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Volumn 225, Issue 3, 2003, Pages 293-300

How robust are switches in intracellular signaling cascades?

Author keywords

MAPK cascade; Robustness; Signal transduction; Ultrasensitivity; Working range

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE;

EID: 17644446947     PISSN: 00225193     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-5193(03)00247-9     Document Type: Article
Times cited : (61)

References (25)
  • 1
    • 0034914737 scopus 로고    scopus 로고
    • A computational study of feedback effects on signal dynamics in a mitogen-activated protein kinase (MAPK) pathway model
    • Asthagiri A., Lauffenburger D. A computational study of feedback effects on signal dynamics in a mitogen-activated protein kinase (MAPK) pathway model. Biotechnol. Progr. 17(2):2001;227-239.
    • (2001) Biotechnol. Progr. , vol.17 , Issue.2 , pp. 227-239
    • Asthagiri, A.1    Lauffenburger, D.2
  • 2
    • 0030797355 scopus 로고    scopus 로고
    • Robustness in simple biochemical networks
    • Barkai N., Leibler S. Robustness in simple biochemical networks. Nature. 387:1997;913-917.
    • (1997) Nature , vol.387 , pp. 913-917
    • Barkai, N.1    Leibler, S.2
  • 3
    • 0033555859 scopus 로고    scopus 로고
    • Emergent properties of networks of biological signaling pathways
    • Bhalla U., Iyengar R. Emergent properties of networks of biological signaling pathways. Science. 283:1999;381-387.
    • (1999) Science , vol.283 , pp. 381-387
    • Bhalla, U.1    Iyengar, R.2
  • 5
    • 0034613112 scopus 로고    scopus 로고
    • Differential feedback regulation of the MAPK cascade underlies the quantitative differences in EGF and NGF signaling in PC12 cells
    • Brightman F., Fell D. Differential feedback regulation of the MAPK cascade underlies the quantitative differences in EGF and NGF signaling in PC12 cells. FEBS Lett. 482(3):2000;169-174.
    • (2000) FEBS Lett. , vol.482 , Issue.3 , pp. 169-174
    • Brightman, F.1    Fell, D.2
  • 6
    • 0031203337 scopus 로고    scopus 로고
    • Why do protein kinase cascades have more than one level?
    • Brown G., Hoek J., Kholodenko B. Why do protein kinase cascades have more than one level? Trends. Biochem. Sci. 22(8):1997;288.
    • (1997) Trends. Biochem. Sci. , vol.22 , Issue.8 , pp. 288
    • Brown, G.1    Hoek, J.2    Kholodenko, B.3
  • 7
    • 0024578338 scopus 로고
    • Characteristics necessary for an interconvertible enzyme cascade to generate a highly sensitive response to an effector
    • Cardenas M., Cornish-Bowden A. Characteristics necessary for an interconvertible enzyme cascade to generate a highly sensitive response to an effector. Biochem. J. 257(2):1989;339-345.
    • (1989) Biochem. J. , vol.257 , Issue.2 , pp. 339-345
    • Cardenas, M.1    Cornish-Bowden, A.2
  • 8
    • 0034644270 scopus 로고    scopus 로고
    • The segment polarity network is a robust developmental module
    • Dassow G., Meir E., Munro E., Odell G. The segment polarity network is a robust developmental module. Nature. 406:2000;188-192.
    • (2000) Nature , vol.406 , pp. 188-192
    • Dassow, G.1    Meir, E.2    Munro, E.3    Odell, G.4
  • 9
    • 0031203921 scopus 로고    scopus 로고
    • How responses get more switch-like as you move down a protein kinase cascade
    • Ferrell J. 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, J.1
  • 10
    • 0030746219 scopus 로고    scopus 로고
    • Mechanistic studies of the dual phosphorylation of mitogen-activated protein kinase
    • Ferrell J., Bhatt R. Mechanistic studies of the dual phosphorylation of mitogen-activated protein kinase. J. Biol. Chem. 272(30):1997;19008-19016.
    • (1997) J. Biol. Chem. , vol.272 , Issue.30 , pp. 19008-19016
    • Ferrell, J.1    Bhatt, R.2
  • 11
    • 0032496358 scopus 로고    scopus 로고
    • The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes
    • Ferrell J., Machleder E. The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Science. 280:1998;895-898.
    • (1998) Science , vol.280 , pp. 895-898
    • Ferrell, J.1    Machleder, E.2
  • 12
    • 0001424903 scopus 로고
    • An amplified sensitivity arising from covalent modification in biological systems
    • Goldbeter A., Koshland D. An amplified sensitivity arising from covalent modification in biological systems. Proc. Natl Acad. Sci. USA. 78(11):1981;6840-6844.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , Issue.11 , pp. 6840-6844
    • Goldbeter, A.1    Koshland, D.2
