메뉴 건너뛰기




Volumn 259, Issue 4, 1996, Pages 718-736

Extended glycoprotein structure of the seven domains in human carcinoembryonic antigen by X-ray and neutron solution scattering and an automated curve fitting procedure: Implications for cellular adhesion

Author keywords

Carcinoembryonic antigen; Glycoprotein; Molecular modelling; Neutron scattering; X ray scattering

Indexed keywords

CARCINOEMBRYONIC ANTIGEN; CELL SURFACE PROTEIN; GLYCOPROTEIN; IMMUNOGLOBULIN; MEMBRANE ANTIGEN; TUMOR MARKER;

EID: 0030596495     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0353     Document Type: Article
Times cited : (58)

References (73)
  • 1
    • 0026726797 scopus 로고
    • Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2 Å resolution
    • Aleshin, A., Golubev, A., Firsov, L. M. & Honzatko, R. B. (1992). Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2 Å resolution. J. Biol. Chem. 267, 19291-19298.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19291-19298
    • Aleshin, A.1    Golubev, A.2    Firsov, L.M.3    Honzatko, R.B.4
  • 2
    • 0028341842 scopus 로고
    • Refined crystal structures of glucoamylase from Aspergillus awamori var. X100
    • Aleshin, A. E., Hoffman, C., Firsov, L. M. & Honzatko, R. B. (1994). Refined crystal structures of glucoamylase from Aspergillus awamori var. X100. J. Mol. Biol. 238, 575-591.
    • (1994) J. Mol. Biol. , vol.238 , pp. 575-591
    • Aleshin, A.E.1    Hoffman, C.2    Firsov, L.M.3    Honzatko, R.B.4
  • 3
    • 0026572279 scopus 로고
    • A predicted three-dimensional structure for the carcinoembryonic antigen (CEA)
    • Bates, P. A., Luo, J. & Sternberg, M. J. E. (1992). A predicted three-dimensional structure for the carcinoembryonic antigen (CEA). FEBS Letters, 301, 207-214.
    • (1992) FEBS Letters , vol.301 , pp. 207-214
    • Bates, P.A.1    Luo, J.2    Sternberg, M.J.E.3
  • 5
    • 0028828789 scopus 로고
    • Bent domain structure of recombinant human IgE-Fc in solution by X-ray and neutron scattering in conjunction with an automated curve fitting procedure
    • Beavil, A. J., Young, R. J., Sutton, B. J. & Perkins, S. J. (1995). Bent domain structure of recombinant human IgE-Fc in solution by X-ray and neutron scattering in conjunction with an automated curve fitting procedure. Biochemistry, 34, 14449-14461.
    • (1995) Biochemistry , vol.34 , pp. 14449-14461
    • Beavil, A.J.1    Young, R.J.2    Sutton, B.J.3    Perkins, S.J.4
  • 7
    • 0024558306 scopus 로고
    • Carcinoembryonic antigen, a human tumor marker, functions as an intercellular adhesion molecule
    • Benchimol, S., Fuks, A., Jothy, S., Beauchemin, N., Shirota, K. & Stanners, C. P. (1989). Carcinoembryonic antigen, a human tumor marker, functions as an intercellular adhesion molecule. Cell, 57, 327-334.
    • (1989) Cell , vol.57 , pp. 327-334
    • Benchimol, S.1    Fuks, A.2    Jothy, S.3    Beauchemin, N.4    Shirota, K.5    Stanners, C.P.6
  • 8
    • 0026542081 scopus 로고
    • The binding site on ICAM-1 for Plasmodium falciparum-infected erythrocytes overlaps but is distinct from the LFA-1 binding site
    • Berendt, A. R., McDowall, A., Craig, A. G., Bates, P. A., Sternberg, M. J. E., Marsh, K., Newbold, C. I. & Hogg, N. (1992). The binding site on ICAM-1 for Plasmodium falciparum-infected erythrocytes overlaps but is distinct from the LFA-1 binding site. Cell, 68, 71-81.
