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Volumn 50, Issue 13, 2011, Pages 2464-2477

Murine interleukin-3: Structure, dynamics, and conformational heterogeneity in solution

Author keywords

[No Author keywords available]

Indexed keywords

ALLERGIC INFLAMMATION; CONFORMATIONAL EXCHANGE; CONFORMATIONAL HETEROGENEITY; CYTOKINES; HELICAL BUNDLE; HIGHER TEMPERATURES; HYDROPHOBIC RESIDUES; IMMUNE RESPONSE; INTERLEUKIN-3; ISOFORMS; LINE BROADENING; NATURALLY OCCURRING; NMR SPECTRUM; OLIGOMERIC STATE; RELAXATION DISPERSION; RELAXATION PARAMETER; SOLUTION CONDITIONS; SOLUTION PROPERTY; STRUCTURAL STUDIES; T CELLS; TEMPERATURE DEPENDENCE; TEMPERATURE-DEPENDENT CHANGES; THREE-DIMENSIONAL STRUCTURE;

EID: 79953211861     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101810f     Document Type: Article
Times cited : (18)

References (58)
  • 1
    • 0021822465 scopus 로고
    • Biologic properties of molecularly cloned and expressed murine interleukin-3
    • Hapel, A. J., Fung, M. C., Johnson, R. M., Young, I. G., Johnson, G., and Metcalf, D. (1985) Biologic properties of molecularly cloned and expressed murine interleukin-3 Blood 65, 1453-1459 (Pubitemid 15057954)
    • (1985) Blood , vol.65 , Issue.6 , pp. 1453-1459
    • Hapel, A.J.1    Fung, M.C.2    Johnson, R.M.3
  • 2
    • 33746520121 scopus 로고    scopus 로고
    • An unexpected role for IL-3 in the embryonic development of hematopoietic stem cells
    • DOI 10.1016/j.devcel.2006.07.002, PII S1534580706003030
    • Robin, C., Ottersbach, K., Durand, C., Peeters, M., Vanes, L., Tybulewicz, V., and Dzierzak, E. (2006) An unexpected role for IL-3 in the embryonic development of hematopoietic stem cells Dev. Cell 11, 171-180 (Pubitemid 44138501)
    • (2006) Developmental Cell , vol.11 , Issue.2 , pp. 171-180
    • Robin, C.1    Ottersbach, K.2    Durand, C.3    Peeters, M.4    Vanes, L.5    Tybulewicz, V.6    Dzierzak, E.7
  • 3
    • 0032485483 scopus 로고    scopus 로고
    • Role for interleukin-3 in mast cell and basophil development and in immunity to parasites
    • DOI 10.1038/32190
    • Lantz, C. S., Boesiger, J., Song, C. H., Mach, N., Kobayashi, T., Mulligan, R. C., Nawa, Y., Dranoff, G., and Galli, S. J. (1998) Role for interleukin-3 in mast-cell and basophil development and in immunity to parasites Nature 392, 90-93 (Pubitemid 28150595)
    • (1998) Nature , vol.392 , Issue.6671 , pp. 90-93
    • Lantz, C.S.1    Boeslger, J.2    Song, C.H.3    Mach, N.4    Kobayashi, T.5    Mulligan, R.C.6    Nawa, Y.7    Dranoff, G.8    Galli, S.J.9
  • 5
    • 67649216604 scopus 로고    scopus 로고
    • Basophils function as antigen-presenting cells for an allergen-induced T helper type 2 response
    • Sokol, C. L., Chu, N. Q., Yu, S., Nish, S. A., Laufer, T. M., and Medzhitov, R. (2009) Basophils function as antigen-presenting cells for an allergen-induced T helper type 2 response Nat. Immunol. 10, 713-720
    • (2009) Nat. Immunol. , vol.10 , pp. 713-720
    • Sokol, C.L.1    Chu, N.Q.2    Yu, S.3    Nish, S.A.4    Laufer, T.M.5    Medzhitov, R.6
  • 7
    • 0028180569 scopus 로고
    • JAK2 associates with the βc chain of the receptor for granulocyte-macrophage colony-stimulating factor, and its activation requires the membrane-proximal region
