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Volumn 145, Issue 2-3, 2009, Pages 111-115

A new kinetic model for biochemical oscillations: Graph-theoretical analysis

Author keywords

Cooperativity; Graph theoretic method; Substrate activation; Sustained oscillation

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE;

EID: 70350199599     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2009.09.008     Document Type: Article
Times cited : (6)

References (37)
  • 3
    • 36749119936 scopus 로고
    • Oscillations in chemical systems. Limit cycle behaviour in a model of a real chemical reaction
    • Field R.J., and Noyes R.M. Oscillations in chemical systems. Limit cycle behaviour in a model of a real chemical reaction. J. Chem. Phys. 60 (1974) 1877-1884
    • (1974) J. Chem. Phys. , vol.60 , pp. 1877-1884
    • Field, R.J.1    Noyes, R.M.2
  • 4
    • 0025111626 scopus 로고
    • Allosteric regulation, cooperativity, and biochemical oscillations
    • Goldbeter A., and Dupont G. Allosteric regulation, cooperativity, and biochemical oscillations. Biophys. Chem. 37 (1990) 341-353
    • (1990) Biophys. Chem. , vol.37 , pp. 341-353
    • Goldbeter, A.1    Dupont, G.2
  • 6
    • 0002013127 scopus 로고
    • Stability of complex reaction networks
    • Clarke B. Stability of complex reaction networks. Adv. Chem. Phys. 43 (1980) 1-115
    • (1980) Adv. Chem. Phys. , vol.43 , pp. 1-115
    • Clarke, B.1
  • 7
    • 0000514550 scopus 로고
    • Conditions for the unique steady state in kinetic systems as connected with the structure of reaction schemes
    • Ivanova A.N. Conditions for the unique steady state in kinetic systems as connected with the structure of reaction schemes. Kinet. Katal. (Moscow) 20 (1979) 1019-1028
    • (1979) Kinet. Katal. (Moscow) , vol.20 , pp. 1019-1028
    • Ivanova, A.N.1
  • 8
    • 0001548131 scopus 로고
    • One approach to the determination of a number of qualitative features in the behavior of kinetic systems, and realization of this approach in a computer (critical conditions, autooscillations)
    • Ivanova A.N., and Tarnopolskii B.L. One approach to the determination of a number of qualitative features in the behavior of kinetic systems, and realization of this approach in a computer (critical conditions, autooscillations). Kinet. Katal. (Moscow) 20 (1979) 1541-1548
    • (1979) Kinet. Katal. (Moscow) , vol.20 , pp. 1541-1548
    • Ivanova, A.N.1    Tarnopolskii, B.L.2
  • 9
    • 0001105645 scopus 로고
    • Mechanistic classification of chemical oscillations and the role of species
    • Eiswirth M., Freund A., and Ross J. Mechanistic classification of chemical oscillations and the role of species. Adv. Chem. Phys. LXXX (1991) 127-199
    • (1991) Adv. Chem. Phys. , vol.LXXX , pp. 127-199
    • Eiswirth, M.1    Freund, A.2    Ross, J.3
  • 10
    • 34547292632 scopus 로고    scopus 로고
    • Graph-theoretic methods for the analysis of chemical and biochemical networks. I. Multistability and oscillations in ordinary differential equation models
    • Mincheva M., and Roussel M.R. Graph-theoretic methods for the analysis of chemical and biochemical networks. I. Multistability and oscillations in ordinary differential equation models. J. Math. Biol. 55 (2007) 61-86
    • (2007) J. Math. Biol. , vol.55 , pp. 61-86
    • Mincheva, M.1    Roussel, M.R.2
  • 11
    • 33751556022 scopus 로고    scopus 로고
    • A graph-theoretic method for detecting potential Turing bifurcations
    • Mincheva M., and Roussel M.R. A graph-theoretic method for detecting potential Turing bifurcations. J. Chem. Phys. 125 (2006) 204102
    • (2006) J. Chem. Phys. , vol.125 , pp. 204102
    • Mincheva, M.1    Roussel, M.R.2
  • 13
    • 0023190458 scopus 로고
    • Hormonal regulation of 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase: kinetic model