    • (1992) Cell , vol.68 , pp. 71-81
    • Berendt, A.R.1    McDowall, A.2    Craig, A.G.3    Bates, P.A.4    Sternberg, M.J.E.5    Marsh, K.6    Newbold, C.I.7    Hogg, N.8
  • 9
    • 0024571818 scopus 로고
    • Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity and mechanism-based inhibitors
    • Bode, W., Meyer, E., Jr & Powers, J. C. (1989). Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity and mechanism-based inhibitors. Biochemistry, 28, 1951-1963.
    • (1989) Biochemistry , vol.28 , pp. 1951-1963
    • Bode, W.1    Meyer E., Jr.2    Powers, J.C.3
  • 10
    • 0028774038 scopus 로고
    • Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution
    • Bodian, D. L., Jones, E. Y., Harlos, K., Stuart, D. I. & Davis, S. J. (1994). Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution. Structure, 2, 755-766.
    • (1994) Structure , vol.2 , pp. 755-766
    • Bodian, D.L.1    Jones, E.Y.2    Harlos, K.3    Stuart, D.I.4    Davis, S.J.5
  • 12
    • 0028773478 scopus 로고
    • Building proteins with fibronectin type III modules
    • Campbell, I. D. & Spitzfaden, C. (1994). Building proteins with fibronectin type III modules. Structure, 2, 333-337.
    • (1994) Structure , vol.2 , pp. 333-337
    • Campbell, I.D.1    Spitzfaden, C.2
  • 13
    • 0020523938 scopus 로고
    • Isolation and structures of the oligosaccharide units of carcinoembryonic antigen
    • Chandrasekaran, E. V., Davila, M., Nixon, D. W., Goldfarb, M. & Mendicino, J. (1983). Isolation and structures of the oligosaccharide units of carcinoembryonic antigen. J. Biol. Chem. 258, 7213-7222.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7213-7222
    • Chandrasekaran, E.V.1    Davila, M.2    Nixon, D.W.3    Goldfarb, M.4    Mendicino, J.5
  • 14
    • 0016606973 scopus 로고
    • Structural invariants in protein folding
    • Chothia, C. (1975). Structural invariants in protein folding. Nature, 254, 304-308.
    • (1975) Nature , vol.254 , pp. 304-308
    • Chothia, C.1
  • 15
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution
    • Deisenhofer, J. (1981). Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution. Biochemistry, 20, 2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 16
    • 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, 255, 306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 17
    • 0002872612 scopus 로고
    • Hydrodynamic properties of macromolecular assemblies
    • Harding, S. E. & Rowe, A. J., eds, Royal Society of Chemistry, Cambridge
    • Garcia de la Torre, J. (1989). Hydrodynamic properties of macromolecular assemblies. In Dynamic Properties of Biomolecular Assemblies (Harding, S. E. & Rowe, A. J., eds), pp. 3-31, Royal Society of Chemistry, Cambridge.
    • (1989) Dynamic Properties of Biomolecular Assemblies , pp. 3-31
    • Garcia De La Torre, J.1
  • 18
    • 0017403408 scopus 로고
    • Hydrodynamic properties of macromolecular complexes. 1. Translation
    • Garcia de la Torre, J. & Bloomfield, V. A. (1977a). Hydrodynamic properties of macromolecular complexes. 1. Translation. Biopolymers, 16, 1747-1761.
    • (1977) Biopolymers , vol.16 , pp. 1747-1761
    • Garcia De La Torre, J.1    Bloomfield, V.A.2
  • 19
    • 0017750547 scopus 로고
    • Hydrodynamics of macromolecular complexes. 3. Bacterial viruses
    • Garcia de la Torre, J. & Bloomfield, V. A. (1977b). Hydrodynamics of macromolecular complexes. 3. Bacterial viruses. Biopolymers, 16, 1779-1793.
