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Volumn 90, Issue 3, 2007, Pages 591-601

Steady state and (bi-) stability evaluation of simple protease signalling networks

Author keywords

Apoptosis; Bistability; Caspases; Proteases; Signalling; Switch; Threshold

Indexed keywords

PROTEINASE; PROTEINASE INHIBITOR;

EID: 34547836607     PISSN: 03032647     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biosystems.2007.01.003     Document Type: Article
Times cited : (32)

References (54)
  • 1
    • 33645085024 scopus 로고    scopus 로고
    • New analysis technique for multistability detection
    • Angeli D. New analysis technique for multistability detection. Syst. Biol. 153 2 (2006) 61-69
    • (2006) Syst. Biol. , vol.153 , Issue.2 , pp. 61-69
    • Angeli, D.1
  • 2
    • 1242274449 scopus 로고    scopus 로고
    • Detection of multistability, bifurcations, and hysteresis in a large class of biological positive-feedback systems
    • Angeli D., Ferrell J.E., and Sontag Jr. E.D. Detection of multistability, bifurcations, and hysteresis in a large class of biological positive-feedback systems. Proc. Natl. Acad. Sci. U.S.A. 101 7 (2004) 1822-1827
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.7 , pp. 1822-1827
    • Angeli, D.1    Ferrell, J.E.2    Sontag Jr., E.D.3
  • 3
    • 33646124974 scopus 로고    scopus 로고
    • Bistability in apoptosis: roles of Bax, Bcl-2 and mitochondrial permeability transition pores
    • Bagci E.Z., Vodovotz Y., Billiar T.R., Ermentrout G.B., and Bahar I. Bistability in apoptosis: roles of Bax, Bcl-2 and mitochondrial permeability transition pores. Biophys. J. 90 (2006) 1546-1559
    • (2006) Biophys. J. , vol.90 , pp. 1546-1559
    • Bagci, E.Z.1    Vodovotz, Y.2    Billiar, T.R.3    Ermentrout, G.B.4    Bahar, I.5
  • 4
    • 0029021898 scopus 로고
    • Mathematical analysis of activation thresholds in enzyme-catalyzed positive feedbacks: application to the feedbacks of blood coagulation
    • Beltrami E., and Jesty J. Mathematical analysis of activation thresholds in enzyme-catalyzed positive feedbacks: application to the feedbacks of blood coagulation. Proc. Natl. Acad. Sci. U.S.A. 92 19 (1995) 8744-8748
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , Issue.19 , pp. 8744-8748
    • Beltrami, E.1    Jesty, J.2
  • 5
    • 0037047611 scopus 로고    scopus 로고
    • MAP kinase phosphatase as a locus of flexibility in a mitogen-activated protein kinase signaling network
    • Bhalla U.S., Ram P.T., and Iyengar R. MAP kinase phosphatase as a locus of flexibility in a mitogen-activated protein kinase signaling network. Science 297 5583 (2002) 1018-1023
    • (2002) Science , vol.297 , Issue.5583 , pp. 1018-1023
    • Bhalla, U.S.1    Ram, P.T.2    Iyengar, R.3
  • 7
    • 0034696445 scopus 로고    scopus 로고
    • How to make a biological switch
    • Cherry J.L., and Adler F.R. How to make a biological switch. J. Theor. Biol. 203 2 (2000) 117-133
    • (2000) J. Theor. Biol. , vol.203 , Issue.2 , pp. 117-133
    • Cherry, J.L.1    Adler, F.R.2
  • 8
    • 0242585716 scopus 로고    scopus 로고
    • Blood coagulation
    • Dahlbäck B. Blood coagulation. Lancet 355 9215 (2000) 1627-1632
    • (2000) Lancet , vol.355 , Issue.9215 , pp. 1627-1632
    • Dahlbäck, B.1
  • 9
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: critical control points
    • Danial N.N., and Korsmeyer S.J. Cell death: critical control points. Cell 116 2 (2004) 205-219
