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Volumn 3, Issue 4, 2009, Pages 308-320

Endocytosis and signalling: A meeting with mathematics

Author keywords

Endocytosis; Mathematical modelling; Signal transduction; Spatial gradients; Spatiotemporal dynamics

Indexed keywords

CELL POLARITY; DYNAMICS; ENDOCYTOSIS; ENDOSOME; MATHEMATICAL MODEL; MEMBRANE TRANSPORT; PRIORITY JOURNAL; REVIEW; SIGNAL TRANSDUCTION; SIMULATION; TRANSPORT KINETICS;

EID: 67949101916     PISSN: 15747891     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molonc.2009.05.009     Document Type: Review
Times cited : (31)

References (88)
  • 1
    • 51049105989 scopus 로고    scopus 로고
    • Effect of antigen turnover rate and expression level on antibody penetration into tumor spheroids
    • Ackerman M.E., Pawlowski D., and Wittrup K.D. Effect of antigen turnover rate and expression level on antibody penetration into tumor spheroids. Mol. Cancer. Ther. 7 (2008) 2233-2240
    • (2008) Mol. Cancer. Ther. , vol.7 , pp. 2233-2240
    • Ackerman, M.E.1    Pawlowski, D.2    Wittrup, K.D.3
  • 2
    • 0024364294 scopus 로고
    • Binding, internalization, and intracellular processing of proteins interacting with recycling receptors. A kinetic analysis
    • Bajzer Z., Myers A.C., and Vuk-Pavlovic S. Binding, internalization, and intracellular processing of proteins interacting with recycling receptors. A kinetic analysis. J. Biol. Chem. 264 (1989) 13623-13631
    • (1989) J. Biol. Chem. , vol.264 , pp. 13623-13631
    • Bajzer, Z.1    Myers, A.C.2    Vuk-Pavlovic, S.3
  • 3
    • 34548267667 scopus 로고    scopus 로고
    • Endocytic mechanisms for targeted drug delivery
    • Bareford L.M., and Swaan P.W. Endocytic mechanisms for targeted drug delivery. Adv. Drug. Deliv. Rev. 59 (2007) 748-758
    • (2007) Adv. Drug. Deliv. Rev. , vol.59 , pp. 748-758
    • Bareford, L.M.1    Swaan, P.W.2
  • 4
    • 34447524004 scopus 로고    scopus 로고
    • Clathrin-coated pits: vive la difference?
    • Benmerah A., and Lamaze C. Clathrin-coated pits: vive la difference?. Traffic 8 (2007) 970-982
    • (2007) Traffic , vol.8 , pp. 970-982
    • Benmerah, A.1    Lamaze, C.2
  • 7
    • 0020670915 scopus 로고
    • Distribution of receptors for transferrin and low density lipoprotein on the surface of giant HeLa cells
    • Bretscher M.S. Distribution of receptors for transferrin and low density lipoprotein on the surface of giant HeLa cells. Proc. Natl. Acad. Sci. U S A 80 (1983) 454-458
    • (1983) Proc. Natl. Acad. Sci. U S A , vol.80 , pp. 454-458
    • Bretscher, M.S.1
  • 8
    • 0032864252 scopus 로고    scopus 로고
    • Spatial gradients of cellular phospho-proteins
    • Brown G.C., and Kholodenko B.N. Spatial gradients of cellular phospho-proteins. FEBS Lett. 457 (1999) 452-454
    • (1999) FEBS Lett. , vol.457 , pp. 452-454
    • Brown, G.C.1    Kholodenko, B.N.2
  • 9
    • 53749092962 scopus 로고    scopus 로고
    • Rab-coupling protein coordinates recycling of alpha5beta1 integrin and EGFR1 to promote cell migration in 3D microenvironments
    • Caswell P.T., Chan M., Lindsay A.J., McCaffrey M.W., Boettiger D., and Norman J.C. Rab-coupling protein coordinates recycling of alpha5beta1 integrin and EGFR1 to promote cell migration in 3D microenvironments. J. Cell. Biol. 183 (2008) 143-155
    • (2008) J. Cell. Biol. , vol.183 , pp. 143-155
    • Caswell, P.T.1    Chan, M.2    Lindsay, A.J.3    McCaffrey, M.W.4    Boettiger, D.5    Norman, J.C.6
  • 10
    • 0031554430 scopus 로고    scopus 로고
    • A mathematical model of the trafficking of acid-dependent enveloped viruses: application to the binding, uptake, and nuclear accumulation of baculovirus
    • Dee K.U., and Shuler M.L. A mathematical model of the trafficking of acid-dependent enveloped viruses: application to the binding, uptake, and nuclear accumulation of baculovirus. Biotechnol. Bioeng. 54 (1997) 468-490
    • (1997) Biotechnol. Bioeng. , vol.54 , pp. 468-490
    • Dee, K.U.1    Shuler, M.L.2
  • 11
    • 0035854367 scopus 로고    scopus 로고
    • Endocytosis and signaling. an inseparable partnership
    • Di Fiore P.P., and De Camilli P. Endocytosis and signaling. an inseparable partnership. Cell 106 (2001) 1-4
