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Volumn 189, Issue 2, 2012, Pages 646-658

A computational model for early events in B cell antigen receptor signaling: Analysis of the roles of lyn and fyn

Author keywords

[No Author keywords available]

Indexed keywords

B LYMPHOCYTE ANTIGEN; BREAKPOINT CLUSTER REGION PROTEIN; CYTOSOLIC PROTEIN TYROSINE KINASE; PROTEIN KINASE FYN; PROTEIN KINASE LYN; PROTEIN KINASE SYK; PROTEIN PAG1; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

EID: 84863630609     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1102003     Document Type: Article
Times cited : (43)

References (80)
  • 2
    • 0029082078 scopus 로고
    • Antigen and Fc receptor signaling: The awesome power of the immunoreceptor tyrosine-based activation motif (ITAM)
    • Cambier, J. C. 1995. Antigen and Fc receptor signaling: the awesome power of the immunoreceptor tyrosine-based activation motif (ITAM). J. Immunol. 155: 3281-3285.
    • (1995) J. Immunol. , vol.155 , pp. 3281-3285
    • Cambier, J.C.1
  • 3
    • 0028125752 scopus 로고
    • Dual role of the tyrosine activation motif of the Ig-a protein during signal transduction via the B cell antigen receptor
    • Flaswinkel, H., and M. Reth. 1994. Dual role of the tyrosine activation motif of the Ig-a protein during signal transduction via the B cell antigen receptor. EMBO J. 13: 83-89.
    • (1994) EMBO J. , vol.13 , pp. 83-89
    • Flaswinkel, H.1    Reth, M.2
  • 4
    • 0036866477 scopus 로고    scopus 로고
    • Amplification of B cell antigen receptor signaling by a Syk/ITAM positive feedback loop
    • DOI 10.1016/S1097-2765(02)00739-6
    • Rolli, V., M. Gallwitz, T. Wossning, A. Flemming, W. W. A. Schamel, C. Zürn, and M. Reth. 2002. Amplification of B cell antigen receptor signaling by a Syk/ITAM positive feedback loop. Mol. Cell 10: 1057-1069. (Pubitemid 36001972)
    • (2002) Molecular Cell , vol.10 , Issue.5 , pp. 1057-1069
    • Rolli, V.1    Gallwitz, M.2    Wossning, T.3    Flemming, A.4    Schamel, W.W.A.5    Zurn, C.6    Reth, M.7
  • 5
    • 61849141064 scopus 로고    scopus 로고
    • Tyrosine kinases and their substrates in B lymphocytes
    • Kurosaki, T., and M. Hikida. 2009. Tyrosine kinases and their substrates in B lymphocytes. Immunol. Rev. 228: 132-148.
    • (2009) Immunol. Rev. , vol.228 , pp. 132-148
    • Kurosaki, T.1    Hikida, M.2
  • 6
    • 67649425382 scopus 로고    scopus 로고
    • Syk and pTyr'd: Signaling through the B cell antigen receptor
    • Geahlen, R. L. 2009. Syk and pTyr'd: signaling through the B cell antigen receptor. Biochim. Biophys. Acta 1793: 1115-1127.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 1115-1127
    • Geahlen, R.L.1
  • 7
    • 7944235830 scopus 로고    scopus 로고
    • Src-family kinases in B-cell development and signaling
    • DOI 10.1038/sj.onc.1208075
    • Gauld, S. B., and J. C. Cambier. 2004. Src-family kinases in B-cell development and signaling. Oncogene 23: 8001-8006. (Pubitemid 39468857)
    • (2004) Oncogene , vol.23 , Issue.48 REV. ISS. 7 , pp. 8001-8006
    • Gauld, S.B.1    Cambier, J.C.2
  • 10
    • 0028176660 scopus 로고
    • Analysis of Ig-a-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-α stimulation of Fyn activity
    • Clark, M. R., S. A. Johnson, and J. C. Cambier. 1994. Analysis of Ig-a-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-α stimulation of Fyn activity. EMBO J. 13: 1911-1919.