    • (2004) Cell , vol.116 , Issue.2 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 10
    • 0037727675 scopus 로고    scopus 로고
    • Aspartic peptidase inhibitors: implications in drug development
    • Dash C., Kulkarni A., Dunn B., and Rao M. Aspartic peptidase inhibitors: implications in drug development. Crit. Rev. Biochem. Mol. Biol. 38 2 (2003) 89-119
    • (2003) Crit. Rev. Biochem. Mol. Biol. , vol.38 , Issue.2 , pp. 89-119
    • Dash, C.1    Kulkarni, A.2    Dunn, B.3    Rao, M.4
  • 11
    • 31144431501 scopus 로고    scopus 로고
    • Robustness properties of apoptosis models with respect to parameter variations and stochastic influences
    • Eißing T., Allgöwer F., and Bullinger E. Robustness properties of apoptosis models with respect to parameter variations and stochastic influences. Syst. Biol. 152 4 (2005) 221-228
    • (2005) Syst. Biol. , vol.152 , Issue.4 , pp. 221-228
    • Eißing, T.1    Allgöwer, F.2    Bullinger, E.3
  • 13
    • 0030445778 scopus 로고    scopus 로고
    • Tripping the switch fantastic: how a protein kinase cascade can convert graded inputs into switch-like outputs
    • Ferrell Jr. J.E. Tripping the switch fantastic: how a protein kinase cascade can convert graded inputs into switch-like outputs. Trends Biochem. Sci. 21 12 (1996) 460-466
    • (1996) Trends Biochem. Sci. , vol.21 , Issue.12 , pp. 460-466
    • Ferrell Jr., J.E.1
  • 14
    • 0031203921 scopus 로고    scopus 로고
    • How responses get more switch-like as you move down a protein kinase cascade
    • Ferrell Jr. J.E. How responses get more switch-like as you move down a protein kinase cascade. Trends Biochem. Sci. 22 8 (1997) 288-289
    • (1997) Trends Biochem. Sci. , vol.22 , Issue.8 , pp. 288-289
    • Ferrell Jr., J.E.1
  • 15
    • 0032496358 scopus 로고    scopus 로고
    • The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes
    • Ferrell J.E., and Machleder Jr. E.M. The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Science 280 5365 (1998) 895-898
    • (1998) Science , vol.280 , Issue.5365 , pp. 895-898
    • Ferrell, J.E.1    Machleder Jr., E.M.2
  • 16
    • 0037605637 scopus 로고    scopus 로고
    • Bistability in cell signaling: how to make continuous processes discontinuous, and reversible processes irreversible
    • Ferrell J.E., and Xiong Jr. W. Bistability in cell signaling: how to make continuous processes discontinuous, and reversible processes irreversible. Chaos 11 1 (2001) 227-236
    • (2001) Chaos , vol.11 , Issue.1 , pp. 227-236
    • Ferrell, J.E.1    Xiong Jr., W.2
  • 17
    • 0001424903 scopus 로고
    • An amplified sensitivity arising from covalent modification in biological systems
    • Goldbeter A., and Koshland D.E. An amplified sensitivity arising from covalent modification in biological systems. Proc. Natl. Acad. Sci. U.S.A. 78 11 (1981) 6840-6844
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , Issue.11 , pp. 6840-6844
    • Goldbeter, A.1    Koshland, D.E.2
  • 18
    • 0021715523 scopus 로고
    • Ultrasensitivity in biochemical systems controlled by covalent modification. Interplay between zero-order and multistep effects
    • Goldbeter A., and Koshland D.E. Ultrasensitivity in biochemical systems controlled by covalent modification. Interplay between zero-order and multistep effects. J. Biol. Chem. 259 23 (1984) 14441-14447
    • (1984) J. Biol. Chem. , vol.259 , Issue.23 , pp. 14441-14447
    • Goldbeter, A.1    Koshland, D.E.2
