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Volumn 14, Issue 6, 2005, Pages 1556-1569

Backbone nuclear relaxation characteristics and calorimetric investigation of the human Grb7-SH2/erbB2 peptide complex

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR 2; GROWTH FACTOR RECEPTOR BOUND PROTEIN 7; PEPTIDE DERIVATIVE; PROTEIN; PROTEIN SH2; UNCLASSIFIED DRUG;

EID: 22444439210     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041102305     Document Type: Article
Times cited : (13)

References (67)
  • 1
    • 0026748968 scopus 로고
    • Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible
    • Barbato, G., Ikura, M., Kay, L.E., Pastor, R.W., and Bax, A. 1992. Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible. Biochemistry 31: 5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 2
    • 0032480810 scopus 로고    scopus 로고
    • Calorimetric investigation of proton linkage by monitoring both the enthalpy and association constant of binding: Application to the interaction of the Src SH2 domain with a high-affinity tyrosyl phosphopeptide
    • Bradshaw, J.M. and Waksman, G. 1998. Calorimetric investigation of proton linkage by monitoring both the enthalpy and association constant of binding: Application to the interaction of the Src SH2 domain with a high-affinity tyrosyl phosphopeptide. Biochemistry 37: 15400-15407.
    • (1998) Biochemistry , vol.37 , pp. 15400-15407
    • Bradshaw, J.M.1    Waksman, G.2
  • 3
    • 0033586726 scopus 로고    scopus 로고
    • Calorimetric examination of high-affinity Src SH2 domain-tyrosyl phosphopeptide binding: Dissection of the phosphopeptide sequence specificity and coupling energetics
    • _. 1999. Calorimetric examination of high-affinity Src SH2 domain-tyrosyl phosphopeptide binding: Dissection of the phosphopeptide sequence specificity and coupling energetics. Biochemistry 38: 5147-5154.
    • (1999) Biochemistry , vol.38 , pp. 5147-5154
  • 4
    • 0036000581 scopus 로고    scopus 로고
    • Assignment of backbone 1H, 13C, and 15N resonances of human Grb7-SH2 domain in complex with a phosphorylated peptide ligand
    • Brescia, P.J., Ivancic, M., and Lyons, B.A. 2002. Assignment of backbone 1H, 13C, and 15N resonances of human Grb7-SH2 domain in complex with a phosphorylated peptide ligand. J. Biomol. NMR 23: 77-78.
    • (2002) J. Biomol. NMR , vol.23 , pp. 77-78
    • Brescia, P.J.1    Ivancic, M.2    Lyons, B.A.3
  • 5
    • 0000702636 scopus 로고
    • Techniques for the study of biological structure and function
    • Freeman, San Francisco
    • Cantor, C.R. and Schimmel, P.R. 1980. Techniques for the study of biological structure and function. In Biophysical chemistry. Freeman, San Francisco.
    • (1980) Biophysical Chemistry
    • Cantor, C.R.1    Schimmel, P.R.2
  • 6
    • 0042804907 scopus 로고    scopus 로고
    • NIK is a component of the EGF/heregulin receptor signaling complexes
    • Chen, D., Xu, L.G., Chen, L., Li, L., Zhai, Z., and Shu, H.B. 2003. NIK is a component of the EGF/heregulin receptor signaling complexes. Oncogene 22: 4348-4355.
    • (2003) Oncogene , vol.22 , pp. 4348-4355
    • Chen, D.1    Xu, L.G.2    Chen, L.3    Li, L.4    Zhai, Z.5    Shu, H.B.6
  • 7
    • 0032530724 scopus 로고    scopus 로고
    • Mass spectrometric and thermodynamic studies reveal the role of water molecules in complexes formed between SH2 domains and tyrosyl phosphopeptides
    • Chung, E., Henriques, D., Renzoni, D., Zvelebil, M., Bradshaw, J.M., Waksman, G., Robinson, C.V., and Ladbury, J.E. 1998. Mass spectrometric and thermodynamic studies reveal the role of water molecules in complexes formed between SH2 domains and tyrosyl phosphopeptides. Structure 6: 1141-1151.