    • (2001) Cell , vol.106 , pp. 1-4
    • Di Fiore, P.P.1    De Camilli, P.2
  • 12
    • 67949097262 scopus 로고    scopus 로고
    • Endocytosis and spatial restriction of cell signalling
    • Disanza A., Frittoli E., Palamidessi A., and Scita G. Endocytosis and spatial restriction of cell signalling. Mol. Oncol. 3 (2009) 280-296
    • (2009) Mol. Oncol. , vol.3 , pp. 280-296
    • Disanza, A.1    Frittoli, E.2    Palamidessi, A.3    Scita, G.4
  • 13
    • 67949117039 scopus 로고    scopus 로고
    • Endocytosis, asymmetric cell division, stem cells and cancer: Unus pro omnibus, omnes pro uno
    • Fürthauer M., and González-Gaitán M. Endocytosis, asymmetric cell division, stem cells and cancer: Unus pro omnibus, omnes pro uno. Mol. Oncol. 3 (2009) 339-353
    • (2009) Mol. Oncol. , vol.3 , pp. 339-353
    • Fürthauer, M.1    González-Gaitán, M.2
  • 14
    • 0021520019 scopus 로고
    • Receptor-mediated endocytosis: a model and its implications for experimental analysis
    • Gex-Fabry M., and DeLisi C. Receptor-mediated endocytosis: a model and its implications for experimental analysis. Am. J. Physiol. 247 (1984) R768-R779
    • (1984) Am. J. Physiol. , vol.247
    • Gex-Fabry, M.1    DeLisi, C.2
  • 15
    • 0023870554 scopus 로고
    • The distribution of cell surface proteins on spreading cells. Comparison of theory with experiment
    • Goldstein B., and Wiegel F.W. The distribution of cell surface proteins on spreading cells. Comparison of theory with experiment. Biophys. J. 53 (1988) 175-184
    • (1988) Biophys. J. , vol.53 , pp. 175-184
    • Goldstein, B.1    Wiegel, F.W.2
  • 16
    • 0037542854 scopus 로고    scopus 로고
    • Ras proteins: different signals from different locations
    • Hancock J.F. Ras proteins: different signals from different locations. Nat. Rev. Mol. Cell Biol. 4 (2003) 373-384
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 373-384
    • Hancock, J.F.1
  • 17
    • 0030997605 scopus 로고    scopus 로고
    • Kinetics of low-density lipoprotein receptor activity in Hep-G2 cells: derivation and validation of a Briggs-Haldane-based kinetic model for evaluating receptor-mediated endocytotic processes in which receptors recycle
    • Harwood Jr. H.J., and Pellarin L.D. Kinetics of low-density lipoprotein receptor activity in Hep-G2 cells: derivation and validation of a Briggs-Haldane-based kinetic model for evaluating receptor-mediated endocytotic processes in which receptors recycle. Biochem. J. 323 Pt 3 (1997) 649-659
    • (1997) Biochem. J. , vol.323 , Issue.PART 3 , pp. 649-659
    • Harwood Jr., H.J.1    Pellarin, L.D.2
  • 18
    • 28644439423 scopus 로고    scopus 로고
    • The inhibitory effect of ErbB2 on epidermal growth factor-induced formation of clathrin-coated pits correlates with retention of epidermal growth factor receptor-ErbB2 oligomeric complexes at the plasma membrane
    • Haslekas C., Breen K., Pedersen K.W., Johannessen L.E., Stang E., and Madshus I.H. The inhibitory effect of ErbB2 on epidermal growth factor-induced formation of clathrin-coated pits correlates with retention of epidermal growth factor receptor-ErbB2 oligomeric complexes at the plasma membrane. Mol. Biol. Cell 16 (2005) 5832-5842
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5832-5842
    • Haslekas, C.1    Breen, K.2    Pedersen, K.W.3    Johannessen, L.E.4    Stang, E.5    Madshus, I.H.6
  • 19
    • 3042843443 scopus 로고    scopus 로고
    • Localization of receptor-mediated signal transduction pathways: the inside story
    • Haugh J.M. Localization of receptor-mediated signal transduction pathways: the inside story. Mol. Interv. 2 (2002) 292-307
    • (2002) Mol. Interv. , vol.2 , pp. 292-307
    • Haugh, J.M.1
  • 20
    • 0033607542 scopus 로고    scopus 로고
    • Internalized epidermal growth factor receptors participate in the activation of p21(ras) in fibroblasts
    • Haugh J.M., Huang A.C., Wiley H.S., Wells A., and Lauffenburger D.A. Internalized epidermal growth factor receptors participate in the activation of p21(ras) in fibroblasts. J. Biol. Chem. 274 (1999) 34350-34360
    • (1999) J. Biol. Chem. , vol.274 , pp. 34350-34360