    • (1977) Biopolymers , vol.16 , pp. 1779-1793
    • Garcia De La Torre, J.1    Bloomfield, V.A.2
  • 26
    • 0011943275 scopus 로고
    • Development of the small-angle diffractometer LOQ at the ISIS pulsed neutron source
    • Dubna, 1st-4th September 1992. Report E3-93-65, Joint Institute for Nuclear Research, Dubna
    • Heenan, R. K. & King, S. M. (1993). Development of the small-angle diffractometer LOQ at the ISIS pulsed neutron source. In Proceedings of an International Seminar on Structural Investigations at Pulsed Neutron Sources, Dubna, 1st-4th September 1992. Report E3-93-65, Joint Institute for Nuclear Research, Dubna.
    • (1993) Proceedings of An International Seminar on Structural Investigations at Pulsed Neutron Sources
    • Heenan, R.K.1    King, S.M.2
  • 27
    • 0004283756 scopus 로고
    • Internal publication RAL-89-128, Rutherford Appleton Laboratory, Didcot, UK
    • Heenan, R. K., King, S. M., Osborn, R. & Stanley, H. B. (1989). COLETTE Users Guide. Internal publication RAL-89-128, Rutherford Appleton Laboratory, Didcot, UK.
    • (1989) COLETTE Users Guide
    • Heenan, R.K.1    King, S.M.2    Osborn, R.3    Stanley, H.B.4
  • 28
    • 0023723045 scopus 로고
    • Carcinoembryonic antigen is anchored to membranes by covalent attachment to a glycosylphosphadidylinositol moiety: Identification of the ethanolamine linkage site
    • Hefta, S. A., Hefta, L. J. F., Lee, T. D., Paxton, R. J. & Shively, J. E. (1988) Carcinoembryonic antigen is anchored to membranes by covalent attachment to a glycosylphosphadidylinositol moiety: identification of the ethanolamine linkage site. Proc. Natl Acad. Sci. USA, 85, 4648-4652.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4648-4652
    • Hefta, S.A.1    Hefta, L.J.F.2    Lee, T.D.3    Paxton, R.J.4    Shively, J.E.5
  • 29
    • 0001232884 scopus 로고
    • The small-angle approximation of X-ray and neutron scatter from rigid rods of non-uniform cross section and finite length
    • Hjelm, R. P. (1985). The small-angle approximation of X-ray and neutron scatter from rigid rods of non-uniform cross section and finite length. J. Appl. Crystallog. 18, 452-460.
    • (1985) J. Appl. Crystallog. , vol.18 , pp. 452-460
    • Hjelm, R.P.1
  • 30
    • 0026564765 scopus 로고
    • Epitope mapping of the carcinoembryonic antigen with various related recombinant proteins expressed in chinese hamster ovary cells and 25 distinct monoclonal antibodies
    • Ikeda, S., Kuroki, M., Haruno, M., Oikawa, S., Nakazato, H., Kosaki, G. & Matsuoka, Y. (1992). Epitope mapping of the carcinoembryonic antigen with various related recombinant proteins expressed in Chinese hamster ovary cells and 25 distinct monoclonal antibodies. Mol. Immunol. 29, 229-240.
    • (1992) Mol. Immunol. , vol.29 , pp. 229-240
    • Ikeda, S.1    Kuroki, M.2    Haruno, M.3    Oikawa, S.4    Nakazato, H.5    Kosaki, G.6    Matsuoka, Y.7
  • 31
    • 0023680553 scopus 로고
    • Cell membrane, but not circulating, carcinoembryonic antigen is linked to a phosphatidylinositol-containing hydrophobic domain
    • Jean, F., Malapert, P., Rougon, G. & Barbet, J. (1988). Cell membrane, but not circulating, carcinoembryonic antigen is linked to a phosphatidylinositol-containing hydrophobic domain. Biochem. Biophys. Res. Commun. 155, 794-800.
    • (1988) Biochem. Biophys. Res. Commun. , vol.155 , pp. 794-800
    • Jean, F.1    Malapert, P.2    Rougon, G.3    Barbet, J.4
  • 32
    • 0026488252 scopus 로고
    • Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2
    • Jones, E. Y., Davis, S. J., Williams, A. F., Harlos, K. & Stuart, D. I. (1992). Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2. Nature, 360, 232-239.
