메뉴 건너뛰기




Volumn 19, Issue 13, 2000, Pages 3192-3203

Structure of the active core of human stem cell factor and analysis of binding to its receptor Kit

Author keywords

Crystal structure; Helical cytokine; Hematopoiesis; Multiwavelength anomalous diffraction (MAD); Stem cell factor

Indexed keywords

COLONY STIMULATING FACTOR 1; CYTOKINE; DIMER; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; INTERLEUKIN 2; INTERLEUKIN 4; INTERLEUKIN 5; PLATELET DERIVED GROWTH FACTOR; STEM CELL FACTOR; STEM CELL FACTOR RECEPTOR; VASCULOTROPIN;

EID: 0034600806     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.13.3192     Document Type: Article
Times cited : (101)

References (70)
  • 1
    • 0025185854 scopus 로고
    • Molecular cloning of mast cell growth factor, a hematopoietin that is active in both membrane bound and soluble forms
    • Anderson, D.M. et al. (1990) Molecular cloning of mast cell growth factor, a hematopoietin that is active in both membrane bound and soluble forms. Cell, 63, 235-243.
    • (1990) Cell , vol.63 , pp. 235-243
    • Anderson, D.M.1
  • 2
    • 0025945327 scopus 로고
    • Glycosylaled and unglycosylated recombinant-derived human stem cell factor are dimeric and have extensive regular secondary structure
    • Arakawa, T. et al. (1991) Glycosylaled and unglycosylated recombinant-derived human stem cell factor are dimeric and have extensive regular secondary structure. J. Biol. Chem., 266, 18942-18948.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18942-18948
    • Arakawa, T.1
  • 3
    • 0028116101 scopus 로고
    • Quantification of tertiary structural conservation despite primary sequence drift in the globin fold
    • Aronson, H.-E.G., Royer, W.E.J. and Hendrickson, W.A. (1994) Quantification of tertiary structural conservation despite primary sequence drift in the globin fold. Protein Sci., 3, 1706-1711.
    • (1994) Protein Sci. , vol.3 , pp. 1706-1711
    • Aronson, H.-E.G.1    Royer, W.E.J.2    Hendrickson, W.A.3
  • 4
    • 0030932842 scopus 로고    scopus 로고
    • Mapping of the sites for ligand binding and receptor dimerization at the extracellular domain of the vascular endothelial growth factor receptor flt-1
    • Barleon, B., Totzke, F., Herzog, C., Blanke, S., Kremmer, E., Siemeister, G., Marme, D. and Matiny-Baron, G. (1997) Mapping of the sites for ligand binding and receptor dimerization at the extracellular domain of the vascular endothelial growth factor receptor flt-1. J. Biol. Chem., 272, 10382-10388.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10382-10388
    • Barleon, B.1    Totzke, F.2    Herzog, C.3    Blanke, S.4    Kremmer, E.5    Siemeister, G.6    Marme, D.7    Matiny-Baron, G.8
  • 5
    • 0025857387 scopus 로고
    • Genetic and structural homology of stem cell factor and macrophage colony-stimulating factor
    • Bazan, J.F. (1991) Genetic and structural homology of stem cell factor and macrophage colony-stimulating factor. Cell, 65, 9-10.
    • (1991) Cell , vol.65 , pp. 9-10
    • Bazan, J.F.1
  • 6
    • 0003256013 scopus 로고    scopus 로고
    • Kit-ligand-stem cell factor
    • Garland, J.M., Quesenberry, P.J. and Hilton, D.J. (eds), Marcel Dekker, Inc., New York, NY
    • Besmer, P. (1997) Kit-ligand-stem cell factor. In Garland, J.M., Quesenberry, P.J. and Hilton, D.J. (eds), Colony-Stimulating Factors: Molecular and Cellular Biology. 2nd edn. Marcel Dekker, Inc., New York, NY, pp. 369-404.