    • Haugh, J.M.1    Huang, A.C.2    Wiley, H.S.3    Wells, A.4    Lauffenburger, D.A.5
  • 21
    • 0033605563 scopus 로고    scopus 로고
    • Effect of epidermal growth factor receptor internalization on regulation of the phospholipase C-gamma1 signaling pathway
    • Haugh J.M., Schooler K., Wells A., Wiley H.S., and Lauffenburger D.A. Effect of epidermal growth factor receptor internalization on regulation of the phospholipase C-gamma1 signaling pathway. J. Biol. Chem. 274 (1999) 8958-8965
    • (1999) J. Biol. Chem. , vol.274 , pp. 8958-8965
    • Haugh, J.M.1    Schooler, K.2    Wells, A.3    Wiley, H.S.4    Lauffenburger, D.A.5
  • 22
    • 31444453554 scopus 로고    scopus 로고
    • Computational modelling of ErbB family phosphorylation dynamics in response to transforming growth factor alpha and heregulin indicates spatial compartmentation of phosphatase activity
    • Hendriks B.S., Cook J., Burke J.M., Beusmans J.M., Lauffenburger D.A., and de Graaf D. Computational modelling of ErbB family phosphorylation dynamics in response to transforming growth factor alpha and heregulin indicates spatial compartmentation of phosphatase activity. Syst. Biol. (Stevenage) 153 (2006) 22-33
    • (2006) Syst. Biol. (Stevenage) , vol.153 , pp. 22-33
    • Hendriks, B.S.1    Cook, J.2    Burke, J.M.3    Beusmans, J.M.4    Lauffenburger, D.A.5    de Graaf, D.6
  • 23
    • 0037931402 scopus 로고    scopus 로고
    • Quantitative analysis of HER2-mediated effects on HER2 and epidermal growth factor receptor endocytosis: distribution of homo- and heterodimers depends on relative HER2 levels
    • Hendriks B.S., Opresko L.K., Wiley H.S., and Lauffenburger D. Quantitative analysis of HER2-mediated effects on HER2 and epidermal growth factor receptor endocytosis: distribution of homo- and heterodimers depends on relative HER2 levels. J. Biol. Chem. 278 (2003) 23343-23351
    • (2003) J. Biol. Chem. , vol.278 , pp. 23343-23351
    • Hendriks, B.S.1    Opresko, L.K.2    Wiley, H.S.3    Lauffenburger, D.4
  • 24
    • 14044276994 scopus 로고    scopus 로고
    • Parsing ERK activation reveals quantitatively equivalent contributions from epidermal growth factor receptor and HER2 in human mammary epithelial cells
    • Hendriks B.S., Orr G., Wells A., Wiley H.S., and Lauffenburger D.A. Parsing ERK activation reveals quantitatively equivalent contributions from epidermal growth factor receptor and HER2 in human mammary epithelial cells. J. Biol. Chem. 280 (2005) 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
  • 25
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke L., and Dunn R. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu. Rev. Cell Dev. Biol. 19 (2003) 141-172
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 26
    • 9244234674 scopus 로고    scopus 로고
    • Fast vesicle transport in PC12 neurites: velocities and forces
    • Hill D.B., Plaza M.J., Bonin K., and Holzwarth G. Fast vesicle transport in PC12 neurites: velocities and forces. Eur. Biophys. J. 33 (2004) 623-632
    • (2004) Eur. Biophys. J. , vol.33 , pp. 623-632
    • Hill, D.B.1    Plaza, M.J.2    Bonin, K.3    Holzwarth, G.4
  • 27
    • 0028321736 scopus 로고
    • Insulin-stimulated GLUT4 glucose transporter recycling. A problem in membrane protein subcellular trafficking through multiple pools
    • Holman G.D., Lo Leggio L., and Cushman S.W. Insulin-stimulated GLUT4 glucose transporter recycling. A problem in membrane protein subcellular trafficking through multiple pools. J. Biol. Chem. 269 (1994) 17516-17524
    • (1994) J. Biol. Chem. , vol.269 , pp. 17516-17524
    • Holman, G.D.1    Lo Leggio, L.2    Cushman, S.W.3
  • 28
    • 0842333853 scopus 로고    scopus 로고
    • Signaling endosome hypothesis: a cellular mechanism for long distance communication
    • Howe C.L., and Mobley W.C. Signaling endosome hypothesis: a cellular mechanism for long distance communication. J. Neurobiol. 58 (2004) 207-216
    • (2004) J. Neurobiol. , vol.58 , pp. 207-216
    • Howe, C.L.1    Mobley, W.C.2
  • 29
    • 33644852909 scopus 로고    scopus 로고
    • Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain
