메뉴 건너뛰기




Volumn 83, Issue 2-3 SPEC. ISS., 2006, Pages 152-166

Trading the micro-world of combinatorial complexity for the macro-world of protein interaction domains

Author keywords

Adapter protein; Complex signaling networks; Model reduction; Scaffold; Time series; Tyrosine kinase receptor

Indexed keywords

MEMBRANE; PROTEIN;

EID: 32044464102     PISSN: 03032647     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biosystems.2005.03.006     Document Type: Conference Paper
Times cited : (32)

References (46)
  • 1
    • 0035895366 scopus 로고    scopus 로고
    • Activation of the insulin receptor's kinase domain changes the rate-determining step of substrate phosphorylation
    • A.J. Ablooglu, and R.A. Kohanski Activation of the insulin receptor's kinase domain changes the rate-determining step of substrate phosphorylation Biochemistry 40 2001 504 513
    • (2001) Biochemistry , vol.40 , pp. 504-513
    • Ablooglu, A.J.1    Kohanski, R.A.2
  • 3
    • 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, and D.A. Lauffenburger A computational study of feedback effects on signal dynamics in a mitogen-activated protein kinase (mapk) pathway model Biotechnol. Prog. 17 2001 227 239
    • (2001) Biotechnol. Prog. , vol.17 , pp. 227-239
    • Asthagiri, A.R.1    Lauffenburger, D.A.2
  • 4
    • 10244219918 scopus 로고    scopus 로고
    • BioNetGen: Software for rule-based modeling of signal transduction based on the interactions of molecular domains
    • M.L. Blinov, J.R. Faeder, B. Goldstein, and W.S. Hlavacek BioNetGen: software for rule-based modeling of signal transduction based on the interactions of molecular domains Bioinformatics 2004
    • (2004) Bioinformatics
    • Blinov, M.L.1    Faeder, J.R.2    Goldstein, B.3    Hlavacek, W.S.4
  • 5
    • 23244465153 scopus 로고    scopus 로고
    • Signaling through receptors and scaffolds: Independent interactions reduce combinatorial complexity
    • N.M. Borisov, N.I. Markevich, J.B. Hoek, and B.N. Kholodenko Signaling through receptors and scaffolds: independent interactions reduce combinatorial complexity Biophys. J. 89 2005 951 966
    • (2005) Biophys. J. , vol.89 , pp. 951-966
    • Borisov, N.M.1    Markevich, N.I.2    Hoek, J.B.3    Kholodenko, B.N.4
  • 6
    • 0031804503 scopus 로고    scopus 로고
    • Signaling complexes: Biophysical constraints on intracellular communication
    • D. Bray Signaling complexes: biophysical constraints on intracellular communication Annu. Rev. Biophys. Biomol. Struct. 27 1998 59 75
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 59-75
    • Bray, D.1
  • 7
  • 10
    • 0001356311 scopus 로고
    • Persistance and smoothness of invariant manifolds for flows
    • N. Fenichel Persistance and smoothness of invariant manifolds for flows Indiana Univ. Math J. 21 1971 193 255
    • (1971) Indiana Univ. Math J. , vol.21 , pp. 193-255
    • Fenichel, N.1
  • 11
    • 33645429016 scopus 로고
    • Exact stochastic simulation of coupled chemical reactions
    • D.T. Gillespie Exact stochastic simulation of coupled chemical reactions J. Phys. Chem. 81 1977 2340 2361
    • (1977) J. Phys. Chem. , vol.81 , pp. 2340-2361
    • Gillespie, D.T.1
  • 13
    • 0033605563 scopus 로고    scopus 로고
    • Effect of epidermal growth factor receptor internalization on regulation of the phospholipase C-gamma1 signaling pathway
    • J.M. Haugh, K. Schooler, A. Wells, H.S. Weley, and D.A. Lauffenburger 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    Weley, H.S.4    Lauffenburger, D.A.5
  • 14
    • 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, and 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. 70 2000 225 238
    • (2000) Biotechnol. Bioeng. , vol.70 , pp. 225-238
    • Haugh, J.M.1    Wells, A.2    Lauffenburger, D.A.3
  • 17
    • 0034614490 scopus 로고    scopus 로고
    • Signaling - 2000 and beyond
    • T. Hunter Signaling - 2000 and beyond Cell 100 2000 113 127
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 18
    • 0032514897 scopus 로고    scopus 로고
    • The Gab1 protein is a docking site for multiple proteins involved in signaling by the B cell antigen receptor