    • (1997) Colony-stimulating Factors: Molecular and Cellular Biology. 2nd Edn. , pp. 369-404
    • Besmer, P.1
  • 7
    • 0027414235 scopus 로고
    • Soluble c-kit proteins and antireceptor monoclonal antibodies confine the binding site of the stem cell factor
    • Blechman, J.M., Lev, S., Brizzi, M.F., Leitner, O., Pegoraro, L., Givol, D. and Yarden, Y. (1993) Soluble c-kit proteins and antireceptor monoclonal antibodies confine the binding site of the stem cell factor. J. Biol. Chem., 268, 4399-4406.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4399-4406
    • Blechman, J.M.1    Lev, S.2    Brizzi, M.F.3    Leitner, O.4    Pegoraro, L.5    Givol, D.6    Yarden, Y.7
  • 8
    • 0028890689 scopus 로고
    • The fourth immunoglobulin domain of the stem cell factor receptor couples ligand binding to signal transduction
    • Blechman, J.M., Lev, S., Barg, J., Eisenstein, M., Vaks, B., Vogel, Z., Givol, D. and Yarden, Y. (1995) The fourth immunoglobulin domain of the stem cell factor receptor couples ligand binding to signal transduction. Cell, 80, 103-113.
    • (1995) Cell , vol.80 , pp. 103-113
    • Blechman, J.M.1    Lev, S.2    Barg, J.3    Eisenstein, M.4    Vaks, B.5    Vogel, Z.6    Givol, D.7    Yarden, Y.8
  • 9
    • 0030846533 scopus 로고    scopus 로고
    • Stem cell factor and hematopoiesis
    • Broudy, V.C. (1997) Stem cell factor and hematopoiesis. Blood, 90, 1345-1364.
    • (1997) Blood , vol.90 , pp. 1345-1364
    • Broudy, V.C.1
  • 10
    • 0023140814 scopus 로고
    • Crystallographic R-factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J. and Karplus, M. (1987) Crystallographic R-factor refinement by molecular dynamics. Science, 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 11
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D, 50, 252-270.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 252-270
  • 12
    • 0029790466 scopus 로고    scopus 로고
    • The second immunoglubulin-like domain of the VEGF tyrosine kinase receptor Flt-1 determines ligand binding and may initiate a signal transduction cascade
    • Davis-Symyth, T., Chen, H., Park, J., Presta, L.G. and Ferrara, N. (1996) The second immunoglubulin-like domain of the VEGF tyrosine kinase receptor Flt-1 determines ligand binding and may initiate a signal transduction cascade. EMBO J., 15, 4919-4927.
    • (1996) EMBO J. , vol.15 , pp. 4919-4927
    • Davis-Symyth, T.1    Chen, H.2    Park, J.3    Presta, L.G.4    Ferrara, N.5
  • 13
    • 0026320870 scopus 로고
    • Novel fold and putative receptor binding site of granulocyle-macrophage colony-stimulating factor
    • Diederichs, K., Boone, T. and Karplus, P.A. (1991) Novel fold and putative receptor binding site of granulocyle-macrophage colony-stimulating factor. Science, 254, 1779-1782.
    • (1991) Science , vol.254 , pp. 1779-1782
    • Diederichs, K.1    Boone, T.2    Karplus, P.A.3
  • 14
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three dimensional solid model representations of macromolecules
    • Evans, S.V. (1993) SETOR: hardware lighted three dimensional solid model representations of macromolecules. J. Mol. Graph., 11, 134-138.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 16
    • 0027196849 scopus 로고
    • A cationic region of the platelet-derived growth factor (PDGF) A-chain (Arg159-Lys160-Lys161) is required for receptor binding and mitogenic activity of the PDGF-AA homodimer
    • Fenstermaker, R.A. et al. (1993) A cationic region of the platelet-derived growth factor (PDGF) A-chain (Arg159-Lys160-Lys161) is required for receptor binding and mitogenic activity of the PDGF-AA homodimer. J. Biol. Chem., 268, 10482-10489.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10482-10489
    • Fenstermaker, R.A.1
  • 17
    • 0029874551 scopus 로고    scopus 로고
    • Fold recognition using sequence-derived predictions
    • Fisher, D. and Eisenberg, D. (1996) Fold recognition using sequence-derived predictions. Protein Sci., 5, 947-955.
    • (1996) Protein Sci. , vol.5 , pp. 947-955
    • Fisher, D.1    Eisenberg, D.2
  • 18
    • 84967852329 scopus 로고
    • MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement
    • Fitzgerald, P.M.D. (1988) MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement. J. Appl. Crystallagr., 21, 273-278.