    • (1994) EMBO J. , vol.13 , pp. 1911-1919
    • Clark, M.R.1    Johnson, S.A.2    Cambier, J.C.3
  • 11
    • 0029615453 scopus 로고
    • Autophosphorylation induces autoactivation and a decrease in the Src homology 2 domain accessibility of the Lyn protein kinase
    • DOI 10.1074/jbc.270.50.29773
    • Sotirellis, N., T. M. Johnson, M. L. Hibbs, I. J. Stanley, E. Stanley, A. R. Dunn, and H. C. Cheng. 1995. Autophosphorylation induces autoactivation and a decrease in the Src homology 2 domain accessibility of the Lyn protein kinase. J. Biol. Chem. 270: 29773-29780. (Pubitemid 26001645)
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.50 , pp. 29773-29780
    • Sotirellis, N.1    Johnson, T.M.2    Hibbs, M.L.3    Stanley, I.J.4    Stanley, E.5    Dunn, A.R.6    Cheng, H.-C.7
  • 12
    • 7944236785 scopus 로고    scopus 로고
    • Src family kinases, key regulators of signal transduction
    • DOI 10.1038/sj.onc.1208160
    • Parsons, S. J., and J. T. Parsons. 2004. Src family kinases, key regulators of signal transduction. Oncogene 23: 7906-7909. (Pubitemid 39468849)
    • (2004) Oncogene , vol.23 , Issue.48 REV. ISS. 7 , pp. 7906-7909
    • Parsons, S.J.1    Parsons, J.T.2
  • 13
    • 0028783396 scopus 로고
    • Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling
    • Kurosaki, T., S. A. Johnson, L. Pao, K. Sada, H. Yamamura, and J. C. Cambier. 1995. Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling. J. Exp. Med. 182: 1815-1823.
    • (1995) J. Exp. Med. , vol.182 , pp. 1815-1823
    • Kurosaki, T.1    Johnson, S.A.2    Pao, L.3    Sada, K.4    Yamamura, H.5    Cambier, J.C.6
  • 14
    • 0028926070 scopus 로고
    • Transmembrane signaling by antigen receptors of B and T lymphocytes
    • DeFranco, A. L. 1995. Transmembrane signaling by antigen receptors of B and T lymphocytes. Curr. Opin. Cell Biol. 7: 163-175.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 163-175
    • DeFranco, A.L.1
  • 15
    • 0029068171 scopus 로고
    • Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig α/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation
    • Rowley, R. B., A. L. Burkhardt, H. G. Chao, G. R. Matsueda, and J. B. Bolen. 1995. Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig α/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation. J. Biol. Chem. 270: 11590-11594.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11590-11594
    • Rowley, R.B.1    Burkhardt, A.L.2    Chao, H.G.3    Matsueda, G.R.4    Bolen, J.B.5
  • 16
    • 0034874786 scopus 로고    scopus 로고
    • Structure and function of Syk protein-tyrosine kinase
    • Sada, K., T. Takano, S. Yanagi, and H. Yamamura. 2001. Structure and function of Syk protein-tyrosine kinase. J. Biochem. 130: 177-186. (Pubitemid 32785863)
    • (2001) Journal of Biochemistry , vol.130 , Issue.2 , pp. 177-186
    • Sada, K.1    Takano, T.2    Yanagi, S.3    Yamamura, H.4
  • 17
    • 33846015045 scopus 로고    scopus 로고
    • Csk-binding protein mediates sequential enzymatic down-regulation and degradation of Lyn in erythropoietin-stimulated cells
    • DOI 10.1074/jbc.M602637200
    • Ingley, E., J. R. Schneider, C. J. Payne, D. J. McCarthy, K. W. Harder, M. L. Hibbs, and S. P. Klinken. 2006. Csk-binding protein mediates sequential enzymatic down-regulation and degradation of Lyn in erythropoietin-stimulated cells. J. Biol. Chem. 281: 31920-31929. (Pubitemid 46041454)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.42 , pp. 31920-31929
    • Ingley, E.1    Schneider, J.R.2    Payne, C.J.3    McCarthy, D.J.4    Harder, K.W.5    Hibbs, M.L.6    Klinken, S.P.7
  • 18
    • 51749107470 scopus 로고    scopus 로고
    • Interactions between the Fyn SH3-domain and adaptor protein Cbp/PAG derived ligands, effects on kinase activity and affinity
    • Solheim, S. A., E. Petsalaki, A. J. Stokka, R. B. Russell, K. Taskén, and T. Berge. 2008. Interactions between the Fyn SH3-domain and adaptor protein Cbp/PAG derived ligands, effects on kinase activity and affinity. FEBS J. 275: 4863-4874.
