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Volumn 3, Issue , 2008, Pages 1061-1081

Computational Methods and Modeling: Modeling Intracellular Signal Transduction Processes

Author keywords

Biochemical mechanisms; Internalized receptors; Kinase activity; serial engagement; Signal transduction

Indexed keywords


EID: 84891308610     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527619375.ch17b     Document Type: Chapter
Times cited : (1)

References (89)
  • 1
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • T. Hunter, Signaling-2000 and beyond, Cell 2000, 100, 113-127.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 2
    • 0031226368 scopus 로고    scopus 로고
    • Reductionism for biochemists: how to survive the protein jungle
    • D. Bray, Reductionism for biochemists: how to survive the protein jungle, Trends Biochem. Sei. 1997, 22, 325-326.
    • (1997) Trends Biochem. Sei. , vol.22 , pp. 325-326
    • Bray, D.1
  • 5
    • 0346502065 scopus 로고    scopus 로고
    • Dynamical and integrative cell signaling: challenges for the new biology
    • A. Levchenko, Dynamical and integrative cell signaling: challenges for the new biology, Biotechnol. Bioeng. 2003, 84, 773-782.
    • (2003) Biotechnol. Bioeng. , vol.84 , pp. 773-782
    • Levchenko, A.1
  • 6
    • 0037376655 scopus 로고    scopus 로고
    • Sniffers, buzzers, toggles and blinkers: dynamics of regulatory and signaling pathways in the cell
    • J.J. Tyson, K.C. Chen, B. Novak, Sniffers, buzzers, toggles and blinkers: dynamics of regulatory and signaling pathways in the cell, Curr. Opin. Cell Biol. 2003, 15, 221-231.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 221-231
    • Tyson, J.J.1    Chen, K.C.2    Novak, B.3
  • 7
    • 9644274131 scopus 로고    scopus 로고
    • Computational approaches for modeling regulatory cellular networks
    • N.J. Eungdamrong, R. Iyengar, Computational approaches for modeling regulatory cellular networks, Trends Cell Biol. 2004, 14, 661-669.
    • (2004) Trends Cell Biol. , vol.14 , pp. 661-669
    • Eungdamrong, N.J.1    Iyengar, R.2
  • 9
    • 0026708050 scopus 로고
    • Implications of epidermal growth factor (EGF) induced EGF receptor aggregation
    • C. Wofsy, B. Goldstein, K. Lund, H.S Wiley, Implications of epidermal growth factor (EGF) induced EGF receptor aggregation, Biophys. J. 1992, 63, 98-110.
    • (1992) Biophys. J. , vol.63 , pp. 98-110
    • Wofsy, C.1    Goldstein, B.2    Lund, K.3    Wiley, S.H.4
  • 10
    • 0032546557 scopus 로고    scopus 로고
    • A unified model of c-erbB receptor homo-and heterodimerisation
    • S.G. Chamberlin, D.E Davies, A unified model of c-erbB receptor homo-and heterodimerisation, Biochim. Biophys. Acta 1998, 1384, 223-232.
    • (1998) Biochim. Biophys. Acta , vol.1384 , pp. 223-232
    • Chamberlin, S.G.1    Davies, D.E.2
  • 11
    • 0033570090 scopus 로고    scopus 로고
    • Quantification of short term signaling by the epidermal growth factor receptor
    • B.N. Kholodenko, O.V. Demin, G. Moehren, J.B Hoek, Quantification of short term signaling by the epidermal growth factor receptor, J. Biol. Chem. 1999, 274, 30169-30181.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30169-30181
    • Kholodenko, B.N.1    Demin, O.V.2    Moehren, G.3    Hoek, J.B.4
  • 13
    • 14044276994 scopus 로고    scopus 로고
    • Parsing ERK activation reveals quantitatively equivalent contributions from epidermal growth factor receptor and HER2 in human mammary epithelial cells
    • B.S. Hendriks, G. Orr, A. Wells, H.S. Wiley, D.A Lauffenburger, Parsing ERK activation reveals quantitatively equivalent contributions from epidermal growth factor receptor and HER2 in human mammary epithelial cells, J. Biol. Chem. 2005, 280, 6157-6169.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6157-6169
    • Hendriks, B.S.1    Orr, G.2    Wells, A.3    Wiley, H.S.4    Lauffenburger, D.A.5
  • 14
    • 0034617763 scopus 로고    scopus 로고
    • Insulin receptor binding kinetics: modeling and simulation studies
    • S. Wanant, M.J Quon, Insulin receptor binding kinetics: modeling and simulation studies, J. Theor. Biol. 2000, 205, 355-364.
    • (2000) J. Theor. Biol. , vol.205 , pp. 355-364
    • Wanant, S.1    Quon, M.J.2
  • 15
    • 0034698012 scopus 로고    scopus 로고
    • Potential mechanisms for the regulation of growth factor binding by heparin
    • K.E. Forsten, M. Fannon, M.A Nugent, Potential mechanisms for the regulation of growth factor binding by heparin, J. Theor. Biol. 2000, 205, 215-230.