    • (1992) Nature , vol.360 , pp. 232-239
    • Jones, E.Y.1    Davis, S.J.2    Williams, A.F.3    Harlos, K.4    Stuart, D.I.5
  • 34
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 35
    • 0017810372 scopus 로고
    • Extraction of CEA from tumour tissue, foetal colon and patients' sera, and the effect of perchloric acid
    • Keep, P. A., Leake, B. A. & Rogers, G. T. (1978). Extraction of CEA from tumour tissue, foetal colon and patients' sera, and the effect of perchloric acid. Brit. J. Cancer, 37, 171-182.
    • (1978) Brit. J. Cancer , vol.37 , pp. 171-182
    • Keep, P.A.1    Leake, B.A.2    Rogers, G.T.3
  • 36
    • 0018193583 scopus 로고
    • Isolation, immunological characterization and structural studies of a tumour antigen releated to carcinoembryonic antigen
    • Kessler, M. J., Shively, J. E., Pritchard, D. G. & Todd, C. W. (1978). Isolation, immunological characterization and structural studies of a tumour antigen releated to carcinoembryonic antigen. Cancer Res. 38, 1041-1048.
    • (1978) Cancer Res. , vol.38 , pp. 1041-1048
    • Kessler, M.J.1    Shively, J.E.2    Pritchard, D.G.3    Todd, C.W.4
  • 37
    • 0024095774 scopus 로고
    • The MRC OX-45 antigen of rat leukocytes and endothelium is in a subset of the immunoglobulin superfamily with CD2, LFA-3 and carcinoembryonic antigens
    • Killeen, N., Moessner, R., Arvieux, J., Willis, A. & Williams, A. F. (1988). The MRC OX-45 antigen of rat leukocytes and endothelium is in a subset of the immunoglobulin superfamily with CD2, LFA-3 and carcinoembryonic antigens. EMBO J. 7, 3087-3091.
    • (1988) EMBO J. , vol.7 , pp. 3087-3091
    • Killeen, N.1    Moessner, R.2    Arvieux, J.3    Willis, A.4    Williams, A.F.5
  • 38
    • 0017845369 scopus 로고
    • A comparison of methods for the isolation of carcinoembryonic antigen
    • Kimball, P. M. & Brattain, M. G. (1978). A comparison of methods for the isolation of carcinoembryonic antigen. Cancer Res. 38, 619-623.
    • (1978) Cancer Res. , vol.38 , pp. 619-623
    • Kimball, P.M.1    Brattain, M.G.2
  • 39
    • 0000980676 scopus 로고
    • X-ray small angle scattering with substances of biological interest in diluted solutions
    • Kratky, O. (1963). X-ray small angle scattering with substances of biological interest in diluted solutions. Prog. Biophys. Chem. 13, 105-173.
    • (1963) Prog. Biophys. Chem. , vol.13 , pp. 105-173
    • Kratky, O.1
  • 40
    • 0014331822 scopus 로고
    • Physicochemical studies of the carcinoembryonic antigens of the human digestive system
    • Krupey, J., Gold, P. & Freedman, S. O. (1968). Physicochemical studies of the carcinoembryonic antigens of the human digestive system. J. Exp. Med. 128, 387-398.
    • (1968) J. Exp. Med. , vol.128 , pp. 387-398
    • Krupey, J.1    Gold, P.2    Freedman, S.O.3
  • 43
    • 0029131402 scopus 로고
    • Demonstration by pulsed neutron scattering that the arrangement of the Fab and Fc fragments in the overall structures of bovine IgG1 and IgG2 in solution is similar
    • Mayans, M. O., Coadwell, W. J., Beale, D., Symons, D. B. A. & Perkins, S. J. (1995). Demonstration by pulsed neutron scattering that the arrangement of the Fab and Fc fragments in the overall structures of bovine IgG1 and IgG2 in solution is similar. Biochem. J. 311, 283-291.