    • (2008) FEBS J. , vol.275 , pp. 4863-4874
    • Solheim, S.A.1    Petsalaki, E.2    Stokka, A.J.3    Russell, R.B.4    Taskén, K.5    Berge, T.6
  • 19
    • 41449099784 scopus 로고    scopus 로고
    • Regulation of FynT function by dual domain docking on PAG/Cbp
    • Solheim, S. A., K. M. Torgersen, K. Taskén, and T. Berge. 2008. Regulation of FynT function by dual domain docking on PAG/Cbp. J. Biol. Chem. 283: 2773-2783.
    • (2008) J. Biol. Chem. , vol.283 , pp. 2773-2783
    • Solheim, S.A.1    Torgersen, K.M.2    Taskén, K.3    Berge, T.4
  • 21
    • 38349014380 scopus 로고    scopus 로고
    • Src family kinases: Regulation of their activities, levels and identification of new pathways
    • Ingley, E. 2008. Src family kinases: regulation of their activities, levels and identification of new pathways. Biochim. Biophys. Acta 1784: 56-65.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 56-65
    • Ingley, E.1
  • 22
    • 38849203194 scopus 로고    scopus 로고
    • CD22: An inhibitory enigma
    • DOI 10.1111/j.1365-2567.2007.02752.x
    • Walker, J. A., and K. G. C. Smith. 2008. CD22: an inhibitory enigma. Immunology 123: 314-325. (Pubitemid 351192818)
    • (2008) Immunology , vol.123 , Issue.3 , pp. 314-325
    • Walker, J.A.1    Smith, K.G.C.2
  • 23
    • 78649851494 scopus 로고    scopus 로고
    • Syk is a dual-specificity kinase that self-regulates the signal output from the B-cell antigen receptor
    • Heizmann, B., M. Reth, and S. Infantino. 2010. Syk is a dual-specificity kinase that self-regulates the signal output from the B-cell antigen receptor. Proc. Natl. Acad. Sci. USA 107: 18563-18568.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 18563-18568
    • Heizmann, B.1    Reth, M.2    Infantino, S.3
  • 28
    • 0030740148 scopus 로고    scopus 로고
    • Characterization of the B lymphocyte populations in lyn-deficient mice and the role of lyn in signal initiation and down-regulation
    • DOI 10.1016/S1074-7613(00)80511-7
    • Chan, V. W., F. Meng, P. Soriano, A. L. DeFranco, and C. A. Lowell. 1997. Characterization of the B lymphocyte populations in Lyn-deficient mice and the role of Lyn in signal initiation and down-regulation. Immunity 7: 69-81. (Pubitemid 27357266)
    • (1997) Immunity , vol.7 , Issue.1 , pp. 69-81
    • Chan, V.W.F.1    Meng, F.2    Soriano, P.3    DeFranco, A.L.4    Lowell, C.A.5
  • 29
    • 0032492994 scopus 로고    scopus 로고
    • Defective negative regulation of antigen receptor signaling in Lyn-deficient B lymphocytes
    • Chan, V. W., C. A. Lowell, and A. L. DeFranco. 1998. Defective negative regulation of antigen receptor signaling in Lyn-deficient B lymphocytes. Curr. Biol. 8: 545-553. (Pubitemid 28222888)
    • (1998) Current Biology , vol.8 , Issue.10 , pp. 545-553
    • Chan, V.W.F.1    Lowell, C.A.2    DeFranco, A.L.3
  • 33
    • 10244219918 scopus 로고    scopus 로고
    • BioNetGen: Software for rule-based modeling of signal transduction based on the interactions of molecular domains
    • DOI 10.1093/bioinformatics/bth378
    • Blinov, M. L., J. R. Faeder, B. Goldstein, and W. S. Hlavacek. 2004. BioNetGen: software for rule-based modeling of signal transduction based on the interactions of molecular domains. Bioinformatics 20: 3289-3291. (Pubitemid 39619231)
    • (2004) Bioinformatics , vol.20 , Issue.17 , pp. 3289-3291
    • Blinov, M.L.1    Faeder, J.R.2    Goldstein, B.3    Hlavacek, W.S.4
  • 34
    • 65649154507 scopus 로고    scopus 로고
    • Rule-based modeling of biochemical systems with BioNetGen
    • Faeder, J. R., M. L. Blinov, and W. S. Hlavacek. 2009. Rule-based modeling of biochemical systems with BioNetGen. Methods Mol. Biol. 500: 113-167.