    • (1998) Structure , vol.6 , pp. 1141-1151
    • Chung, E.1    Henriques, D.2    Renzoni, D.3    Zvelebil, M.4    Bradshaw, J.M.5    Waksman, G.6    Robinson, C.V.7    Ladbury, J.E.8
  • 8
    • 0025063347 scopus 로고
    • Analysis of the backbone dynamics of interleukin-1 b using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy
    • Clore, G.M., Driscoll, P.C., Wingfield, P.T., and Gronenborn, A.M. 1990. Analysis of the backbone dynamics of interleukin-1 b using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy. Biochemistry 29: 7387-7401.
    • (1990) Biochemistry , vol.29 , pp. 7387-7401
    • Clore, G.M.1    Driscoll, P.C.2    Wingfield, P.T.3    Gronenborn, A.M.4
  • 10
    • 0001307815 scopus 로고    scopus 로고
    • The cost of releasing site-specific, bound water molecules from proteins: Toward a quantitative guide for structure-based drug design
    • eds. J.E. Ladbury and P.R. Connelly, Springer-Verlag, Berlin
    • Connelly, P.R. 1997. The cost of releasing site-specific, bound water molecules from proteins: Toward a quantitative guide for structure-based drug design. In Structure-based drug design: Thermodynamics, modeling, and strategy (eds. J.E. Ladbury and P.R. Connelly), pp. 143-157. Springer-Verlag, Berlin.
    • (1997) Structure-based Drug Design: Thermodynamics, Modeling, and Strategy , pp. 143-157
    • Connelly, P.R.1
  • 11
    • 0037180757 scopus 로고    scopus 로고
    • Inflammation and cancer
    • Coussens, L.M. and Werb, Z. 2002. Inflammation and cancer. Nature 420: 860-867.
    • (2002) Nature , vol.420 , pp. 860-867
    • Coussens, L.M.1    Werb, Z.2
  • 12
    • 17544378927 scopus 로고    scopus 로고
    • Cloning and characterization of GRB14, a novel member of the GRB7 gene family
    • Daly, R.J., Sanderson, G.M., Janes, P.W., and Sutherland, R.L. 1996. Cloning and characterization of GRB14, a novel member of the GRB7 gene family. J. Biol. Chem. 271: 12502-12510.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12502-12510
    • Daly, R.J.1    Sanderson, G.M.2    Janes, P.W.3    Sutherland, R.L.4
  • 13
    • 2942733237 scopus 로고    scopus 로고
    • Changes in structural dynamics of the Grb2 adaptor protein upon binding of phosphotyrosine ligand to its SH2 domain
    • de Mol, N.J., Catalina, M.I., Fischer, M.J., Broutin, I., Maier, C.S., and Heck, A.J. 2004. Changes in structural dynamics of the Grb2 adaptor protein upon binding of phosphotyrosine ligand to its SH2 domain. Biochim. Biophys. Acta 1700: 53-64.
    • (2004) Biochim. Biophys. Acta , vol.1700 , pp. 53-64
    • De Mol, N.J.1    Catalina, M.I.2    Fischer, M.J.3    Broutin, I.4    Maier, C.S.5    Heck, A.J.6
  • 14
    • 0025706147 scopus 로고
    • The meaning of hydrophobicity
    • Dill, K.A. 1990. The meaning of hydrophobicity. Science 250: 297-298.
    • (1990) Science , vol.250 , pp. 297-298
    • Dill, K.A.1
  • 15
    • 0027502504 scopus 로고
    • Recognition of a highaffinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck
    • Eck, M.J., Shoelson, S.E., and Harrison, S.C. 1993. Recognition of a highaffinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck. Nature 362: 87-91.
