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Volumn 229, Issue 1, 2004, Pages 127-138

Analysis of compartmental models of ligand-induced endocytosis

Author keywords

Analytical approximations; Growth factors; In Sur plot; Initial transient; Linear stability

Indexed keywords

LIGAND;

EID: 2642584695     PISSN: 00225193     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jtbi.2004.03.009     Document Type: Article
Times cited : (21)

References (42)
  • 1
    • 0024364294 scopus 로고
    • Binding, internalization, and intracellular processing of proteins interacting with recycling receptors
    • Bajzer Z., Myers A.C., Kovach J.S., Vuk-Pavlovic S. Binding, internalization, and intracellular processing of proteins interacting with recycling receptors. J. Biol. Chem. 264:1989;13623-13631
    • (1989) J. Biol. Chem. , vol.264 , pp. 13623-13631
    • Bajzer, Z.1    Myers, A.C.2    Kovach, J.S.3    Vuk-Pavlovic, S.4
  • 2
    • 0028277901 scopus 로고
    • Sequential approach for describing channel opening and desensitization
    • Buchman E., Parnas H. Sequential approach for describing channel opening and desensitization. J. Theor. Biol. 167:1994;381-395
    • (1994) J. Theor. Biol. , vol.167 , pp. 381-395
    • Buchman, E.1    Parnas, H.2
  • 3
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • Damke H., Baba T., Warnock D.E., Schmid S.L. Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J. Cell. Biol. 127:1994;915-934
    • (1994) J. Cell. Biol. , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 4
    • 0024842857 scopus 로고
    • Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome
    • Dunn K.W., McGraw T.E., Maxfield F.R. Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome. J. Cell. Biol. 109:1989;3303-3314
    • (1989) J. Cell. Biol. , vol.109 , pp. 3303-3314
    • Dunn, K.W.1    McGraw, T.E.2    Maxfield, F.R.3
  • 5
    • 14844349947 scopus 로고
    • Epidermal growth factor and transforming growth factor alpha: Differential intracellular routing and processing of ligand-receptor complexes
    • Ebner R., Derynck R. Epidermal growth factor and transforming growth factor alpha. differential intracellular routing and processing of ligand-receptor complexes Cell Regul. 2:1991;599-612
    • (1991) Cell Regul. , vol.2 , pp. 599-612
    • Ebner, R.1    Derynck, R.2
  • 6
    • 0034281442 scopus 로고    scopus 로고
    • Computational model for effects of ligand/receptor binding properties on interleukin-2 trafficking dynamics and T cell proliferation response
    • Fallon E.M., Lauffenburger D.A. Computational model for effects of ligand/receptor binding properties on interleukin-2 trafficking dynamics and T cell proliferation response. Biotechnol. Prog. 16:2000;905-916
    • (2000) Biotechnol. Prog. , vol.16 , pp. 905-916
    • Fallon, E.M.1    Lauffenburger, D.A.2
  • 7
    • 0029999241 scopus 로고    scopus 로고
    • Basic fibroblast growth factor binds its receptors, is internalized, and stimulates DNA synthesis in Balb/c3T3 cells in the absence of heparan sulfate
    • Fannon M., Nugent M.A. Basic fibroblast growth factor binds its receptors, is internalized, and stimulates DNA synthesis in Balb/c3T3 cells in the absence of heparan sulfate. J. Biol. Chem. 271:1996;17949-17956
    • (1996) J. Biol. Chem. , vol.271 , pp. 17949-17956
    • Fannon, M.1    Nugent, M.A.2
  • 8
    • 0028224965 scopus 로고
    • Postendocytic trafficking of epidermal growth factor-receptor complexes is mediated through saturable and specific endosomal interactions
    • French A.R., Sudlow G.P., Wiley H.S., Lauffenburger D.A. Postendocytic trafficking of epidermal growth factor-receptor complexes is mediated through saturable and specific endosomal interactions. J. Biol. Chem. 269:1994;15749-15755
    • (1994) J. Biol. Chem. , vol.269 , pp. 15749-15755