    • (2009) Methods Mol. Biol. , vol.500 , pp. 113-167
    • Faeder, J.R.1    Blinov, M.L.2    Hlavacek, W.S.3
  • 36
    • 70350364712 scopus 로고    scopus 로고
    • Molecular machines or pleiomorphic ensembles: Signaling complexes revisited
    • Mayer, B. J., M. L. Blinov, and L. M. Loew. 2009. Molecular machines or pleiomorphic ensembles: signaling complexes revisited. J. Biol. 8: 81.
    • (2009) J. Biol. , vol.8 , pp. 81
    • Mayer, B.J.1    Blinov, M.L.2    Loew, L.M.3
  • 38
    • 57049089108 scopus 로고    scopus 로고
    • Statistical model checking in BioLab: Applications to the automated analysis of T-cell receptor signaling pathway
    • Clarke, E. M., J. R. Faeder, C. J. Langmead, L. A. Harris, S. K. Jha, and A. Legay. 2008. Statistical model checking in BioLab: applications to the automated analysis of T-cell receptor signaling pathway. Lect. Notes Comput. Sci. 5307: 231-250.
    • (2008) Lect. Notes Comput. Sci. , vol.5307 , pp. 231-250
    • Clarke, E.M.1    Faeder, J.R.2    Langmead, C.J.3    Harris, L.A.4    Jha, S.K.5    Legay, A.6
  • 42
    • 79551555393 scopus 로고    scopus 로고
    • Efficient modeling, simulation and coarse-graining of biological complexity with NFsim
    • Sneddon, M. W., J. R. Faeder, and T. Emonet. 2011. Efficient modeling, simulation and coarse-graining of biological complexity with NFsim. Nat. Methods 8: 177-183.
    • (2011) Nat. Methods , vol.8 , pp. 177-183
    • Sneddon, M.W.1    Faeder, J.R.2    Emonet, T.3
  • 43
    • 79958124076 scopus 로고    scopus 로고
    • RuleBender: A visual interface for rule-based modeling
    • Xu, W., A. M. Smith, J. R. Faeder, and G. E. Marai. 2011. RuleBender: a visual interface for rule-based modeling. Bioinformatics 27: 1721-1722.
    • (2011) Bioinformatics , vol.27 , pp. 1721-1722
    • Xu, W.1    Smith, A.M.2    Faeder, J.R.3    Marai, G.E.4
  • 46
    • 84859354949 scopus 로고    scopus 로고
    • B-cell receptor: From resting state to activate
    • Treanor, B. 2012. B-cell receptor: from resting state to activate. Immunology 136: 21-27.
    • (2012) Immunology , vol.136 , pp. 21-27
    • Treanor, B.1
  • 47
    • 80052685806 scopus 로고    scopus 로고
    • Exact solutions to a spatially extended model of kinase-receptor interaction
    • Szopa, P., T. Lipniacki, and B. Kazmierczak. 2011. Exact solutions to a spatially extended model of kinase-receptor interaction. Phys. Biol. 8: 055005.