    • Huang F., Kirkpatrick D., Jiang X., Gygi S., and Sorkin A. Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol. Cell 21 (2006) 737-748
    • (2006) Mol. Cell , vol.21 , pp. 737-748
    • Huang, F.1    Kirkpatrick, D.2    Jiang, X.3    Gygi, S.4    Sorkin, A.5
  • 30
    • 22944455544 scopus 로고    scopus 로고
    • Regulators of endocytosis maintain localized receptor tyrosine kinase signaling in guided migration
    • Jekely G., Sung H.H., Luque C.M., and Rorth P. Regulators of endocytosis maintain localized receptor tyrosine kinase signaling in guided migration. Dev. Cell 9 (2005) 197-207
    • (2005) Dev. Cell , vol.9 , pp. 197-207
    • Jekely, G.1    Sung, H.H.2    Luque, C.M.3    Rorth, P.4
  • 31
    • 0035999983 scopus 로고    scopus 로고
    • Coordinated traffic of Grb2 and Ras during epidermal growth factor receptor endocytosis visualized in living cells
    • Jiang X., and Sorkin A. Coordinated traffic of Grb2 and Ras during epidermal growth factor receptor endocytosis visualized in living cells. Mol. Biol. Cell 13 (2002) 1522-1535
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1522-1535
    • Jiang, X.1    Sorkin, A.2
  • 32
    • 34548172649 scopus 로고    scopus 로고
    • Macropinocytosis: searching for an endocytic identity and role in the uptake of cell penetrating peptides
    • Jones A.T. Macropinocytosis: searching for an endocytic identity and role in the uptake of cell penetrating peptides. J. Cell Mol. Med. 11 (2007) 670-684
    • (2007) J. Cell Mol. Med. , vol.11 , pp. 670-684
    • Jones, A.T.1
  • 33
    • 0037192461 scopus 로고    scopus 로고
    • Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts
    • Kalab P., Weis K., and Heald R. Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts. Science 295 (2002) 2452-2456
    • (2002) Science , vol.295 , pp. 2452-2456
    • Kalab, P.1    Weis, K.2    Heald, R.3
  • 34
    • 67949093073 scopus 로고    scopus 로고
    • Four-dimensional dynamics of MAPK information-processing systems
    • Kholodenko B.N., and Birtwistle M.R. Four-dimensional dynamics of MAPK information-processing systems. WIREs: Syst. Biol. Med. 1 (2009) 28-44
    • (2009) WIREs: Syst. Biol. Med. , vol.1 , pp. 28-44
    • Kholodenko, B.N.1    Birtwistle, M.R.2
  • 35
    • 0036536713 scopus 로고    scopus 로고
    • MAP kinase cascade signaling and endocytic trafficking: a marriage of convenience?
    • Kholodenko B.N. MAP kinase cascade signaling and endocytic trafficking: a marriage of convenience?. Trends Cell Biol. 12 (2002) 173-177
    • (2002) Trends Cell Biol. , vol.12 , pp. 173-177
    • Kholodenko, B.N.1
  • 36
    • 0038608273 scopus 로고    scopus 로고
    • Four-dimensional organization of protein kinase signaling cascades: the roles of diffusion, endocytosis and molecular motors
    • Kholodenko B.N. Four-dimensional organization of protein kinase signaling cascades: the roles of diffusion, endocytosis and molecular motors. J. Exp. Biol. 206 (2003) 2073-2082
    • (2003) J. Exp. Biol. , vol.206 , pp. 2073-2082
    • Kholodenko, B.N.1
  • 37
    • 33644524741 scopus 로고    scopus 로고
    • Cell-signalling dynamics in time and space
    • Kholodenko B.N. Cell-signalling dynamics in time and space. Nat. Rev. Mol. Cell Biol. 7 (2006) 165-176
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 165-176
    • Kholodenko, B.N.1
  • 38
    • 33847392514 scopus 로고    scopus 로고
    • Untangling the signalling wires
    • Kholodenko B.N. Untangling the signalling wires. Nat. Cell Biol. 9 (2007) 247-249
    • (2007) Nat. Cell Biol. , vol.9 , pp. 247-249
    • Kholodenko, B.N.1
  • 39
    • 0033570090 scopus 로고    scopus 로고
    • Quantification of short term signaling by the epidermal growth factor receptor
    • Kholodenko B.N., Demin O.V., Moehren G., and Hoek J.B. Quantification of short term signaling by the epidermal growth factor receptor. J. Biol. Chem. 274 (1999) 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
  • 40
    • 27644575157 scopus 로고    scopus 로고
    • Coordinating ERK/MAPK signalling through scaffolds and inhibitors
    • Kolch W. Coordinating ERK/MAPK signalling through scaffolds and inhibitors. Nat. Rev. Mol. Cell Biol. 6 (2005) 827-837
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 827-837