    • French, A.R.1    Sudlow, G.P.2    Wiley, H.S.3    Lauffenburger, D.A.4
  • 9
    • 0028969961 scopus 로고
    • Intracellular trafficking of epidermal growth factor family ligands is directly by the pH sensitivity of the receptor/ligand interaction
    • French A.R., Tadaki D.K., Niyogi S.K., Lauffenburger D.A. Intracellular trafficking of epidermal growth factor family ligands is directly by the pH sensitivity of the receptor/ligand interaction. J. Biol. Chem. 270:1995;4334-4340
    • (1995) J. Biol. Chem. , vol.270 , pp. 4334-4340
    • French, A.R.1    Tadaki, D.K.2    Niyogi, S.K.3    Lauffenburger, D.A.4
  • 10
    • 0028085865 scopus 로고
    • Quantification of low-density lipoprotein and transferrin endocytotic sorting in hep2 cells using confocal microscopy
    • Ghosh R.N., Gelman D.L., Maxfield F.R. Quantification of low-density lipoprotein and transferrin endocytotic sorting in hep2 cells using confocal microscopy. J. Cell Sci. 107:1994;2177-2189
    • (1994) J. Cell Sci. , vol.107 , pp. 2177-2189
    • Ghosh, R.N.1    Gelman, D.L.2    Maxfield, F.R.3
  • 11
    • 0034685807 scopus 로고    scopus 로고
    • Characterization of rapid membrane internalization and recycling
    • Hao M., Maxfield F.R. Characterization of rapid membrane internalization and recycling. J. Biol. Chem. 275:2000;15279-15286
    • (2000) J. Biol. Chem. , vol.275 , pp. 15279-15286
    • Hao, M.1    Maxfield, F.R.2
  • 13
    • 0025777103 scopus 로고
    • Internalization and down-regulation of the human epidermal growth factor receptor are regulated by the carboxyl-terminal tyrosines
    • Helin K., Beguinot L. Internalization and down-regulation of the human epidermal growth factor receptor are regulated by the carboxyl-terminal tyrosines. J. Biol. Chem. 266:1991;8363-8368
    • (1991) J. Biol. Chem. , vol.266 , pp. 8363-8368
    • Helin, K.1    Beguinot, L.2
  • 14
    • 2642575321 scopus 로고
    • The rate equations of consecutive reactions
    • Hill T.A. The rate equations of consecutive reactions. J. Am. Chem. Soc. 64:1942;465-467
    • (1942) J. Am. Chem. Soc. , vol.64 , pp. 465-467
    • Hill, T.A.1
  • 19
    • 0022871191 scopus 로고
    • Progesterone receptor synthesis and degradation in MCF-7 human breast cancer cells as studied by dense amino acid incorporation. Evidence for a non-hormone binding receptor precursor
    • Mullick A., Katzenellenbogen B.S. Progesterone receptor synthesis and degradation in MCF-7 human breast cancer cells as studied by dense amino acid incorporation. Evidence for a non-hormone binding receptor precursor. J. Biol. Chem. 261:1986;13236-13246
    • (1986) J. Biol. Chem. , vol.261 , pp. 13236-13246
    • Mullick, A.1    Katzenellenbogen, B.S.2
  • 20
    • 0023654775 scopus 로고
    • Binding, internalization, and intracellular processing of protein ligands
    • Myers A.C., Kovach J.S., Vuk-Pavlovic S. Binding, internalization, and intracellular processing of protein ligands. J. Biol. Chem. 262:1987;6494-6499
    • (1987) J. Biol. Chem. , vol.262 , pp. 6494-6499
    • Myers, A.C.1    Kovach, J.S.2    Vuk-Pavlovic, S.3
  • 21
    • 0023664107 scopus 로고
    • Receptor mediated endocytosis in Xenopus Oocytes. II. Evidence for two novel mechanisms of hormonal regulation
    • Opresko L.K., Wiley S.H. Receptor mediated endocytosis in Xenopus Oocytes. II. Evidence for two novel mechanisms of hormonal regulation. J. Biol. Chem. 262:1987;4116-4123
    • (1987) J. Biol. Chem. , vol.262 , pp. 4116-4123
    • Opresko, L.K.1    Wiley, S.H.2
  • 22
    • 0032479156 scopus 로고    scopus 로고
    • High-affinity binding of epidermal growth factor (EGF) to EGF receptor is disrupted by overexpression of mutant dynamin (K44A)
    • Ringerike T., Stang E., Johannessen L.E., Sandnes D., Levy F.O., Madshus I.H. High-affinity binding of epidermal growth factor (EGF) to EGF receptor is disrupted by overexpression of mutant dynamin (K44A). J. Biol. Chem. 273:1998;16639-16642