    • Quelle, F. W., Sato, N., Witthuhn, B. A., Inhorn, R. C., Eder, M., Miyajima, A., Griffin, J. D., and Ihle, J. N. (1994) JAK2 associates with the βc chain of the receptor for granulocyte-macrophage colony-stimulating factor, and its activation requires the membrane-proximal region Mol. Cell. Biol. 14, 4335-4341
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4335-4341
    • Quelle, F.W.1    Sato, N.2    Witthuhn, B.A.3    Inhorn, R.C.4    Eder, M.5    Miyajima, A.6    Griffin, J.D.7    Ihle, J.N.8
  • 8
    • 0026733625 scopus 로고
    • Critical cytoplasmic domains of the common β subunit of the human GM-CSF, IL-3 and IL-5 receptors for growth signal transduction and tyrosine phosphorylation
    • Sakamaki, K., Miyajima, I., Kitamura, T., and Miyajima, A. (1992) Critical cytoplasmic domains of the common β subunit of the human GM-CSF, IL-3 and IL-5 receptors for growth signal transduction and tyrosine phosphorylation EMBO J. 11, 3541-3549
    • (1992) EMBO J. , vol.11 , pp. 3541-3549
    • Sakamaki, K.1    Miyajima, I.2    Kitamura, T.3    Miyajima, A.4
  • 9
    • 65549106958 scopus 로고    scopus 로고
    • A new isoform of interleukin-3 receptor α with novel differentiation activity and high affinity binding mode
    • Chen, J., Olsen, J., Ford, S., Mirza, S., Walker, A., Murphy, J. M., and Young, I. G. (2009) A new isoform of interleukin-3 receptor α with novel differentiation activity and high affinity binding mode J. Biol. Chem. 284, 5763-5773
    • (2009) J. Biol. Chem. , vol.284 , pp. 5763-5773
    • Chen, J.1    Olsen, J.2    Ford, S.3    Mirza, S.4    Walker, A.5    Murphy, J.M.6    Young, I.G.7
  • 10
    • 0344281948 scopus 로고
    • Role of disulfide bridges in determining the biological activity of interleukin 3
    • Clark-Lewis, I., Hood, L. E., and Kent, S. B. (1988) Role of disulfide bridges in determining the biological activity of interleukin 3 Proc. Natl. Acad. Sci. U.S.A. 85, 7897-7901
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 7897-7901
    • Clark-Lewis, I.1    Hood, L.E.2    Kent, S.B.3
  • 11
    • 77949440667 scopus 로고    scopus 로고
    • A convenient method for preparation of an engineered mouse interleukin-3 analog with high solubility and wild-type bioactivity
    • Murphy, J. M., Metcalf, D., Young, I. G., and Hilton, D. J. (2010) A convenient method for preparation of an engineered mouse interleukin-3 analog with high solubility and wild-type bioactivity Growth Factors 28, 104-110
    • (2010) Growth Factors , vol.28 , pp. 104-110
    • Murphy, J.M.1    Metcalf, D.2    Young, I.G.3    Hilton, D.J.4
  • 12
    • 0028988974 scopus 로고
    • 15N NMR resonance assignments, secondary structure, and backbone topology of a variant of human interleukin-3
    • 15N NMR resonance assignments, secondary structure, and backbone topology of a variant of human interleukin-3 Biochemistry 34, 6540-6551
    • (1995) Biochemistry , vol.34 , pp. 6540-6551
    • Feng, Y.1    Klein, B.K.2    Vu, L.3    Aykent, S.4    McWherter, C.A.5
  • 13
    • 0029938639 scopus 로고    scopus 로고
    • Three-dimensional solution structure and backbone dynamics of a variant of human interleukin-3
    • DOI 10.1006/jmbi.1996.0337
    • Feng, Y., Klein, B. K., and McWherter, C. A. (1996) Three-dimensional solution structure and backbone dynamics of a variant of human interleukin-3 J. Mol. Biol. 259, 524-541 (Pubitemid 26179026)
    • (1996) Journal of Molecular Biology , vol.259 , Issue.3 , pp. 524-541
    • Feng, Y.1    Klein, B.K.2    McWherter, C.A.3