    • (2000) J. Theor. Biol. , vol.205 , pp. 215-230
    • Forsten, K.E.1    Fannon, M.2    Nugent, M.A.3
  • 16
    • 14644399153 scopus 로고    scopus 로고
    • The kinetics of FGF-2 binding to heparan sulfate proteoglycans and MAP kinase signaling
    • K. Forsten-Williams, C.C. Chua, M.A Nugent, The kinetics of FGF-2 binding to heparan sulfate proteoglycans and MAP kinase signaling, J. Theor. Biol. 2005, 233, 483-499.
    • (2005) J. Theor. Biol. , vol.233 , pp. 483-499
    • Forsten-Williams, K.1    Chua, C.C.2    Nugent, M.A.3
  • 17
    • 0033587769 scopus 로고    scopus 로고
    • One Lyn molecule is sufficient to initiate phosphorylation of aggregated high-affinity IgE receptors
    • C. Wofsy, B.M. Vonakis, H. Metzger, B. Goldstein, One Lyn molecule is sufficient to initiate phosphorylation of aggregated high-affinity IgE receptors, Proc. Natl. Acad. Sei. U.S.A. 1999, 96, 8615-8620.
    • (1999) Proc. Natl. Acad. Sei. U.S.A. , vol.96 , pp. 8615-8620
    • Wofsy, C.1    Vonakis, B.M.2    Metzger, H.3    Goldstein, B.4
  • 19
    • 0141733263 scopus 로고    scopus 로고
    • Kinetic analysis of platelet-derived growth factor receptor/phosphoinositide 3-kinase/Akt signaling in fibroblasts
    • C.S. Park, I.C. Schneider, J.M Haugh, Kinetic analysis of platelet-derived growth factor receptor/phosphoinositide 3-kinase/Akt signaling in fibroblasts, J. Biol. Chem. 2003, 278, 37064-37072.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37064-37072
    • Park, C.S.1    Schneider, I.C.2    Haugh, J.M.3
  • 20
    • 84995826606 scopus 로고
    • Receptor dimerization determines the effects of growth hormone in primary rat adipocytes and cultured human IM-9 lymphocytes
    • M.M. Hondo, A.B. Damholt, B.C. Cunningham, J.A. Wells, P. De Meyts, R.M Shymko, Receptor dimerization determines the effects of growth hormone in primary rat adipocytes and cultured human IM-9 lymphocytes, Endocrinology 1994, 134, 2397-2403.
    • (1994) Endocrinology , vol.134 , pp. 2397-2403
    • Hondo, M.M.1    Damholt, A.B.2    Cunningham, B.C.3    Wells, J.A.4    De Meyts, P.5    Shymko, R.M.6
  • 21
    • 5444235675 scopus 로고    scopus 로고
    • Mathematical model of human growth hormone (hGH)-stimulated cell proliferation explains the efficacy of hGH variants as receptor agonists or antagonists
    • J.M. Haugh, Mathematical model of human growth hormone (hGH)-stimulated cell proliferation explains the efficacy of hGH variants as receptor agonists or antagonists, Biotechnol. Prog. 2004, 20, 1337-1344.
    • (2004) Biotechnol. Prog. , vol.20 , pp. 1337-1344
    • Haugh, J.M.1
  • 22
    • 0026570314 scopus 로고
    • Evidence for p55-p75 heterodimers in the absence of IL-2 from Scatchard plot analysis
    • B. Goldstein, D. Jones, I.G. Kevrekidis, A.S Perelson, Evidence for p55-p75 heterodimers in the absence of IL-2 from Scatchard plot analysis, Int. Immunol. 1992, 4, 23-32.
    • (1992) Int. Immunol. , vol.4 , pp. 23-32
    • Goldstein, B.1    Jones, D.2    Kevrekidis, I.G.3    Perelson, A.S.4
  • 23
    • 0019404817 scopus 로고
    • A steady state model for analyzing the cellular binding, internalization and degradation of polypeptide ligands
    • H.S. Wiley, D.D Cunningham, A steady state model for analyzing the cellular binding, internalization and degradation of polypeptide ligands, Cell 1981, 25, 433-440.
    • (1981) Cell , vol.25 , pp. 433-440
    • Wiley, H.S.1    Cunningham, D.D.2
  • 24
    • 0026833077 scopus 로고
    • Mathematical model for the effects of epidermal growth factor receptor trafficking dynamics on fibroblast proliferation responses
    • C. Starbuck, D.A Lauffenburger, Mathematical model for the effects of epidermal growth factor receptor trafficking dynamics on fibroblast proliferation responses, Biotechnol. Prog. 1992, 8, 132-143.