    • (1998) J. Biol. Chem. , vol.273 , pp. 16639-16642
    • Ringerike, T.1    Stang, E.2    Johannessen, L.E.3    Sandnes, D.4    Levy, F.O.5    Madshus, I.H.6
  • 23
    • 0001436528 scopus 로고
    • On the geometry of transient relaxation
    • Roussel M.R., Fraser S.J. On the geometry of transient relaxation. J. Chem. Phys. 94:1991;7106-7113
    • (1991) J. Chem. Phys. , vol.94 , pp. 7106-7113
    • Roussel, M.R.1    Fraser, S.J.2
  • 24
    • 0018797992 scopus 로고
    • Analysis of the quasi-steady-state approximation for an enzymatic one-substrate reaction
    • Schauer M., Heinrich R. Analysis of the quasi-steady-state approximation for an enzymatic one-substrate reaction. J. Theor. Biol. 79:1979;425-442
    • (1979) J. Theor. Biol. , vol.79 , pp. 425-442
    • Schauer, M.1    Heinrich, R.2
  • 25
    • 0033778534 scopus 로고    scopus 로고
    • Enzyme kinetics at high enzyme concentration
    • Schnell S., Maini P.K. Enzyme kinetics at high enzyme concentration. Bull. Math. Biol. 62:2000;483-499
    • (2000) Bull. Math. Biol. , vol.62 , pp. 483-499
    • Schnell, S.1    Maini, P.K.2
  • 26
    • 0031582628 scopus 로고    scopus 로고
    • A closed-form solution for time-dependent enzyme kinetic
    • Schnell S., Mendoza C. A closed-form solution for time-dependent enzyme kinetic. J. Theor. Biol. 187:1997;207-212
    • (1997) J. Theor. Biol. , vol.187 , pp. 207-212
    • Schnell, S.1    Mendoza, C.2
  • 27
    • 0033789559 scopus 로고    scopus 로고
    • Time-dependent closed form solution for fully competitive enzyme reactions
    • Schnell S., Mendoza C. Time-dependent closed form solution for fully competitive enzyme reactions. Bull. Math. Biol. 62:2000;321-336
    • (2000) Bull. Math. Biol. , vol.62 , pp. 321-336
    • Schnell, S.1    Mendoza, C.2
  • 28
    • 0034339080 scopus 로고    scopus 로고
    • Enzyme kinetics of multiple alternative substrates
    • Schnell S., Mendoza C. Enzyme kinetics of multiple alternative substrates. J. Math. Chem. 27:2000;155-170
    • (2000) J. Math. Chem. , vol.27 , pp. 155-170
    • Schnell, S.1    Mendoza, C.2
  • 29
    • 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.D., Muller G. Computational modeling of the dynamics of the MAP kinase cascade activated by surface and internalized EGF receptors. Nature Biotech. 20:2002;370-375
    • (2002) Nature Biotech. , vol.20 , pp. 370-375
    • Schoeberl, B.1    Eichler-Jonsson, C.2    Gilles, E.D.3    Muller, G.4
  • 30
    • 0024390310 scopus 로고
    • Kinetics of internalization and degradation of I-labeled follicle-stimulating hormone in mouse sertoli cells and its relevance to other systems
    • Shimizu A., Kawashima S. Kinetics of internalization and degradation of I-labeled follicle-stimulating hormone in mouse sertoli cells and its relevance to other systems. J. Biol. Chem. 264:1989;13632-13638
    • (1989) J. Biol. Chem. , vol.264 , pp. 13632-13638
    • Shimizu, A.1    Kawashima, S.2
  • 31
    • 0037178805 scopus 로고    scopus 로고
    • Effect of tyrosine kinase inhibitors on clathrin-coated pit recruitment and internalization of epidermal growth factor receptor
    • Sorkina T., Huang F., Beguinot L., Sorkin A. Effect of tyrosine kinase inhibitors on clathrin-coated pit recruitment and internalization of epidermal growth factor receptor. J. Biol. Chem. 277:2002;27433-27441
    • (2002) J. Biol. Chem. , vol.277 , pp. 27433-27441
    • Sorkina, T.1    Huang, F.2    Beguinot, L.3    Sorkin, A.4
  • 32
    • 0026833077 scopus 로고
    • Mathematical model for the effects of epidermal growth factor receptor trafficking dynamics on fibroblast proliferation responses
    • Starbuck C., Lauffenburger D.A. Mathematical model for the effects of epidermal growth factor receptor trafficking dynamics on fibroblast proliferation responses. Biotechnol. Prog. 8:1992;132-143
