메뉴 건너뛰기




Volumn 16, Issue 2, 1998, Pages 190-195

Design, synthesis, and application of a protein a mimetic

Author keywords

Affinity chromatography; Molecular modeling; Rational molecular design

Indexed keywords

DIPEPTIDE; HYDROGEN; HYDROXYL GROUP; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; PHENYLALANINE; PROTEIN A; TYROSINE;

EID: 0031912061     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/nbt0298-190     Document Type: Article
Times cited : (298)

References (39)
  • 1
    • 0028221121 scopus 로고
    • NMR and crystallography - Complementary approaches to structure determination
    • Macarthur, M.W., Driscoll, P.C., and Thornton, J.M. 1994. NMR and crystallography - complementary approaches to structure determination. Trends Biotech. 12:149-153.
    • (1994) Trends Biotech. , vol.12 , pp. 149-153
    • Macarthur, M.W.1    Driscoll, P.C.2    Thornton, J.M.3
  • 2
    • 0028298124 scopus 로고
    • Remotely related sequences and structures-analysis and predictive modeling
    • Taylor, W.R. 1994. Remotely related sequences and structures-analysis and predictive modeling. Trends Biotech. 12:154-158.
    • (1994) Trends Biotech. , vol.12 , pp. 154-158
    • Taylor, W.R.1
  • 4
    • 0029915191 scopus 로고    scopus 로고
    • Oriented immobilization of antibodies and its applications in immunoassays and immunosensors
    • Lu. B., Smyth, M.R., and Okennedy, R. 1996. Oriented immobilization of antibodies and its applications in immunoassays and immunosensors. Analyst 121:r29-r32.
    • (1996) Analyst , vol.121
    • Lu, B.1    Smyth, M.R.2    Okennedy, R.3
  • 5
    • 0028961281 scopus 로고
    • Semiquantitative spect tumor uptake of Tc-99m-labeled anti-CEA monoclonal-antibody in colorectal tumor
    • Oriuchi, N., Endo, K., Watanabe, N., Sugiyama, S., Asao, T., Takenoshita, S., et al. 1995. Semiquantitative spect tumor uptake of Tc-99m-labeled anti-CEA monoclonal-antibody in colorectal tumor. J. Nucl. Med. 36:679-683.
    • (1995) J. Nucl. Med. , vol.36 , pp. 679-683
    • Oriuchi, N.1    Endo, K.2    Watanabe, N.3    Sugiyama, S.4    Asao, T.5    Takenoshita, S.6
  • 8
    • 0025465357 scopus 로고
    • Immunotoxins - Status and prospects
    • Spooner, R A and Lord, J.M. 1990. Immunotoxins - status and prospects. Trends Biotech. 8:189-193.
    • (1990) Trends Biotech. , vol.8 , pp. 189-193
    • Spooner, R.A.1    Lord, J.M.2
  • 9
    • 0001524095 scopus 로고
    • Immunoaffinity purification - Basic principles and operational considerations
    • Yarmush, M.L., Weiss, A.M., Antonsen, K.P., Odde, D.J., and Yarmush, D.M. 1992. Immunoaffinity purification - basic principles and operational considerations. Biotech. Adv. 10:413-446.
    • (1992) Biotech. Adv. , vol.10 , pp. 413-446
    • Yarmush, M.L.1    Weiss, A.M.2    Antonsen, K.P.3    Odde, D.J.4    Yarmush, D.M.5
  • 10
    • 0016756272 scopus 로고
    • Continuous culture of fused cells secreting antibody of predefined specificity
    • Kohler, G. and Milstein, C. 1975. Continuous culture of fused cells secreting antibody of predefined specificity. Nature 256:495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 11
    • 0028222932 scopus 로고
    • Antigen-specific human-antibodies from mice comprising 4 distinct genetic modifications