    • Kolch, W.1
  • 41
    • 33747165872 scopus 로고    scopus 로고
    • Vascular endothelial cadherin controls VEGFR-2 internalization and signaling from intracellular compartments
    • Lampugnani M.G., Orsenigo F., Gagliani M.C., Tacchetti C., and Dejana E. Vascular endothelial cadherin controls VEGFR-2 internalization and signaling from intracellular compartments. J. Cell Biol. 174 (2006) 593-604
    • (2006) J. Cell Biol. , vol.174 , pp. 593-604
    • Lampugnani, M.G.1    Orsenigo, F.2    Gagliani, M.C.3    Tacchetti, C.4    Dejana, E.5
  • 42
    • 15844395340 scopus 로고    scopus 로고
    • Characterization of endocytic vesicles using magnetic microbeads coated with signalling ligands
    • Li H.S., Stolz D.B., and Romero G. Characterization of endocytic vesicles using magnetic microbeads coated with signalling ligands. Traffic 6 (2005) 324-334
    • (2005) Traffic , vol.6 , pp. 324-334
    • Li, H.S.1    Stolz, D.B.2    Romero, G.3
  • 43
    • 0025160570 scopus 로고
    • Quantitative analysis of the endocytic system involved in hormone-induced receptor internalization
    • Lund K.A., Opresko L.K., Starbuck C., Walsh B.J., and Wiley H.S. Quantitative analysis of the endocytic system involved in hormone-induced receptor internalization. J. Biol. Chem. 265 (1990) 15713-15723
    • (1990) J. Biol. Chem. , vol.265 , pp. 15713-15723
    • Lund, K.A.1    Opresko, L.K.2    Starbuck, C.3    Walsh, B.J.4    Wiley, H.S.5
  • 45
    • 0037154885 scopus 로고    scopus 로고
    • Retrograde support of neuronal survival without retrograde transport of nerve growth factor
    • MacInnis B.L., and Campenot R.B. Retrograde support of neuronal survival without retrograde transport of nerve growth factor. Science 295 (2002) 1536-1539
    • (2002) Science , vol.295 , pp. 1536-1539
    • MacInnis, B.L.1    Campenot, R.B.2
  • 46
    • 0142090754 scopus 로고    scopus 로고
    • Spatial requirements for TrkA kinase activity in the support of neuronal survival and axon growth in rat sympathetic neurons
    • MacInnis B.L., Senger D.L., and Campenot R.B. Spatial requirements for TrkA kinase activity in the support of neuronal survival and axon growth in rat sympathetic neurons. Neuropharmacology 45 (2003) 995-1010
    • (2003) Neuropharmacology , vol.45 , pp. 995-1010
    • MacInnis, B.L.1    Senger, D.L.2    Campenot, R.B.3
  • 47
    • 35748968807 scopus 로고    scopus 로고
    • Spatial regulation of Fus3 MAP kinase activity through a reaction-diffusion mechanism in yeast pheromone signalling
    • Maeder C.I., Hink M.A., Kinkhabwala A., Mayr R., Bastiaens P.I., and Knop M. Spatial regulation of Fus3 MAP kinase activity through a reaction-diffusion mechanism in yeast pheromone signalling. Nat. Cell Biol. 9 (2007) 1319-1326
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1319-1326
    • Maeder, C.I.1    Hink, M.A.2    Kinkhabwala, A.3    Mayr, R.4    Bastiaens, P.I.5    Knop, M.6
  • 48
    • 0031847229 scopus 로고    scopus 로고
    • Sterol-independent, sterol response element-dependent, regulation of low density lipoprotein receptor gene expression
    • Makar R.S., Lipsky P.E., and Cuthbert J.A. Sterol-independent, sterol response element-dependent, regulation of low density lipoprotein receptor gene expression. J. Lipid Res. 39 (1998) 1647-1654
    • (1998) J. Lipid Res. , vol.39 , pp. 1647-1654
    • Makar, R.S.1    Lipsky, P.E.2    Cuthbert, J.A.3
  • 49
    • 34147175165 scopus 로고    scopus 로고
    • Endocytosis optimizes the dynamic localization of membrane proteins that regulate cortical polarity
    • Marco E., Wedlich-Soldner R., Li R., Altschuler S.J., and Wu L.F. Endocytosis optimizes the dynamic localization of membrane proteins that regulate cortical polarity. Cell 129 (2007) 411-422
    • (2007) Cell , vol.129 , pp. 411-422
    • Marco, E.1    Wedlich-Soldner, R.2    Li, R.3    Altschuler, S.J.4    Wu, L.F.5
  • 50
    • 33846042014 scopus 로고    scopus 로고
    • Long-range signaling by phosphoprotein waves arising from bistability in protein kinase cascades
    • Markevich N.I., Tsyganov M.A., Hoek J.B., and Kholodenko B.N. Long-range signaling by phosphoprotein waves arising from bistability in protein kinase cascades. Mol. Syst. Biol. 2 (2006) 61
