nemethy, G.2    Filmer, D.3
  • 47
    • 0000941724 scopus 로고
    • Switches, thresholds and ultrasensitivity
    • Koshland D.E. Switches, thresholds and ultrasensitivity. Trends Biochem. Sci. 1987, 12:225-229.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 225-229
    • Koshland, D.E.1
  • 48
    • 77950456083 scopus 로고    scopus 로고
    • How did LUCA make a living? Chemiosmosis in the origin of life
    • Lane N., Allen J.F., Martin W. How did LUCA make a living? Chemiosmosis in the origin of life. Bioessays 2010, 32:271-280.
    • (2010) Bioessays , vol.32 , pp. 271-280
    • Lane, N.1    Allen, J.F.2    Martin, W.3
  • 49
    • 12044250952 scopus 로고
    • Boltzmann's entropy and Time's arrow
    • Lebowitz J.L. Boltzmann's entropy and Time's arrow. Phys. Today 1993, 46:32-38.
    • (1993) Phys. Today , vol.46 , pp. 32-38
    • Lebowitz, J.L.1
  • 50
    • 84860407905 scopus 로고    scopus 로고
    • Cooperative behavior in simple and complex systems. Science for Survival and Sustainable development, Pointifical Academy of Sciences
    • Lebowitz J.L. Cooperative behavior in simple and complex systems. Science for Survival and Sustainable development, Pointifical Academy of Sciences. Scripta Varia 1999, 98(98):321-325.
    • (1999) Scripta Varia , vol.98 , Issue.98 , pp. 321-325
    • Lebowitz, J.L.1
  • 52
    • 0025285220 scopus 로고
    • Demonstration of a slow conformational change in liver glucokinase by fluorescence spectroscopy
    • Lin S.X., Neet K.E. Demonstration of a slow conformational change in liver glucokinase by fluorescence spectroscopy. J. Biol. Chem. 1990, 265:9670-9675.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9670-9675
    • Lin, S.X.1    Neet, K.E.2
  • 53
    • 0041856190 scopus 로고    scopus 로고
    • Native human TATA-binding protein simultaneously binds and bends promoter DNA without a slow isomerization step or TFIIB requirement
    • Masters K.M., Parkhurst K.M., Daugherty M.A., Parkhurst L.J. Native human TATA-binding protein simultaneously binds and bends promoter DNA without a slow isomerization step or TFIIB requirement. J. Biol. Chem. 2003, 278:31685-31690.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31685-31690
    • Masters, K.M.1    Parkhurst, K.M.2    Daugherty, M.A.3    Parkhurst, L.J.4
  • 54
    • 33746931732 scopus 로고    scopus 로고
    • Threshold responses to morphogen gradients by zero-order ultrasensitivity
    • Melen G.J., Levy S., Barkai N., Shilo B.Z. Threshold responses to morphogen gradients by zero-order ultrasensitivity. Mol. Syst. Biol. 2005, 1:0028.
    • (2005) Mol. Syst. Biol. , vol.1 , pp. 0028
    • Melen, G.J.1    Levy, S.2    Barkai, N.3    Shilo, B.Z.4
  • 55
    • 34547677692 scopus 로고    scopus 로고
    • Cooperative equilibrium curves generated by ordered ligand binding to multi-site molecules
    • Michel D. Cooperative equilibrium curves generated by ordered ligand binding to multi-site molecules. Biophys. Chem. 2007, 129:284-288.
    • (2007) Biophys. Chem. , vol.129 , pp. 284-288
    • Michel, D.1
  • 56
    • 45849096417 scopus 로고    scopus 로고
    • An alternative theoretical formula for hemoglobin oxygenation
    • Michel D. An alternative theoretical formula for hemoglobin oxygenation. Eur. Biophys. J. 2008, 37:823-827.
    • (2008) Eur. Biophys. J. , vol.37 , pp. 823-827
    • Michel, D.1
  • 57
    • 67349180635 scopus 로고    scopus 로고
    • Fine tuning gene expression through short DNA-protein binding cycles
    • Michel D. Fine tuning gene expression through short DNA-protein binding cycles. Biochimie 2009, 91:933-941.
    • (2009) Biochimie , vol.91 , pp. 933-941
    • Michel, D.1
  • 58
    • 76349086026 scopus 로고    scopus 로고
    • How transcription factors can adjust the gene expression floodgates
    • Michel D. How transcription factors can adjust the gene expression floodgates. Prog. Biophys. Mol. Biol. 2010, 32:16-37.