    • Lonberg, N., Taylor, D., Harding, F.A., Trounstine, M., Higgins, K.M., Schramm, S.R., et al. 1994. Antigen-specific human-antibodies from mice comprising 4 distinct genetic modifications. Nature 368:856-859.
    • (1994) Nature , vol.368 , pp. 856-859
    • Lonberg, N.1    Taylor, D.2    Harding, F.A.3    Trounstine, M.4    Higgins, K.M.5    Schramm, S.R.6
  • 12
    • 0027963484 scopus 로고
    • Antigen-specific human monoclonal-antibodies from mice engineered with human ig heavy and light-chain YACs
    • Green, L.L., Hardy, M.C., Maynardcurrie, C.E., Tsuda, H., Louie, D.M., Mendez, M.J., et al. 1994. Antigen-specific human monoclonal-antibodies from mice engineered with human ig heavy and light-chain YACs. Nat. Genet 7:13-21.
    • (1994) Nat. Genet , vol.7 , pp. 13-21
    • Green, L.L.1    Hardy, M.C.2    Maynardcurrie, C.E.3    Tsuda, H.4    Louie, D.M.5    Mendez, M.J.6
  • 13
    • 0004999536 scopus 로고
    • Affinity-chromatography purification using protein A immobilized to traditional matrices and to hplc matrices
    • Sparrmann, M., Ottosson, T., Magnusson, B., and Nilsson, A. 1987. Affinity-chromatography purification using protein A immobilized to traditional matrices and to hplc matrices. Biol. Chem. Hoppe-Seyler 368:776.
    • (1987) Biol. Chem. Hoppe-Seyler , vol.368 , pp. 776
    • Sparrmann, M.1    Ottosson, T.2    Magnusson, B.3    Nilsson, A.4
  • 14
    • 0023734619 scopus 로고
    • A novel-approach to monoclonal-antibody separation using high-performance liquid affinity-chromatography (hplac) with selectispher-10 protein G
    • Ohlson, S., Nilsson, R., Miss, U., Kjellberg, B.M., and Freiburghaus, C. 1988. A novel-approach to monoclonal-antibody separation using high-performance liquid affinity-chromatography (hplac) with selectispher-10 protein G. J. Immunol. Methods 114:175-180.
    • (1988) J. Immunol. Methods , vol.114 , pp. 175-180
    • Ohlson, S.1    Nilsson, R.2    Miss, U.3    Kjellberg, B.M.4    Freiburghaus, C.5
  • 15
    • 0024804921 scopus 로고
    • Comparison of immunoglobulin binding-capacities and ligand leakage using 8 different protein-A affinity-chromatography matrices
    • Fuglistaller, P. 1989. Comparison of immunoglobulin binding-capacities and ligand leakage using 8 different protein-A affinity-chromatography matrices. J. Immunol. Methods 124:171-177.
    • (1989) J. Immunol. Methods , vol.124 , pp. 171-177
    • Fuglistaller, P.1
  • 16
    • 0027394507 scopus 로고
    • Assessment of the suitability of commercially available spa affinity solid-phases for the purification of murine monoclonal-antibodies at process scale
    • Godfrey, M.A.J., Kwasowski, P., Clift, R., and Marks, V. 1993. Assessment of the suitability of commercially available spa affinity solid-phases for the purification of murine monoclonal-antibodies at process scale. J. Immunol. Methods 160:97-105.
    • (1993) J. Immunol. Methods , vol.160 , pp. 97-105
    • Godfrey, M.A.J.1    Kwasowski, P.2    Clift, R.3    Marks, V.4
  • 17
    • 0021832928 scopus 로고
    • Thiophilic adsorption - A new method for protein fractionation
    • Porath, J., Maisano, F., and Belew, M. 1985. Thiophilic adsorption - a new method for protein fractionation. FEBS Lett. 185:306-310.
    • (1985) FEBS Lett. , vol.185 , pp. 306-310
    • Porath, J.1    Maisano, F.2    Belew, M.3
  • 18
    • 33847444074 scopus 로고
    • Thiophilic interaction and the selective adsorption of proteins