    • (1993) Nature , vol.362 , pp. 87-91
    • Eck, M.J.1    Shoelson, S.E.2    Harrison, S.C.3
  • 17
    • 0037058897 scopus 로고    scopus 로고
    • The dynamic behavior of CheW from Thermotoga maritima in solution, as determined by nuclear magnetic resonance: Implications for potential protein-protein interaction sites
    • Griswold, I.J. and Dahlquist, F.W. 2002. The dynamic behavior of CheW from Thermotoga maritima in solution, as determined by nuclear magnetic resonance: Implications for potential protein-protein interaction sites. Biophys. Chem. 101-102: 359-373.
    • (2002) Biophys. Chem. , vol.101-102 , pp. 359-373
    • Griswold, I.J.1    Dahlquist, F.W.2
  • 18
    • 0000226650 scopus 로고    scopus 로고
    • Association of focal adhesion kinase with Grb7 and its role in cell migration
    • Han, D.C. and Guan, J.L. 1999. Association of focal adhesion kinase with Grb7 and its role in cell migration. J. Biol. Chem. 274: 24425-24430.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24425-24430
    • Han, D.C.1    Guan, J.L.2
  • 19
    • 0034666146 scopus 로고    scopus 로고
    • Role of Grb7 targeting to focal contacts and its phosphorylation by focal adhesion kinase in regulation of cell migration
    • Han, D.C., Shen, T.L., and Guan, J.L. 2000. Role of Grb7 targeting to focal contacts and its phosphorylation by focal adhesion kinase in regulation of cell migration. J. Biol. Chem. 275: 28911-28917.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28911-28917
    • Han, D.C.1    Shen, T.L.2    Guan, J.L.3
  • 20
    • 0032549647 scopus 로고    scopus 로고
    • Grb10 interacts differentially with the insulin receptor, insulin-like growth factor I receptor, and epidermal growth factor receptor via the Grb10 Src homology 2 (SH2) domain and a second novel domain located between the pleckstrin homology and SH2 domains
    • He, W., Rose, D.W., Olefsky, J.M., and Gustafson, T.A. 1998. Grb10 interacts differentially with the insulin receptor, insulin-like growth factor I receptor, and epidermal growth factor receptor via the Grb10 Src homology 2 (SH2) domain and a second novel domain located between the pleckstrin homology and SH2 domains. J. Biol. Chem. 273: 6860-6867.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6860-6867
    • He, W.1    Rose, D.W.2    Olefsky, J.M.3    Gustafson, T.A.4
  • 21
    • 0141502350 scopus 로고    scopus 로고
    • Solution structure of the human Grb7-SH2 domain/erbB2 peptide complex and structural basis for Grb7 binding to ErbB2
    • Ivancic, M., Daly, R.J., and Lyons, B.A. 2003. Solution structure of the human Grb7-SH2 domain/erbB2 peptide complex and structural basis for Grb7 binding to ErbB2. J. Biomol. NMR 27: 205-219.
    • (2003) J. Biomol. NMR , vol.27 , pp. 205-219
    • Ivancic, M.1    Daly, R.J.2    Lyons, B.A.3
  • 22
    • 0036146082 scopus 로고    scopus 로고
    • Role for the adaptor protein Grb10 in the activation of Akt
    • Jahn, T., Seipel, P., Urschel, S., Peschel, C., and Duyster, J. 2002. Role for the adaptor protein Grb10 in the activation of Akt. Mol. Cell Biol. 22: 979-991.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 979-991
    • Jahn, T.1    Seipel, P.2    Urschel, S.3    Peschel, C.4    Duyster, J.5
  • 23
    • 0030929332 scopus 로고    scopus 로고
    • Structural determinants of the interaction between the erbB2 receptor and the Src homology 2 domain of Grb7
    • Janes, P.W., Lackmann, M., Church, W.B., Sanderson, G.M., Sutherland, R.L., and Daly, R.J. 1997. Structural determinants of the interaction between the erbB2 receptor and the Src homology 2 domain of Grb7. J. Biol. Chem. 272: 8490-8497.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8490-8497
    • Janes, P.W.1    Lackmann, M.2    Church, W.B.3    Sanderson, G.M.4    Sutherland, R.L.5    Daly, R.J.6
  • 24
    • 0032199623 scopus 로고    scopus 로고
    • Propagation of experimental uncertainties using the Lipari-Szabo model-free analysis of protein dynamics
    • Jin, D., Andrec, M., Montelione, G.T., and Levy, R.M. 1998. Propagation of experimental uncertainties using the Lipari-Szabo model-free analysis of protein dynamics. J. Biomol. NMR 12: 471-492.