    • (1988) J. Appl. Crystallagr. , vol.21 , pp. 273-278
    • Fitzgerald, P.M.D.1
  • 20
    • 0003615263 scopus 로고
    • Yale University, New Haven, CT
    • Gewirth, D. (1995) The HKL Manual. Yale University, New Haven, CT.
    • (1995) The HKL Manual
    • Gewirth, D.1
  • 21
    • 0029947810 scopus 로고    scopus 로고
    • Clinical applications of stem cell factor
    • Glaspy, J. (1996) Clinical applications of stem cell factor. Curr. Opin. Hematol., 3, 223-229.
    • (1996) Curr. Opin. Hematol. , vol.3 , pp. 223-229
    • Glaspy, J.1
  • 22
    • 0028361540 scopus 로고
    • Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains
    • Harpaz, Y. and Chothia, C. (1994) Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J. Mol. Biol., 238, 528-539.
    • (1994) J. Mol. Biol. , vol.238 , pp. 528-539
    • Harpaz, Y.1    Chothia, C.2
  • 23
    • 0025153862 scopus 로고
    • Chimeric α- and β-platelet-derived growth factor (PDGF) receptors define three immunoglobulin-like domains of the α-PDGF receptor that determine PDGF-AA binding specificity
    • Heidaran, M.A., Pierce, J.H., Jensen, R.A., Matsui, T. and Aaronson, S.A. (1990) Chimeric α- and β-platelet-derived growth factor (PDGF) receptors define three immunoglobulin-like domains of the α-PDGF receptor that determine PDGF-AA binding specificity. J. Biol. Chem., 265, 18741-18744.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18741-18744
    • Heidaran, M.A.1    Pierce, J.H.2    Jensen, R.A.3    Matsui, T.4    Aaronson, S.A.5
  • 24
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin, C.-H. (1995) Dimerization of cell surface receptors in signal transduction. Cell, 80, 213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.-H.1
  • 25
    • 0000933280 scopus 로고
    • Transformations to optimize the superposition of similar structures
    • Hendrickson, W.A. (1979) Transformations to optimize the superposition of similar structures. Acta Cryatallogr. A, 35, 158-163.
    • (1979) Acta Cryatallogr. A , vol.35 , pp. 158-163
    • Hendrickson, W.A.1
  • 26
    • 0022317258 scopus 로고
    • Direct phase determination based on anomalous scattering
    • Hendrickson, W.A., Smith, J.L. and Sheriff, S. (1985) Direct phase determination based on anomalous scattering. Methods Enzymol., 115, 41-55.
    • (1985) Methods Enzymol. , vol.115 , pp. 41-55
    • Hendrickson, W.A.1    Smith, J.L.2    Sheriff, S.3
  • 27
    • 0029897141 scopus 로고    scopus 로고
    • In vitro methionine oxidation of Escherichia coli-derived human stem cell factor: Effects on the molecular structure, biological activity, and dimerization
    • Hsu, Y.-R., Narhi, L.O., Spahr, C., Langley, K.E. and Lu, H.S. (1996) In vitro methionine oxidation of Escherichia coli-derived human stem cell factor: effects on the molecular structure, biological activity, and dimerization. Protein Sci., 5, 1165-1173.
    • (1996) Protein Sci. , vol.5 , pp. 1165-1173
    • Hsu, Y.-R.1    Narhi, L.O.2    Spahr, C.3    Langley, K.E.4    Lu, H.S.5
  • 28
    • 0032562225 scopus 로고    scopus 로고
    • Selective deamidation of recombinant human stem cell factor during in vitro aging: Isolation and characterization of the aspartyl and isoaspartyl homodimers and heterodimers
    • Hsu, Y.-R., Chang, W.-C., Mendiaz, E.A., Hara, S., Chow, D.T., Mann, M.B., Langley, K.E. and Lu, H.S. (1998) Selective deamidation of recombinant human stem cell factor during in vitro aging: isolation and characterization of the aspartyl and isoaspartyl homodimers and heterodimers. Biochemistry, 37, 2251-2262.