  • 14
    • 0020606416 scopus 로고
    • Biologic properties of homogeneous interleukin 3. I. Demonstration of WEHI-3 growth factor activity, mast cell growth factor activity, P cell-stimulating factor activity, colony-stimulating factor activity, and histamine-producing cell-stimulating factor activity
    • Ihle, J. N., Keller, J., Oroszlan, S., Henderson, L. E., Copeland, T. D., Fitch, F., Prystowsky, M. B., Goldwasser, E., Schrader, J. W., Palaszynski, E., Dy, M., and Lebel, B. (1983) Biologic properties of homogeneous interleukin 3. I. Demonstration of WEHI-3 growth factor activity, mast cell growth factor activity, p cell-stimulating factor activity, colony-stimulating factor activity, and histamine-producing cell-stimulating factor activity J. Immunol. 131, 282-287 (Pubitemid 13067894)
    • (1983) Journal of Immunology , vol.131 , Issue.1 , pp. 282-287
    • Ihle, J.N.1    Keller, J.2    Oroszlan, S.3
  • 15
    • 0027155448 scopus 로고
    • A novel dimer configuration revealed by the crystal structure at 2.4 Å resolution of human interleukin-5
    • DOI 10.1038/363172a0
    • Milburn, M. V., Hassell, A. M., Lambert, M. H., Jordan, S. R., Proudfoot, A. E., Graber, P., and Wells, T. N. (1993) A novel dimer configuration revealed by the crystal structure at 2.4 Å resolution of human interleukin-5 Nature 363, 172-176 (Pubitemid 23147017)
    • (1993) Nature , vol.363 , Issue.6425 , pp. 172-176
    • Milburn, M.V.1    Hassell, A.M.2    Lambert, M.H.3    Jordan, S.R.4    Proudfoot, A.E.I.5    Graber, P.6    Wells, T.N.C.7
  • 16
    • 0026520373 scopus 로고
    • Three-dimensional structure of recombinant human granulocyte-macrophage colony-stimulating factor
    • Walter, M. R., Cook, W. J., Ealick, S. E., Nagabhushan, T. L., Trotta, P. P., and Bugg, C. E. (1992) Three-dimensional structure of recombinant human granulocyte-macrophage colony-stimulating factor J. Mol. Biol. 224, 1075-1085
    • (1992) J. Mol. Biol. , vol.224 , pp. 1075-1085
    • Walter, M.R.1    Cook, W.J.2    Ealick, S.E.3    Nagabhushan, T.L.4    Trotta, P.P.5    Bugg, C.E.6
  • 17
    • 77954597135 scopus 로고    scopus 로고
    • Two modes of β-receptor recognition are mediated by distinct epitopes on mouse and human interleukin-3
    • Mirza, S., Chen, J., Wen, B., Ewens, C. L., Dai, J., Murphy, J. M., and Young, I. G. (2010) Two modes of β-receptor recognition are mediated by distinct epitopes on mouse and human interleukin-3 J. Biol. Chem. 285, 22370-22381
    • (2010) J. Biol. Chem. , vol.285 , pp. 22370-22381
    • Mirza, S.1    Chen, J.2    Wen, B.3    Ewens, C.L.4    Dai, J.5    Murphy, J.M.6    Young, I.G.7
  • 18
    • 77951879899 scopus 로고    scopus 로고
    • 15N resonance assignments of a highly-soluble murine interleukin-3 analogue with wild-type bioactivity
    • 15N resonance assignments of a highly-soluble murine interleukin-3 analogue with wild-type bioactivity Biomol. NMR Assign. 4, 73-77
    • (2010) Biomol. NMR Assign. , vol.4 , pp. 73-77
    • Yao, S.1    Murphy, J.M.2    Low, A.3    Norton, R.S.4
  • 19
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins, D. K., Grimshaw, S. B., Receveur, V., Dobson, C. M., Jones, J. A., and Smith, L. J. (1999) Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques Biochemistry 38, 16424-16431
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 20
    • 0034010302 scopus 로고    scopus 로고