  • 20
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner M.O. The biochemistry of apoptosis. Nature 407 6805 (2000) 770-776
    • (2000) Nature , vol.407 , Issue.6805 , pp. 770-776
    • Hengartner, M.O.1
  • 21
    • 35649001607 scopus 로고
    • A quantitative description of membrane current and its application to conduction and excitation in nerve
    • Hodgkin A.L., and Huxley A.F. A quantitative description of membrane current and its application to conduction and excitation in nerve. J. Physiol. 117 4 (1952) 500-544
    • (1952) J. Physiol. , vol.117 , Issue.4 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 22
    • 0029790351 scopus 로고    scopus 로고
    • Ultrasensitivity in the mitogen-activated protein kinase cascade
    • Huang C.Y., and Ferrell Jr. J.E. Ultrasensitivity in the mitogen-activated protein kinase cascade. Proc. Natl. Acad. Sci. U.S.A. 93 19 (1996) 10078-10083
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , Issue.19 , pp. 10078-10083
    • Huang, C.Y.1    Ferrell Jr., J.E.2
  • 23
    • 2642661483 scopus 로고    scopus 로고
    • The era of pathway quantification
    • Koshland D.E. The era of pathway quantification. Science 280 5365 (1998) 852-853
    • (1998) Science , vol.280 , Issue.5365 , pp. 852-853
    • Koshland, D.E.1
  • 24
    • 33749370199 scopus 로고    scopus 로고
    • Mathematical modeling identifies inhibitors of apoptosis as mediators of positive feedback and bistability
    • Legewie S., Blüthgen N., and Herzel H. Mathematical modeling identifies inhibitors of apoptosis as mediators of positive feedback and bistability. PLoS Comput. Biol. 2 9 (2006) e120
    • (2006) PLoS Comput. Biol. , vol.2 , Issue.9
    • Legewie, S.1    Blüthgen, N.2    Herzel, H.3
  • 25
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: from caspases to alternative mechanisms
    • Leist M., and Jaattela M. Four deaths and a funeral: from caspases to alternative mechanisms. Nat. Rev. Mol. Cell Biol. 2 8 (2001) 589-598
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , Issue.8 , pp. 589-598
    • Leist, M.1    Jaattela, M.2
  • 26
    • 0010424768 scopus 로고
    • A mechanism for memory storage insensitive to molecular turnover: a bistable autophosphorylating kinase
    • Lisman J.E. A mechanism for memory storage insensitive to molecular turnover: a bistable autophosphorylating kinase. Proc. Natl. Acad. Sci. U.S.A. 82 9 (1985) 3055-3057
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , Issue.9 , pp. 3055-3057
    • Lisman, J.E.1
  • 27
    • 0642281331 scopus 로고    scopus 로고
    • Quantifying robustness of biochemical network models
    • Ma L., and Iglesias P.A. Quantifying robustness of biochemical network models. BMC Bioinformat. 3 (2002) 38
    • (2002) BMC Bioinformat. , vol.3 , pp. 38
    • Ma, L.1    Iglesias, P.A.2
  • 28
    • 0142027814 scopus 로고    scopus 로고
    • Structure and function of the feed-forward loop network motif
    • Mangan S., and Alon U. Structure and function of the feed-forward loop network motif. Proc. Natl. Acad. Sci. U.S.A. 100 21 (2003) 11980-11985
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , Issue.21 , pp. 11980-11985
    • Mangan, S.1    Alon, U.2
  • 29
    • 0842288229 scopus 로고    scopus 로고
    • Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades
    • Markevich N.I., Hoek J.B., and Kholodenko B.N. Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades. J. Cell Biol. 164 3 (2004) 353-359