    • (1998) Biochemistry , vol.37 , pp. 2251-2262
    • Hsu, Y.-R.1    Chang, W.-C.2    Mendiaz, E.A.3    Hara, S.4    Chow, D.T.5    Mann, M.B.6    Langley, K.E.7    Lu, H.S.8
  • 29
    • 0025077796 scopus 로고
    • The hematopoietic growth factor KL is encoded by the Sl locus and is the ligand of the c-kit receptor, the product of the W locus
    • Huang, E., Nocka, K., Beier, D.R., Chu, T.-Y., Buck, J., Lahm, H.-W., Wellner, D., Leder, P. and Besmer, P. (1990) The hematopoietic growth factor KL is encoded by the Sl locus and is the ligand of the c-kit receptor, the product of the W locus. Cell, 63, 225-233.
    • (1990) Cell , vol.63 , pp. 225-233
    • Huang, E.1    Nocka, K.2    Beier, D.R.3    Chu, T.-Y.4    Buck, J.5    Lahm, H.-W.6    Wellner, D.7    Leder, P.8    Besmer, P.9
  • 31
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A, 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 32
    • 0025622837 scopus 로고
    • Molecular biology of macrophage colony-stimulating factor
    • Kawasaki, E.S. and Ladner, M.B. (1990) Molecular biology of macrophage colony-stimulating factor, Immunol. Ser., 49, 155-176.
    • (1990) Immunol. Ser. , vol.49 , pp. 155-176
    • Kawasaki, E.S.1    Ladner, M.B.2
  • 33
    • 0002700643 scopus 로고
    • Halloween... Masks and bones
    • Bailey, S., Hubbard, R. and Waller, D. (eds), Daresbury Laboratory, Warrington, UK
    • Kleywegt, G.J. and Jones, T.A. (1994) Halloween... masks and bones. In Bailey, S., Hubbard, R. and Waller, D. (eds), From First Map to Final Model, Proceedings of the CCP4 Study Weekend. Daresbury Laboratory, Warrington, UK. pp. 59-66.
    • (1994) From First Map to Final Model, Proceedings of the CCP4 Study Weekend , pp. 59-66
    • Kleywegt, G.J.1    Jones, T.A.2
  • 34
    • 0026625636 scopus 로고
    • Purification and characterization of soluble forms of human and rat stem cell factor recombinantly expressed by Escherichia coli and by Chinese hamster ovary cells
    • Langley, K.E. et al. (1992) Purification and characterization of soluble forms of human and rat stem cell factor recombinantly expressed by Escherichia coli and by Chinese hamster ovary cells. Arch. Biochem. Biophys., 295, 21-28.
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 21-28
    • Langley, K.E.1
  • 35
    • 0028309019 scopus 로고
    • Properties of variant forms of human stem cell factor recombinantly expressed in Escherichia coli
    • Langley, K.E. et al. (1994) Properties of variant forms of human stem cell factor recombinantly expressed in Escherichia coli. Arch. Biochem. Biophys., 311, 55-61.
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 55-61
    • Langley, K.E.1
  • 36
  • 37
    • 0030889905 scopus 로고    scopus 로고
    • Kit receptor dimerization is driven by bivalent binding of stem cell factor
    • Lemmon, M.A., Pinchasi, D., Zhou, M., Lax, I. and Schlessinger, J. (1997) Kit receptor dimerization is driven by bivalent binding of stem cell factor. J. Biol. Chem., 272, 6311-6317.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6311-6317
    • Lemmon, M.A.1    Pinchasi, D.2    Zhou, M.3    Lax, I.4    Schlessinger, J.5
  • 38
    • 0026720074 scopus 로고
    • Dimerization and activation of the Kit receptor by monovalent and bivalent binding of the stem cell factor
    • Lev, S., Yarden, Y. and Givol, D. (1992) Dimerization and activation of the Kit receptor by monovalent and bivalent binding of the stem cell factor. J. Biol. Chem., 267, 15970-15977.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15970-15977
    • Lev, S.1    Yarden, Y.2    Givol, D.3
  • 39
    • 0027477388 scopus 로고
    • Interspecies molecular chimeras of kit help define the binding site of the stem cell factor
    • Lev, S., Blechman, J., Nishikawa, S.-I., Givol, D. and Yarden, Y. (1993) Interspecies molecular chimeras of Kit help define the binding site of the stem cell factor. Mol. Cell. Biol., 13, 2224-2234.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2224-2234
    • Lev, S.1    Blechman, J.2    Nishikawa, S.-I.3    Givol, D.4    Yarden, Y.5
  • 40
    • 0028252924 scopus 로고
    • Steel factor and c-kit protooncogene: Genetic lessons in signal transduction
    • Lev, S., Blechman, J.M. Givol, D. and Yarden, Y. (1994) Steel factor and c-kit protooncogene: genetic lessons in signal transduction. Crit. Rev. Oncog., 5, 141-168.