    • Porath, J. and Belew, M. 1987. Thiophilic interaction and the selective adsorption of proteins. Trends Biotech. 5225-229.
    • (1987) Trends Biotech. , pp. 5225-5229
    • Porath, J.1    Belew, M.2
  • 19
    • 0023197325 scopus 로고
    • A one-step purification method for monoclonal-antibodies based on salt-promoted adsorption chromatography on a thiophilic adsorbent
    • Belew, M., Juntti, N., Larsson, A., and Porath, J. 1987.A one-step purification method for monoclonal-antibodies based on salt-promoted adsorption chromatography on a thiophilic adsorbent. J. Immunol. Methods 102:173-182.
    • (1987) J. Immunol. Methods , vol.102 , pp. 173-182
    • Belew, M.1    Juntti, N.2    Larsson, A.3    Porath, J.4
  • 20
    • 0022863117 scopus 로고
    • Thiophilic adsorption of immunoglobulins - Analysis of conditions optimal for selective immobilization and purification
    • Hutchens, T.W. and Porath, J. 1986. Thiophilic adsorption of immunoglobulins - analysis of conditions optimal for selective immobilization and purification. Anal. Biochem. 159:217-226.
    • (1986) Anal. Biochem. , vol.159 , pp. 217-226
    • Hutchens, T.W.1    Porath, J.2
  • 21
    • 0025824119 scopus 로고
    • Study of the separation of mouse monoclonal-antibodies by pseudobioaffinity chromatography using matrix-linked histidine and histamine
    • Elkak, A. and Vijayalakshmi, M.A. 1991.Study of the separation of mouse monoclonal-antibodies by pseudobioaffinity chromatography using matrix-linked histidine and histamine. J. Chromatogr.-Biomed. Appl. 570:29-41.
    • (1991) J. Chromatogr.-Biomed. Appl. , vol.570 , pp. 29-41
    • Elkak, A.1    Vijayalakshmi, M.A.2
  • 22
    • 0026663810 scopus 로고
    • Interaction of immunoglobulin G with immobilized histidine - Mechanistic and kinetic aspects
    • Elkak, A., Manjini, S., and Vijayalakshmi, M.A. 1992. Interaction of immunoglobulin G with immobilized histidine - mechanistic and kinetic aspects. J. Chromatogr. 604:29-37.
    • (1992) J. Chromatogr. , vol.604 , pp. 29-37
    • Elkak, A.1    Manjini, S.2    Vijayalakshmi, M.A.3
  • 23
    • 0025287461 scopus 로고
    • Chemistry and preparation of affinity ligands useful in. immunoglobulin isolation and serum-protein separation
    • Ngo, T.T. and Khatter, N. 1990. Chemistry and preparation of affinity ligands useful in. immunoglobulin isolation and serum-protein separation. J. Chromatogr. 510:281-291.
    • (1990) J. Chromatogr. , vol.510 , pp. 281-291
    • Ngo, T.T.1    Khatter, N.2
  • 24
    • 0026195110 scopus 로고
    • Rapid and simple isolation of multigram goat IgG from serum using Avid AL and radial flow column
    • Ngo, T.T. and Khatter, N.1991. Rapid and simple isolation of multigram goat IgG from serum using Avid AL and radial flow column. Appl. Biochem. Biotech. 30:111-119.
    • (1991) Appl. Biochem. Biotech. , vol.30 , pp. 111-119
    • Ngo, T.T.1    Khatter, N.2
  • 25
    • 0026606066 scopus 로고
    • Avid AL, a synthetic ligand affinity gel mimicking immobilized bacterial antibody receptor for purification of immunoglobulin G
    • Ngo, T.T. and Khatter, N. 1992. Avid AL, a synthetic ligand affinity gel mimicking immobilized bacterial antibody receptor for purification of immunoglobulin G. J. Chromatogr. 597:101-109.
    • (1992) J. Chromatogr. , vol.597 , pp. 101-109
    • Ngo, T.T.1    Khatter, N.2
  • 26