    • Peptide self-association in aqueous trifluoroethanol monitored by pulsed field gradient NMR diffusion measurements
    • DOI 10.1023/A:1008382624724
    • Yao, S., Howlett, G. J., and Norton, R. S. (2000) Peptide self-association in aqueous trifluoroethanol monitored by pulsed field gradient NMR diffusion measurements J. Biomol. NMR 16, 109-119 (Pubitemid 30139885)
    • (2000) Journal of Biomolecular NMR , vol.16 , Issue.2 , pp. 109-119
    • Yao, S.1    Howlett, G.J.2    Norton, R.S.3
  • 21
    • 46049109892 scopus 로고    scopus 로고
    • Protein effective rotational correlation times from translational self-diffusion coefficients measured by PFG-NMR
    • Yao, S., Babon, J. J., and Norton, R. S. (2008) Protein effective rotational correlation times from translational self-diffusion coefficients measured by PFG-NMR Biophys. Chem. 136, 145-151
    • (2008) Biophys. Chem. , vol.136 , pp. 145-151
    • Yao, S.1    Babon, J.J.2    Norton, R.S.3
  • 22
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • DOI 10.1023/A:1008392405740
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13, 289-302 (Pubitemid 29143535)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 23
    • 0026858537 scopus 로고
    • Positive Phi-angles in proteins by nuclear magnetic resonance spectroscopy
    • Ludvigsen, S. and Poulsen, F. M. (1992) Positive Phi-angles in proteins by nuclear magnetic resonance spectroscopy J. Biomol. NMR 2, 227-233
    • (1992) J. Biomol. NMR , vol.2 , pp. 227-233
    • Ludvigsen, S.1    Poulsen, F.M.2
  • 24
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • DOI 10.1016/S0022-2836(02)00241-3
    • Herrmann, T., Guntert, P., and Wüthrich, K. (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA J. Mol. Biol. 319, 209-227 (Pubitemid 34729497)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.1 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 28
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graphics 14 (51-55) 29-32
    • (1996) J. Mol. Graphics , vol.14 , Issue.51-55 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 30
    • 4444258777 scopus 로고    scopus 로고
    • C-terminal domain of insulin-like growth factor (IGF) binding protein 6: Conformational exchange and its correlation with IGF-II binding
    • DOI 10.1021/bi049456+
    • Yao, S., Headey, S. J., Keizer, D. W., Bach, L. A., and Norton, R. S. (2004) C-terminal domain of insulin-like growth factor (IGF) binding protein 6: conformational exchange and its correlation with IGF-II binding Biochemistry 43, 11187-11195 (Pubitemid 39180362)
    • (2004) Biochemistry , vol.43 , Issue.35 , pp. 11187-11195
    • Yao, S.1    Headey, S.J.2    Keizer, D.W.3    Bach, L.A.4    Norton, R.S.5
  • 31
    • 33751535118 scopus 로고    scopus 로고
    • Dynamics of the SPRY domain-containing SOCS box protein 2: Flexibility of key functional loops
    • DOI 10.1110/ps.062477806
    • Yao, S., Liu, M. S., Masters, S. L., Zhang, J. G., Babon, J. J., Nicola, N. A., Nicholson, S. E., and Norton, R. S. (2006) Dynamics of the SPRY domain-containing SOCS box protein 2: flexibility of key functional loops Protein Sci. 15, 2761-2772 (Pubitemid 44833757)
    • (2006) Protein Science , vol.15 , Issue.12 , pp. 2761-2772
    • Yao, S.1    Liu, M.S.2    Masters, S.L.3    Zhang, J.-G.4    Babon, J.J.5    Nicola, N.A.6    Nicholson, S.E.7    Norton, R.S.8
