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Volumn 6, Issue 9, 1998, Pages 1153-1167

VEGF and the Fab fragment of a humanized neutralizing antibody: Crystal structure of the complex at 2.4 Å resolution and mutational analysis of the interface

Author keywords

Angiogenesis; Antibody antigen recognition; Mutagenesis; Phage display; X ray structure

Indexed keywords

MURINAE;

EID: 0032530717     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00116-6     Document Type: Article
Times cited : (255)

References (57)
  • 1
    • 0029004025 scopus 로고
    • Vascular permeability factor/vascular endothelial growth factor, microvascular hyperpermeability and angiogenesis
    • Dvorak, H.F., Brown, L.F., Detmar, M. & Dvorak, A.M. (1995). Vascular permeability factor/vascular endothelial growth factor, microvascular hyperpermeability and angiogenesis. Am. J. Pathol. 146, 1029-1039.
    • (1995) Am. J. Pathol. , vol.146 , pp. 1029-1039
    • Dvorak, H.F.1    Brown, L.F.2    Detmar, M.3    Dvorak, A.M.4
  • 2
    • 0029127218 scopus 로고
    • The role of vascular endothelial growth factor in pathological angiogenesis
    • Ferrara, N. (1995). The role of vascular endothelial growth factor in pathological angiogenesis. Breast Cancer Res. Treat. 36, 127-137.
    • (1995) Breast Cancer Res. Treat. , vol.36 , pp. 127-137
    • Ferrara, N.1
  • 3
    • 0028929803 scopus 로고
    • Angiogenesis in cancer, vascular, rheumatoid and other disease
    • Folkman, J. (1995). Angiogenesis in cancer, vascular, rheumatoid and other disease. Nat. Med. 1, 27-31.
    • (1995) Nat. Med. , vol.1 , pp. 27-31
    • Folkman, J.1
  • 4
    • 0343920277 scopus 로고    scopus 로고
    • Abnormal blood vessel development and lethality in embryos lacking a single VEGF allele
    • Carmeliet, P., et al., & Nagy, A. (1996). Abnormal blood vessel development and lethality in embryos lacking a single VEGF allele. Nature 380, 435-439.
    • (1996) Nature , vol.380 , pp. 435-439
    • Carmeliet, P.1    Nagy, A.2
  • 5
    • 0030004485 scopus 로고    scopus 로고
    • Heterozygous embryonic lethality induced by targeted inactivation of the VEGF gene
    • Ferrara, N., et al., & Moore, M.W. (1996). Heterozygous embryonic lethality induced by targeted inactivation of the VEGF gene. Nature 380, 439-442.
    • (1996) Nature , vol.380 , pp. 439-442
    • Ferrara, N.1    Moore, M.W.2
  • 6
    • 0027197245 scopus 로고
    • Inhibition of vascular endothelial growth factor-induced angiogenesis suppresses tumour growth in vivo
    • Kim, K.J., et al., & Ferrara, N. (1993). Inhibition of vascular endothelial growth factor-induced angiogenesis suppresses tumour growth in vivo. Nature 362, 841-844.
    • (1993) Nature , vol.362 , pp. 841-844
    • Kim, K.J.1    Ferrara, N.2
  • 7
    • 0030993418 scopus 로고    scopus 로고
    • Antibody humanization using monovalent phage display
    • Baca, M., Presta, L.G., O'Connor, S.J. & Wells, J.A. (1997). Antibody humanization using monovalent phage display. J. Biol. Chem. 272, 10678-10684.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10678-10684
    • Baca, M.1    Presta, L.G.2    O'Connor, S.J.3    Wells, J.A.4
  • 8
    • 0030856731 scopus 로고    scopus 로고
    • Humanization of an antivascular endothelial growth factor monoclonal antibody for the therapy of solid tumors and other disorders
    • Presta, L.G, et al., & Ferrara, N. (1997). Humanization of an antivascular endothelial growth factor monoclonal antibody for the therapy of solid tumors and other disorders. Cancer Res. 47, 4593-4599.