    • (2006) Mol. Syst. Biol. , vol.2 , pp. 61
    • Markevich, N.I.1    Tsyganov, M.A.2    Hoek, J.B.3    Kholodenko, B.N.4
  • 51
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation
    • Marshall C.J. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80 (1995) 179-185
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 52
    • 33947547741 scopus 로고    scopus 로고
    • Quantitative transcriptional control of ErbB receptor signaling undergoes graded to biphasic response for cell differentiation
    • Nagashima T., Shimodaira H., Ide K., Nakakuki T., Tani Y., Takahashi K., Yumoto N., and Hatakeyama M. Quantitative transcriptional control of ErbB receptor signaling undergoes graded to biphasic response for cell differentiation. J. Biol. Chem. 282 (2007) 4045-4056
    • (2007) J. Biol. Chem. , vol.282 , pp. 4045-4056
    • Nagashima, T.1    Shimodaira, H.2    Ide, K.3    Nakakuki, T.4    Tani, Y.5    Takahashi, K.6    Yumoto, N.7    Hatakeyama, M.8
  • 53
    • 1642322097 scopus 로고    scopus 로고
    • Stathmin-tubulin interaction gradients in motile and mitotic cells
    • Niethammer P., Bastiaens P., and Karsenti E. Stathmin-tubulin interaction gradients in motile and mitotic cells. Science 303 (2004) 1862-1866
    • (2004) Science , vol.303 , pp. 1862-1866
    • Niethammer, P.1    Bastiaens, P.2    Karsenti, E.3
  • 54
    • 0023664107 scopus 로고
    • Receptor-mediated endocytosis in Xenopus oocytes. II. Evidence for two novel mechanisms of hormonal regulation
    • Opresko L.K., and Wiley H.S. 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, H.S.2
  • 55
    • 14644404885 scopus 로고    scopus 로고
    • Vimentin-dependent spatial translocation of an activated MAP kinase in injured nerve
    • Perlson E., Hanz S., Ben-Yaakov K., Segal-Ruder Y., Seger R., and Fainzilber M. Vimentin-dependent spatial translocation of an activated MAP kinase in injured nerve. Neuron 45 (2005) 715-726
    • (2005) Neuron , vol.45 , pp. 715-726
    • Perlson, E.1    Hanz, S.2    Ben-Yaakov, K.3    Segal-Ruder, Y.4    Seger, R.5    Fainzilber, M.6
  • 57
    • 33644769212 scopus 로고    scopus 로고
    • Endocytosis conducts the cell signaling orchestra
    • Polo S., and Di Fiore P.P. Endocytosis conducts the cell signaling orchestra. Cell 124 (2006) 897-900
    • (2006) Cell , vol.124 , pp. 897-900
    • Polo, S.1    Di Fiore, P.P.2
  • 58
    • 67949106368 scopus 로고    scopus 로고
    • Endocytic proteins in the regulation of nuclear signaling, transcription and tumorigenesis
    • Pyrzynska B., Pilecka I., and Miaczynska M. Endocytic proteins in the regulation of nuclear signaling, transcription and tumorigenesis. Mol. Oncol. 3 (2009) 321-338
    • (2009) Mol. Oncol. , vol.3 , pp. 321-338
    • Pyrzynska, B.1    Pilecka, I.2    Miaczynska, M.3
  • 60
    • 0041843750 scopus 로고    scopus 로고
    • An integrated model of epidermal growth factor receptor trafficking and signal transduction
    • Resat H., Ewald J.A., Dixon D.A., and Wiley H.S. An integrated model of epidermal growth factor receptor trafficking and signal transduction. Biophys. J. 85 (2003) 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
  • 61
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • Rink J., Ghigo E., Kalaidzidis Y., and Zerial M. Rab conversion as a mechanism of progression from early to late endosomes. Cell 122 (2005) 735-749
    • (2005) Cell , vol.122 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 62
    • 34547843507 scopus 로고    scopus 로고
    • Kiss-and-run, collapse and 'readily retrievable' vesicles
    • Rizzoli S.O., and Jahn R. Kiss-and-run, collapse and 'readily retrievable' vesicles. Traffic 8 (2007) 1137-1144
    • (2007) Traffic , vol.8 , pp. 1137-1144
    • Rizzoli, S.O.1    Jahn, R.2
  • 63
    • 25844526639 scopus 로고    scopus 로고
    • Molecular and cellular barriers limiting the effectiveness of antisense oligonucleotides
    • Roth C.M. Molecular and cellular barriers limiting the effectiveness of antisense oligonucleotides. Biophys. J. 89 (2005) 2286-2295
    • (2005) Biophys. J. , vol.89 , pp. 2286-2295
    • Roth, C.M.1
  • 65