  • 32
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules
    • Bartels, C., Xia, T. H., Billeter, M., Güntert, P., and Wüthrich, K. (1995) The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules J. Biomol. NMR 6, 1-10
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 34
    • 0034048847 scopus 로고    scopus 로고
    • Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data
    • DOI 10.1023/A:1008305808620
    • Dosset, P., Hus, J. C., Blackledge, M., and Marion, D. (2000) Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data J. Biomol. NMR 16, 23-28 (Pubitemid 30114721)
    • (2000) Journal of Biomolecular NMR , vol.16 , Issue.1 , pp. 23-28
    • Dosset, P.1    Hus, J.-C.2    Blackledge, M.3    Marion, D.4
  • 37
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy [13]
    • DOI 10.1021/ja983961a
    • Loria, J. P., Rance, M., and Palmer, A. G. (1999) A relaxation- compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy J. Am. Chem. Soc. 121, 2331-2332 (Pubitemid 29152458)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.10 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer III, A.G.3
  • 39
    • 36849127400 scopus 로고
    • Nuclear magnetic resonance study of the protolysis of trimethylammonium ion in aqueous solution-order of the reaction with respect to solvent
    • Lux, Z. and Meiboom, S. (1963) Nuclear magnetic resonance study of the protolysis of trimethylammonium ion in aqueous solution-order of the reaction with respect to solvent J. Chem. Phys. 366-370
    • (1963) J. Chem. Phys. , pp. 366-370
    • Lux, Z.1    Meiboom, S.2
  • 41
    • 0029872895 scopus 로고    scopus 로고
    • Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions
    • Lefevre, J. F., Dayie, K. T., Peng, J. W., and Wagner, G. (1996) Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions Biochemistry 35, 2674-2686
    • (1996) Biochemistry , vol.35 , pp. 2674-2686
    • Lefevre, J.F.1    Dayie, K.T.2    Peng, J.W.3    Wagner, G.4
  • 42
    • 0033525126 scopus 로고    scopus 로고
    • Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: Implications for the entropy of association with DNA
    • DOI 10.1006/jmbi.1998.2429
    • Bracken, C., Carr, P. A., Cavanagh, J., and Palmer, A. G., III (1999) Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: implications for the entropy of association with DNA J. Mol. Biol. 285, 2133-2146 (Pubitemid 29078176)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.5 , pp. 2133-2146
    • Bracken, C.1    Carr, P.A.2    Cavanagh, J.3    Palmer III, A.G.4
  • 44
    • 0032545169 scopus 로고    scopus 로고
    • Characterisation of low free-energy excited states of folded proteins
    • DOI 10.1006/jmbi.1998.2265
    • Baxter, N. J., Hosszu, L. L., Waltho, J. P., and Williamson, M. P. (1998) Characterisation of low free-energy excited states of folded proteins J. Mol. Biol. 284, 1625-1639 (Pubitemid 28566092)
    • (1998) Journal of Molecular Biology , vol.284 , Issue.5 , pp. 1625-1639
    • Baxter, N.J.1    Hosszu, L.L.P.2    Waltho, J.P.3    Williamson, M.P.4
  • 45
    • 0037154884 scopus 로고    scopus 로고
    • Enzyme dynamics during catalysis
    • DOI 10.1126/science.1066176
    • Eisenmesser, E. Z., Bosco, D. A., Akke, M., and Kern, D. (2002) Enzyme dynamics during catalysis Science 295, 1520-1523 (Pubitemid 34174006)
    • (2002) Science , vol.295 , Issue.5559 , pp. 1520-1523