    • (1992) Biotechnol. Prog. , vol.8 , pp. 132-143
    • Starbuck, C.1    Lauffenburger, D.A.2
  • 25
    • 0030570842 scopus 로고    scopus 로고
    • Intracellular receptor/ligand sorting based on endosomal retention components
    • A.R. French, D.A Lauffenburger, Intracellular receptor/ligand sorting based on endosomal retention components, Biotechnol. Bioeng. 1996, 51, 281-297.
    • (1996) Biotechnol. Bioeng. , vol.51 , pp. 281-297
    • French, A.R.1    Lauffenburger, D.A.2
  • 26
    • 0034281442 scopus 로고    scopus 로고
    • Computational model for effects of ligand/receptor binding properties on interleukin-2 trafficking dynamics and T cell proliferation response
    • E.M. Fallon, D.A Lauffenburger, Computational model for effects of ligand/receptor binding properties on interleukin-2 trafficking dynamics and T cell proliferation response, Biotechnol. Prog. 2000, 16, 905-916.
    • (2000) Biotechnol. Prog. , vol.16 , pp. 905-916
    • Fallon, E.M.1    Lauffenburger, D.A.2
  • 27
    • 0037222528 scopus 로고    scopus 로고
    • Cell-level pharmacokinetic model of granulocyte colony-stimulating factor: implications for ligand lifetime and potency in vivo
    • C.A. Sarkar, D.A. Lauffenburger, Cell-level pharmacokinetic model of granulocyte colony-stimulating factor: implications for ligand lifetime and potency in vivo, Mol. Pharmacol. 2003, 63, 147-158.
    • (2003) Mol. Pharmacol. , vol.63 , pp. 147-158
    • Sarkar, C.A.1    Lauffenburger, D.A.2
  • 28
    • 0032556454 scopus 로고    scopus 로고
    • Analysis of receptor internalization as a mechanism for modulating signal transduction
    • J.M. Haugh, D.A Lauffenburger, Analysis of receptor internalization as a mechanism for modulating signal transduction, J. Theor. Biol. 1998, 195, 187-218.
    • (1998) J. Theor. Biol. , vol.195 , pp. 187-218
    • Haugh, J.M.1    Lauffenburger, D.A.2
  • 29
    • 0036212767 scopus 로고    scopus 로고
    • Computational modeling of the dynamics of the MAP kinase cascade activated by surface and internalized EGF receptors
    • B. Schoeberl, C. Eichler-Jonsson, E.D. Gilles, G. Muller, Computational modeling of the dynamics of the MAP kinase cascade activated by surface and internalized EGF receptors, Nat. Biotechnol. 2002, 20, 370-375.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 370-375
    • Schoeberl, B.1    Eichler-Jonsson, C.2    Gilles, E.D.3    Muller, G.4
  • 30
    • 3242722271 scopus 로고    scopus 로고
    • On the cross-regulation of protein tyrosine phosphatases and receptor tyrosine kinases in intracellular signaling
    • J.M. Haugh, I.C. Schneider, J.M Lewis, On the cross-regulation of protein tyrosine phosphatases and receptor tyrosine kinases in intracellular signaling, J. Theor. Biol. 2004, 230, 119-132.
    • (2004) J. Theor. Biol. , vol.230 , pp. 119-132
    • Haugh, J.M.1    Schneider, I.C.2    Lewis, J.M.3
  • 31
    • 0028931731 scopus 로고
    • The kinetics of bivalent ligand-bivalent receptor aggregation: ring formation and the breakdown of the equivalent site approximation
    • R.G. Posner, C. Wofsy, B. Goldstein, The kinetics of bivalent ligand-bivalent receptor aggregation: ring formation and the breakdown of the equivalent site approximation, Math. Biosci. 1995, 126, 171-190.
    • (1995) Math. Biosci. , vol.126 , pp. 171-190
    • Posner, R.G.1    Wofsy, C.2    Goldstein, B.3
  • 32
    • 0033555859 scopus 로고    scopus 로고
    • Emergent properties of networks of biological signaling pathways
    • U.S. Bhalla, R. Iyengar, Emergent properties of networks of biological signaling pathways, Science 1999, 283, 381-387.
    • (1999) Science , vol.283 , pp. 381-387
    • Bhalla, U.S.1    Iyengar, R.2
  • 34
    • 0034693459 scopus 로고    scopus 로고
    • Mathematical modeling of epidermal growth factor receptor signaling through the phospholipase C pathway: mechanistic insights and predictions for molecular interventions
    • J.M. Haugh, A. Wells, D.A Lauffenburger, Mathematical modeling of epidermal growth factor receptor signaling through the phospholipase C pathway: mechanistic insights and predictions for molecular interventions, Biotechnol. Bioeng. 2000, 70, 225-238.