    • (1992) Biotechnol. Prog. , vol.8 , pp. 132-143
    • Starbuck, C.1    Lauffenburger, D.A.2
  • 33
    • 0037417886 scopus 로고    scopus 로고
    • Identification of nucleocytoplasmic cycling as a remote sensor in cellular signaling by database modeling
    • Swameye I., Muller T.G., Timmer J., Sandra O., Klingmuler U. Identification of nucleocytoplasmic cycling as a remote sensor in cellular signaling by database modeling. Proc. Natl Acad. Sci. USA. 100:2003;1028-1033
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1028-1033
    • Swameye, I.1    Muller, T.G.2    Timmer, J.3    Sandra, O.4    Klingmuler, U.5
  • 34
    • 0344395658 scopus 로고    scopus 로고
    • Michaelis-menten enzyme kinetics at high enzyme concentrations
    • Tzafriri A.R. Michaelis-menten enzyme kinetics at high enzyme concentrations. Bull. Math. Biol. 65:2003;1111-1129
    • (2003) Bull. Math. Biol. , vol.65 , pp. 1111-1129
    • Tzafriri, A.R.1
  • 35
    • 0344393718 scopus 로고    scopus 로고
    • The total quasi steady state approximation is valid for reversible enzyme kinetics
    • Tzafriri A.R., Edelman E.R. The total quasi steady state approximation is valid for reversible enzyme kinetics. J. Theor. Biol. 226:2004;303-313
    • (2004) J. Theor. Biol. , vol.226 , pp. 303-313
    • Tzafriri, A.R.1    Edelman, E.R.2
  • 36
    • 0035997003 scopus 로고    scopus 로고
    • Reaction diffusion model of the enzymatic erosion of insoluble fibrillar matrices
    • Tzafriri A.R., Bercovier M., Parnas H. Reaction diffusion model of the enzymatic erosion of insoluble fibrillar matrices. Biophys. J. 83:2002;776-793
    • (2002) Biophys. J. , vol.83 , pp. 776-793
    • Tzafriri, A.R.1    Bercovier, M.2    Parnas, H.3
  • 38
    • 0025240654 scopus 로고
    • Rate constants of binding, dissociation, and internalization of EGF: Effect of receptor occupancy and ligand concentration
    • Waters C.M., Oberg K.C., Carpenter G., Overholser K.A. Rate constants of binding, dissociation, and internalization of EGF. effect of receptor occupancy and ligand concentration Biochemistry. 29:1990;3563-3569
    • (1990) Biochemistry , vol.29 , pp. 3563-3569
    • Waters, C.M.1    Oberg, K.C.2    Carpenter, G.3    Overholser, K.A.4
  • 39
    • 0019404817 scopus 로고
    • A steady state model for analyzing the cellular binding, internalization and degradation of polypeptide ligands
    • Wiley S.H., Cunningham D.D. A steady state model for analyzing the cellular binding, internalization and degradation of polypeptide ligands. Cell. 25:1981;433-440
    • (1981) Cell. , vol.25 , pp. 433-440
    • Wiley, S.H.1    Cunningham, D.D.2
  • 40
    • 0019945866 scopus 로고
    • The endocytotic rate constant: A cellular parameter for quantifying receptor-mediated endocytosis
    • Wiley S.H., Cunningham D.D. The endocytotic rate constant. a cellular parameter for quantifying receptor-mediated endocytosis J. Biol. Chem. 257:1982;4222-4229
    • (1982) J. Biol. Chem. , vol.257 , pp. 4222-4229
    • Wiley, S.H.1    Cunningham, D.D.2
  • 41
    • 0037213006 scopus 로고    scopus 로고
    • Computational modeling of the EGF-receptor system: A paradigm for system biology
    • Wiley S.H., Shvartsman S.Y., Lauffenburger D.A. Computational modeling of the EGF-receptor system. a paradigm for system biology Trends Cell Biol. 13:2003;43-50
    • (2003) Trends Cell Biol. , vol.13 , pp. 43-50
    • Wiley, S.H.1    Shvartsman, S.Y.2    Lauffenburger, D.A.3
  • 42
    • 0020026141 scopus 로고
    • Kinetic analysis of chemotactic peptide receptor modulation
    • Zigmond S., Sullivan S.J., Lauffenburger D.A. Kinetic analysis of chemotactic peptide receptor modulation. J. Cell Biol. 92:1982;34-43
    • (1982) J. Cell Biol. , vol.92 , pp. 34-43
    • Zigmond, S.1    Sullivan, S.J.2    Lauffenburger, D.A.3


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