  • 13
    • 0037154231 scopus 로고    scopus 로고
    • Robustness of circadian rhythms with respect to molecular noise
    • Gonze D., Halloy J., Goldbeter A. Robustness of circadian rhythms with respect to molecular noise. Proc. Natl Acad. Sci. USA. 99(2):2002;673-678.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , Issue.2 , pp. 673-678
    • Gonze, D.1    Halloy, J.2    Goldbeter, A.3
  • 14
    • 0035830860 scopus 로고    scopus 로고
    • Principles for the buffering of genetic variation
    • Hartman J., Garvik B., Hartwell L. Principles for the buffering of genetic variation. Science. 291:2001;1001-1004.
    • (2001) Science , vol.291 , pp. 1001-1004
    • Hartman, J.1    Garvik, B.2    Hartwell, L.3
  • 15
    • 0030878161 scopus 로고    scopus 로고
    • Theoretical biology. A robust view of biochemical pathways
    • Hartwell L. Theoretical biology. A robust view of biochemical pathways. Nature. 387:1997;855-857.
    • (1997) Nature , vol.387 , pp. 855-857
    • Hartwell, L.1
  • 16
    • 0003043542 scopus 로고
    • The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves
    • Hill, A., 1910. The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves. J. Physiol. 40, iv-vii.
    • (1910) J. Physiol. , vol.40
    • Hill, A.1
  • 17
    • 0029790351 scopus 로고    scopus 로고
    • Ultrasensitivity in the mitogen-activated protein kinase cascade
    • Huang C., Ferrell J. Ultrasensitivity in the mitogen-activated protein kinase cascade. Proc. Natl Acad. Sci. USA. 93(19):1996;10078-10083.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , Issue.19 , pp. 10078-10083
    • Huang, C.1    Ferrell, J.2
  • 18
    • 0034019315 scopus 로고    scopus 로고
    • Negative feedback and ultrasensitivity can bring about oscillations in the mitogen-activated protein kinase cascades
    • Kholodenko B. Negative feedback and ultrasensitivity can bring about oscillations in the mitogen-activated protein kinase cascades. Eur. J. Biochem. 267(6):2000;1583-1588.
    • (2000) Eur. J. Biochem. , vol.267 , Issue.6 , pp. 1583-1588
    • Kholodenko, B.1
  • 19
    • 0031559933 scopus 로고    scopus 로고
    • Quantification of information transfer via cellular signal transduction pathways
    • Kholodenko B., Hoek J., Westerhoff H., Brown G. Quantification of information transfer via cellular signal transduction pathways. FEBS Lett. 414(2):1997;430-434.
    • (1997) FEBS Lett. , vol.414 , Issue.2 , pp. 430-434
    • Kholodenko, B.1    Hoek, J.2    Westerhoff, H.3    Brown, G.4
  • 20
    • 0036500993 scopus 로고    scopus 로고
    • Systems biology: A brief overview
    • Kitano H. Systems biology. a brief overview Science. 295:2002;1662-1664.
    • (2002) Science , vol.295 , pp. 1662-1664
    • Kitano, H.1
  • 22
    • 0036212767 scopus 로고    scopus 로고
    • Computational modeling of the dynamics of the MAP kinase cascade activated by surface and internalized EGF receptors
    • Schoeberl B., Eichler-Jonsson C., Gilles E., Muller G. Computational modeling of the dynamics of the MAP kinase cascade activated by surface and internalized EGF receptors. Nat. Biotechnol. 20(4):2002;370-375.
    • (2002) Nat. Biotechnol. , vol.20 , Issue.4 , pp. 370-375
    • Schoeberl, B.1    Eichler-Jonsson, C.2    Gilles, E.3    Muller, G.4
  • 23
    • 0034023974 scopus 로고    scopus 로고
    • Cellular information transfer regarded from a stoichiometry and control analysis perspective
    • Schuster S., Kholodenko B., Westerhoff H. Cellular information transfer regarded from a stoichiometry and control analysis perspective. Biosystems. 55(1-3):2000;73-81.
    • (2000) Biosystems , vol.55 , Issue.1-3 , pp. 73-81
    • Schuster, S.1    Kholodenko, B.2    Westerhoff, H.3
  • 24
    • 0025371578 scopus 로고
    • Covalent modification and metabolic control analysis
    • Small R., Fell D. Covalent modification and metabolic control analysis. Eur. J. Biochem. 191(2):1990;405-411.
    • (1990) Eur. J. Biochem. , vol.191 , Issue.2 , pp. 405-411
    • Small, R.1    Fell, D.2
  • 25
    • 0032928614 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase: Conservation of a three-kinase module from yeast to human
    • Widmann C., Gibson S., Jarpe M., Johnson G. Mitogen-activated protein kinase. conservation of a three-kinase module from yeast to human Physiol. Rev. 79(1):1999;143-180.
    • (1999) Physiol. Rev. , vol.79 , Issue.1 , pp. 143-180
    • Widmann, C.1    Gibson, S.2    Jarpe, M.3    Johnson, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.