    • (2000) Biotechnol. Bioeng. , vol.70 , pp. 225-238
    • Haugh, J.M.1    Wells, A.2    Lauffenburger, D.A.3
  • 35
    • 0029063148 scopus 로고
    • Kinetic proofreading in T-cell receptor signal transduction
    • T.W. McKeithan, Kinetic proofreading in T-cell receptor signal transduction, Proc. Natl. Acad. Sei. U.S.A. 1995, 92, 5042-5046.
    • (1995) Proc. Natl. Acad. Sei. U.S.A. , vol.92 , pp. 5042-5046
    • McKeithan, T.W.1
  • 36
    • 0036739732 scopus 로고    scopus 로고
    • Kinetic proofreading in receptor-mediated transduction of cellular signals: receptor aggregation, partially activated receptors, and cytosolic messengers
    • W.S. Hlavaček, A. Redondo, C. Wofsy, B. Goldstein, Kinetic proofreading in receptor-mediated transduction of cellular signals: receptor aggregation, partially activated receptors, and cytosolic messengers, Bull. Math. Biol. 2002, 64, 887-911.
    • (2002) Bull. Math. Biol. , vol.64 , pp. 887-911
    • Hlavaček, W.S.1    Redondo, A.2    Wofsy, C.3    Goldstein, B.4
  • 38
    • 0035146577 scopus 로고    scopus 로고
    • Calculations show substantial serial engagement of T cell receptors
    • C. Wofsy, D. Coombs, B. Goldstein, Calculations show substantial serial engagement of T cell receptors, Biophys.J. 2001, 80, 606-612.
    • (2001) Biophys.J. , vol.80 , pp. 606-612
    • Wofsy, C.1    Coombs, D.2    Goldstein, B.3
  • 39
    • 0036795530 scopus 로고    scopus 로고
    • Activated TCRs remain marked for internalization after dissociation from pMHC
    • D. Coombs, A.M. Kalergis, S.G. Nathenson, C. Wofsy, B. Goldstein, Activated TCRs remain marked for internalization after dissociation from pMHC, Nat. Immunol. 2002, 3, 926-931.
    • (2002) Nat. Immunol. , vol.3 , pp. 926-931
    • Coombs, D.1    Kalergis, A.M.2    Nathenson, S.G.3    Wofsy, C.4    Goldstein, B.5
  • 41
    • 0347057016 scopus 로고    scopus 로고
    • Analysis of nonlinear dynamics on arbitrary geometries with the virtual cell
    • J.C. Schaff, B.M. Slepchenko, Y.S. Choi, J. Wagner, D. Resasco, L.M Loew, Analysis of nonlinear dynamics on arbitrary geometries with the virtual cell, Chaos 2001, 11, 115-131.
    • (2001) Chaos , vol.11 , pp. 115-131
    • Schaff, J.C.1    Slepchenko, B.M.2    Choi, Y.S.3    Wagner, J.4    Resasco, D.5    Loew, L.M.6
  • 42
    • 0037047132 scopus 로고    scopus 로고
    • Shooting from the hip: spatial control of signal release by intracellular waves
    • S.Y. Shvartsman, Shooting from the hip: spatial control of signal release by intracellular waves, Proc. Natl. Acad. Sei. U.S.A. 2002, 99, 9087-9089.
    • (2002) Proc. Natl. Acad. Sei. U.S.A. , vol.99 , pp. 9087-9089
    • Shvartsman, S.Y.1
  • 43
    • 0034665002 scopus 로고    scopus 로고
    • Diffusion control of protein phosphorylation in signal transduction pathways
    • B.N. Kholodenko, G.C. Brown, J.B Hoek, Diffusion control of protein phosphorylation in signal transduction pathways, Biochem. J. 2000, 350, 901-907.
    • (2000) Biochem. J. , vol.350 , pp. 901-907
    • Kholodenko, B.N.1    Brown, G.C.2    Hoek, J.B.3
  • 44
    • 0036536713 scopus 로고    scopus 로고
    • MAP kinase cascade signaling and endocytic trafficking: a marriage of convenience?
    • B.N. Kholodenko, MAP kinase cascade signaling and endocytic trafficking: a marriage of convenience? Trends Cell Biol. 2002, 12, 173-177.
    • (2002) Trends Cell Biol. , vol.12 , pp. 173-177
    • Kholodenko, B.N.1
  • 45
    • 0346688723 scopus 로고    scopus 로고
    • Self-organization of polarized cell signaling via autocrine circuits: computational model analysis
    • I.V. Maly, H.S. Wiley, D.A. Lauffenburger, Self-organization of polarized cell signaling via autocrine circuits: computational model analysis, Biophys.J. 2004, 86, 10-22.
    • (2004) Biophys.J. , vol.86 , pp. 10-22
    • Maly, I.V.1    Wiley, H.S.2    Lauffenburger, D.A.3
  • 46
    • 0015454185 scopus 로고
    • A theory of biological pattern formation
    • A. Gierer, H. Meinhardt, A theory of biological pattern formation, Kybernetik 1972, 12, 30-39.
