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Volumn 41, Issue 1, 2012, Pages 179-204

Cooperativity in cellular biochemical processes: Noise-enhanced sensitivity, fluctuating enzyme, bistability with nonlinear feedback, and other mechanisms for sigmoidal responses

Author keywords

Hysteretic enzyme; Kinetic proofreading; Nonequilibrium; Open chemical systems; Signal transduction

Indexed keywords

ENZYME;

EID: 84861384820     PISSN: 1936122X     EISSN: 19361238     Source Type: Book Series    
DOI: 10.1146/annurev-biophys-050511-102240     Document Type: Review
Times cited : (88)

References (110)
  • 1
    • 0015502072 scopus 로고
    • Transients and cooperativity: A slow transition model for relating transients and cooperative kinetics of enzymes
    • Ainslie GR, Shill JP, Neet KE. 1972. Transients and cooperativity: a slow transition model for relating transients and cooperative kinetics of enzymes. J. Biol. Chem. 247:7088-96
    • (1972) J. Biol. Chem. , vol.247 , pp. 7088-7096
    • Ainslie, G.R.1    Shill, J.P.2    Neet, K.E.3
  • 2
    • 38749098685 scopus 로고    scopus 로고
    • Cancer as robust intrinsic state of endogenous molecular-cellular network shaped by evolution
    • Ao P, Galas D, Hood L, Zhu X. 2008. Cancer as robust intrinsic state of endogenous molecular-cellular network shaped by evolution. Med. Hypoth. 70:678-84
    • (2008) Med. Hypoth. , vol.70 , pp. 678-684
    • Ao, P.1    Galas, D.2    Hood, L.3    Zhu, X.4
  • 3
    • 37649018636 scopus 로고    scopus 로고
    • Purely stochastic binary decisions in cell signaling models without underlying deterministic bistabilities
    • Artyomov MN, Das J, Kardar M, Chakraborty AK. 2007. Purely stochastic binary decisions in cell signaling models without underlying deterministic bistabilities. Proc. Natl. Acad. Sci. USA 104:18958-63
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 18958-18963
    • Artyomov, M.N.1    Das, J.2    Kardar, M.3    Chakraborty, A.K.4
  • 6
    • 0033855774 scopus 로고    scopus 로고
    • Fluctuations and quality of control in biological cells: Zero-order ultrasensitivity reinvestigated
    • Berg OG, Paulsson J, Ehrenberg M. 2000. Fluctuations and quality of control in biological cells: zero-order ultrasensitivity reinvestigated. Biophys. J. 79:1228-36
    • (2000) Biophys. J. , vol.79 , pp. 1228-1236
    • Berg, O.G.1    Paulsson, J.2    Ehrenberg, M.3
  • 7
    • 0033638791 scopus 로고    scopus 로고
    • Fluctuations in repressor control: Thermodynamic constraints on stochastic focusing
    • Berg OG, Paulsson J, Ehrenberg M. 2000. Fluctuations in repressor control: thermodynamic constraints on stochastic focusing. Biophys. J. 79:2944-53
    • (2000) Biophys. J. , vol.79 , pp. 2944-2953
    • Berg, O.G.1    Paulsson, J.2    Ehrenberg, M.3
  • 8
    • 74049092279 scopus 로고    scopus 로고
    • Stochastic bistability and bifurcation in a mesoscopic signaling system with autocatalytic kinase
    • Bishop LM, Qian H. 2010. Stochastic bistability and bifurcation in a mesoscopic signaling system with autocatalytic kinase. Biophys. J. 98:1-11
    • (2010) Biophys. J. , vol.98 , pp. 1-11
    • Bishop, L.M.1    Qian, H.2
  • 9
    • 70350336588 scopus 로고    scopus 로고
    • Architecture-dependent noise discriminates functionally analogous differentiation circuits
    • Caǧatay T, Turcotte M, Elowitz MB, Garcia-Ojalvo J, Süel GM. 2009. Architecture-dependent noise discriminates functionally analogous differentiation circuits. Cell 139:512-22
    • (2009) Cell , vol.139 , pp. 512-522
    • Caǧatay, T.1    Turcotte, M.2    Elowitz, M.B.3    Garcia-Ojalvo, J.4    Süel, G.M.5
  • 10
    • 78649871073 scopus 로고    scopus 로고
    • Probability landscape of heritable and robust epigenetic state of lysogeny in phage lambda
    • Cao Y, Lu H-M, Liang J. 2010. Probability landscape of heritable and robust epigenetic state of lysogeny in phage lambda. Proc. Natl. Acad. Sci. USA 107:18445-50
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 18445-18450
    • Cao, Y.1    Lu, H.-M.2    Liang, J.3
  • 11
    • 0023295224 scopus 로고
    • Asymmetry and external noise-induced free energy transduction