    • (1995) Biochem. J. , vol.311 , pp. 283-291
    • Mayans, M.O.1    Coadwell, W.J.2    Beale, D.3    Symons, D.B.A.4    Perkins, S.J.5
  • 44
    • 0028965197 scopus 로고
    • A reference of the GOLD classification of monoclonal antibodies against carcinoembryonic antigen to the domain structure of the carcinoembryonic antigen molecule
    • Murakami, M., Kuroki, M., Arakawa, F., Kuwahara, M., Oikawa, S., Nazakato, H. & Matsuoka, Y, (1995). A reference of the GOLD classification of monoclonal antibodies against carcinoembryonic antigen to the domain structure of the carcinoembryonic antigen molecule. Hybridoma, 14, 19-28.
    • (1995) Hybridoma , vol.14 , pp. 19-28
    • Murakami, M.1    Kuroki, M.2    Arakawa, F.3    Kuwahara, M.4    Oikawa, S.5    Nazakato, H.6    Matsuoka, Y.7
  • 46
    • 0023147934 scopus 로고
    • Primary structure of human carcinoembryonic antigen (CEA) deduced from cDNA sequence
    • Oikawa, S., Nakazato, H. & Kosaki, G. (1987). Primary structure of human carcinoembryonic antigen (CEA) deduced from cDNA sequence. Biochem. Biophys. Res. Commun. 142, 511-518.
    • (1987) Biochem. Biophys. Res. Commun. , vol.142 , pp. 511-518
    • Oikawa, S.1    Nakazato, H.2    Kosaki, G.3
  • 47
    • 0025821477 scopus 로고
    • A specific heterotypic cell adhesion between members of carcinoembryonic antigen family W272 and NCA is mediated by N-domains
    • Oikawa, S., Inuzuka, C., Kuroki, M., Arakawa, F., Matsuoka, Y., Kosaki, G. & Nakazato, H. (1991). A specific heterotypic cell adhesion between members of carcinoembryonic antigen family W272 and NCA is mediated by N-domains. J. Biol. Chem. 266, 7995-8001.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7995-8001
    • Oikawa, S.1    Inuzuka, C.2    Kuroki, M.3    Arakawa, F.4    Matsuoka, Y.5    Kosaki, G.6    Nakazato, H.7
  • 49
    • 0023114390 scopus 로고
    • Sequence analysis of carcinoembryonic antigen: Identification of glycosylation sites and homology with the immunoglobulin supergene family
    • Paxton, R. J., Mooser, G., Pande, H., Lee, T. D. & Shively, J. E. (1987). Sequence analysis of carcinoembryonic antigen: identification of glycosylation sites and homology with the immunoglobulin supergene family. Proc. Natl Acad. Sci. USA, 84, 920-924.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 920-924
    • Paxton, R.J.1    Mooser, G.2    Pande, H.3    Lee, T.D.4    Shively, J.E.5
  • 50
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects: The calculation of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins, S. J. (1986). Protein volumes and hydration effects: the calculation of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 157, 169-180.
    • (1986) Eur. J. Biochem. , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 51
    • 77956826381 scopus 로고
    • X-ray and neutron solution scattering
    • Perkins, S. J. (1988). X-ray and neutron solution scattering. New Comp. Biochem. 11B, 143-264.
    • (1988) New Comp. Biochem. , vol.11 B , pp. 143-264
    • Perkins, S.J.1
  • 52
    • 0022650448 scopus 로고
    • Unusual ultrastructure of complement component C4b-binding protein of human complement by synchrotron X-ray scattering and hydrodynamic analysis
    • Perkins, S. J., Chung, L. P. & Reid, K. B. M. (1986). Unusual ultrastructure of complement component C4b-binding protein of human complement by synchrotron X-ray scattering and hydrodynamic analysis. Biochem. J. 233, 799-807.