    • (1972) Kybernetik , vol.12 , pp. 30-39
    • Gierer, A.1    Meinhardt, H.2
  • 47
    • 0034866573 scopus 로고    scopus 로고
    • A diffusion-translocation model for gradient sensing by chemotactic cells
    • M. Postma, P.J.M. Van Haastert, A diffusion-translocation model for gradient sensing by chemotactic cells, Biophys.J. 2001, 81, 1314-1323.
    • (2001) Biophys.J. , vol.81 , pp. 1314-1323
    • Postma, M.1    Van Haastert, P.J.M.2
  • 48
    • 0036219106 scopus 로고    scopus 로고
    • Models of eukaryotic gradient sensing: application to Chemotaxis of amoebae and neutrophils
    • A. Levchenko, P.A Iglesias, Models of eukaryotic gradient sensing: application to Chemotaxis of amoebae and neutrophils, Biophys.J. 2002, 82, 50-63.
    • (2002) Biophys.J. , vol.82 , pp. 50-63
    • Levchenko, A.1    Iglesias, P.A.2
  • 49
    • 4444271530 scopus 로고    scopus 로고
    • A mechanistic model for eukaryotic gradient sensing: spontaneous and induced phosphoinositide polarization
    • K.K. Subramanian, A. Narang, A mechanistic model for eukaryotic gradient sensing: spontaneous and induced phosphoinositide polarization, J. Theor. Biol. 2004, 231, 49-67.
    • (2004) J. Theor. Biol. , vol.231 , pp. 49-67
    • Subramanian, K.K.1    Narang, A.2
  • 50
    • 10044250005 scopus 로고    scopus 로고
    • Two complementary, local excitation, global inhibition mechanisms acting in parallel can explain the chemoattractant-induced regulation of PI(3, 4, 5)P3 response in Dictyostelium cells
    • L. Ma, C. Janetopoulos, L. Yang, P.N. Devreotes, P.A Iglesias, Two complementary, local excitation, global inhibition mechanisms acting in parallel can explain the chemoattractant-induced regulation of PI(3, 4, 5)P3 response in Dictyostelium cells, Biophys. J. 2004, 87, 3764-3774.
    • (2004) Biophys. J. , vol.87 , pp. 3764-3774
    • Ma, L.1    Janetopoulos, C.2    Yang, L.3    Devreotes, P.N.4    Iglesias, P.A.5
  • 51
    • 0034638836 scopus 로고    scopus 로고
    • Spatial sensing in fibroblasts mediated by 3' phosphoinositides
    • J.M. Haugh, F. Codazzi, M. Teruel, T. Meyer, Spatial sensing in fibroblasts mediated by 3' phosphoinositides, J. Cell Biol. 2000, 151, 1269-1279.
    • (2000) J. Cell Biol. , vol.151 , pp. 1269-1279
    • Haugh, J.M.1    Codazzi, F.2    Teruel, M.3    Meyer, T.4
  • 52
    • 0347319164 scopus 로고    scopus 로고
    • Spatial analysis of 3' phosphoinositide signaling in living fibroblasts: I. Uniform stimulation model and bounds on dimensionless groups
    • J.M. Haugh, I.C Schneider, Spatial analysis of 3' phosphoinositide signaling in living fibroblasts: I. Uniform stimulation model and bounds on dimensionless groups, Biophys. J. 2004, 86, 589-598.
    • (2004) Biophys. J. , vol.86 , pp. 589-598
    • Haugh, J.M.1    Schneider, I.C.2
  • 53
    • 0003064682 scopus 로고
    • Reduction of dimensionality in biological diffusion processes
    • in, (Eds.: A. Rich, N. Davidson), W.H. Freeman and Co., San Fransisco
    • G. Adam, M. Delbrück, Reduction of dimensionality in biological diffusion processes, in Structural Chemistry and Molecular Biology, (Eds.: A. Rich, N. Davidson), W.H. Freeman and Co., San Fransisco, 1968, 198-215.
    • (1968) Structural Chemistry and Molecular Biology , pp. 198-215
    • Adam, G.1    Delbrück, M.2
  • 54
    • 0017664223 scopus 로고
    • Physics of chemoreception
    • H.C. Berg, E.M Purcell, Physics of chemoreception, Biophys. J. 1977, 20, 193-219.
    • (1977) Biophys. J. , vol.20 , pp. 193-219
    • Berg, H.C.1    Purcell, E.M.2
  • 55
    • 0030834849 scopus 로고    scopus 로고
    • Calculation of diffusion-limited kinetics for the reactions in collision coupling and receptor cross-linking
    • L.D. Shea, G.M. Omann, J.J Linderman, Calculation of diffusion-limited kinetics for the reactions in collision coupling and receptor cross-linking, Biophys. J. 1997, 73, 2949-2959.