    • (1998) J. Biomol. NMR , vol.12 , pp. 471-492
    • Jin, D.1    Andrec, M.2    Montelione, G.T.3    Levy, R.M.4
  • 25
    • 0024449503 scopus 로고
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease. Biochemistry 28: 8972-8979.
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 26
    • 44049118502 scopus 로고
    • Pulse sequences for removal of the effects of cross-correlation between dipolar and chemical-shift anisotropy relaxation mechanism on the measurement of heteronuclear T1 and T2 values in proteins
    • Kay, L.E., Nicholson, L.K., Delaglio, F., Bax, A., and Torchia, D.A. 1992. Pulse sequences for removal of the effects of cross-correlation between dipolar and chemical-shift anisotropy relaxation mechanism on the measurement of heteronuclear T1 and T2 values in proteins. J. Magn. Reson. 97: 359-375.
    • (1992) J. Magn. Reson. , vol.97 , pp. 359-375
    • Kay, L.E.1    Nicholson, L.K.2    Delaglio, F.3    Bax, A.4    Torchia, D.A.5
  • 28
    • 0029757456 scopus 로고    scopus 로고
    • Alternative modes of tyrosyl phosphopeptide binding to a Src family SH2 domain: Implications for regulation of tyrosine kinase activity
    • Ladbury, J.E., Hensmann, M., Panayotou, G., and Campbell, I.D. 1996. Alternative modes of tyrosyl phosphopeptide binding to a Src family SH2 domain: Implications for regulation of tyrosine kinase activity. Biochemistry 35: 11062-11069.
    • (1996) Biochemistry , vol.35 , pp. 11062-11069
    • Ladbury, J.E.1    Hensmann, M.2    Panayotou, G.3    Campbell, I.D.4
  • 30
    • 0028303266 scopus 로고
    • Thermodynamic studies of tyrosyl-phosphopeptide binding to the SH2 domain of p56lck
    • Lemmon, M.A. and Ladbury, J.E. 1994. Thermodynamic studies of tyrosyl-phosphopeptide binding to the SH2 domain of p56lck. Biochemistry 33: 5070-5076.
    • (1994) Biochemistry , vol.33 , pp. 5070-5076
    • Lemmon, M.A.1    Ladbury, J.E.2
  • 31
    • 0028985308 scopus 로고
    • Human type-α transforming growth factor undergoes slow conformational exchange between multiple backbone conformations as characterized by nitrogen-15 relaxation measurements
    • Li, Y.C. and Montelione, G.T. 1995. Human type-α transforming growth factor undergoes slow conformational exchange between multiple backbone conformations as characterized by nitrogen-15 relaxation measurements. Biochemistry 34: 2408-2423.