    • (1986) Biochem. J. , vol.233 , pp. 799-807
    • Perkins, S.J.1    Chung, L.P.2    Reid, K.B.M.3
  • 53
    • 0025180336 scopus 로고
    • The two-domain structure of the native and reaction centre cleaved forms of C1 inhibitor of human complement by neutron scattering
    • Perkins, S. J., Smith, K. F., Amatayakul, S., Ashford, D., Rademacher, T. W., Dwek, R. A., Lachmann, P. J. & Harrison, R. A. (1990). The two-domain structure of the native and reaction centre cleaved forms of C1 inhibitor of human complement by neutron scattering. J. Mol. Biol. 214, 751-763.
    • (1990) J. Mol. Biol. , vol.214 , pp. 751-763
    • Perkins, S.J.1    Smith, K.F.2    Amatayakul, S.3    Ashford, D.4    Rademacher, T.W.5    Dwek, R.A.6    Lachmann, P.J.7    Harrison, R.A.8
  • 54
    • 0026009904 scopus 로고
    • The solution structure of human and mouse immunoglobulin IgM by synchrotron X-ray scattering and molecular graphics modelling: A possible mechanism for complement activation
    • Perkins, S. J., Nealis, A. S., Sutton, B. J. & Feinstein, A. (1991). The solution structure of human and mouse immunoglobulin IgM by synchrotron X-ray scattering and molecular graphics modelling: a possible mechanism for complement activation. J. Mol. Biol. 221, 1345-1366.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1345-1366
    • Perkins, S.J.1    Nealis, A.S.2    Sutton, B.J.3    Feinstein, A.4
  • 55
    • 0027377159 scopus 로고
    • Modelling of the serine protease fold by X-ray and neutron scattering and sedimentation analyses: Its occurrence in factor D of the complement system
    • Perkins, S. J., Smith, K. F., Kilpatrick, J. M., Volanakis, J. E. & Sim, R. B. (1993). Modelling of the serine protease fold by X-ray and neutron scattering and sedimentation analyses: its occurrence in factor D of the complement system. Biochem. J. 295, 87-99.
    • (1993) Biochem. J. , vol.295 , pp. 87-99
    • Perkins, S.J.1    Smith, K.F.2    Kilpatrick, J.M.3    Volanakis, J.E.4    Sim, R.B.5
  • 57
    • 0023712882 scopus 로고
    • Analysis of the specificity of CEA reactive monoclonal antibodies. Immunological support for the domain model of CEA
    • Schwarz, K., Mehnert-Solzer, C., von Kleist, S. & Grunert, F. (1988). Analysis of the specificity of CEA reactive monoclonal antibodies. Immunological support for the domain model of CEA. Mol. Immunol. 25, 889-898.
    • (1988) Mol. Immunol. , vol.25 , pp. 889-898
    • Schwarz, K.1    Mehnert-Solzer, C.2    Von Kleist, S.3    Grunert, F.4
  • 58
    • 0015791092 scopus 로고
    • Size and configuration of glycoprotein fragments cleaved from tumor cells by proteolysis
    • Slayter, H. S. & Codington, J. F. (1973). Size and configuration of glycoprotein fragments cleaved from tumor cells by proteolysis. J. Biol. Chem. 248, 3405-3410.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3405-3410
    • Slayter, H.S.1    Codington, J.F.2
  • 59
    • 0016694476 scopus 로고
    • Electron microscopy and physical characterization of the carcinoembryonic antigen
    • Slayter, H. S. & Coligan, J. E. (1975). Electron microscopy and physical characterization of the carcinoembryonic antigen. Biochemistry, 14, 2323-2330.
    • (1975) Biochemistry , vol.14 , pp. 2323-2330
    • Slayter, H.S.1    Coligan, J.E.2
  • 61
    • 0025269047 scopus 로고
    • The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus
    • Staunton, D. E., Dustin, M. L., Erickson, H. P. & Springer, T. A. (1990). The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus. Cell, 61, 243-254.