    • (2010) Prog. Biophys. Mol. Biol. , vol.32 , pp. 16-37
    • Michel, D.1
  • 59
    • 80051583095 scopus 로고    scopus 로고
    • Hierarchical cooperativity mediated by chromatin remodeling; the model of the MMTV transcription regulation
    • in press, doi:10.1016/j.jtbi.2011.07.020
    • Michel, D. Hierarchical cooperativity mediated by chromatin remodeling; the model of the MMTV transcription regulation. J. Theor. Biol., in press, . doi:10.1016/j.jtbi.2011.07.020.
    • J. Theor. Biol.
    • Michel, D.1
  • 60
    • 69149090263 scopus 로고    scopus 로고
    • Role of conformational dynamics in kinetics of an enzymatic cycle in a nonequilibrium steady state
    • Min W., Xie X.S., Bagchi B. Role of conformational dynamics in kinetics of an enzymatic cycle in a nonequilibrium steady state. J. Chem. Phys. 2009, 131:065104.
    • (2009) J. Chem. Phys. , vol.131 , pp. 065104
    • Min, W.1    Xie, X.S.2    Bagchi, B.3
  • 61
    • 78651107675 scopus 로고    scopus 로고
    • Nucleosome-mediated cooperativity between transcription factors
    • Mirny L.A. Nucleosome-mediated cooperativity between transcription factors. Proc. Natl. Acad. Sci. U.S.A 2010, 107:22534-22539.
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 22534-22539
    • Mirny, L.A.1
  • 62
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: a plausible model
    • Monod J., Wyman J., Changeux J.-P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 1965, 12:88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 63
    • 0016793283 scopus 로고
    • Kinetic amplification of enzyme discrimination
    • Ninio J. Kinetic amplification of enzyme discrimination. Biochimie 1975, 57:587-595.
    • (1975) Biochimie , vol.57 , pp. 587-595
    • Ninio, J.1
  • 64
    • 77449141025 scopus 로고    scopus 로고
    • Biophysics and systems biology
    • Noble D. Biophysics and systems biology. Phil. Trans. R. Soc. A 2010, 368:1125-1139.
    • (2010) Phil. Trans. R. Soc. A , vol.368 , pp. 1125-1139
    • Noble, D.1
  • 65
    • 0028919503 scopus 로고
    • Pre-bending of a promoter sequence enhances affinity for the TATA-binding factor
    • Parvin J.D., McCormick R.J., Sharp P.A., Fisher D.E. Pre-bending of a promoter sequence enhances affinity for the TATA-binding factor. Nature 1995, 373:724-727.
    • (1995) Nature , vol.373 , pp. 724-727
    • Parvin, J.D.1    McCormick, R.J.2    Sharp, P.A.3    Fisher, D.E.4
  • 66
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz M.F. Stereochemistry of cooperative effects in haemoglobin. Nature 1970, 228:726-739.
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.F.1
  • 67
    • 0038762202 scopus 로고
    • Hemoglobin structure and respiratory transport
    • Perutz M.F. Hemoglobin structure and respiratory transport. Scientific Am. 1978, 259:68-86.
    • (1978) Scientific Am. , vol.259 , pp. 68-86
    • Perutz, M.F.1
  • 68
    • 12244261838 scopus 로고
    • Time, structure and fluctuations
    • Nobel lecture 8 December, 1977.
    • Prigogine, I., 1977. Time, structure and fluctuations. Nobel lecture 8 December, 1977. http://nobelprize.org/nobel_prizes/chemistry/laureates/1977/prigogine-lecture.html.
    • (1977)
    • Prigogine, I.1
  • 69
    • 0037268381 scopus 로고    scopus 로고
    • The driving force for life's emergence: kinetic and thermodynamic considerations
    • Pross A. The driving force for life's emergence: kinetic and thermodynamic considerations. J. Theor. Biol. 2003, 220:393-406.
    • (2003) J. Theor. Biol. , vol.220 , pp. 393-406
    • Pross, A.1
  • 70
    • 0014057553 scopus 로고
    • Co-operative effects in enzyme catalysis: a possible kinetic model based on substrate-induced conformation isomerization
    • Rabin B.R. Co-operative effects in enzyme catalysis: a possible kinetic model based on substrate-induced conformation isomerization. Biochem. J. 1967, 102:22C-23C.
    • (1967) Biochem. J. , vol.102
    • Rabin, B.R.1
  • 71
    • 53549123008 scopus 로고    scopus 로고
    • Nature nurture, or chance: stochastic gene expression and its consequences
    • Raj A., van Oudenaarden A. Nature nurture, or chance: stochastic gene expression and its consequences. Cell 2008, 135:216-226.
    • (2008) Cell , vol.135 , pp. 216-226
    • Raj, A.1    van Oudenaarden, A.2
  • 73
    • 67649826220 scopus 로고    scopus 로고
    • From DNA sequence to transcriptional behaviour: a quantitative approach
    • Segal E., Widom J. From DNA sequence to transcriptional behaviour: a quantitative approach. Nat. Rev. Genet. 2009, 10:443-456.