    • Chen Y-D. 1987. Asymmetry and external noise-induced free energy transduction. Proc. Natl. Acad. Sci. USA 84:729-33
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 729-733
    • Chen, Y.-D.1
  • 12
    • 58249092059 scopus 로고    scopus 로고
    • Digital signaling and hysteresis characterize Ras activation in lymphoid cells
    • Das J, Ho M, Zikherman J, Govern C, Yang M, et al. 2009. Digital signaling and hysteresis characterize Ras activation in lymphoid cells. Cell 136:337-51
    • (2009) Cell , vol.136 , pp. 337-351
    • Das, J.1    Ho, M.2    Zikherman, J.3    Govern, C.4    Yang, M.5
  • 13
    • 0000296912 scopus 로고
    • Statistical fluctuations in autocatalytic reactions
    • Delbrück M. 1940. Statistical fluctuations in autocatalytic reactions. J. Chem. Phys. 8:120-24
    • (1940) J. Chem. Phys. , vol.8 , pp. 120-124
    • Delbrück, M.1
  • 15
    • 34249080596 scopus 로고    scopus 로고
    • Theoretical analysis of epigenetic cell memory by nucleosome modification
    • Dodd IB, Micheelsen MA, Sneppen K, Thon G. 2007. Theoretical analysis of epigenetic cell memory by nucleosome modification. Cell 129:813-22
    • (2007) Cell , vol.129 , pp. 813-822
    • Dodd, I.B.1    Micheelsen, M.A.2    Sneppen, K.3    Thon, G.4
  • 16
    • 47649130574 scopus 로고    scopus 로고
    • Capturing cooperativity
    • Editorial.
    • Editorial. 2008. Capturing cooperativity. Nat. Chem. Biol. 4:433-47
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 433-447
  • 18
    • 0032496358 scopus 로고    scopus 로고
    • The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes
    • Ferrell JE, Machleder EM. 1998. The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Science 280:895-98
    • (1998) Science , vol.280 , pp. 895-898
    • Ferrell, J.E.1    MacHleder, E.M.2
  • 19
    • 0037605637 scopus 로고    scopus 로고
    • Bistability in cell signaling: How to make continuous processes discontinuous, and reversible processes irreversible
    • Ferrell JE, Xiong W. 2001. Bistability in cell signaling: how to make continuous processes discontinuous, and reversible processes irreversible. Chaos 11:227-36
    • (2001) Chaos , vol.11 , pp. 227-236
    • Ferrell, J.E.1    Xiong, W.2
  • 21
    • 0014940726 scopus 로고
    • Kinetic aspects of regulation of metabolic processes: The hysteretic enzyme concept
    • Frieden C. 1970. Kinetic aspects of regulation of metabolic processes: the hysteretic enzyme concept. J. Biol. Chem. 245:5788-99
    • (1970) J. Biol. Chem. , vol.245 , pp. 5788-5799
    • Frieden, C.1
  • 23
    • 70349931588 scopus 로고    scopus 로고
    • Thermodynamic limit of a nonequilibrium steady-state: Maxwell-type construction for a bistable biochemical system
    • Ge H, Qian H. 2009. Thermodynamic limit of a nonequilibrium steady-state: Maxwell-type construction for a bistable biochemical system. Phys. Rev. Lett. 103:148103
    • (2009) Phys. Rev. Lett. , vol.103 , pp. 148103
    • Ge, H.1    Qian, H.2
  • 24
    • 78649786267 scopus 로고    scopus 로고
    • Nonequilibrium phase transition in mesoscopic biochemical systems: From stochastic to nonlinear dynamics and beyond
    • Ge H, Qian H. 2011. Nonequilibrium phase transition in mesoscopic biochemical systems: from stochastic to nonlinear dynamics and beyond. J. R. Soc. Interf. 8:107-16
    • (2011) J. R. Soc. Interf. , vol.8 , pp. 107-116
    • Ge, H.1    Qian, H.2
  • 25
    • 46749104726 scopus 로고    scopus 로고
    • Sensitivity amplification in the phosphorylation-dephosphorylation cycle: Nonequi-librium steady states, chemical master equation and temporal cooperativity
    • Ge H, Qian M. 2008. Sensitivity amplification in the phosphorylation- dephosphorylation cycle: nonequi-librium steady states, chemical master equation and temporal cooperativity. J. Chem. Phys. 129:015104
    • (2008) J. Chem. Phys. , vol.129 , pp. 015104
    • Ge, H.1    Qian, M.2
  • 26
    • 83255165435 scopus 로고    scopus 로고
    • Stochastic theory of nonequilibrium steady states. Part II: Applications in chemical biophysics
    • Ge H, Qian M, Qian H. 2012. Stochastic theory of nonequilibrium steady states. Part II: applications in chemical biophysics. Phys. Rep. 510:87-118