    • (2004) J. Cell Biol. , vol.164 , Issue.3 , pp. 353-359
    • Markevich, N.I.1    Hoek, J.B.2    Kholodenko, B.N.3
  • 30
    • 0037022274 scopus 로고    scopus 로고
    • Product dependence and bifunctionality compromise the ultrasensitivity of signal transduction cascades
    • Ortega F., Acerenza L., Westerhoff H.V., Mas F., and Cascante M. Product dependence and bifunctionality compromise the ultrasensitivity of signal transduction cascades. Proc. Natl. Acad. Sci. U.S.A. 99 3 (2002) 1170-1175
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , Issue.3 , pp. 1170-1175
    • Ortega, F.1    Acerenza, L.2    Westerhoff, H.V.3    Mas, F.4    Cascante, M.5
  • 31
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: innovations for the post-trial era
    • Overall C.M., and López-Otín C. Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat. Rev. Cancer 2 9 (2002) 657-672
    • (2002) Nat. Rev. Cancer , vol.2 , Issue.9 , pp. 657-672
    • Overall, C.M.1    López-Otín, C.2
  • 32
    • 0037025005 scopus 로고    scopus 로고
    • Remarks on excitability, stability and sign of equilibria in cooperative systems
    • Piccardi C., and Rinaldi S. Remarks on excitability, stability and sign of equilibria in cooperative systems. Syst. Cont. Lett. 46 (2002) 153-163
    • (2002) Syst. Cont. Lett. , vol.46 , pp. 153-163
    • Piccardi, C.1    Rinaldi, S.2
  • 33
    • 0344982141 scopus 로고    scopus 로고
    • Dynamics of the cell cycle: checkpoints, sizers, and timers
    • Qu Z., MacLellan W.R., and Weiss J.N. Dynamics of the cell cycle: checkpoints, sizers, and timers. Biophys. J. 85 6 (2003) 3600-3611
    • (2003) Biophys. J. , vol.85 , Issue.6 , pp. 3600-3611
    • Qu, Z.1    MacLellan, W.R.2    Weiss, J.N.3
  • 34
    • 33748941571 scopus 로고    scopus 로고
    • Systems analysis of effector caspase activation and its control by X-linked inhibitor of apoptosis protein
    • Rehm M., Huber H.J., Dussmann H., and Prehn J.H.M. Systems analysis of effector caspase activation and its control by X-linked inhibitor of apoptosis protein. EMBO J. 25 18 (2006) 4338-4349
    • (2006) EMBO J. , vol.25 , Issue.18 , pp. 4338-4349
    • Rehm, M.1    Huber, H.J.2    Dussmann, H.3    Prehn, J.H.M.4
  • 35
    • 26444561930 scopus 로고    scopus 로고
    • Eukaryotic cells are dynamically ordered or critical but not chaotic
    • Shmulevich I., Kauffman S.A., and Aldana M. Eukaryotic cells are dynamically ordered or critical but not chaotic. Proc. Natl. Acad. Sci. U.S.A. 102 38 (2005) 13439-13444
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , Issue.38 , pp. 13439-13444
    • Shmulevich, I.1    Kauffman, S.A.2    Aldana, M.3
  • 38
    • 14044252160 scopus 로고    scopus 로고
    • Caspase-8 can be activated by interchain proteolysis without receptor-triggered dimerization during drug-induced apoptosis
    • Sohn D., Schulze-Osthoff K., and Jänicke R.U. Caspase-8 can be activated by interchain proteolysis without receptor-triggered dimerization during drug-induced apoptosis. J. Biol. Chem. 280 7 (2005) 5267-5273
    • (2005) J. Biol. Chem. , vol.280 , Issue.7 , pp. 5267-5273
    • Sohn, D.1    Schulze-Osthoff, K.2    Jänicke, R.U.3
  • 40
    • 0032762563 scopus 로고    scopus 로고
    • Catalytic properties of the caspases
    • Stennicke H.R., and Salvesen G.S. Catalytic properties of the caspases. Cell Death Differ. 6 11 (1999) 1054-1059
    • (1999) Cell Death Differ. , vol.6 , Issue.11 , pp. 1054-1059