    • R.J. Ingham, M. Holgado-Madruga, C. Siu, A.J. Wong, and M.R. Gold The Gab1 protein is a docking site for multiple proteins involved in signaling by the B cell antigen receptor J. Biol. Chem. 273 1998 30630 30637
    • (1998) J. Biol. Chem. , vol.273 , pp. 30630-30637
    • Ingham, R.J.1    Holgado-Madruga, M.2    Siu, C.3    Wong, A.J.4    Gold, M.R.5
  • 19
    • 0033570090 scopus 로고    scopus 로고
    • Quantification of short term signaling by the epidermal growth factor receptor
    • B.N. Kholodenko, O.V. Demin, G. Moehren, and J.B. Hoek 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
  • 21
    • 0034961694 scopus 로고    scopus 로고
    • STOCHSIM: Modelling of stochastic biomolecular processes
    • N. Le Novere, and T.S. Shimizu STOCHSIM: modelling of stochastic biomolecular processes Bioinformatics 17 2001 575 576
    • (2001) Bioinformatics , vol.17 , pp. 575-576
    • Le Novere, N.1    Shimizu, T.S.2
  • 22
    • 0034609569 scopus 로고    scopus 로고
    • Identification of major tyrosine phosphorylation sites in the human insulin receptor substrate Gab-1 by insulin receptor kinase in vitro
    • S. Lehr, J. Kotzka, A. Herkner, A. Sikmann, H.E. Meyer, W. Krone, and D. Muller-Wieland Identification of major tyrosine phosphorylation sites in the human insulin receptor substrate Gab-1 by insulin receptor kinase in vitro Biochemistry 39 2000 10898 10907
    • (2000) Biochemistry , vol.39 , pp. 10898-10907
    • Lehr, S.1    Kotzka, J.2    Herkner, A.3    Sikmann, A.4    Meyer, H.E.5    Krone, W.6    Muller-Wieland, D.7
  • 23
    • 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, and P.W. Sternberg Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties Proc. Natl. Acad. Sci. U.S.A. 97 2000 5818 5823
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5818-5823
    • Levchenko, A.1    Bruck, J.2    Sternberg, P.W.3
  • 26
    • 0037039289 scopus 로고    scopus 로고
    • Temperature dependence of the epidermal growth factor receptor signaling network can be accounted for by a kinetic model
    • G. Moehren, N. Markevich, O. Demin, A. Kiyatkin, I. Goryanin, J.B. Hoek, and B.N. Kholodenko Temperature dependence of the epidermal growth factor receptor signaling network can be accounted for by a kinetic model Biochemistry 41 2002 306 320
    • (2002) Biochemistry , vol.41 , pp. 306-320
    • Moehren, G.1    Markevich, N.2    Demin, O.3    Kiyatkin, A.4    Goryanin, I.5    Hoek, J.B.6    Kholodenko, B.N.7
  • 27
    • 0032492834 scopus 로고    scopus 로고
    • Predicting temporal fluctuations in an intracellular signalling pathway
    • C.J. Morton-Firth, and D. Bray Predicting temporal fluctuations in an intracellular signalling pathway J. Theor. Biol. 192 1998 117 128
    • (1998) J. Theor. Biol. , vol.192 , pp. 117-128
    • Morton-Firth, C.J.1    Bray, D.2
  • 30
    • 0347660479 scopus 로고    scopus 로고
    • The role of Gab family scaffolding adapter proteins in the signal transduction of cytokine and growth factor receptors
    • K. Nishida, and T. Hirano The role of Gab family scaffolding adapter proteins in the signal transduction of cytokine and growth factor receptors Cancer Sci. 94 2003 1029 1033
    • (2003) Cancer Sci. , vol.94 , pp. 1029-1033
    • Nishida, K.1    Hirano, T.2
  • 31
    • 0034633993 scopus 로고    scopus 로고
    • Mechanism of transmembrane signaling: Insulin binding and the insulin receptor
    • F.P. Ottensmeyer, D.R. Beniac, R.Z. Luo, and C.C. Yip Mechanism of transmembrane signaling: insulin binding and the insulin receptor Biochemistry 39 2000 12103 12112
    • (2000) Biochemistry , vol.39 , pp. 12103-12112
    • Ottensmeyer, F.P.1    Beniac, D.R.2    Luo, R.Z.3    Yip, C.C.4
  • 32
    • 0021267830 scopus 로고
    • Evidence that insulin receptor from human placenta has a high affinity for only one molecule of insulin
    • D.T. Pang, and J.A. Shafer Evidence that insulin receptor from human placenta has a high affinity for only one molecule of insulin J. Biol. Chem. 259 1984 8589 8596
    • (1984) J. Biol. Chem. , vol.259 , pp. 8589-8596
    • Pang, D.T.1    Shafer, J.A.2
  • 33
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • T. Pawson, and P. Nash Assembly of cell regulatory systems through protein interaction domains Science 300 2003 445 452