    • (2012) Phys. Rep. , vol.510 , pp. 87-118
    • Ge, H.1    Qian, M.2    Qian, H.3
  • 27
    • 34249950625 scopus 로고    scopus 로고
    • Stochastic simulation of chemical kinetics
    • Gillespie DT. 2007. Stochastic simulation of chemical kinetics. Annu. Rev. Phys. Chem. 58:35-55
    • (2007) Annu. Rev. Phys. Chem. , vol.58 , pp. 35-55
    • Gillespie, D.T.1
  • 28
    • 0001424903 scopus 로고
    • An amplified sensitivity arising from covalent modification in biological systems
    • Goldbeter A, Koshland DE. 1981. An amplified sensitivity arising from covalent modification in biological systems. Proc. Natl. Acad. Sci. USA 78:6840-44
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6840-6844
    • Goldbeter, A.1    Koshland, D.E.2
  • 29
    • 33750121794 scopus 로고    scopus 로고
    • Protein synthesis molecule by molecule
    • Golding I, Cox EC. 2006. Protein synthesis molecule by molecule. Genome Biol. 7:212-13
    • (2006) Genome Biol. , vol.7 , pp. 212-213
    • Golding, I.1    Cox, E.C.2
  • 30
    • 77949916347 scopus 로고    scopus 로고
    • Two-component signaling circuit structure and properties
    • Goulian M. 2010. Two-component signaling circuit structure and properties. Curr. Opin. Microbiol. 13:184-89
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 184-189
    • Goulian, M.1
  • 31
    • 26844571282 scopus 로고    scopus 로고
    • Multisite protein phosphorylation makes a good threshold but can be a poor switch
    • Gunawardena J. 2005. Multisite protein phosphorylation makes a good threshold but can be a poor switch. Proc. Natl. Acad. Sci. USA 102:14617-22
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14617-14622
    • Gunawardena, J.1
  • 35
    • 0015698515 scopus 로고
    • Relation between structure, cooperativity and spectra in a model of hemoglobin action
    • Hopfield JJ. 1973. Relation between structure, cooperativity and spectra in a model of hemoglobin action. J. Mol. Biol. 77:207-22
    • (1973) J. Mol. Biol. , vol.77 , pp. 207-222
    • Hopfield, J.J.1
  • 36
    • 0000359208 scopus 로고
    • Kinetic proofreading: A new mechanism for reducing errors in biosynthetic processes requiring high specificity
    • Hopfield JJ. 1974. Kinetic proofreading: a new mechanism for reducing errors in biosynthetic processes requiring high specificity. Proc. Natl. Acad. Sci. USA 71:4135-39
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4135-4139
    • Hopfield, J.J.1
  • 37
    • 0019134996 scopus 로고
    • The energy relay: A proofreading scheme based on dynamic cooperativity and lacking all characteristic symptoms of kinetic proofreading in DNA replication and protein synthesis
    • Hopfield JJ. 1980. The energy relay: a proofreading scheme based on dynamic cooperativity and lacking all characteristic symptoms of kinetic proofreading in DNA replication and protein synthesis. Proc. Natl. Acad. Sci. USA 77:5248-52
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5248-5252
    • Hopfield, J.J.1
  • 39
    • 0000481233 scopus 로고
    • Noise-induced transitions: Theory, applications in physics, chemistry, and biology
    • Berlin: Springer-Verlag
    • Horsthemke W, Lefever R. 1984. Noise-Induced Transitions: Theory, Applications in Physics, Chemistry, and Biology. Springer Ser. Synergetics, Vol. 15. Berlin: Springer-Verlag
    • (1984) Springer Ser. Synergetics , vol.15
    • Horsthemke, W.1    Lefever, R.2
  • 40
    • 84861387553 scopus 로고    scopus 로고
    • The dynamics of zeroth-order ultrasensitivity: A critical phenomenon in cell biology
    • Huang Q, Qian H. 2011. The dynamics of zeroth-order ultrasensitivity: a critical phenomenon in cell biology. Discr. Cont. Dyn. Sys. S 4:1457-64
    • (2011) Discr. Cont. Dyn. Sys. S , vol.4 , pp. 1457-1464
    • Huang, Q.1    Qian, H.2
  • 44
    • 0035193294 scopus 로고    scopus 로고
    • Stochasticity in transcriptional regulation: Origins, consequences, and mathematical representations
    • Kepler TB, Elston TC. 2001. Stochasticity in transcriptional regulation: origins, consequences, and mathematical representations. Biophys. J. 81:3116-36