    • (1997) Cancer Res. , vol.47 , pp. 4593-4599
    • Presta, L.G.1    Ferrara, N.2
  • 9
    • 0027997863 scopus 로고
    • Different signal transduction properties of KDR and Flt1, two receptors for vascular endothelial growth factor
    • Waltenberger, J., Claesson-Welsh, L., Siegbahn, A., Shibuya, M. & Heldin, C.-H. (1994). Different signal transduction properties of KDR and Flt1, two receptors for vascular endothelial growth factor. J. Biol. Chem. 269, 26988-26995.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26988-26995
    • Waltenberger, J.1    Claesson-Welsh, L.2    Siegbahn, A.3    Shibuya, M.4    Heldin, C.-H.5
  • 10
    • 0026395163 scopus 로고
    • The vascular endothelial growth factor family: Identification of a fourth molecular species and characterization of alternative splicing of RNA
    • Houck, K.A., Ferrara, N., Winer, J., Cachianes, G., Li, B. & Leung, D.W. (1991). The vascular endothelial growth factor family: identification of a fourth molecular species and characterization of alternative splicing of RNA. Mol. Endocrinol. 5, 1806-1814.
    • (1991) Mol. Endocrinol. , vol.5 , pp. 1806-1814
    • Houck, K.A.1    Ferrara, N.2    Winer, J.3    Cachianes, G.4    Li, B.5    Leung, D.W.6
  • 11
    • 0029937679 scopus 로고    scopus 로고
    • The carboxyl-terminal domain (111-165) of vascular endothelial growth factor is critical for its mitogenic potency
    • Keyt, B.A., et al., & Ferrara, N. (1996). The carboxyl-terminal domain (111-165) of vascular endothelial growth factor is critical for its mitogenic potency. J. Biol. Chem. 271, 7788-7795.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7788-7795
    • Keyt, B.A.1    Ferrara, N.2
  • 12
    • 0031572858 scopus 로고    scopus 로고
    • The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 Å resolution: Multiple copy flexibility and receptor binding
    • Muller, Y.A., Christinger, H.W., Keyt, B.A. & De Vos, A.M. (1997). The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 Å resolution: multiple copy flexibility and receptor binding. Structure 5, 1325-1338.
    • (1997) Structure , vol.5 , pp. 1325-1338
    • Muller, Y.A.1    Christinger, H.W.2    Keyt, B.A.3    De Vos, A.M.4
  • 14
    • 0029920944 scopus 로고    scopus 로고
    • Identification of vascular endothelial growth factor determinants for binding KDR and FLT-1 receptors
    • Keyt, B.A., et al., & Ferrara, N. (1996). Identification of vascular endothelial growth factor determinants for binding KDR and FLT-1 receptors. J. Biol. Chem. 271, 5638-5646.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5638-5646
    • Keyt, B.A.1    Ferrara, N.2
  • 15
    • 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. & 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
  • 16
    • 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. & 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
  • 17
    • 0024403619 scopus 로고
    • High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis
    • Cunningham, B.C. & Wells, J.A. (1989). High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 244, 1081-1085.
    • (1989) Science , vol.244 , pp. 1081-1085
    • Cunningham, B.C.1    Wells, J.A.2
  • 18
    • 0027228495 scopus 로고
    • Thermodynamic analysis of an antibody functional epitope
    • Kelley, R.F. & O'Connell, M.P. (1993). Thermodynamic analysis of an antibody functional epitope. Biochemistry 32, 6828-6835.
    • (1993) Biochemistry , vol.32 , pp. 6828-6835
    • Kelley, R.F.1    O'Connell, M.P.2
  • 19
    • 0029982521 scopus 로고    scopus 로고
    • Hematopoietic receptor complexes
    • Wells, J.A. & De Vos, A.M. (1996). Hematopoietic receptor complexes. Annu. Rev. Biochem. 65, 609-634.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 609-634
    • Wells, J.A.1    De Vos, A.M.2
  • 20
    • 0029851571 scopus 로고    scopus 로고
    • Crystallization of the receptor binding domain of vascular endothelial growth factor
    • Christinger, H.W., et al., & De Vos, A.M. (1996). Crystallization of the receptor binding domain of vascular endothelial growth factor. Proteins 26, 353-357.