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 34
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • T. Pawson, and J.D. Scott Signaling through scaffold, anchoring, and adaptor proteins Science 278 1997 2075 2080
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 35
    • 0029924172 scopus 로고    scopus 로고
    • Interaction between the insulin receptor and its downstream effectors, use of individually expressed receptor domains for structure/function analysis
    • K. Paz, H. Voliovitch, Y.R. Hadari, C.T. Roberts Jr., D. LeRoith, and Y. Zick Interaction between the insulin receptor and its downstream effectors, use of individually expressed receptor domains for structure/function analysis J. Biol. Chem. 271 1996 6998 7003
    • (1996) J. Biol. Chem. , vol.271 , pp. 6998-7003
    • Paz, K.1    Voliovitch, H.2    Hadari, Y.R.3    Roberts Jr., C.T.4    Leroith, D.5    Zick, Y.6
  • 36
    • 0037078982 scopus 로고    scopus 로고
    • Control, exploitation and tolerance of intracellular noise
    • C.V. Rao, D.M. Wolf, and A.P. Arkin Control, exploitation and tolerance of intracellular noise Nature 420 2002 231 237
    • (2002) Nature , vol.420 , pp. 231-237
    • Rao, C.V.1    Wolf, D.M.2    Arkin, A.P.3
  • 37
    • 0033959896 scopus 로고    scopus 로고
    • A novel positive feedback loop mediated by the docking protein Gab1 and phosphatidylinositol 3-kinase in epidermal growth factor receptor signaling
    • G.A. Rodrigues, M. Falasca, Z. Zhang, S.H. Ong, and J. Schlessinger A novel positive feedback loop mediated by the docking protein Gab1 and phosphatidylinositol 3-kinase in epidermal growth factor receptor signaling Mol. Cell Biol. 20 2000 1448 1459
    • (2000) Mol. Cell Biol. , vol.20 , pp. 1448-1459
    • Rodrigues, G.A.1    Falasca, M.2    Zhang, Z.3    Ong, S.H.4    Schlessinger, J.5
  • 38
    • 0036470213 scopus 로고    scopus 로고
    • Insulin signaling pathways in time and space
    • A.R. Saltiel, and J.E. Pessin Insulin signaling pathways in time and space Trends Cell Biol. 12 2002 65 71
    • (2002) Trends Cell Biol. , vol.12 , pp. 65-71
    • Saltiel, A.R.1    Pessin, J.E.2
  • 39
    • 0347511691 scopus 로고    scopus 로고
    • Next generation simulation tools: The Systems Biology Workbench and BioSPICE integration
    • H.M. Sauro, M. Hucka, A. Finney, C. Wellock, H. Bolouri, J. Doyle, and H. Kitano Next generation simulation tools: the Systems Biology Workbench and BioSPICE integration Omics 7 2003 355 372
    • (2003) Omics , vol.7 , pp. 355-372
    • Sauro, H.M.1    Hucka, M.2    Finney, A.3    Wellock, C.4    Bolouri, H.5    Doyle, J.6    Kitano, H.7
  • 40
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • J. Schlessinger Cell signaling by receptor tyrosine kinases Cell 103 2000 211 225
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 41
    • 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, and G. Muller 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
  • 42
    • 0032143284 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase: The key switch mechanism in insulin signalling
    • P.R. Shepherd, D.J. Withers, and K. Siddle Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling Biochem. J. 333 Pt. 3 1998 471 490
    • (1998) Biochem. J. , vol.333 , Issue.3 PART , pp. 471-490
    • Shepherd, P.R.1    Withers, D.J.2    Siddle, K.3
  • 44
    • 0031918624 scopus 로고    scopus 로고
    • The IRS-signalling system: A network of docking proteins that mediate insulin action
    • M.F. White The IRS-signalling system: a network of docking proteins that mediate insulin action Mol. Cell Biochem. 182 1998 3 11
    • (1998) Mol. Cell Biochem. , vol.182 , pp. 3-11
    • White, M.F.1
  • 45
  • 46
    • 0037435036 scopus 로고    scopus 로고
    • Gab1 is required for EGF receptor signaling and the transformation by activated ErbB2
    • S. Yamasaki, K. Nishida, Y. Yoshida, M. Itoh, M. Hibi, and T. Hirano Gab1 is required for EGF receptor signaling and the transformation by activated ErbB2 Oncogene 22 2003 1546 1556
    • (2003) Oncogene , vol.22 , pp. 1546-1556
    • Yamasaki, S.1    Nishida, K.2    Yoshida, Y.3    Itoh, M.4    Hibi, M.5    Hirano, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.