    • (2001) Biophys. J. , vol.81 , pp. 3116-3136
    • Kepler, T.B.1    Elston, T.C.2
  • 45
    • 77249103975 scopus 로고    scopus 로고
    • Stochastic kinetic model of two component system signalling reveals all-or-none, graded and mixed mode stochastic switching responses
    • Kierzek AM, Zhou L, Wanner BL. 2010. Stochastic kinetic model of two component system signalling reveals all-or-none, graded and mixed mode stochastic switching responses. Mol. Biosyst. 6:531-42
    • (2010) Mol. Biosyst. , vol.6 , pp. 531-542
    • Kierzek, A.M.1    Zhou, L.2    Wanner, B.L.3
  • 46
    • 33947304756 scopus 로고    scopus 로고
    • Substrate competition as a source of ultrasensitivity in the inactivation of Wee1
    • Kim SY, Ferrell JE. 2007. Substrate competition as a source of ultrasensitivity in the inactivation of Wee1. Cell 128:1133-45
    • (2007) Cell , vol.128 , pp. 1133-1145
    • Kim, S.Y.1    Ferrell, J.E.2
  • 47
    • 0019996706 scopus 로고
    • Amplification and adaptation in regulatory and sensory systems
    • Koshland DE, Goldbeter A, Stock JB. 1982. Amplification and adaptation in regulatory and sensory systems. Science 217:220-25
    • (1982) Science , vol.217 , pp. 220-225
    • Koshland, D.E.1    Goldbeter, A.2    Stock, J.B.3
  • 48
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland DE, Némethy G, Filmer D. 1966. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5:365-85
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland, D.E.1    Némethy, G.2    Filmer, D.3
  • 50
    • 0036729047 scopus 로고    scopus 로고
    • Can a biologist fix a radio? Or, what i learned while studying apoptosis
    • Lazebnik Y. 2002. Can a biologist fix a radio? Or, what I learned while studying apoptosis. Cancer Cell 2:179-82
    • (2002) Cancer Cell , vol.2 , pp. 179-182
    • Lazebnik, Y.1
  • 51
    • 34547177356 scopus 로고    scopus 로고
    • Stochastic fluctuations in metabolic pathways
    • Levine E, Hwa T. 2007. Stochastic fluctuations in metabolic pathways. Proc. Natl. Acad. Sci. USA 104:9224-29
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 9224-9229
    • Levine, E.1    Hwa, T.2
  • 52
    • 0009100742 scopus 로고
    • The symmetry of time in physics
    • Lewis GN. 1930. The symmetry of time in physics. Science 71:569-77
    • (1930) Science , vol.71 , pp. 569-577
    • Lewis, G.N.1
  • 53
    • 79960630264 scopus 로고    scopus 로고
    • Central dogma at the single-molecule level in living cells
    • Li G-W, Xie XS. 2011. Central dogma at the single-molecule level in living cells. Nature 475:308-15
    • (2011) Nature , vol.475 , pp. 308-315
    • Li, G.-W.1    Xie, X.S.2
  • 54
    • 75749152362 scopus 로고    scopus 로고
    • Computational cellular dynamics based on the chemical master equation: A challenge for understanding complexity (survey)
    • Liang J, Qian H. 2010. Computational cellular dynamics based on the chemical master equation: a challenge for understanding complexity (survey). J. Comput. Sci. Technol. 25:154-68
    • (2010) J. Comput. Sci. Technol. , vol.25 , pp. 154-168
    • Liang, J.1    Qian, H.2
  • 55
    • 0038637779 scopus 로고    scopus 로고
    • Perfect and near-perfect adaptation in a model of bacterial chemotaxis
    • Mello BA, Tu Y. 2003. Perfect and near-perfect adaptation in a model of bacterial chemotaxis. Biophys. J. 84:2943-56
    • (2003) Biophys. J. , vol.84 , pp. 2943-2956
    • Mello, B.A.1    Tu, Y.2
  • 56
    • 19344362210 scopus 로고    scopus 로고
    • The stability of a stochastic CaMKII switch: Dependence on the number of enzyme molecules and protein turnover
    • Miller P, Zhabotinsky AM, Lisman JE, Wang X-J. 2005. The stability of a stochastic CaMKII switch: dependence on the number of enzyme molecules and protein turnover. PLoS Biol. 3:e107
    • (2005) PLoS Biol. , vol.3
    • Miller, P.1    Zhabotinsky, A.M.2    Lisman, J.E.3    Wang, X.-J.4
  • 58
    • 77951770226 scopus 로고    scopus 로고
    • Complex kinetics of fluctuating enzymes: Phase diagram characterization of a minimal kinetic scheme
    • Min W, Jiang L, Xie XS. 2010. Complex kinetics of fluctuating enzymes: phase diagram characterization of a minimal kinetic scheme. Chem. Asian J. 5:1129-38