    • (1996) Proteins , vol.26 , pp. 353-357
    • Christinger, H.W.1    De Vos, A.M.2
  • 21
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using partial structures with errors
    • Read, R.J. (1986). Improved Fourier coefficients for maps using partial structures with errors. Acta Cryst. A 42, 140-149.
    • (1986) Acta Cryst. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 22
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). Procheck: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 23
    • 0031558771 scopus 로고    scopus 로고
    • Neutralizing epitopes on the extracellular interferon γ receptor (IFNγR) α-chain characterized by homolog scanning mutagenesis and x-ray crystal structure of the A6 FAB-IFNγR1-108 complex
    • Sogabe, S., et al., & Robinson, J.A. (1997). Neutralizing epitopes on the extracellular interferon γ receptor (IFNγR) α-chain characterized by homolog scanning mutagenesis and x-ray crystal structure of the A6 FAB-IFNγR1-108 complex. J. Mol. Biol. 273, 882-897.
    • (1997) J. Mol. Biol. , vol.273 , pp. 882-897
    • Sogabe, S.1    Robinson, J.A.2
  • 24
    • 0030596154 scopus 로고    scopus 로고
    • Ribosomal protein L9: A structure determination by the combined use of x-ray crystallography and NMR spectroscopy
    • Hoffman, D.W., Cameron, C.S., Davies, C., White, S.W. & Ramakrishnan, V. (1996). Ribosomal protein L9: a structure determination by the combined use of x-ray crystallography and NMR spectroscopy. J. Mol. Biol. 264, 1058-1071.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1058-1071
    • Hoffman, D.W.1    Cameron, C.S.2    Davies, C.3    White, S.W.4    Ramakrishnan, V.5
  • 25
    • 0026744790 scopus 로고
    • Crystal structure of human platelet-derived growth factor BB
    • Oefner, C., D'Arcy, A., Winkler, F.K., Eggimann, B. & 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    D'Arcy, A.2    Winkler, F.K.3    Eggimann, B.4    Hosang, M.5
  • 28
    • 0028606741 scopus 로고
    • Antibody-antigen interactions: New structures and new conformational changes
    • Wilson, I.A. & Stanfield, R.L. (1994). Antibody-antigen interactions: new structures and new conformational changes. Curr. Opin. Struct. Biol. 4, 857-867.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 857-867
    • Wilson, I.A.1    Stanfield, R.L.2
  • 29
    • 0024844388 scopus 로고
    • Conformations of immunoglobulin hypervariable regions
    • Chothia, C., et al., & Poljak, R.J. (1989). Conformations of immunoglobulin hypervariable regions. Nature 342, 877-883.
    • (1989) Nature , vol.342 , pp. 877-883
    • Chothia, C.1    Poljak, R.J.2
  • 30
    • 0028828994 scopus 로고
    • The crystal structure of the antibody N10-Staphylococcal nuclease complex at 2.9 Å resolution
    • Bossart-Whitaker, P., Chang, C.Y.Y., Novotny, J., Benjamin, D.C. & Sheriff, S. (1995). The crystal structure of the antibody N10-Staphylococcal nuclease complex at 2.9 Å resolution. J. Mol. Biol. 253, 559-575.
    • (1995) J. Mol. Biol. , vol.253 , pp. 559-575
    • Bossart-Whitaker, P.1    Chang, C.Y.Y.2    Novotny, J.3    Benjamin, D.C.4    Sheriff, S.5
  • 31
    • 10144235477 scopus 로고    scopus 로고
    • Refined structures of bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 FAB fragment
    • Chacko, S., et al., & Sheriff, S. (1996). Refined structures of bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 FAB fragment. Proteins 26, 55-65.