    • 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 Å 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 Å and 2.8 Å resolution. Biochemistry 20:2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 27
    • 0027918556 scopus 로고
    • Water - Now you see it, now you don't
    • Levitt, M. and Park, B.H. 1993. Water - now you see it, now you don't. Structure 1:223-226.
    • (1993) Structure , vol.1 , pp. 223-226
    • Levitt, M.1    Park, B.H.2
  • 28
    • 0020011459 scopus 로고
    • Protein-A of Staphylococcus-aureus and related immunoglobulin receptors produced by streptococci and pneumococci
    • Langone, J.J. 1982. Protein-A of Staphylococcus-aureus and related immunoglobulin receptors produced by streptococci and pneumococci. Adv. Immunol. 32:157-252.
    • (1982) Adv. Immunol. , vol.32 , pp. 157-252
    • Langone, J.J.1
  • 32
  • 33
    • 0027163186 scopus 로고
    • The structural basis of germline-encoded VH3 immunoglobulin binding to staphylococcal protein A
    • Hillson, J.L., Karr, N.S., Oppliger, I.R., Mannik, M., and Sasso, H. 1993. The structural basis of germline-encoded VH3 immunoglobulin binding to staphylococcal protein A. J. Exp. Med. 178:331-336.
    • (1993) J. Exp. Med. , vol.178 , pp. 331-336
    • Hillson, J.L.1    Karr, N.S.2    Oppliger, I.R.3    Mannik, M.4    Sasso, H.5
  • 34
    • 38249021720 scopus 로고
    • Protein-protein interactions on the surface of immunoglobulin molecules
    • Ito, W., Nakamura, H. and Arata, Y. 1989. Protein-protein interactions on the surface of immunoglobulin molecules. J. Mol. Graph. 7:60-63.
    • (1989) J. Mol. Graph. , vol.7 , pp. 60-63
    • Ito, W.1    Nakamura, H.2    Arata, Y.3
  • 35
    • 0016752271 scopus 로고
    • a from normal human sera and from a patient with multiple myeloma by using protein A-Sepharose 4B
    • a from normal human sera and from a patient with multiple myeloma by using protein A-Sepharose 4B. Scand. J. Immunol. 4:633-640.
    • (1975) Scand. J. Immunol. , vol.4 , pp. 633-640
    • Hjelm, H.1
  • 36
    • 0026730489 scopus 로고
    • Structure-based strategies for drug design and discovery
    • Kuntz, I.D. 1992. Structure-based strategies for drug design and discovery. Science 257:1078-1082.
    • (1992) Science , vol.257 , pp. 1078-1082
    • Kuntz, I.D.1
  • 37
    • 0022994503 scopus 로고
    • Functional-groups, drug receptor interactions and drug design
    • Andrews, P. 1986. Functional-groups, drug receptor interactions and drug design. Trends Pharmacol. Sci. 7:148-151.
    • (1986) Trends Pharmacol. Sci. , vol.7 , pp. 148-151
    • Andrews, P.1
  • 38
    • 0003481596 scopus 로고
    • Fersht, A. (ed.), W.H. Freeman and Company, Reading, UK
    • Fersht, A. 1977. p. 236 in Enzyme structure and mechanism. Fersht, A. (ed.), W.H. Freeman and Company, Reading, UK.
    • (1977) Enzyme Structure and Mechanism , pp. 236
    • Fersht, A.1
  • 39
    • 0019087738 scopus 로고
    • P-Toluenesulfonyl chloride as an activating agent of agarose for preparation of immobilized affinity ligands and proteins
    • Nilsson, K. and Mosbach, K. 1980. p-Toluenesulfonyl chloride as an activating agent of agarose for preparation of immobilized affinity ligands and proteins. Eur. J. Biochem. 112:397-402.
    • (1980) Eur. J. Biochem. , vol.112 , pp. 397-402
    • Nilsson, K.1    Mosbach, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.