    • Goldstein B.N., and Ivanova A.N. Hormonal regulation of 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase: kinetic model. FEBS Lett. 217 (1987) 212-215
    • (1987) FEBS Lett. , vol.217 , pp. 212-215
    • Goldstein, B.N.1    Ivanova, A.N.2
  • 14
    • 0024081181 scopus 로고
    • Simple kinetic models for critical phenomena in enzyme reactions with enzyme and substrate isomerization
    • Goldstein B.N., and Ivanova A.N. Simple kinetic models for critical phenomena in enzyme reactions with enzyme and substrate isomerization. Molek. Biol. (Moscow) 22 (1988) 1381-1392
    • (1988) Molek. Biol. (Moscow) , vol.22 , pp. 1381-1392
    • Goldstein, B.N.1    Ivanova, A.N.2
  • 15
    • 0025690358 scopus 로고
    • Graph-theoretic approach to metabolic pathways
    • Goldstein B.N., and Selivanov V.A. Graph-theoretic approach to metabolic pathways. Biomed. Biochim. Acta 49 (1990) 645-650
    • (1990) Biomed. Biochim. Acta , vol.49 , pp. 645-650
    • Goldstein, B.N.1    Selivanov, V.A.2
  • 16
    • 0018401599 scopus 로고
    • Slow transition and hysteretic behavior in enzymes
    • Frieden C. Slow transition and hysteretic behavior in enzymes. Annu. Rev. Biochem. 48 (1979) 471-489
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 471-489
    • Frieden, C.1
  • 18
    • 0016299203 scopus 로고
    • Regulatory behaviour of monomeric enzymes. 1. The mnemonical enzyme concept
    • Ricard J., Mennier J.-C., and Buc J. Regulatory behaviour of monomeric enzymes. 1. The mnemonical enzyme concept. Eur. J. Biochem. 49 (1974) 195-208
    • (1974) Eur. J. Biochem. , vol.49 , pp. 195-208
    • Ricard, J.1    Mennier, J.-C.2    Buc, J.3
  • 19
    • 0032556477 scopus 로고    scopus 로고
    • Slowly reverting enzyme inactivation: a mechanism for generating long-lived damped oscillations
    • Roussel M.R. Slowly reverting enzyme inactivation: a mechanism for generating long-lived damped oscillations. J. Theor. Biol. 195 (1998) 233-244
    • (1998) J. Theor. Biol. , vol.195 , pp. 233-244
    • Roussel, M.R.1
  • 20
    • 33846319397 scopus 로고    scopus 로고
    • Switching mechanism for branched biochemical fluxes: graph-theoretic analysis
    • Goldstein B. Switching mechanism for branched biochemical fluxes: graph-theoretic analysis. Biophys. Chem. 125 (2007) 314-319
    • (2007) Biophys. Chem. , vol.125 , pp. 314-319
    • Goldstein, B.1
  • 22
    • 59049086698 scopus 로고    scopus 로고
    • Dynein swings into action
    • Houdusse A., and Carter A.P. Dynein swings into action. Cell 136 (2009) 395-396
    • (2009) Cell , vol.136 , pp. 395-396
    • Houdusse, A.1    Carter, A.P.2
  • 23
    • 62549152622 scopus 로고    scopus 로고
    • Transient enzyme kinetics: graph-theoretic approach
    • Goldstein B.N. Transient enzyme kinetics: graph-theoretic approach. Biophys. Chem. 141 (2009) 193-197
    • (2009) Biophys. Chem. , vol.141 , pp. 193-197
    • Goldstein, B.N.1
  • 24
    • 27744522623 scopus 로고    scopus 로고
    • Cyclical interactions between two outer doublet microtubules in split flagellar axonemes
    • Aoyama S., and Kamiya R. Cyclical interactions between two outer doublet microtubules in split flagellar axonemes. Biophys. J. 89 (2005) 3261-3268
    • (2005) Biophys. J. , vol.89 , pp. 3261-3268
    • Aoyama, S.1    Kamiya, R.2
  • 25
    • 1242274449 scopus 로고    scopus 로고
    • Detection of multistability, bifurcation, and hysteresis in a large class of biological positive-feedback systems
    • Angeli D., Ferrell Jr. J.E., and Sontag E.D. Detection of multistability, bifurcation, and hysteresis in a large class of biological positive-feedback systems. Proc. Natl. Acad. Sci. 101 (2004) 1822-1827
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 1822-1827
    • Angeli, D.1    Ferrell Jr., J.E.2    Sontag, E.D.3
  • 26
    • 0032825010 scopus 로고    scopus 로고