    • (1994) Crit. Rev. Oncog. , vol.5 , pp. 141-168
    • Lev, S.1    Blechman, J.M.2    Givol, D.3    Yarden, Y.4
  • 41
    • 0025781622 scopus 로고
    • Amino acid sequence and post-translational modification of stem cell factor isolated from buffalo rat liver cell-conditioned medium
    • Lu, H.S., Clogston, C.L., Wypych, J., Fausset, P., Lauren, S., Mendiaz, E.A., Zsebo, K. and Langley, K.E. (1991) Amino acid sequence and post-translational modification of stem cell factor isolated from buffalo rat liver cell-conditioned medium. J. Biol Chem., 266, 8102-8107.
    • (1991) J. Biol Chem. , vol.266 , pp. 8102-8107
    • Lu, H.S.1    Clogston, C.L.2    Wypych, J.3    Fausset, P.4    Lauren, S.5    Mendiaz, E.A.6    Zsebo, K.7    Langley, K.E.8
  • 42
    • 0026739279 scopus 로고
    • Post-translational processing of membrane-associated recombinant human stem cell factor expressed in Chinese hamster ovary cells
    • Lu, H.S. et al. (1992) Post-translational processing of membrane-associated recombinant human stem cell factor expressed in Chinese hamster ovary cells. Arch. Biochem. Biophys., 298, 150-158.
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 150-158
    • Lu, H.S.1
  • 44
    • 0032519768 scopus 로고    scopus 로고
    • c-Kit ligand and flt3 ligand: Stem/progenitor cell factors with overlapping yet distinct activities
    • Lyman, S.D. and Jacobsen, S.E.W. (1998) c-Kit ligand and Flt3 ligand: stem/progenitor cell factors with overlapping yet distinct activities. Blood, 91, 1101-1134.
    • (1998) Blood , vol.91 , pp. 1101-1134
    • Lyman, S.D.1    Jacobsen, S.E.W.2
  • 45
    • 0025065459 scopus 로고
    • Primary structure and functional expression of rat and human stem cell factor DNAs
    • Martin, F.H. et al. (1990) Primary structure and functional expression of rat and human stem cell factor DNAs. Cell, 63, 203-211.
    • (1990) Cell , vol.63 , pp. 203-211
    • Martin, F.H.1
  • 46
    • 0029999856 scopus 로고    scopus 로고
    • Structure-function relationships of stem cell factor: An analysis based on a series of human-murine scf chimera and the mapping of a neutralizing monoclonal antibody
    • Matous, J.V., Langley, K.E. and Kaushansky, K. (1996) Structure-function relationships of stem cell factor: an analysis based on a series of human-murine SCF chimera and the mapping of a neutralizing monoclonal antibody. Blood, 88, 437-144.
    • (1996) Blood , vol.88 , pp. 437-1144
    • Matous, J.V.1    Langley, K.E.2    Kaushansky, K.3
  • 47
    • 0026763387 scopus 로고
    • Unraveling the structure of IL-2
    • McKay, D.B. (1992) Unraveling the structure of IL-2. Science, 257, 412-413.
    • (1992) Science , vol.257 , pp. 412-413
    • McKay, D.B.1
  • 50
    • 0027155448 scopus 로고
    • A novel dimer configuration revealed by the crystal structure at 2.4 Å resolution of human interleukin-5
    • Milburn, W.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.