    • (2011) Phys. Biol. , vol.8 , pp. 055005
    • Szopa, P.1    Lipniacki, T.2    Kazmierczak, B.3
  • 48
    • 80055091826 scopus 로고    scopus 로고
    • B cell activation triggered by the formation of the small receptor cluster: A computational study
    • Hat, B., B. Kazmierczak, and T. Lipniacki. 2011. B cell activation triggered by the formation of the small receptor cluster: a computational study. PLOS Comput. Biol. 7: e1002197.
    • (2011) PLOS Comput. Biol. , vol.7
    • Hat, B.1    Kazmierczak, B.2    Lipniacki, T.3
  • 49
    • 0030956912 scopus 로고    scopus 로고
    • Role of Tyr518 and Tyr519 in the regulation of catalytic activity and substrate phosphorylation by Syk protein-tyrosine kinase
    • Couture, C., S. Williams, N. Gauthier, P. Tailor, and T. Mustelin. 1997. Role of Tyr518 and Tyr519 in the regulation of catalytic activity and substrate phosphorylation by Syk protein-tyrosine kinase. Eur. J. Biochem. 246: 447-451. (Pubitemid 27232522)
    • (1997) European Journal of Biochemistry , vol.246 , Issue.2 , pp. 447-451
    • Couture, C.1    Williams, S.2    Gauthier, N.3    Tailor, P.4    Mustelin, T.5
  • 50
    • 0029001897 scopus 로고
    • Flow cytometric analysis of T-independent antigen binding to dinitrophenyl-specific cells
    • Woodard, S. L., M. Aldo-Benson, D. A. Roess, and B. G. Barisas. 1995. Flow cytometric analysis of T-independent antigen binding to dinitrophenyl-specific cells. J. Immunol. 155: 163-171.
    • (1995) J. Immunol. , vol.155 , pp. 163-171
    • Woodard, S.L.1    Aldo-Benson, M.2    Roess, D.A.3    Barisas, B.G.4
  • 51
    • 0025291580 scopus 로고
    • Membrane biogenesis during B cell differentiation: Most endoplasmic reticulum proteins are expressed coordinately
    • Wiest, D. L., J. K. Burkhardt, S. Hester, M. Hortsch, D. I. Meyer, and Y. Argon. 1990. Membrane biogenesis during B cell differentiation: most endoplasmic reticulum proteins are expressed coordinately. J. Cell Biol. 110: 1501-1511.
    • (1990) J. Cell Biol. , vol.110 , pp. 1501-1511
    • Wiest, D.L.1    Burkhardt, J.K.2    Hester, S.3    Hortsch, M.4    Meyer, D.I.5    Argon, Y.6
  • 53
    • 0014124105 scopus 로고
    • Ultrastructural differences between thymic and lymph node small lymphocytes of mice: Nucleolar size and cytoplasmic volume
    • Heiniger, H. J., H. Riedwyl, H. Giger, B. Sordat, and H. Cottier. 1967. Ultrastructural differences between thymic and lymph node small lymphocytes of mice: nucleolar size and cytoplasmic volume. Blood 30: 288-300.
    • (1967) Blood , vol.30 , pp. 288-300
    • Heiniger, H.J.1    Riedwyl, H.2    Giger, H.3    Sordat, B.4    Cottier, H.5
  • 54
    • 7944223078 scopus 로고    scopus 로고
    • Structure and regulation of Src family kinases
    • DOI 10.1038/sj.onc.1208081
    • Boggon, T. J., and M. J. Eck. 2004. Structure and regulation of Src family kinases. Oncogene 23: 7918-7927. (Pubitemid 39468851)
    • (2004) Oncogene , vol.23 , Issue.48 REV. ISS. 7 , pp. 7918-7927
    • Boggon, T.J.1    Eck, M.J.2
  • 55
    • 0031573523 scopus 로고    scopus 로고
    • Exploiting the Difference between Intrinsic and Extrinsic Kinases: Implications for Regulation of Signaling by Immunoreceptors
    • Wofsy, C., C. Torigoe, U. M. Kent, H. Metzger, and B. Goldstein. 1997. Exploiting the difference between intrinsic and extrinsic kinases: implications for regulation of signaling by immunoreceptors. J. Immunol. 159: 5984-5992. (Pubitemid 127471534)
    • (1997) Journal of Immunology , vol.159 , Issue.12 , pp. 5984-5992
    • Wofsy, C.1    Torigoe, C.2    Kent, U.M.3    Metzger, H.4    Goldstein, B.5
  • 57
    • 79551482915 scopus 로고    scopus 로고
    • Predicting kinetic constants of protein-protein interactions based on structural properties
    • Bai, H., K. Yang, D. Yu, C. Zhang, F. Chen, and L. Lai. 2011. Predicting kinetic constants of protein-protein interactions based on structural properties. Proteins 79: 720-734.