    • (1997) Biophys. J. , vol.73 , pp. 2949-2959
    • Shea, L.D.1    Omann, G.M.2    Linderman, J.J.3
  • 56
    • 0036154167 scopus 로고    scopus 로고
    • A unified model for signal transduction reactions in cellular membranes
    • J.M. Haugh, A unified model for signal transduction reactions in cellular membranes, Biophys. J. 2002, 82, 591-604.
    • (2002) Biophys. J. , vol.82 , pp. 591-604
    • Haugh, J.M.1
  • 57
    • 0036789480 scopus 로고    scopus 로고
    • Monte Carlo simulations of enzyme reactions in two dimensions: fractal kinetics and spatial segregation
    • H. Berry, Monte Carlo simulations of enzyme reactions in two dimensions: fractal kinetics and spatial segregation, Biophys. J. 2002, 83, 1891-1901.
    • (2002) Biophys. J. , vol.83 , pp. 1891-1901
    • Berry, H.1
  • 58
    • 0037215808 scopus 로고    scopus 로고
    • Untangling ligand induced activation and desensitization of G-protein-coupled receptors
    • P.J. Woolf, J.J Linderman, Untangling ligand induced activation and desensitization of G-protein-coupled receptors, Biophys. J. 2003, 84, 3-13.
    • (2003) Biophys. J. , vol.84 , pp. 3-13
    • Woolf, P.J.1    Linderman, J.J.2
  • 59
    • 0030956033 scopus 로고    scopus 로고
    • Single-particle tracking: applications to membrane dynamics
    • M.J. Saxton, K. Jacobson, Single-particle tracking: applications to membrane dynamics, Annu. Rev. Biophys. Biomol. Struct. 1997, 26, 373-399.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 373-399
    • Saxton, M.J.1    Jacobson, K.2
  • 60
    • 0032492636 scopus 로고    scopus 로고
    • Compartmentalization of receptors and enzymes affects activation for a collision coupling mechanism
    • L.D. Shea, J.J Linderman, Compartmentalization of receptors and enzymes affects activation for a collision coupling mechanism, J. Theor. Biol. 1998, 191, 249-258.
    • (1998) J. Theor. Biol. , vol.191 , pp. 249-258
    • Shea, L.D.1    Linderman, J.J.2
  • 61
    • 21244494104 scopus 로고    scopus 로고
    • Detection of non-brownian diffusion in the cell membrane in single molecule tracking
    • K. Ritchie, X. Shan, J. Kondo, K. Iwasawa, T. Fujiwara, A. Kusumi, Detection of non-brownian diffusion in the cell membrane in single molecule tracking, Biophys. J. 2005, 88, 2266-2277.
    • (2005) Biophys. J. , vol.88 , pp. 2266-2277
    • Ritchie, K.1    Shan, X.2    Kondo, J.3    Iwasawa, K.4    Fujiwara, T.5    Kusumi, A.6
  • 62
    • 0025276049 scopus 로고
    • Intracellular signaling as a parallel distributed process
    • D. Bray, Intracellular signaling as a parallel distributed process, J. Theor. Biol. 1990, 143, 215-231.
    • (1990) J. Theor. Biol. , vol.143 , pp. 215-231
    • Bray, D.1
  • 63
    • 0031559933 scopus 로고    scopus 로고
    • Quantification of information transfer via cellular signal transduction pathways
    • B.N. Kholodenko, J.B. Hoek, H.V. Westerhofs G.C Brown, Quantification of information transfer via cellular signal transduction pathways, FEBS Lett. 1997, 414, 430-434.
    • (1997) FEBS Lett. , vol.414 , pp. 430-434
    • Kholodenko, B.N.1    Hoek, J.B.2    Westerhofs, H.V.3    Brown, G.C.4
  • 64
    • 0001424903 scopus 로고
    • An amplified sensitivity arising from covalent modification in biological systems
    • A. Goldbeter, D.E. Koshland Jr, An amplified sensitivity arising from covalent modification in biological systems, Proc. Natl. Acad. Sei. U.S.A. 1981, 78, 6840-6844.
    • (1981) Proc. Natl. Acad. Sei. U.S.A. , vol.78 , pp. 6840-6844
    • Goldbeter, A.1    Koshland Jr., D.E.2
  • 65
    • 0021715523 scopus 로고
    • Ultrasensitivity in biochemical systems controlled by covalent modification: interplay between zero-order and multistep effects
    • A. Goldbeter, D.E. Koshland Jr, Ultrasensitivity in biochemical systems controlled by covalent modification: interplay between zero-order and multistep effects, J. Biol. Chem. 1984, 259, 14441-14447.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14441-14447
    • Goldbeter, A.1    Koshland Jr., D.E.2
  • 66
    • 0030445778 scopus 로고    scopus 로고
    • Tripping the switch fantastic: how a protein kinase cascade can convert graded inputs into switch-like outputs
    • J.E. Ferrell Jr, Tripping the switch fantastic: how a protein kinase cascade can convert graded inputs into switch-like outputs, Trends Biochem. Sei. 1996, 21, 460-466.