    • (2010) Chem. Asian J. , vol.5 , pp. 1129-1138
    • Min, W.1    Jiang, L.2    Xie, X.S.3
  • 59
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J, Changeux J-P. 1965. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12:88-118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 61
    • 0016793283 scopus 로고
    • Kinetic amplification of enzyme discrimination
    • Ninio J. 1975. Kinetic amplification of enzyme discrimination. Biochimie 57:587-95
    • (1975) Biochimie , vol.57 , pp. 587-595
    • Ninio, J.1
  • 63
    • 20344389483 scopus 로고    scopus 로고
    • Models of stochastic gene expression
    • Paulsson J. 2005. Models of stochastic gene expression. Phys. Life Rev. 2:157-75
    • (2005) Phys. Life Rev. , vol.2 , pp. 157-175
    • Paulsson, J.1
  • 64
    • 0034691214 scopus 로고    scopus 로고
    • Stochastic focusing: Fluctuation-enhanced sensitivity of in-tracellular regulation
    • Paulsson J, Berg OG, Ehrenberg M. 2000. Stochastic focusing: fluctuation-enhanced sensitivity of in-tracellular regulation. Proc. Natl. Acad. Sci. USA 97:7148-53
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7148-7153
    • Paulsson, J.1    Berg, O.G.2    Ehrenberg, M.3
  • 65
    • 0034608143 scopus 로고    scopus 로고
    • Random signal fluctuation can reduce random fluctuations in regulated components of chemical regulatory networks
    • Paulsson J, Ehrenberg M. 2000. Random signal fluctuation can reduce random fluctuations in regulated components of chemical regulatory networks. Phys. Rev. Lett. 84:5447-50
    • (2000) Phys. Rev. Lett. , vol.84 , pp. 5447-5450
    • Paulsson, J.1    Ehrenberg, M.2
  • 66
    • 0037187085 scopus 로고    scopus 로고
    • Equations for stochastic macromolecular mechanics of single proteins: Equilibrium fluctuations, transient kinetics and nonequilibrium steady-state
    • Qian H. 2002. Equations for stochastic macromolecular mechanics of single proteins: equilibrium fluctuations, transient kinetics and nonequilibrium steady-state. J. Phys. Chem. B 106:2065-73
    • (2002) J. Phys. Chem. B , vol.106 , pp. 2065-2073
    • Qian, H.1
  • 67
    • 0141560467 scopus 로고    scopus 로고
    • Thermodynamic and kinetic analysis of sensitivity amplification in biological signal transduction
    • Qian H. 2003. Thermodynamic and kinetic analysis of sensitivity amplification in biological signal transduction. Biophys. Chem. 105:585-93
    • (2003) Biophys. Chem. , vol.105 , pp. 585-593
    • Qian, H.1
  • 68
    • 33748094844 scopus 로고    scopus 로고
    • Reducing intrinsic biochemical noise in cells and its thermodynamic limit
    • Qian H. 2006. Reducing intrinsic biochemical noise in cells and its thermodynamic limit. J. Mol. Biol. 362:387-92
    • (2006) J. Mol. Biol. , vol.362 , pp. 387-392
    • Qian, H.1
  • 69
    • 33748107406 scopus 로고    scopus 로고
    • Phosphorylation energy hypothesis: Open chemical systems and their biological functions
    • Qian H. 2007. Phosphorylation energy hypothesis: open chemical systems and their biological functions. Annu. Rev. Phys. Chem. 58:113-42
    • (2007) Annu. Rev. Phys. Chem. , vol.58 , pp. 113-142
    • Qian, H.1
  • 70
    • 46749083416 scopus 로고    scopus 로고
    • Cooperativity and specificity in enzyme kinetics: A single-molecule time-based perspective
    • Qian H. 2008. Cooperativity and specificity in enzyme kinetics: a single-molecule time-based perspective. Biophys. J. 95:10-17
    • (2008) Biophys. J. , vol.95 , pp. 10-17
    • Qian, H.1
  • 71
    • 78649795390 scopus 로고    scopus 로고
    • Cellular biology in terms of stochastic nonlinear biochemical dynamics: Emergent properties, isogenetic variations and chemical system inheritability
    • Qian H. 2010. Cellular biology in terms of stochastic nonlinear biochemical dynamics: emergent properties, isogenetic variations and chemical system inheritability. J. Stat. Phys. 141:990-1013
    • (2010) J. Stat. Phys. , vol.141 , pp. 990-1013
    • Qian, H.1
  • 72
    • 78650154269 scopus 로고    scopus 로고
    • Cyclic conformational modification of an enzyme: Serial engagement, energy relay, hysteretic enzyme, and Fischer's hypothesis