    • Mathematical simulation and analysis of cellular metabolism and regulation
    • Goryanin I.I., Hogman T.C., and Sel'kov E.E. Mathematical simulation and analysis of cellular metabolism and regulation. Bioinformatics 15 (1999) 749-758
    • (1999) Bioinformatics , vol.15 , pp. 749-758
    • Goryanin, I.I.1    Hogman, T.C.2    Sel'kov, E.E.3
  • 27
    • 22244464863 scopus 로고
    • Kinetic resonance in the open biochemical reaction catalyzed by an enzyme in forms with different activity
    • Nazarenko V.G., and Sel'kov E.E. Kinetic resonance in the open biochemical reaction catalyzed by an enzyme in forms with different activity. Biophysics 29 (1984) 626-630
    • (1984) Biophysics , vol.29 , pp. 626-630
    • Nazarenko, V.G.1    Sel'kov, E.E.2
  • 28
    • 0031142849 scopus 로고    scopus 로고
    • The peroxidase-oxidase oscillator and its constituent chemistries
    • Scheeline A., Olson D.L., Williksen E.P., and Horras G.A. The peroxidase-oxidase oscillator and its constituent chemistries. Chem. Rev. 97 (1997) 739-756
    • (1997) Chem. Rev. , vol.97 , pp. 739-756
    • Scheeline, A.1    Olson, D.L.2    Williksen, E.P.3    Horras, G.A.4
  • 29
    • 0001841140 scopus 로고    scopus 로고
    • Oscillations in peroxidase-catalyzed reactions and their potential function in vivo
    • Moller A.Ch., Hauser M.J.B., and Olsen L.F. Oscillations in peroxidase-catalyzed reactions and their potential function in vivo. Biophys. Chem. 72 (1998) 63-72
    • (1998) Biophys. Chem. , vol.72 , pp. 63-72
    • Moller, A.Ch.1    Hauser, M.J.B.2    Olsen, L.F.3
  • 30
    • 20444459104 scopus 로고    scopus 로고
    • On the mechanisms of glycolytic oscillations in yeast
    • Madsen M.F., Dano S., and Sorensen P.G. On the mechanisms of glycolytic oscillations in yeast. FEBS J. 272 (2005) 2648-2660
    • (2005) FEBS J. , vol.272 , pp. 2648-2660
    • Madsen, M.F.1    Dano, S.2    Sorensen, P.G.3
  • 31
    • 18144424439 scopus 로고    scopus 로고
    • Chemical interpretation of oscillatory modes at a Hopf point
    • Dano S., Madsen M.F., and Sorensen P.G. Chemical interpretation of oscillatory modes at a Hopf point. Phys. Chem. Chem. Phys. 7 (2005) 1674-1679
    • (2005) Phys. Chem. Chem. Phys. , vol.7 , pp. 1674-1679
    • Dano, S.1    Madsen, M.F.2    Sorensen, P.G.3
  • 32
  • 34
    • 68049128316 scopus 로고    scopus 로고
    • Normal-mode-based modeling of allosteric couplings that underlie cyclic conformational transition in F(1)ATPase
    • Zheng W. Normal-mode-based modeling of allosteric couplings that underlie cyclic conformational transition in F(1)ATPase. Proteins 76 (2009) 747-762
    • (2009) Proteins , vol.76 , pp. 747-762
    • Zheng, W.1
  • 35
    • 3543101941 scopus 로고    scopus 로고
    • Enzyme isomerization and concentration oscillations in the five-component biochemical systems
    • Bayramov Sh.K. Enzyme isomerization and concentration oscillations in the five-component biochemical systems. Biochemistry (Moscow) 69 (2004) 317-322
    • (2004) Biochemistry (Moscow) , vol.69 , pp. 317-322
    • Bayramov, Sh.K.1
  • 36
    • 0026009444 scopus 로고
    • Cooperativity in axonemal motion: analysis of a four-state two-site kinetic model
    • Omoto Ch.K., Palmer J.S., and Moody M.E. Cooperativity in axonemal motion: analysis of a four-state two-site kinetic model. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 5562-5566
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 5562-5566
    • Omoto, Ch.K.1    Palmer, J.S.2    Moody, M.E.3
  • 37
    • 33646171262 scopus 로고    scopus 로고
    • A simple theoretical model explains dynein's response to load
    • Gao Y.Q. A simple theoretical model explains dynein's response to load. Biophys. J. 90 (2006) 811-821
    • (2006) Biophys. J. , vol.90 , pp. 811-821
    • Gao, Y.Q.1


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