    • (1995) Biochemistry , vol.34 , pp. 2408-2423
    • Li, Y.C.1    Montelione, G.T.2
  • 32
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G. and Szabo, A. 1982a. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104: 4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 33
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
    • _. 1982b. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results. J. Am. Chem. Soc. 104: 4559-4570.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
  • 34
    • 0033613158 scopus 로고    scopus 로고
    • Backbone dynamics of inactive, active, and effector-bound Cdc42Hs from measurements of (15)N relaxation parameters at multiple field strengths
    • Loh, A.P., Guo, W., Nicholson, L.K., and Oswald, R.E. 1999. Backbone dynamics of inactive, active, and effector-bound Cdc42Hs from measurements of (15)N relaxation parameters at multiple field strengths. Biochemistry 38: 12547-12557.
    • (1999) Biochemistry , vol.38 , pp. 12547-12557
    • Loh, A.P.1    Guo, W.2    Nicholson, L.K.3    Oswald, R.E.4
  • 35
    • 0035901519 scopus 로고    scopus 로고
    • An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs
    • Loh, A.P., Pawley, N., Nicholson, L.K., and Oswald, R.E. 2001. An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs. Biochemistry 40: 4590-4600.
    • (2001) Biochemistry , vol.40 , pp. 4590-4600
    • Loh, A.P.1    Pawley, N.2    Nicholson, L.K.3    Oswald, R.E.4
  • 37
    • 0028252996 scopus 로고
    • The GRB family of SH2 domain proteins
    • Margolis, B. 1994. The GRB family of SH2 domain proteins. Prog. Biophys. Mol. Biol. 62: 223-244.
    • (1994) Prog. Biophys. Mol. Biol. , vol.62 , pp. 223-244
    • Margolis, B.1
  • 40
    • 0035964181 scopus 로고    scopus 로고
    • Structure, dynamics, and thermodynamics of the structural domain of troponin C in complex with the regulatory peptide 1-40 of troponin I
    • Mercier, P., Spyracopoulos, L., and Sykes, B.D. 2001. Structure, dynamics, and thermodynamics of the structural domain of troponin C in complex with the regulatory peptide 1-40 of troponin I. Biochemistry 40: 10063-10077.
    • (2001) Biochemistry , vol.40 , pp. 10063-10077
    • Mercier, P.1    Spyracopoulos, L.2    Sykes, B.D.3
  • 41
    • 0141791271 scopus 로고    scopus 로고
    • Direct observation of protein-ligand interaction kinetics
    • Mittag, T., Schaffhausen, B., and Gunther, U.L. 2003. Direct observation of protein-ligand interaction kinetics. Biochemistry 42: 11128-11136.
    • (2003) Biochemistry , vol.42 , pp. 11128-11136
    • Mittag, T.1    Schaffhausen, B.2    Gunther, U.L.3
  • 43
    • 0032562691 scopus 로고    scopus 로고
    • Interaction of the Grb10 adapter protein with the Raf1 and MEK1 kinases
    • Nantel, A., Mohammad-Ali, K., Sherk, J., Posner, B.I., and Thomas, D.Y. 1998. Interaction of the Grb10 adapter protein with the Raf1 and MEK1 kinases. J. Biol. Chem. 273: 10475-10484.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10475-10484
    • Nantel, A.1    Mohammad-Ali, K.2    Sherk, J.3    Posner, B.I.4    Thomas, D.Y.5
  • 49
    • 0027195236 scopus 로고
    • Interactions between SH2 domains and tyrosine-phosphorylated platelet-derived growth factor β-receptor sequences: Analysis of kinetic parameters by a novel biosensor-based approach
    • Panayotou, G., Gish, G., End, P., Truong, O., Gout, I., Dhand, R., Fry, M.J., Hiles, I., Pawson, T., and Waterfield, M.D. 1993. Interactions between SH2 domains and tyrosine-phosphorylated platelet-derived growth factor β-receptor sequences: Analysis of kinetic parameters by a novel biosensor-based approach. Mol. Cell Biol. 13: 3567-3576.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 3567-3576
    • Panayotou, G.1    Gish, G.2    End, P.3    Truong, O.4    Gout, I.5    Dhand, R.6    Fry, M.J.7    Hiles, I.8    Pawson, T.9    Waterfield, M.D.10
  • 50
    • 0028982261 scopus 로고
    • The Ret receptor protein tyrosine kinase associates with the SH2-containing adapter protein Grb10
    • Pandey, A., Duan, H., Di Fiore, P.P., and Dixit, V.M. 1995. The Ret receptor protein tyrosine kinase associates with the SH2-containing adapter protein Grb10. J. Biol. Chem. 270: 21461-21463.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21461-21463
    • Pandey, A.1    Duan, H.2    Di Fiore, P.P.3    Dixit, V.M.4
  • 51
    • 0028354446 scopus 로고
    • Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-γ 1 complexed with a high affinity binding peptide
    • Pascal, S.M., Singer, A.U., Gish, G., Yamazaki, T., Shoelson, S.E., Pawson, T., Kay, L.E., and Forman-Kay, J.D. 1994. Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-γ 1 complexed with a high affinity binding peptide. Cell 77: 461-472.