    • Qian H. 2010. Cyclic conformational modification of an enzyme: serial engagement, energy relay, hysteretic enzyme, and Fischer's hypothesis. J. Phys. Chem. B 114:16105-11
    • (2010) J. Phys. Chem. B , vol.114 , pp. 16105-16111
    • Qian, H.1
  • 73
    • 79957877141 scopus 로고    scopus 로고
    • Nonlinear stochastic dynamics of mesoscopic homogeneous biochemical reactions systems-an analytical theory
    • Qian H. 2011. Nonlinear stochastic dynamics of mesoscopic homogeneous biochemical reactions systems-an analytical theory. Nonlinearity 24:R19-49
    • (2011) Nonlinearity , vol.24
    • Qian, H.1
  • 74
    • 17244378347 scopus 로고    scopus 로고
    • Thermodynamics of stoichiometric biochemical networks in living systems far from equilibrium
    • Qian H, Beard DA. 2005. Thermodynamics of stoichiometric biochemical networks in living systems far from equilibrium. Biophys. Chem. 114:213-20
    • (2005) Biophys. Chem. , vol.114 , pp. 213-220
    • Qian, H.1    Beard, D.A.2
  • 75
    • 77958514250 scopus 로고    scopus 로고
    • The chemical master equation approach to nonequilibrium steady-state of open biochemical systems: Linear single-molecule enzyme kinetics and nonlinear biochemical reaction networks
    • Qian H, Bishop LM. 2010. The chemical master equation approach to nonequilibrium steady-state of open biochemical systems: linear single-molecule enzyme kinetics and nonlinear biochemical reaction networks. Int. J. Mol. Sci. 11:3472-500
    • (2010) Int. J. Mol. Sci. , vol.11 , pp. 3472-3500
    • Qian, H.1    Bishop, L.M.2
  • 76
    • 39749178412 scopus 로고    scopus 로고
    • Temporal cooperativity and sensitivity amplification in biological signal transduction
    • Qian H, Cooper JA. 2008. Temporal cooperativity and sensitivity amplification in biological signal transduction. Biochemistry 47:2211-20
    • (2008) Biochemistry , vol.47 , pp. 2211-2220
    • Qian, H.1    Cooper, J.A.2
  • 77
    • 1542327697 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy with high-order and dual-color correlation to probe nonequilibrium steady states
    • Qian H, Elson EL. 2004. Fluorescence correlation spectroscopy with high-order and dual-color correlation to probe nonequilibrium steady states. Proc. Natl. Acad. Sci. USA 101:2828-33
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2828-2833
    • Qian, H.1    Elson, E.L.2
  • 78
    • 18144407314 scopus 로고    scopus 로고
    • Nonequilibrium thermodynamics and nonlinear kineticsin a cellular signaling switch
    • Qian H, Reluga TC. 2005. Nonequilibrium thermodynamics and nonlinear kineticsin a cellular signaling switch. Phys. Rev. Lett. 94:028101
    • (2005) Phys. Rev. Lett. , vol.94 , pp. 028101
    • Qian, H.1    Reluga, T.C.2
  • 79
    • 0036679175 scopus 로고    scopus 로고
    • Concentration fluctuations in a mesoscopic oscillating chemical reaction system
    • Qian H, Saffarian S, Elson EL. 2002. Concentration fluctuations in a mesoscopic oscillating chemical reaction system. Proc. Natl. Acad. Sci. USA 99:10376-81
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10376-10381
    • Qian, H.1    Saffarian, S.2    Elson, E.L.3
  • 80
    • 65249133487 scopus 로고    scopus 로고
    • Fluctuating enzyme and its biological functions: Positive cooperativity without multiple states
    • Qian H, Shi P-Z. 2009. Fluctuating enzyme and its biological functions: positive cooperativity without multiple states. J. Phys. Chem. B 113:2225-30
    • (2009) J. Phys. Chem. B , vol.113 , pp. 2225-2230
    • Qian, H.1    Shi, P.-Z.2
  • 81
    • 68849093960 scopus 로고    scopus 로고
    • Stochastic bifurcation, slow fluctuations, and bistability as an origin of biochemical complexity
    • Qian H, Shi P-Z, Xing J. 2009. Stochastic bifurcation, slow fluctuations, and bistability as an origin of biochemical complexity. Phys. Chem. Chem. Phys. 11:4861-70
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 4861-4870
    • Qian, H.1    Shi, P.-Z.2    Xing, J.3
  • 82
    • 0023655481 scopus 로고
    • Cooperative and allosteric enzymes: 20 years on