    • (2011) Proteins , vol.79 , pp. 720-734
    • Bai, H.1    Yang, K.2    Yu, D.3    Zhang, C.4    Chen, F.5    Lai, L.6
  • 58
    • 78650961103 scopus 로고    scopus 로고
    • Energetics of Src homology domain interactions in receptor tyrosine kinase-mediated signaling
    • Ladbury, J. E., and S. T. Arold. 2011. Energetics of Src homology domain interactions in receptor tyrosine kinase-mediated signaling. Methods Enzymol. 488: 147-183.
    • (2011) Methods Enzymol. , vol.488 , pp. 147-183
    • Ladbury, J.E.1    Arold, S.T.2
  • 59
    • 33845929089 scopus 로고    scopus 로고
    • Protein flexibility and ligand rigidity: A thermodynamic and kinetic study of ITAM-based ligand binding to Syk tandem SH2
    • de Mol, N. J., M. I. Catalina, F. J. Dekker, M. J. E. Fischer, A. J. R. Heck, and R. M. J. Liskamp. 2005. Protein flexibility and ligand rigidity: a thermodynamic and kinetic study of ITAM-based ligand binding to Syk tandem SH2. Chem-BioChem 6: 2261-2270.
    • (2005) Chem-BioChem , vol.6 , pp. 2261-2270
    • De Mol, N.J.1    Catalina, M.I.2    Dekker, F.J.3    Fischer, M.J.E.4    Heck, A.J.R.5    Liskamp, R.M.J.6
  • 60
    • 50149105176 scopus 로고    scopus 로고
    • Tyr130 phosphorylation triggers Syk release from antigen receptor by long-distance conformational uncoupling
    • Zhang, Y., H. Oh, R. A. Burton, J. W. Burgner, R. L. Geahlen, and C. B. Post. 2008. Tyr130 phosphorylation triggers Syk release from antigen receptor by long-distance conformational uncoupling. Proc. Natl. Acad. Sci. USA 105: 11760-11765.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11760-11765
    • Zhang, Y.1    Oh, H.2    Burton, R.A.3    Burgner, J.W.4    Geahlen, R.L.5    Post, C.B.6
  • 61
    • 0029979054 scopus 로고    scopus 로고
    • Binding affinities of the SH2 domains of ZAP-70, p56lck and Shc to the z chain ITAMs of the T-cell receptor determined by surface plasmon resonance
    • Labadia, M. E., R. H. Ingraham, J. Schembri-King, M. M. Morelock, and S. Jakes. 1996. Binding affinities of the SH2 domains of ZAP-70, p56lck and Shc to the z chain ITAMs of the T-cell receptor determined by surface plasmon resonance. J. Leukoc. Biol. 59: 740-746.