    • (1993) Nature , vol.363 , pp. 172-176
    • Milburn, W.V.1    Hassell, A.M.2    Lambert, M.H.3    Jordan, S.R.4    Proudfoot, A.E.5    Graber, P.6    Wells, T.N.7
  • 51
    • 0030795733 scopus 로고    scopus 로고
    • Vascular endothelial growth factor: Crystal structure and functional mapping of the kinase domain receptor binding site
    • Muller, Y.A., Li, B., Christinger, H.W., Wells, J.A., Cunningham, B.C. and de Vos, A.M. (1997) Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site. Proc. Natl. Acad. Sci. USA, 94, 7192-7197.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7192-7197
    • Muller, Y.A.1    Li, B.2    Christinger, H.W.3    Wells, J.A.4    Cunningham, B.C.5    De Vos, A.M.6
  • 52
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins, 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 53
    • 0026744790 scopus 로고
    • Crystal structure of human platelet-derived growth factor BB
    • Oefner, C., DíArcy, A., Winker, F.K., Eggimann, B. and Hosang, M. (1992) Crystal structure of human platelet-derived growth factor BB. EMBO J., 11, 3921-3926.
    • (1992) EMBO J. , vol.11 , pp. 3921-3926
    • Oefner, C.1    Díarcy, A.2    Winker, F.K.3    Eggimann, B.4    Hosang, M.5
  • 54
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Sawyer, N.I.L. and Bailey, S. (eds). Science and Engineering Research Council, Warrington, UK
    • Otwinowski, Z. (1993) Oscillation data reduction program. In Sawyer, N.I.L. and Bailey, S. (eds). Data Collection and Processing. Science and Engineering Research Council, Warrington, UK, pp. 55-62.
    • (1993) Data Collection and Processing , pp. 55-62
    • Otwinowski, Z.1
  • 55
    • 0038581953 scopus 로고
    • A probability representation for phase information from multiwavelength anomalous dispersion
    • Pähler, A., Smith, J.L. and Hendrickson, W.A. (1990) A probability representation for phase information from multiwavelength anomalous dispersion. Acta Crystallogr. A, 46, 537-540.
    • (1990) Acta Crystallogr. A , vol.46 , pp. 537-540
    • Pähler, A.1    Smith, J.L.2    Hendrickson, W.A.3
  • 56
    • 0026727235 scopus 로고
    • Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor
    • Pandit, J., Bohm, A., Jancarik, J., Halenbeck, R., Koths, K. and Kim, S.-H. (1992) Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor. Science. 258, 1358-1362.
    • (1992) Science , vol.258 , pp. 1358-1362
    • Pandit, J.1    Bohm, A.2    Jancarik, J.3    Halenbeck, R.4    Koths, K.5    Kim, S.-H.6
  • 57
    • 0029864410 scopus 로고    scopus 로고
    • Human stem cell factor dimer forms a complex with two molecules of the extracellular domain of its receptor. Kit
    • Philo, J.S., Wen, J., Wypych, J., Schwartz, M.G., Mendiaz, E.A. and Langley, K.E. (1996) Human stem cell factor dimer forms a complex with two molecules of the extracellular domain of its receptor. Kit. J. Biol. Chem., 271, 6895-6902.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6895-6902
    • Philo, J.S.1    Wen, J.2    Wypych, J.3    Schwartz, M.G.4    Mendiaz, E.A.5    Langley, K.E.6
  • 58
    • 0033520472 scopus 로고    scopus 로고
    • Structural basis for fgf receptor dimerization and activation
    • Plotnikov, A.N., Schlessinger, J., Hubbard, S.R. and Mohammadi, M. (1999) Structural basis for FGF receptor dimerization and activation. Cell, 98, 641-650.
    • (1999) Cell , vol.98 , pp. 641-650
    • Plotnikov, A.N.1    Schlessinger, J.2    Hubbard, S.R.3    Mohammadi, M.4
  • 59
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986) Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A, 42, 140-149.
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 60
    • 0029126850 scopus 로고
    • Molecular evolution of the genes encoding receptor tyrosine kinase with immunoglobulin-like domains
    • Rousset, D., Agnes, F., Lachaume, P., Andre, C. and Galibert, F. (1995) Molecular evolution of the genes encoding receptor tyrosine kinase with immunoglobulin-like domains. J. Mol. Evol., 41, 421-430.