    • Ricard J, Cornish-Bowden A. 1987. Cooperative and allosteric enzymes: 20 years on. Eur. J. Biochem. 166:255-72
    • (1987) Eur. J. Biochem. , vol.166 , pp. 255-272
    • Ricard, J.1    Cornish-Bowden, A.2
  • 83
    • 0035778150 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: Theory and applications
    • New York: Springer
    • Rigler R, Elson EL, eds. 2001. Fluorescence Correlation Spectroscopy: Theory and Applications. Springer Ser. Chem. Phys., Vol. 65. New York: Springer
    • (2001) Springer Ser. Chem. Phys. , vol.65
    • Rigler, R.1    Elson, E.L.2
  • 84
    • 14044265753 scopus 로고    scopus 로고
    • Stochastic amplification and signaling in enzymatic futile cycles through noise-induced bistability with oscillations
    • Samoilov M, Plyasunov S, Arkin AP. 2005. Stochastic amplification and signaling in enzymatic futile cycles through noise-induced bistability with oscillations. Proc. Natl. Acad. Sci. USA 102:2310-15
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2310-2315
    • Samoilov, M.1    Plyasunov, S.2    Arkin, A.P.3
  • 85
    • 33947476272 scopus 로고
    • The factors affecting the stability of hydrogen-bonded polypeptide structures in solution
    • Schellman JA. 1958. The factors affecting the stability of hydrogen-bonded polypeptide structures in solution. J. Phys. Chem. 62:1485-94
    • (1958) J. Phys. Chem. , vol.62 , pp. 1485-1494
    • Schellman, J.A.1
  • 86
  • 87
    • 49549120841 scopus 로고    scopus 로고
    • The stochastic nature of biochemical networks
    • Shahrezaei V, Swain PS. 2008. The stochastic nature of biochemical networks. Curr. Opin. Biotechnol. 19:369-74
    • (2008) Curr. Opin. Biotechnol. , vol.19 , pp. 369-374
    • Shahrezaei, V.1    Swain, P.S.2
  • 88
    • 0022429106 scopus 로고
    • The or control system of bacteriophage lambda. A physical-chemical model for gene regulation
    • Shea MA, Ackers GK. 1985. The OR control system of bacteriophage lambda. A physical-chemical model for gene regulation. J. Mol. Biol. 181:211-30
    • (1985) J. Mol. Biol. , vol.181 , pp. 211-230
    • Shea, M.A.1    Ackers, G.K.2
  • 89
    • 79951795015 scopus 로고    scopus 로고
    • A perturbation analysis of rate theory of self-regulating genes and signaling networks
    • Shi P-Z, Qian H. 2011. A perturbation analysis of rate theory of self-regulating genes and signaling networks. J. Chem. Phys. 134:065104
    • (2011) J. Chem. Phys. , vol.134 , pp. 065104
    • Shi, P.-Z.1    Qian, H.2
  • 91
    • 31144467483 scopus 로고    scopus 로고
    • The quantal theory of immunity
    • Smith KA. 2006. The quantal theory of immunity. Cell Res. 16:11-19
    • (2006) Cell Res. , vol.16 , pp. 11-19
    • Smith, K.A.1
  • 94
    • 57349131603 scopus 로고    scopus 로고
    • A genetic timer through noise-induced stabilization of an unstable state
    • Turcotte M, Garcia-Ojalvo J, Süel GM. 2008. A genetic timer through noise-induced stabilization of an unstable state. Proc. Natl. Acad. Sci. USA 105:15732-37
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15732-15737
    • Turcotte, M.1    Garcia-Ojalvo, J.2    Süel, G.M.3
  • 95
    • 34250698472 scopus 로고    scopus 로고
    • A quasistationary analysis of a stochastic chemical reaction: Keizer's paradox
    • Vellela M, Qian H. 2007. A quasistationary analysis of a stochastic chemical reaction: Keizer's paradox. Bull. Math. Biol. 69:1727-46
    • (2007) Bull. Math. Biol. , vol.69 , pp. 1727-1746
    • Vellela, M.1    Qian, H.2
  • 96
    • 77749308573 scopus 로고    scopus 로고
    • On Poincaré-Hill cycle map of rotational random walk: Locating stochastic limit cycle in reversible Schnakenberg model
    • Vellela M, Qian H. 2010. On Poincaré-Hill cycle map of rotational random walk: locating stochastic limit cycle in reversible Schnakenberg model. Proc. R. Sci. A. 466:771-88
    • (2010) Proc. R. Sci. A. , vol.466 , pp. 771-788
    • Vellela, M.1    Qian, H.2
  • 98
    • 34347235771 scopus 로고    scopus 로고
    • From "simple" DNA-protein interactions to the macromolecular machines of gene expression
    • von Hippel PH. 2007. From "simple" DNA-protein interactions to the macromolecular machines of gene expression. Annu. Rev. Biophys. Biomol. Struct. 36:79-105