    • (1996) Trends Biochem. Sei. , vol.21 , pp. 460-466
    • Ferrell Jr., J.E.1
  • 67
    • 0030998039 scopus 로고    scopus 로고
    • Physical modulation of intracellular signaling processes by locational regulation
    • J.M. Haugh, D.A Lauffenburger, Physical modulation of intracellular signaling processes by locational regulation, Biophys. J. 1997, 72, 2014-2031.
    • (1997) Biophys. J. , vol.72 , pp. 2014-2031
    • Haugh, J.M.1    Lauffenburger, D.A.2
  • 68
    • 0032409387 scopus 로고    scopus 로고
    • How regulated protein translocation can produce switch-like responses
    • J.E. Ferrell Jr, How regulated protein translocation can produce switch-like responses, Trends Biochem. Sei. 1998, 23, 461-465.
    • (1998) Trends Biochem. Sei. , vol.23 , pp. 461-465
    • Ferrell Jr., J.E.1
  • 69
    • 0034705227 scopus 로고    scopus 로고
    • Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties
    • A. Levchenko, J. Bruck, P.W Sternberg, Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties, Proc. Natl. Acad. Sei. U.S.A. 2000, 97, 5818-5823.
    • (2000) Proc. Natl. Acad. Sei. U.S.A. , vol.97 , pp. 5818-5823
    • Levchenko, A.1    Bruck, J.2    Sternberg, P.W.3
  • 70
    • 0036285634 scopus 로고    scopus 로고
    • Mathematical models of protein kinase signal transduction
    • R. Heinrich, B.G. Neel, T.A Rapoport, Mathematical models of protein kinase signal transduction, Mol. Cells 2002, 9, 957-970.
    • (2002) Mol. Cells , vol.9 , pp. 957-970
    • Heinrich, R.1    Neel, B.G.2    Rapoport, T.A.3
  • 71
    • 0842281546 scopus 로고    scopus 로고
    • Robust global sensitivity in multiple enzyme cascade system explains how the downstream cascade structure may remain unaffected by cross-talk
    • V.K. Mutalik, A.P. Singh, J.S. Edwards, K.V Venkatesh, Robust global sensitivity in multiple enzyme cascade system explains how the downstream cascade structure may remain unaffected by cross-talk, FEBS Lett. 2004, 558, 79-84.
    • (2004) FEBS Lett. , vol.558 , pp. 79-84
    • Mutalik, V.K.1    Singh, A.P.2    Edwards, J.S.3    Venkatesh, K.V.4
  • 72
    • 0036532226 scopus 로고    scopus 로고
    • Self-perpetuating states in signal transduction: positive feedback, double-negative feedback and bistability
    • J.E. Ferrell Jr, Self-perpetuating states in signal transduction: positive feedback, double-negative feedback and bistability, Curr. Opin. Cell Biol. 2002, 14, 140-148.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 140-148
    • Ferrell Jr., J.E.1
  • 73
    • 0041843750 scopus 로고    scopus 로고
    • An integrated model of epidermal growth factor receptor trafficking and signal transduction
    • H. Resat, J.A. Ewald, D.A. Dixon, H.S Wiley, An integrated model of epidermal growth factor receptor trafficking and signal transduction, Biophys.J. 2003, 85, 730-743.
    • (2003) Biophys.J. , vol.85 , pp. 730-743
    • Resat, H.1    Ewald, J.A.2    Dixon, D.A.3    Wiley, H.S.4
  • 74
    • 0029790351 scopus 로고    scopus 로고
    • Ultrasensitivity in the mitogen-activated protein kinase cascade
    • C.F. Huang, J.E. Ferrell Jr, Ultrasensitivity in the mitogen-activated protein kinase cascade, Proc. Natl. Acad. Sei. U.S.A. 1996, 93, 10078-10083.
    • (1996) Proc. Natl. Acad. Sei. U.S.A. , vol.93 , pp. 10078-10083
    • Huang, C.F.1    Ferrell Jr., J.E.2
  • 75
    • 0030972112 scopus 로고    scopus 로고
    • The activating dual phosphorylation of MAPK by MEK is nonprocessive
    • W.R. Burack, T.W Sturgill, The activating dual phosphorylation of MAPK by MEK is nonprocessive, Biochemistry 1997, 36, 5929-5933.
    • (1997) Biochemistry , vol.36 , pp. 5929-5933
    • Burack, W.R.1    Sturgill, T.W.2
  • 76
    • 0034613112 scopus 로고    scopus 로고
    • Differential feedback regulation of the MAPK cascade underlies the quantitative differences in EGF and NGF signalling in PC12 cells
    • F.A. Brightman, D.A Fell, Differential feedback regulation of the MAPK cascade underlies the quantitative differences in EGF and NGF signalling in PC12 cells, FEBS Lett. 2000, 482, 169-174.