    • (1996) J. Leukoc. Biol. , vol.59 , pp. 740-746
    • Labadia, M.E.1    Ingraham, R.H.2    Schembri-King, J.3    Morelock, M.M.4    Jakes, S.5
  • 62
    • 34249071629 scopus 로고    scopus 로고
    • Defining SH2 domain and PTP specificity by screening combinatorial peptide libraries
    • DOI 10.1016/j.ymeth.2007.02.010, PII S1046202307000369, Emerging New Techniques for Studying Protein Phosphatases
    • Wavreille, A.-S., M. Garaud, Y. Zhang, and D. Pei. 2007. Defining SH2 domain and PTP specificity by screening combinatorial peptide libraries. Methods 42: 207-219. (Pubitemid 46783585)
    • (2007) Methods , vol.42 , Issue.3 , pp. 207-219
    • Wavreille, A.-S.1    Garaud, M.2    Zhang, Y.3    Pei, D.4
  • 63
    • 0030105583 scopus 로고    scopus 로고
    • CVODE, A stiff/nonstiff ODE solver in C
    • Cohen, S. D., and A. C. Hindmarsh. 1996. CVODE, A stiff/nonstiff ODE solver in C. Comput. Phys. 10: 138-143.
    • (1996) Comput. Phys. , vol.10 , pp. 138-143
    • Cohen, S.D.1    Hindmarsh, A.C.2
  • 65
    • 20144385752 scopus 로고    scopus 로고
    • Rule-based modeling of biochemical networks
    • DOI 10.1002/cplx.20074
    • Faeder, J. R., M. L. Blinov, B. Goldstein, and W. S. Hlavacek. 2005. Rule-based modeling of biochemical networks. Complexity 10: 22-41. (Pubitemid 40772240)
    • (2005) Complexity , vol.10 , Issue.4 , pp. 22-41
    • Faeder, J.R.1    Blinov, M.L.2    Goldstein, B.3    Hlavacek, W.S.4
  • 67
    • 70349549913 scopus 로고    scopus 로고
    • Exploring mechanisms of oscillations in p53 and nuclear factor-B systems
    • Hat, B., K. Puszynski, and T. Lipniacki. 2009. Exploring mechanisms of oscillations in p53 and nuclear factor-B systems. IET Syst. Biol. 3: 342-355.
    • (2009) IET Syst. Biol. , vol.3 , pp. 342-355
    • Hat, B.1    Puszynski, K.2    Lipniacki, T.3
  • 69
    • 0028073936 scopus 로고
    • Functional analysis of Csk in signal transduction through the B-cell antigen receptor
    • Hata, A., H. Sabe, T. Kurosaki, M. Takata, and H. Hanafusa. 1994. Functional analysis of Csk in signal transduction through the B-cell antigen receptor. Mol. Cell. Biol. 14: 7306-7313. (Pubitemid 24326395)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.11 , pp. 7306-7313
    • Hata, A.1    Sabe, H.2    Kurosaki, T.3    Takata, M.4    Hanafusa, H.5
  • 70
    • 27944447718 scopus 로고    scopus 로고
    • The ubiquitously expressed Csk adaptor protein Cbp is dispensable for embryogenesis and T-cell development and function
    • DOI 10.1128/MCB.25.23.10533-10542.2005
    • Dobenecker, M. W., C. Schmedt, M. Okada, and A. Tarakhovsky. 2005. The ubiquitously expressed Csk adaptor protein Cbp is dispensable for embryogenesis and T-cell development and function. Mol. Cell. Biol. 25: 10533-10542. (Pubitemid 41681974)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.23 , pp. 10533-10542
    • Dobenecker, M.-W.1    Schmedt, C.2    Okada, M.3    Tarakhovsky, A.4
  • 71
    • 33747872720 scopus 로고    scopus 로고
    • Bistable switching and excitable behaviour in the activation of Src at mitosis
    • DOI 10.1093/bioinformatics/btl201
    • Fuss, H., W. Dubitzky, S. Downes, and M. J. Kurth. 2006. Bistable switching and excitable behaviour in the activation of Src at mitosis. Bioinformatics 22: e158-e165. (Pubitemid 44288282)
    • (2006) Bioinformatics , vol.22 , Issue.14
    • Fuss, H.1    Dubitzky, W.2    Downes, S.3    Kurth, M.J.4
  • 72
    • 36049005923 scopus 로고    scopus 로고
    • Deactivation of Src family kinases: Hypothesis testing using a Monte Carlo sensitivity analysis of systems-level properties
    • DOI 10.1089/cmb.2007.0095
    • Fuss, H., W. Dubitzky, C. S. Downes, and M. J. Kurth. 2007. Deactivation of Src family kinases: hypothesis testing using a Monte Carlo sensitivity analysis of systems-level properties. J. Comput. Biol. 14: 1185-1200. (Pubitemid 350100400)
    • (2007) Journal of Computational Biology , vol.14 , Issue.9 , pp. 1185-1200
    • Fuss, H.1    Dubitzky, W.2    Downes, C.S.3    Kurth, M.J.4
  • 73
    • 68149171467 scopus 로고    scopus 로고
    • Toggle switches, pulses and oscillations are intrinsic properties of the Src activation/deactivation cycle
    • Kaimachnikov, N. P., and B. N. Kholodenko. 2009. Toggle switches, pulses and oscillations are intrinsic properties of the Src activation/deactivation cycle. FEBS J. 276: 4102-4118.