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 79-105
    • Von Hippel, P.H.1
  • 100
    • 77952334362 scopus 로고    scopus 로고
    • Potential and flux landscapes quantify the stability and robustness of budding yeast cell cycle network
    • Wang J, Li C, Wang E. 2010. Potential and flux landscapes quantify the stability and robustness of budding yeast cell cycle network. Proc. Natl. Acad. Sci. USA 107:8195-200
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 8195-8200
    • Wang, J.1    Li, C.2    Wang, E.3
  • 101
    • 50449104011 scopus 로고    scopus 로고
    • Potential landscape and flux framework of nonequilibrium networks: Robustness, dissipation, and coherence of biochemical oscillations
    • Wang J, Xu L, Wang E. 2008. Potential landscape and flux framework of nonequilibrium networks: robustness, dissipation, and coherence of biochemical oscillations. Proc. Natl. Acad. Sci. USA 105:12271-76
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 12271-12276
    • Wang, J.1    Xu, L.2    Wang, E.3
  • 102
    • 77957307520 scopus 로고    scopus 로고
    • Non-essential sites improve phosphorylation switch
    • Wang L, Nie Q, Enciso G. 2010. Non-essential sites improve phosphorylation switch. Biophys. J. 99:L41-43
    • (2010) Biophys. J. , vol.99
    • Wang, L.1    Nie, Q.2    Enciso, G.3
  • 103
    • 5044227742 scopus 로고    scopus 로고
    • The evolution of molecular biology into systems biology
    • Westerhoff HV, Palsson BO. 2004. The evolution of molecular biology into systems biology. Nat. Biotechnol. 22:1249-52
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1249-1252
    • Westerhoff, H.V.1    Palsson, B.O.2
  • 104
    • 48249095613 scopus 로고    scopus 로고
    • Single-molecule approach to molecular biology in living bacterial cells
    • Xie XS, Choi PJ, Li G-W, Lee NK, Lia G. 2008. Single-molecule approach to molecular biology in living bacterial cells. Annu. Rev. Biophys. 37:417-44
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 417-444
    • Xie, X.S.1    Choi, P.J.2    Li, G.-W.3    Lee, N.K.4    Lia, G.5
  • 105
    • 0033523011 scopus 로고    scopus 로고
    • Single-molecule enzymology
    • Xie XS, Lu HP. 1999. Single-molecule enzymology. J. Biol. Chem. 274:15967-70
    • (1999) J. Biol. Chem. , vol.274 , pp. 15967-15970
    • Xie, X.S.1    Lu, H.P.2
  • 106
    • 0345359924 scopus 로고    scopus 로고
    • A positive-feedback-based bistable 'memory module' that governs a cell fate decision
    • Xiong W, Ferrell JE. 2003. A positive-feedback-based bistable 'memory module' that governs a cell fate decision. Nature 426:460-65
    • (2003) Nature , vol.426 , pp. 460-465
    • Xiong, W.1    Ferrell, J.E.2
  • 107
    • 33645033645 scopus 로고    scopus 로고
    • Probing gene expression in live E. coli cells: One molecule at a time
    • Yu J, Xiao J, Ren X, Lao K, Xie XS. 2006. Probing gene expression in live E. coli cells: one molecule at a time. Science 311:1600-3
    • (2006) Science , vol.311 , pp. 1600-1603
    • Yu, J.1    Xiao, J.2    Ren, X.3    Lao, K.4    Xie, X.S.5
  • 108
    • 82455192486 scopus 로고    scopus 로고
    • Stochastic theory of nonequilibrium steady states and its applications. Part i
    • Zhang X-J, Qian H, Qian M. 2012. Stochastic theory of nonequilibrium steady states and its applications. Part I. Phys. Rep. 510:1-86
    • (2012) Phys. Rep. , vol.510 , pp. 1-86
    • Zhang, X.-J.1    Qian, H.2    Qian, M.3
  • 109
    • 79960629007 scopus 로고    scopus 로고
    • Role of fluctuations in ligand binding cooperativity of membrane receptors
    • Zhu L, Frenkel D, Bolhuis PG. 2011. Role of fluctuations in ligand binding cooperativity of membrane receptors. Phys. Rev. Lett. 106:168103
    • (2011) Phys. Rev. Lett. , vol.106 , pp. 168103
    • Zhu, L.1    Frenkel, D.2    Bolhuis, P.G.3
  • 110
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • Zimm BH, Bragg JK. 1959. Theory of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31:526-31
    • (1959) J. Chem. Phys. , vol.31 , pp. 526-531
    • Zimm, B.H.1    Bragg, J.K.2


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