    • 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., and Muller G. Computational modeling of the dynamics of the MAP kinase cascade activated by surface and internalized EGF receptors. Nat. Biotechnol. 20 (2002) 370-375
    • (2002) Nat. Biotechnol. , vol.20 , pp. 370-375
    • Schoeberl, B.1    Eichler-Jonsson, C.2    Gilles, E.D.3    Muller, G.4
  • 66
    • 34347355576 scopus 로고    scopus 로고
    • Cell surface receptors for signal transduction and ligand transport: a design principles study
    • Shankaran H., Resat H., and Wiley H.S. Cell surface receptors for signal transduction and ligand transport: a design principles study. PLoS Comput. Biol. 3 (2007) e101
    • (2007) PLoS Comput. Biol. , vol.3
    • Shankaran, H.1    Resat, H.2    Wiley, H.S.3
  • 67
    • 39149098113 scopus 로고    scopus 로고
    • Receptor downregulation and desensitization enhance the information processing ability of signalling receptors
    • Shankaran H., Wiley H.S., and Resat H. Receptor downregulation and desensitization enhance the information processing ability of signalling receptors. BMC Syst. Biol. 1 (2007) 48
    • (2007) BMC Syst. Biol. , vol.1 , pp. 48
    • Shankaran, H.1    Wiley, H.S.2    Resat, H.3
  • 68
    • 0033525930 scopus 로고    scopus 로고
    • The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions
    • Sheff D.R., Daro E.A., Hull M., and Mellman I. The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions. J. Cell Biol. 145 (1999) 123-139
    • (1999) J. Cell Biol. , vol.145 , pp. 123-139
    • Sheff, D.R.1    Daro, E.A.2    Hull, M.3    Mellman, I.4
  • 69
    • 62649159446 scopus 로고    scopus 로고
    • Endocytosis and intracellular trafficking of ErbBs
    • Sorkin A., and Goh L.K. Endocytosis and intracellular trafficking of ErbBs. Exp. Cell Res. 315 (2009) 683-696
    • (2009) Exp. Cell Res. , vol.315 , pp. 683-696
    • Sorkin, A.1    Goh, L.K.2
  • 70
    • 0036341207 scopus 로고    scopus 로고
    • Signal transduction and endocytosis: close encounters of many kinds
    • Sorkin A., and Von Zastrow M. Signal transduction and endocytosis: close encounters of many kinds. Nat. Rev. Mol. Cell Biol. 3 (2002) 600-614
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 600-614
    • Sorkin, A.1    Von Zastrow, M.2
  • 71
    • 44849135212 scopus 로고    scopus 로고
    • Quantitative spatiotemporal analysis of antibody fragment diffusion and endocytic consumption in tumor spheroids
    • Thurber G.M., and Wittrup K.D. Quantitative spatiotemporal analysis of antibody fragment diffusion and endocytic consumption in tumor spheroids. Cancer Res. 68 (2008) 3334-3341
    • (2008) Cancer Res. , vol.68 , pp. 3334-3341
    • Thurber, G.M.1    Wittrup, K.D.2
  • 72
    • 0141727533 scopus 로고    scopus 로고
    • Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling
    • Valdez-Taubas J., and Pelham H.R. Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling. Curr. Biol. 13 (2003) 1636-1640
    • (2003) Curr. Biol. , vol.13 , pp. 1636-1640
    • Valdez-Taubas, J.1    Pelham, H.R.2
  • 73
    • 33645754505 scopus 로고    scopus 로고
    • Signal processing in the TGF-beta superfamily ligand-receptor network
    • Vilar J.M., Jansen R., and Sander C. Signal processing in the TGF-beta superfamily ligand-receptor network. PLoS Comput. Biol. 2 (2006) e3
    • (2006) PLoS Comput. Biol. , vol.2
    • Vilar, J.M.1    Jansen, R.2    Sander, C.3
  • 74
    • 0030747463 scopus 로고    scopus 로고
    • Microtubule-dependent transport of secretory vesicles visualized in real time with a GFP-tagged secretory protein
    • Wacker I., Kaether C., Kromer A., Migala A., Almers W., and Gerdes H.H. Microtubule-dependent transport of secretory vesicles visualized in real time with a GFP-tagged secretory protein. J. Cell Sci. 110 Pt 13 (1997) 1453-1463
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 13 , pp. 1453-1463
    • Wacker, I.1    Kaether, C.2    Kromer, A.3    Migala, A.4    Almers, W.5    Gerdes, H.H.6
  • 75
    • 60749087137 scopus 로고    scopus 로고
    • PI3K-dependent cross-talk interactions converge with Ras as quantifiable inputs integrated by Erk
    • Wang C.C., Cirit M., and Haugh J.M. PI3K-dependent cross-talk interactions converge with Ras as quantifiable inputs integrated by Erk. Mol. Syst. Biol. 5 (2009) 246