    • (1990) Cell , vol.61 , pp. 243-254
    • Staunton, D.E.1    Dustin, M.L.2    Erickson, H.P.3    Springer, T.A.4
  • 62
    • 0024245156 scopus 로고
    • A flexible method to align large numbers of biological sequences
    • Taylor, W. R. (1988). A flexible method to align large numbers of biological sequences. J. Mol. Evol. 28, 161-169.
    • (1988) J. Mol. Evol. , vol.28 , pp. 161-169
    • Taylor, W.R.1
  • 63
    • 0023679092 scopus 로고
    • The carcinoembryonic antigen gene family: Structure, expression and evolution
    • Thompson, J. & Zimmermann, W. (1988). The carcinoembryonic antigen gene family: structure, expression and evolution. Tumor Biol. 9, 63-83.
    • (1988) Tumor Biol. , vol.9 , pp. 63-83
    • Thompson, J.1    Zimmermann, W.2
  • 64
    • 0026048664 scopus 로고
    • Carcinoembryonic antigen gene family: Molecular biology and clinical perspectives
    • Thompson, J. A., Grunert, F. & Zimmermann, W. (1991). Carcinoembryonic antigen gene family: molecular biology and clinical perspectives. J. Clin. Lab. Anal. 5, 344-366.
    • (1991) J. Clin. Lab. Anal. , vol.5 , pp. 344-366
    • Thompson, J.A.1    Grunert, F.2    Zimmermann, W.3
  • 67
    • 85055706702 scopus 로고
    • Absolute calibration of small angle neutron scattering data
    • Wignall, G. D. & Bates, F. S. (1987). Absolute calibration of small angle neutron scattering data. J. Appl. Crystallog. 20, 28-40.
    • (1987) J. Appl. Crystallog. , vol.20 , pp. 28-40
    • Wignall, G.D.1    Bates, F.S.2
  • 68
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily - Domains for cell surface recognition
    • Williams, A. F. & Barclay, A. N. (1988). The immunoglobulin superfamily - domains for cell surface recognition. Annu. Rev. Immunol. 6, 381-405.
    • (1988) Annu. Rev. Immunol. , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 71
    • 0023221836 scopus 로고
    • Structural studies of the carbohydrate moieties of carcinoembryonic antigens
    • Yamashita, K., Totani, K., Kuroki, M., Matsuoka, Y., Ueda, I. & Kobata, A. (1987). Structural studies of the carbohydrate moieties of carcinoembryonic antigens. Cancer Res. 47, 3451-3459.
    • (1987) Cancer Res. , vol.47 , pp. 3451-3459
    • Yamashita, K.1    Totani, K.2    Kuroki, M.3    Matsuoka, Y.4    Ueda, I.5    Kobata, A.6
  • 72
    • 0024443864 scopus 로고
    • Carbohydrate structures of nonspecific cross-reacting antigen-2, a glycoprotein purified from meconium as an antigen cross-reacting with anticarcinoembryonic antigen antibody
    • Yamashita, K., Totani, K., Iwaki, Y., Kuroki, M., Matsuoka, Y., Endo, T. & Kobata, A. (1989). Carbohydrate structures of nonspecific cross-reacting antigen-2, a glycoprotein purified from meconium as an antigen cross-reacting with anticarcinoembryonic antigen antibody. J. Biol. Chem. 264, 17873-17881.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17873-17881
    • Yamashita, K.1    Totani, K.2    Iwaki, Y.3    Kuroki, M.4    Matsuoka, Y.5    Endo, T.6    Kobata, A.7
  • 73
    • 0027184253 scopus 로고
    • Homophilic adhesion between Ig superfamily carcinoembryonic antigen molecules involves double reciprocal bonds
    • Zhou, H., Fuks, A., Alcaraz, G., Boiling, T. J. & Stanners, C. P. (1993). Homophilic adhesion between Ig superfamily carcinoembryonic antigen molecules involves double reciprocal bonds. J. Cell Biol. 122, 951-960.
    • (1993) J. Cell Biol. , vol.122 , pp. 951-960
    • Zhou, H.1    Fuks, A.2    Alcaraz, G.3    Boiling, T.J.4    Stanners, C.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.