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 42
    • 0028260263 scopus 로고
    • Theoretical dynamics of the cyclin B-MPF system: a possible role for p13suc1
    • Thron C.D. Theoretical dynamics of the cyclin B-MPF system: a possible role for p13suc1. BioSystems 32 2 (1994) 97-109
    • (1994) BioSystems , vol.32 , Issue.2 , pp. 97-109
    • Thron, C.D.1
  • 43
    • 0030767422 scopus 로고    scopus 로고
    • Bistable biochemical switching and the control of the events of the cell cycle
    • Thron C.D. Bistable biochemical switching and the control of the events of the cell cycle. Oncogene 15 3 (1997) 317-325
    • (1997) Oncogene , vol.15 , Issue.3 , pp. 317-325
    • Thron, C.D.1
  • 45
    • 0037376655 scopus 로고    scopus 로고
    • Sniffers, buzzers, toggles and blinkers: dynamics of regulatory and signaling pathways in the cell
    • Tyson J.J., Chen K.C., and Novak B. Sniffers, buzzers, toggles and blinkers: dynamics of regulatory and signaling pathways in the cell. Curr. Opin. Cell Biol. 15 2 (2003) 221-231
    • (2003) Curr. Opin. Cell Biol. , vol.15 , Issue.2 , pp. 221-231
    • Tyson, J.J.1    Chen, K.C.2    Novak, B.3
  • 46
    • 0002275384 scopus 로고
    • The dynamics of feedback control circuits in biochemical pathways
    • Academic Press, New York
    • Tyson J.J., and Othmer H.G. The dynamics of feedback control circuits in biochemical pathways. Progress in Theoretical Biology, vol. 5 (1978), Academic Press, New York 1-62
    • (1978) Progress in Theoretical Biology, vol. 5 , pp. 1-62
    • Tyson, J.J.1    Othmer, H.G.2
  • 49
    • 0030768931 scopus 로고    scopus 로고
    • The Hill equation revisited: uses and misuses
    • Weiss J.N. The Hill equation revisited: uses and misuses. FASEB J. 11 11 (1997) 835-841
    • (1997) FASEB J. , vol.11 , Issue.11 , pp. 835-841
    • Weiss, J.N.1
  • 50
    • 0037676107 scopus 로고    scopus 로고
    • Motifs, modules and games in bacteria
    • Wolf D.M., and Arkin A.P. Motifs, modules and games in bacteria. Curr. Opin. Microbiol. 6 2 (2003) 125-134
    • (2003) Curr. Opin. Microbiol. , vol.6 , Issue.2 , pp. 125-134
    • Wolf, D.M.1    Arkin, A.P.2
  • 51
    • 0345359924 scopus 로고    scopus 로고
    • A positive-feedback-based bistable 'memory module' that governs a cell fate decision
    • Xiong W., and Ferrell Jr. J.E. A positive-feedback-based bistable 'memory module' that governs a cell fate decision. Nature 426 6965 (2003) 460-465
    • (2003) Nature , vol.426 , Issue.6965 , pp. 460-465
    • Xiong, W.1    Ferrell Jr., J.E.2
  • 52
    • 3342900223 scopus 로고    scopus 로고
    • 2+-dependent proteases in ischemic neuronal death: a conserved 'calpain-cathepsin cascade' from nematodes to primates
    • 2+-dependent proteases in ischemic neuronal death: a conserved 'calpain-cathepsin cascade' from nematodes to primates. Cell Calcium 36 3/4 (2004) 285-293
    • (2004) Cell Calcium , vol.36 , Issue.3-4 , pp. 285-293
    • Yamashima, T.1
  • 54
    • 0002556664 scopus 로고    scopus 로고
    • Dynamics of spatially nonuniform patterning in the model of blood coagulation
    • Zarnitsina V.I., Ataullakhanov F.I., Lobanov A.I., and Morozova O.L. Dynamics of spatially nonuniform patterning in the model of blood coagulation. Chaos 11 1 (2001) 57-70
    • (2001) Chaos , vol.11 , Issue.1 , pp. 57-70
    • Zarnitsina, V.I.1    Ataullakhanov, F.I.2    Lobanov, A.I.3    Morozova, O.L.4


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