참고문헌
- Vox Sang v.78 Introduction to antibody engineering and phage display Watkins, N. A.;Ouwehand, W. H. https://doi.org/10.1046/j.1423-0410.2000.7820072.x
- J. Gerontol. A. Biol. Sci. Med. Sci. v.50 Variations in activity of the human natural anti-Gal antibody in young and elderly populations Wang, L.;Anaraki, F.;Henion, T. R.;Galili, U.
- Glycoconj. J. v.17 A journey to the world of glycobiology Kobata, A. https://doi.org/10.1023/A:1011006122704
- Proc. Natl. Acad. Sci. U.S.A. v.99 Glycosylation defining cancer malignancy : new wine in an old bottle Hakomori, S. https://doi.org/10.1073/pnas.172380699
- Proc. Natl. Acad. Sci. U.S.A. v.98 Mutated plant lectin library useful to identify different cells Yim, M.;Ono, T.;Irimura, T. https://doi.org/10.1073/pnas.041621998
- Proc. Natl. Acad. Sci. U.S.A. v.91 Lambda foo: a lambda phage vector for the expression of foreign proteins Maruyama, I. N.;Maruyama, H. I.;Brenner, S. https://doi.org/10.1073/pnas.91.17.8273
- Nat. Biotechnol. v.15 Efficient epitope mapping by bacteriophage lambda surface display Kuwabara, I.;Maruyama, H.;Mikawa, Y. G.;Zuberi, R. I.;Liu, F. T.;Maruyama, I. N. https://doi.org/10.1038/nbt0197-74
- Proc. Natl. Acad. Sci. U.S.A. v.88 Assembly of combinatorial antibody libraries on phage surfaces: the gene III site Barbas, C. F. 3rd;Kang, A. S.;Lerner, R. A.;Benkovic, S. J. https://doi.org/10.1073/pnas.88.18.7978
- Proc. Natl. Acad. Sci. U.S.A. v.88 Antibody redesign by chain shuffling from random combinatorial immunoglobulin libraries Kang, A. S.;Jones, T. M.;Burton, D. R. https://doi.org/10.1073/pnas.88.24.11120
- J. Immunol. v.149 Application of a filamentous phage pⅧ fusion protein system suitable for efficient produciton, screening, and mutagenesis of F(ab) antibody fragments Huse, W. D.;Stinchcombe, T. J.;Glaser, S. M.;Starr, L.;MacLean, M.;Hellstrom, K. E.;Hellstrom, I.;Yelton, D. E.
- Mol. Immunol. v.34 Cloning of anti-Gal Fabs from combinatorial phage display libraries: structural analysis and comparison of Fab expression in pComb3H and pComb8 phage Wang, L.;Radic, M. Z.;Siegel, D.;Chang, T.;Bracy, J.;Galili, U. https://doi.org/10.1016/S0161-5890(97)00082-5
- Biochemistry v.15 Elucidation of lectin receptors by quantitative inhibition of lectin binding to human erythrocytes and lymphocytes Kawaguchi, T.;Osawa, T. https://doi.org/10.1021/bi00666a006
- FEBS. Lett. v.342 of Maackia amurensis hemagglutinin (MAH) for sialic acid-containing Ser/Thr-linked carbohydrate chains of N-terminal octapeptides from human glycophorin A Konami, Y.;Yamamoto, K.;Osawa, T.;Irimura, T. https://doi.org/10.1016/0014-5793(94)80527-X
- J. Biochem.(Tokyo) v.115 A unique amino acid sequence involved in the putative carbohydrate-binding domain of a legume lectin specific for sialylated carbohydrate chains: primary sequence determination of Maackia amurensis hemagglutinin (MAH) Konami, Y.;Ishida, C.;Yamamoto, K.;Osawa, T.;Irimura, T. https://doi.org/10.1093/oxfordjournals.jbchem.a124408
- J. Biochem. (Tokyo) v.121 Sialic acid-binding motif of Maackia amurensis lectins Yamamoto, K.;Konami, Y.;Irimura, T. https://doi.org/10.1093/oxfordjournals.jbchem.a021650
- J. Biol. Chem. v.275 An unusual carbohydrate binding site revealed by the structures of two Maackia amurensis lectins complexed with sialic acid-containing oligosaccharides Imberty, A.;Gautier, C.;Lescar, C.;Lescar, J.;Perez, S.;Wyns, L.;Loris, R. https://doi.org/10.1074/jbc.M000560200
- Glycobiology v.2 Diversity in the sialic acids Varki, A. https://doi.org/10.1093/glycob/2.1.25
- Glycobiology v.2 Polysialylation: from bacteria to brains Troy, F. A. 2nd. https://doi.org/10.1093/glycob/2.1.5