    • (1994) Cell , vol.77 , pp. 461-472
    • Pascal, S.M.1    Singer, A.U.2    Gish, G.3    Yamazaki, T.4    Shoelson, S.E.5    Pawson, T.6    Kay, L.E.7    Forman-Kay, J.D.8
  • 52
    • 0037073474 scopus 로고    scopus 로고
    • Backbone dynamics and thermodynamics of Borrelia outer surface protein A
    • Pawley, N.H., Koide, S., and Nicholson, L.K. 2002. Backbone dynamics and thermodynamics of Borrelia outer surface protein A. J. Mol. Biol. 324: 991-1002.
    • (2002) J. Mol. Biol. , vol.324 , pp. 991-1002
    • Pawley, N.H.1    Koide, S.2    Nicholson, L.K.3
  • 53
    • 0034654352 scopus 로고    scopus 로고
    • A method for directly fitting the timer derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions
    • Philo, J.S. 2000. A method for directly fitting the timer derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions. Anal. Biochem. 279: 151-163.
    • (2000) Anal. Biochem. , vol.279 , pp. 151-163
    • Philo, J.S.1
  • 54
    • 0025706147 scopus 로고
    • The meaning of hydrophobicity: Response to Dill
    • Privalov, P.L., Gill, S.J., and Murphy, K.P. 1990. The meaning of hydrophobicity: Response to Dill. Science 250: 297-298.
    • (1990) Science , vol.250 , pp. 297-298
    • Privalov, P.L.1    Gill, S.J.2    Murphy, K.P.3
  • 56
    • 0026711032 scopus 로고
    • Fast internal mainchain dynamics of human ubiquitin
    • Schneider, D.M., Dellwo, M.J., and Wand, A.J. 1992. Fast internal mainchain dynamics of human ubiquitin. Biochemistry 31: 3645-3652.
    • (1992) Biochemistry , vol.31 , pp. 3645-3652
    • Schneider, D.M.1    Dellwo, M.J.2    Wand, A.J.3
  • 57
    • 0035875975 scopus 로고    scopus 로고
    • Differential regulation of cell migration and cell cycle progression by FAK complexes with Src, PI3K, Grb7 and Grb2 in focal contacts
    • Shen, T.L. and Guan, J.L. 2001. Differential regulation of cell migration and cell cycle progression by FAK complexes with Src, PI3K, Grb7 and Grb2 in focal contacts. FEBS Lett. 499: 176-181.