    • (1995) J. Mol. Evol. , vol.41 , pp. 421-430
    • Rousset, D.1    Agnes, F.2    Lachaume, P.3    Andre, C.4    Galibert, F.5
  • 62
    • 0018625422 scopus 로고
    • Hereditary anemias of the mouse: A review for geneticists
    • Russell, E.S. (1979) Hereditary anemias of the mouse: a review for geneticists. Acta. Genet., 20, 357-459.
    • (1979) Acta. Genet. , vol.20 , pp. 357-459
    • Russell, E.S.1
  • 63
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms. Lysozyme and insulin
    • Shrake, A. and Rupley, J.A. (1973) Environment and exposure to solvent of protein atoms. Lysozyme and insulin. J. Mol. Biol., 79, 351-371.
    • (1973) J. Mol. Biol. , vol.79 , pp. 351-371
    • Shrake, A.1    Rupley, J.A.2
  • 64
    • 0026674062 scopus 로고
    • Canine stem cell factor (c-kit ligand) supports the survival of hematopoietic progenitors in long-term canine marrow culture
    • Shull, R.M., Suggs, S.V., Langley, K.E., Okino, K.H., Jacobsen, F.W. and Martin, F.H. (1992) Canine stem cell factor (c-kit ligand) supports the survival of hematopoietic progenitors in long-term canine marrow culture. Evol. Hematol., 20, 1118-1124.
    • (1992) Evol. Hematol. , vol.20 , pp. 1118-1124
    • Shull, R.M.1    Suggs, S.V.2    Langley, K.E.3    Okino, K.H.4    Jacobsen, F.W.5    Martin, F.H.6
  • 65
    • 0027145507 scopus 로고
    • Cytokine structural taxonomy and mechanisms of receptor engagement
    • Sprang, S.R. and Bazan J.F. (1993) Cytokine structural taxonomy and mechanisms of receptor engagement. Curr. Opin. Struct. Biol., 3, 815-827.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 815-827
    • Sprang, S.R.1    Bazan, J.F.2
  • 67
    • 0028053407 scopus 로고
    • Structure-function studies on recombinant human macrophage colony-stimulating factor (M-CSF)
    • Taylor, E.W., Fear, A.L., Bohm, A., Kim, S.-H. and Koths, K. (1994) Structure-function studies on recombinant human macrophage colony-stimulating factor (M-CSF). J. Biol. Chem., 269, 31171-31177.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31171-31177
    • Taylor, E.W.1    Fear, A.L.2    Bohm, A.3    Kim, S.-H.4    Koths, K.5
  • 68
    • 0027240263 scopus 로고
    • Identification of the ligand-binding regions in the macrophage colony-stimulating factor receptor extracellular domain
    • Wang, Z., Myles, G.M., Brandt, C.S., Liouhin, M.N. and Rohrschneider, L. (1993) Identification of the ligand-binding regions in the macrophage colony-stimulating factor receptor extracellular domain. Mol. Cell. Biol., 13, 5348-5359.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5348-5359
    • Wang, Z.1    Myles, G.M.2    Brandt, C.S.3    Liouhin, M.N.4    Rohrschneider, L.5
  • 69
    • 0030782410 scopus 로고    scopus 로고
    • Crystal structure at 1.7 Å resolution of VEGF in complex with domain 2 of the Flt-1 receptor
    • Wiesmann, C., Fuh, G., Christinger, H.W., Eigenbrot, C., Wells, J.A. and de Vos, A.M. (1997) Crystal structure at 1.7 Å resolution of VEGF in complex with domain 2 of the Flt-1 receptor. Cell, 91, 695-704.
    • (1997) Cell , vol.91 , pp. 695-704
    • Wiesmann, C.1    Fuh, G.2    Christinger, H.W.3    Eigenbrot, C.4    Wells, J.A.5    De Vos, A.M.6
  • 70
    • 0026661731 scopus 로고
    • Crystal structure of human recombinant interleukin-4 at 2.25 Å
    • Wlodawer, A., Pavlovsky, A. and Gustchina, A. (1992) Crystal structure of human recombinant interleukin-4 at 2.25 Å. FEBS Lett., 309, 59-64.
    • (1992) FEBS Lett. , vol.309 , pp. 59-64
    • Wlodawer, A.1    Pavlovsky, A.2    Gustchina, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.