    • (2000) FEBS Lett. , vol.482 , pp. 169-174
    • Brightman, F.A.1    Fell, D.A.2
  • 77
    • 0034019315 scopus 로고    scopus 로고
    • Negative feedback and ultrasensitivity can bring about oscillations in the mitogen-activated protein kinase cascades
    • B.N. Kholodenko, Negative feedback and ultrasensitivity can bring about oscillations in the mitogen-activated protein kinase cascades, Eur. J. Biochem. 2000, 267, 1583-1588.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1583-1588
    • Kholodenko, B.N.1
  • 78
    • 0034914737 scopus 로고    scopus 로고
    • A computational study of feedback effects on signal dynamics in a mitogen-activated protein kinase (MAPK) pathway model
    • A.R. Asthagiri, D.A Lauffenburger, A computational study of feedback effects on signal dynamics in a mitogen-activated protein kinase (MAPK) pathway model, Biotechnol. Prog. 2001, 17, 227-239.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 227-239
    • Asthagiri, A.R.1    Lauffenburger, D.A.2
  • 79
    • 17344362384 scopus 로고    scopus 로고
    • Prediction and validation of the distinct dynamics of transient and sustained ERK activation
    • S. Sasagawa, Y. Ozaki, K. Fujita, S. Kuroda, Prediction and validation of the distinct dynamics of transient and sustained ERK activation, Nat. Cell Biol. 2005, 7, 365-373.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 365-373
    • Sasagawa, S.1    Ozaki, Y.2    Fujita, K.3    Kuroda, S.4
  • 80
    • 0038576209 scopus 로고    scopus 로고
    • Kinetic analysis of receptor-activated phosphoinositide turnover
    • C. Xu, J. Watras, L.M Loew, Kinetic analysis of receptor-activated phosphoinositide turnover, J. Cell Biol. 2003, 361, 779-791.
    • (2003) J. Cell Biol. , vol.361 , pp. 779-791
    • Xu, C.1    Watras, J.2    Loew, L.M.3
  • 81
    • 0037044575 scopus 로고    scopus 로고
    • The Ik-B-NF-kB signaling module: temporal control and selective gene activation
    • A. Hoffmann, A. Levchenko, M.L. Scott, D. Baltimore, The Ik-B-NF-kB signaling module: temporal control and selective gene activation, Science 2002, 298, 1241-1245.
    • (2002) Science , vol.298 , pp. 1241-1245
    • Hoffmann, A.1    Levchenko, A.2    Scott, M.L.3    Baltimore, D.4
  • 82
    • 0037448456 scopus 로고    scopus 로고
    • Control mechanism of JAK/STAT signal transduction pathway
    • S. Yamada, S. Shiono, A. Joo, A. Yoshimura, Control mechanism of JAK/STAT signal transduction pathway, FEBS Lett. 2003, 534, 190-196.
    • (2003) FEBS Lett. , vol.534 , pp. 190-196
    • Yamada, S.1    Shiono, S.2    Joo, A.3    Yoshimura, A.4
  • 83
    • 2142653082 scopus 로고    scopus 로고
    • The sonic hedgehog signaling system as a bistable genetic switch
    • K. Lai, M.J. Robertson, D.V Schaffer, The sonic hedgehog signaling system as a bistable genetic switch, Biophys. J. 2004, 86, 2748-2757.
    • (2004) Biophys. J. , vol.86 , pp. 2748-2757
    • Lai, K.1    Robertson, M.J.2    Schaffer, D.V.3
  • 86
    • 0037047611 scopus 로고    scopus 로고
    • MAP kinase phosphatase as a locus of flexibility in a mitogen-activated protein kinase signaling network
    • U.S. Bhalla, P.T. Ram, R. Iyengar, MAP kinase phosphatase as a locus of flexibility in a mitogen-activated protein kinase signaling network, Science 2002, 297, 1018-1023.
    • (2002) Science , vol.297 , pp. 1018-1023
    • Bhalla, U.S.1    Ram, P.T.2    Iyengar, R.3
  • 87
    • 0033515888 scopus 로고    scopus 로고
    • Complexity in biological signaling systems
    • G. Weng, U.S. Bhalla, R. Iyengar, Complexity in biological signaling systems, Science 1999, 284, 92-96.
    • (1999) Science , vol.284 , pp. 92-96
    • Weng, G.1    Bhalla, U.S.2    Iyengar, R.3
  • 89
    • 0030739712 scopus 로고    scopus 로고
    • A general computational framework for modeling cellular structure and function
    • J. Schaff, C.C. Fink, B. Slepchenko, J.H. Carson, L.M Loew, A general computational framework for modeling cellular structure and function, Biophys.J. 1997, 73, 1135-1146.
    • (1997) Biophys.J. , vol.73 , pp. 1135-1146
    • Schaff, J.1    Fink, C.C.2    Slepchenko, B.3    Carson, J.H.4    Loew, L.M.5


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