    • (1996) Proteins , vol.26 , pp. 55-65
    • Chacko, S.1    Sheriff, S.2
  • 32
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • Davies, D.R. & Cohen, G.H. (1996). Interactions of protein antigens with antibodies. Proc. Natl Acad. Sci. USA 93, 7-12.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 33
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones, S. & Thornton, J.M. (1996). Principles of protein-protein interactions. Proc. Natl Acad. Sci. USA 93, 13-20.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 35
    • 0024279235 scopus 로고
    • Analysis and prediction of the different types of β-turn in proteins
    • Wilmot, C.M. & Thornton, J.M. (1988). Analysis and prediction of the different types of β-turn in proteins. J. Mol. Biol. 203, 221-232.
    • (1988) J. Mol. Biol. , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 36
    • 0025275610 scopus 로고
    • On the nature of antibody combining sites: Unusual structural features that may confer on these sites an enhanced capacity for binding ligands
    • Padlan, E.A. (1990). On the nature of antibody combining sites: unusual structural features that may confer on these sites an enhanced capacity for binding ligands. Proteins 7, 112-124.
    • (1990) Proteins , vol.7 , pp. 112-124
    • Padlan, E.A.1
  • 37
    • 0027132013 scopus 로고
    • Comparison of a structural and a functional epitope
    • Cunningham, B.C. & Wells, J.A. (1993). Comparison of a structural and a functional epitope. J. Mol. Biol. 234, 554-563.
    • (1993) J. Mol. Biol. , vol.234 , pp. 554-563
    • Cunningham, B.C.1    Wells, J.A.2
  • 38
    • 0024362070 scopus 로고
    • On the attribution of binding energy in antigen-antibody complexes McPC 603, D1-3, and HyHEL-5
    • Novotny, J., Bruccoleri, R.E. & Saul, F.A. (1989). On the attribution of binding energy in antigen-antibody complexes McPC 603, D1-3, and HyHEL-5. Biochemistry 28, 4735-4749.
    • (1989) Biochemistry , vol.28 , pp. 4735-4749
    • Novotny, J.1    Bruccoleri, R.E.2    Saul, F.A.3
  • 39
    • 0022519337 scopus 로고
    • Three-dimensional structure of an antigen-antibody complex at 2.8 Å resolution
    • Amit, A.G., Mariuzza, R.A., Phillips, S.E.V. & Poljak, R.J. (1986). Three-dimensional structure of an antigen-antibody complex at 2.8 Å resolution. Science 233, 747-753.
    • (1986) Science , vol.233 , pp. 747-753
    • Amit, A.G.1    Mariuzza, R.A.2    Phillips, S.E.V.3    Poljak, R.J.4
  • 40
    • 0032540358 scopus 로고    scopus 로고
    • Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity
    • Clackson, T., Ultsch, M.H., Wells, J.A. & De Vos, A.M. (1998). Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity. J. Mol. Biol. 277, 1111-1128.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1111-1128
    • Clackson, T.1    Ultsch, M.H.2    Wells, J.A.3    De Vos, A.M.4
  • 41
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • De Vos, A.M., Ultsch, M. & Kossiakoff, A.A. (1992). Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 225, 306-312.
    • (1992) Science , vol.225 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 42
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson, T. & Wells, J.A. (1995). A hot spot of binding energy in a hormone-receptor interface. Science 267, 383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 43
    • 0029926396 scopus 로고    scopus 로고
    • The crystal structure of the complex of blood coagulation factor Vila with soluble tissue factor
    • Banner, D.W., et al., & Kirchhofer, D. (1996). The crystal structure of the complex of blood coagulation factor Vila with soluble tissue factor. Nature 380, 41-46.
    • (1996) Nature , vol.380 , pp. 41-46
    • Banner, D.W.1    Kirchhofer, D.2
  • 44
    • 0029093452 scopus 로고
    • Analysis of the factor Vila binding site on human tissue factor: Effects of tissue factor mutations on the kinetics and thermodynamics of binding
    • Kelley, R.F., Costas, K.E., O'Connell, M.P. & Lazarus, R.A. (1995). Analysis of the factor Vila binding site on human tissue factor: effects of tissue factor mutations on the kinetics and thermodynamics of binding. Biochemistry 34, 10383-10392.