    • Eisenmesser, E.Z.1    Bosco, D.A.2    Akke, M.3    Kern, D.4
  • 46
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • DOI 10.1126/science.1130258
    • Boehr, D. D., McElheny, D., Dyson, H. J., and Wright, P. E. (2006) The dynamic energy landscape of dihydrofolate reductase catalysis Science 313, 1638-1642 (Pubitemid 44414038)
    • (2006) Science , vol.313 , Issue.5793 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wrightt, P.E.4
  • 49
    • 77951908853 scopus 로고    scopus 로고
    • The Ig-like domain of human GM-CSF receptor α plays a critical role in cytokine binding and receptor activation
    • Mirza, S., Walker, A., Chen, J., Murphy, J. M., and Young, I. G. (2010) The Ig-like domain of human GM-CSF receptor α plays a critical role in cytokine binding and receptor activation Biochem. J. 426, 307-317
    • (2010) Biochem. J. , vol.426 , pp. 307-317
    • Mirza, S.1    Walker, A.2    Chen, J.3    Murphy, J.M.4    Young, I.G.5
  • 51
    • 0030062246 scopus 로고    scopus 로고
    • Creation of a biologically active interleukin-5 monomer
    • DOI 10.1038/379652a0
    • Dickason, R. R. and Huston, D. P. (1996) Creation of a biologically active interleukin-5 monomer Nature 379, 652-655 (Pubitemid 26053454)
    • (1996) Nature , vol.379 , Issue.6566 , pp. 652-655
    • Dickason, R.R.1    Huston, D.P.2
  • 52
    • 0035814903 scopus 로고    scopus 로고
    • Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics
    • DOI 10.1021/bi002898a
    • Viles, J. H., Donne, D., Kroon, G., Prusiner, S. B., Cohen, F. E., Dyson, H. J., and Wright, P. E. (2001) Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics Biochemistry 40, 2743-2753 (Pubitemid 32198276)
    • (2001) Biochemistry , vol.40 , Issue.9 , pp. 2743-2753
    • Viles, J.H.1    Donne, D.2    Kroon, G.3    Prusiner, S.B.4    Cohen, F.E.5    Dyson, H.J.6    Wright, P.E.7
  • 53
    • 33751051488 scopus 로고    scopus 로고
    • Structure, Dynamics and Heparin Binding of the C-terminal Domain of Insulin-like Growth Factor-binding Protein-2 (IGFBP-2)
    • DOI 10.1016/j.jmb.2006.09.006, PII S0022283606011788
    • Kuang, Z., Yao, S., Keizer, D. W., Wang, C. C., Bach, L. A., Forbes, B. E., Wallace, J. C., and Norton, R. S. (2006) Structure, dynamics and heparin binding of the C-terminal domain of insulin-like growth factor-binding protein-2 (IGFBP-2) J. Mol. Biol. 364, 690-704 (Pubitemid 44755318)
    • (2006) Journal of Molecular Biology , vol.364 , Issue.4 , pp. 690-704
    • Kuang, Z.1    Yao, S.2    Keizer, D.W.3    Wang, C.C.4    Bach, L.A.5    Forbes, B.E.6    Wallace, J.C.7    Norton, R.S.8
  • 56
    • 70449769332 scopus 로고    scopus 로고
    • Observing biological dynamics at atomic resolution using NMR
    • Mittermaier, A. K. and Kay, L. E. (2009) Observing biological dynamics at atomic resolution using NMR Trends Biochem. Sci. 34, 601-611
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 601-611
    • Mittermaier, A.K.1    Kay, L.E.2
  • 58
    • 33947724974 scopus 로고    scopus 로고
    • IL-3, IL-5, and GM-CSF signaling: Crystal structure of the human β-common receptor
    • Murphy, J. M. and Young, I. G. (2006) IL-3, IL-5, and GM-CSF signaling: crystal structure of the human β-common receptor Vitam. Horm. 74, 1-30
    • (2006) Vitam. Horm. , vol.74 , pp. 1-30
    • Murphy, J.M.1    Young, I.G.2


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