    • (2009) FEBS J. , vol.276 , pp. 4102-4118
    • Kaimachnikov, N.P.1    Kholodenko, B.N.2
  • 74
    • 4444298148 scopus 로고    scopus 로고
    • CD4 enhances T cell sensitivity to antigen by coordinating Lck accumulation at the immunological synapse
    • DOI 10.1038/ni1095
    • Li, Q.-J., A. R. Dinner, S. Qi, D. J. Irvine, J. B. Huppa, M. M. Davis, and A. K. Chakraborty. 2004. CD4 enhances T cell sensitivity to antigen by coordinating Lck accumulation at the immunological synapse. Nat. Immunol. 5: 791-799. (Pubitemid 39172972)
    • (2004) Nature Immunology , vol.5 , Issue.8 , pp. 791-799
    • Li, Q.-J.1    Dinner, A.R.2    Qi, S.3    Irvine, D.J.4    Huppa, J.B.5    Davis, M.M.6    Chakraborty, A.K.7
  • 76
    • 78649871736 scopus 로고    scopus 로고
    • A detailed mathematical model predicts that serial engagement of IgE-FcεRI complexes can enhance Syk activation in mast cells
    • Nag, A., M. I. Monine, M. L. Blinov, and B. Goldstein. 2010. A detailed mathematical model predicts that serial engagement of IgE-FcεRI complexes can enhance Syk activation in mast cells. J. Immunol. 185: 3268-3276.
    • (2010) J. Immunol. , vol.185 , pp. 3268-3276
    • Nag, A.1    Monine, M.I.2    Blinov, M.L.3    Goldstein, B.4
  • 77
    • 77449103109 scopus 로고    scopus 로고
    • A method for analyzing protein-protein interactions in the plasma membrane of live B cells by fluorescence resonance energy transfer imaging as acquired by total internal reflection fluorescence microscopy
    • Sohn, H. W., P. Tolar, J. Brzostowski, and S. K. Pierce. 2010. A method for analyzing protein-protein interactions in the plasma membrane of live B cells by fluorescence resonance energy transfer imaging as acquired by total internal reflection fluorescence microscopy. Methods Mol. Biol. 591: 159-183.
    • (2010) Methods Mol. Biol. , vol.591 , pp. 159-183
    • Sohn, H.W.1    Tolar, P.2    Brzostowski, J.3    Pierce, S.K.4
  • 78
    • 48249124978 scopus 로고    scopus 로고
    • Membrane heterogeneities in the formation of B cell receptor-Lyn kinase microclusters and the immune synapse
    • Sohn, H. W., P. Tolar, and S. K. Pierce. 2008. Membrane heterogeneities in the formation of B cell receptor-Lyn kinase microclusters and the immune synapse. J. Cell Biol. 182: 367-379.
    • (2008) J. Cell Biol. , vol.182 , pp. 367-379
    • Sohn, H.W.1    Tolar, P.2    Pierce, S.K.3
  • 80
    • 77952944052 scopus 로고    scopus 로고
    • Designing customized cell signalling circuits
    • Lim, W. A. 2010. Designing customized cell signalling circuits. Nat. Rev. Mol. Cell Biol. 11: 393-403.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 393-403
    • Lim, W.A.1


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