    • (2001) FEBS Lett. , vol.499 , pp. 176-181
    • Shen, T.L.1    Guan, J.L.2
  • 59
    • 0037969630 scopus 로고    scopus 로고
    • Structural basis for dimerization of the Grb10 Src homology 2 domain. Implications for ligand specificity
    • Stein, E.G., Ghirlando, R., and Hubbard, S.R. 2003. Structural basis for dimerization of the Grb10 Src homology 2 domain. Implications for ligand specificity. J. Biol. Chem. 278: 13257-13264.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13257-13264
    • Stein, E.G.1    Ghirlando, R.2    Hubbard, S.R.3
  • 61
    • 0038219754 scopus 로고    scopus 로고
    • Molecular dynamics, free energy, and SPR analyses of the interactions between the SH2 domain of Grb2 and ErbB phosphotyrosyl peptides
    • Suenaga, A., Hatakeyama, M., Ichikawa, M., Yu, X., Futatsugi, N., Narumi, T., Fukui, K., Terada, T., Taiji, M., Shirouzu, M., et al. 2003. Molecular dynamics, free energy, and SPR analyses of the interactions between the SH2 domain of Grb2 and ErbB phosphotyrosyl peptides. Biochemistry 42: 5195-5200.
    • (2003) Biochemistry , vol.42 , pp. 5195-5200
    • Suenaga, A.1    Hatakeyama, M.2    Ichikawa, M.3    Yu, X.4    Futatsugi, N.5    Narumi, T.6    Fukui, K.7    Terada, T.8    Taiji, M.9    Shirouzu, M.10
  • 62
    • 0024025743 scopus 로고
    • Frictional models for stochastic simulations of proteins
    • Venable, R.M. and Pastor, R.W. 1988. Frictional models for stochastic simulations of proteins. Biopolymers 27: 1001-1014.
    • (1988) Biopolymers , vol.27 , pp. 1001-1014
    • Venable, R.M.1    Pastor, R.W.2
  • 63
    • 0027409064 scopus 로고
    • Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms
    • Waksman, G., Shoelson, S.E., Pant, N., Cowburn, D., and Kuriyan, J. 1993. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms. Cell 72: 779-790.
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 64
    • 0032784061 scopus 로고    scopus 로고
    • Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis
    • Wang, J., Dai, H., Yousaf, N., Moussaif, M., Deng, Y., Boufelliga, A., Swamy, O.R., Leone, M.E., and Riedel, H. 1999. Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis. Mol. Cell Biol. 19: 6217-6228.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 6217-6228
    • Wang, J.1    Dai, H.2    Yousaf, N.3    Moussaif, M.4    Deng, Y.5    Boufelliga, A.6    Swamy, O.R.7    Leone, M.E.8    Riedel, H.9
  • 65
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., Williston, S., Brandts, J.F., and Lin, L.N. 1989. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179: 131-137.
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 66
    • 0033609359 scopus 로고    scopus 로고
    • Sequence analysis identifies a ras-associating (RA)-like domain in the N-termini of band 4.1/JEF domains and in the Grb7/10/14 adapter family
    • Wojcik, J., Girault, J.A., Labesse, G., Chomilier, J., Mornon, J.P., and Callebaut, I. 1999. Sequence analysis identifies a ras-associating (RA)-like domain in the N-termini of band 4.1/JEF domains and in the Grb7/10/14 adapter family. Biochem. Biophys. Res. Commun. 259: 113-120.
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 113-120
    • Wojcik, J.1    Girault, J.A.2    Labesse, G.3    Chomilier, J.4    Mornon, J.P.5    Callebaut, I.6
  • 67
    • 0034631701 scopus 로고    scopus 로고
    • Isothermal titration calorimetry measurements of Ni(II) and Cu(II) binding to His, GlyGlyHis, HisGlyHis, and bovine serum albumin: A critical evaluation
    • Zhang, Y., Akilesh, S., and Wilcox, D.E. 2000. Isothermal titration calorimetry measurements of Ni(II) and Cu(II) binding to His, GlyGlyHis, HisGlyHis, and bovine serum albumin: A critical evaluation. Inorg. Chem. 39: 3057-3064.
    • (2000) Inorg. Chem. , vol.39 , pp. 3057-3064
    • Zhang, Y.1    Akilesh, S.2    Wilcox, D.E.3


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