    • (1995) Biochemistry , vol.34 , pp. 10383-10392
    • Kelley, R.F.1    Costas, K.E.2    O'Connell, M.P.3    Lazarus, R.A.4
  • 45
    • 0027410832 scopus 로고
    • The basics of binding: Mechanisms of antigen recognition and mimicry by antibodies
    • Mariuzza, R.A. & Poljak, R.J. (1993). The basics of binding: mechanisms of antigen recognition and mimicry by antibodies. Curr. Opin. Immunol. 5, 50-55.
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 50-55
    • Mariuzza, R.A.1    Poljak, R.J.2
  • 47
    • 0002452464 scopus 로고
    • Oscillation Data Reduction Program
    • Sawyer, L., Isaacs, N. & Bailey, S. eds. SERC Daresbury Laboratory, UK
    • Otwinowski, Z. (1993). Oscillation Data Reduction Program. In Proceedings of the CCP4 Study Weekend: Data Collection and Processing. (Sawyer, L., Isaacs, N. & Bailey, S. eds). pp. 56-62, SERC Daresbury Laboratory, UK.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 48
    • 84944812221 scopus 로고
    • Extension of molecular replacement: A new search strategy based on Patterson correlation refinement
    • Brünger, AT. (1990). Extension of molecular replacement: a new search strategy based on Patterson correlation refinement. Acta Cryst. A 46, 46-57.
    • (1990) Acta Cryst. A , vol.46 , pp. 46-57
    • Brünger, A.T.1
  • 49
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, AT., Kuriyan, J. & 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
  • 50
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4
    • CCP4 (1994). The CCP4 suite: Programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 51
    • 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. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 52
    • 0025888264 scopus 로고
    • Efficient site-directed mutagenesis using uracil-containing DNA
    • Kunkel, T.A., Bebenek, K. & McClary, J. (1991). Efficient site-directed mutagenesis using uracil-containing DNA. Methods Enzymol. 204, 125-139.
    • (1991) Methods Enzymol. , vol.204 , pp. 125-139
    • Kunkel, T.A.1    Bebenek, K.2    McClary, J.3
  • 53
    • 0031611316 scopus 로고    scopus 로고
    • Phage display of peptide libraries on protein scaffolds
    • Cabilly,S., ed.. Humana Press, Totowa, NJ, USA
    • Lowman, H.B. (1998). Phage display of peptide libraries on protein scaffolds. In Methods in Molecular Biology, vol. 87: Combinatorial Peptide Library Protocols. (Cabilly,S., ed.). pp. 249-264, Humana Press, Totowa, NJ, USA.
    • (1998) Methods in Molecular Biology, Vol. 87: Combinatorial Peptide Library Protocols , vol.87 , pp. 249-264
    • Lowman, H.B.1
  • 54
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system
    • Karlsson, R., Michaelsson, A. & Mattson, A. (1991). Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system J. Immunol. Methods 145, 229-240.
    • (1991) J. Immunol. Methods , vol.145 , pp. 229-240
    • Karlsson, R.1    Michaelsson, A.2    Mattson, A.3
  • 55
    • 0000732609 scopus 로고
    • GRASP: Graphical representation and analysis of surface properties
    • Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP: graphical representation and analysis of surface properties. Biophys. J. 64, 166-170.
    • (1993) Biophys. J. , vol.64 , pp. 166-170
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 57
    • 0026482961 scopus 로고
    • Tracking conformational states in allosteric transitions of phosphorylase
    • Browner, M.F., Fauman, E.B. & Fletterick, R.J. (1992). Tracking conformational states in allosteric transitions of phosphorylase. Biochemistry 31, 11297-11304.
    • (1992) Biochemistry , vol.31 , pp. 11297-11304
    • Browner, M.F.1    Fauman, E.B.2    Fletterick, R.J.3


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