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 443-456
    • Segal, E.1    Widom, J.2
  • 74
    • 0345902803 scopus 로고
    • Direct observation of intermediate ligation states of hemoglobin
    • Simonneaux G., Bondon A., Brunel C., Sodano P. Direct observation of intermediate ligation states of hemoglobin. J. Am. Chem. Soc. 1988, 110:7637-7640.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 7637-7640
    • Simonneaux, G.1    Bondon, A.2    Brunel, C.3    Sodano, P.4
  • 75
    • 33845500268 scopus 로고    scopus 로고
    • Stepwise binding and bending of DNA by Escherichia coli integration host factor
    • Sugimura S., Crothers D.M. Stepwise binding and bending of DNA by Escherichia coli integration host factor. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:18510-18514.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 18510-18514
    • Sugimura, S.1    Crothers, D.M.2
  • 76
    • 52949089027 scopus 로고    scopus 로고
    • Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection
    • Sullivan S.M., Holyoak T. Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:13829-13834.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 13829-13834
    • Sullivan, S.M.1    Holyoak, T.2
  • 77
    • 0001273302 scopus 로고
    • The principle of microscopic reversibility
    • Tolman T.C. The principle of microscopic reversibility. Proc. Natl. Acad. Sci. U. S. A. 1925, 11:436-439.
    • (1925) Proc. Natl. Acad. Sci. U. S. A. , vol.11 , pp. 436-439
    • Tolman, T.C.1
  • 78
    • 70349977175 scopus 로고    scopus 로고
    • The origin of the genetic code and of the earliest oligopeptides
    • Trifonov E.N. The origin of the genetic code and of the earliest oligopeptides. Res. Microbiol. 2009, 160:481-486.
    • (2009) Res. Microbiol. , vol.160 , pp. 481-486
    • Trifonov, E.N.1
  • 79
    • 70349985700 scopus 로고    scopus 로고
    • From the primordial soup to the latest universal common ancestor
    • Vaneechoutte M., Fani R. From the primordial soup to the latest universal common ancestor. Res. Microbiol. 2009, 160:437-440.
    • (2009) Res. Microbiol. , vol.160 , pp. 437-440
    • Vaneechoutte, M.1    Fani, R.2
  • 81
    • 0005604172 scopus 로고
    • Evolutionary systems; animal and human
    • Waddington C.H. Evolutionary systems; animal and human. Nature 1959, 183:1634-1638.
    • (1959) Nature , vol.183 , pp. 1634-1638
    • Waddington, C.H.1
  • 82
    • 0037194057 scopus 로고    scopus 로고
    • Experimental demonstration of violations of the second law of thermodynamics for small systems and short iime scales
    • Wang G.M., Sevick E.M., Mittag E., Searles D.J., Evans D.J. Experimental demonstration of violations of the second law of thermodynamics for small systems and short iime scales. Phys. Rev. Lett. 2002, 89:050601.
    • (2002) Phys. Rev. Lett. , vol.89 , pp. 050601
    • Wang, G.M.1    Sevick, E.M.2    Mittag, E.3    Searles, D.J.4    Evans, D.J.5
  • 83
    • 65249090946 scopus 로고    scopus 로고
    • Selected-fit versus induced-fit protein binding: kinetic differences and mutational analysis
    • Weikl T.R., von Deuster C. Selected-fit versus induced-fit protein binding: kinetic differences and mutational analysis. Proteins 2009, 75:104-110.
    • (2009) Proteins , vol.75 , pp. 104-110
    • Weikl, T.R.1    von Deuster, C.2
  • 84
    • 0030768931 scopus 로고    scopus 로고
    • The Hill equation revisited: uses and misuses
    • Weiss J.N. The Hill equation revisited: uses and misuses. FASEB J. 1997, 11:835-841.
    • (1997) FASEB J. , vol.11 , pp. 835-841
    • Weiss, J.N.1
  • 85
    • 0014728574 scopus 로고
    • The regulation of enzyme activity and allosteric transition
    • Whitehead E. The regulation of enzyme activity and allosteric transition. Prog. Biophys. Mol. Biol. 1970, 21:321-397.
    • (1970) Prog. Biophys. Mol. Biol. , vol.21 , pp. 321-397
    • Whitehead, E.1
  • 87
    • 0037040419 scopus 로고    scopus 로고
    • A regulated two-step mechanism of TBP binding to DNA: a solvent-exposed surface of TBP inhibits TATA box recognition
    • Zhao X., Herr W. A regulated two-step mechanism of TBP binding to DNA: a solvent-exposed surface of TBP inhibits TATA box recognition. Cell 2002, 108:615-627.
    • (2002) Cell , vol.108 , pp. 615-627
    • Zhao, X.1    Herr, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.