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 246
    • Wang, C.C.1    Cirit, M.2    Haugh, J.M.3
  • 76
    • 0022443438 scopus 로고
    • Mitogenic agents induce redistribution of transferrin receptors from internal pools to the cell surface
    • Ward D.M., and Kaplan J. Mitogenic agents induce redistribution of transferrin receptors from internal pools to the cell surface. Biochem. J. 238 (1986) 721-728
    • (1986) Biochem. J. , vol.238 , pp. 721-728
    • Ward, D.M.1    Kaplan, J.2
  • 77
    • 0025240654 scopus 로고
    • Rate constants for binding, dissociation, and internalization of EGF: effect of receptor occupancy and ligand concentration
    • Waters C.M., Oberg K.C., Carpenter G., and Overholser K.A. Rate constants for 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
  • 79
    • 0023677140 scopus 로고
    • Anomalous binding of epidermal growth factor to A431 cells is due to the effect of high receptor densities and a saturable endocytic system
    • Wiley H.S. Anomalous binding of epidermal growth factor to A431 cells is due to the effect of high receptor densities and a saturable endocytic system. J. Cell Biol. 107 (1988) 801-810
    • (1988) J. Cell Biol. , vol.107 , pp. 801-810
    • Wiley, H.S.1
  • 80
    • 0019404817 scopus 로고
    • A steady state model for analyzing the cellular binding, internalization and degradation of polypeptide ligands
    • Wiley H.S., and 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, H.S.1    Cunningham, D.D.2
  • 81
    • 0019945866 scopus 로고
    • The endocytotic rate constant. A cellular parameter for quantitating receptor-mediated endocytosis
    • Wiley H.S., and Cunningham D.D. The endocytotic rate constant. A cellular parameter for quantitating receptor-mediated endocytosis. J. Biol. Chem. 257 (1982) 4222-4229
    • (1982) J. Biol. Chem. , vol.257 , pp. 4222-4229
    • Wiley, H.S.1    Cunningham, D.D.2
  • 82
    • 0037213006 scopus 로고    scopus 로고
    • Computational modeling of the EGF-receptor system: a paradigm for systems biology
    • Wiley H.S., Shvartsman S.Y., and Lauffenburger D.A. Computational modeling of the EGF-receptor system: a paradigm for systems biology. Trends Cell Biol. 13 (2003) 43-50
    • (2003) Trends Cell Biol. , vol.13 , pp. 43-50
    • Wiley, H.S.1    Shvartsman, S.Y.2    Lauffenburger, D.A.3
  • 83
    • 34247342216 scopus 로고    scopus 로고
    • The emerging shape of the ESCRT machinery
    • Williams R.L., and Urbe S. The emerging shape of the ESCRT machinery. Nat. Rev. Mol. Cell Biol. 8 (2007) 355-368
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 355-368
    • Williams, R.L.1    Urbe, S.2
  • 84
    • 0025756553 scopus 로고
    • Kinetic analysis of receptor-mediated endocytosis of epidermal growth factor by isolated rat hepatocytes
    • Yanai S., Sugiyama Y., Kim D.C., Iga T., Fuwa T., and Hanano M. Kinetic analysis of receptor-mediated endocytosis of epidermal growth factor by isolated rat hepatocytes. Am. J. Physiol. 260 (1991) C457-467
    • (1991) Am. J. Physiol. , vol.260
    • Yanai, S.1    Sugiyama, Y.2    Kim, D.C.3    Iga, T.4    Fuwa, T.5    Hanano, M.6
  • 86
    • 0028876227 scopus 로고
    • Kinetic analysis of glucose transporter trafficking in fibroblasts and adipocytes
    • Yeh J.I., Verhey K.J., and Birnbaum M.J. Kinetic analysis of glucose transporter trafficking in fibroblasts and adipocytes. Biochemistry 34 (1995) 15523-15531
    • (1995) Biochemistry , vol.34 , pp. 15523-15531
    • Yeh, J.I.1    Verhey, K.J.2    Birnbaum, M.J.3
  • 88
    • 39049089241 scopus 로고    scopus 로고
    • Brownian diffusion and surface kinetics of liposome and viral particle uptake by human lung cancer cells in-vitro
    • Zhu D., Lennon S.P., Peters M.H., Finney W.C., and Singh M. Brownian diffusion and surface kinetics of liposome and viral particle uptake by human lung cancer cells in-vitro. Ann. Biomed. Eng. 34 (2006) 1573-1586
    • (2006) Ann. Biomed. Eng. , vol.34 , pp. 1573-1586
    • Zhu, D.1    Lennon, S.P.2    Peters, M.H.3    Finney, W.C.4    Singh, M.5


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