메뉴 건너뛰기




Volumn 3, Issue NOV, 2012, Pages

Natural and man-made V-gene repertoires for antibody discovery

Author keywords

Antibody structure; Antigen binding site; Structure function relationship; Therapeutic antibodies

Indexed keywords


EID: 84874213990     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2012.00342     Document Type: Review
Times cited : (64)

References (186)
  • 1
    • 77956016509 scopus 로고    scopus 로고
    • Analysis and prediction of VH/VL packing in antibodies
    • Abhinandan, K. R., and Martin, A. C. (2010). Analysis and prediction of VH/VL packing in antibodies. Protein Eng Des. Sel. 23, 689-697.
    • (2010) Protein Eng Des. Sel. , vol.23 , pp. 689-697
    • Abhinandan, K.R.1    Martin, A.C.2
  • 2
    • 17044449205 scopus 로고    scopus 로고
    • A single diversified VH gene family dominates the bovine immunoglobulin repertoire
    • Aitken, R., Gilchrist, J., and Sinclair, M. C. (1997). A single diversified VH gene family dominates the bovine immunoglobulin repertoire. Biochem. Soc. Trans. 25, 326S.
    • (1997) Biochem. Soc. Trans. , vol.25
    • Aitken, R.1    Gilchrist, J.2    Sinclair, M.C.3
  • 3
    • 0031558798 scopus 로고    scopus 로고
    • Standard conformations for the canonical structures of immunoglobulins
    • Al-Lazikani, B., Lesk, A. M., and Chothia, C. (1997). Standard conformations for the canonical structures of immunoglobulins. J. Mol. Biol. 273, 927-948.
    • (1997) J. Mol. Biol. , vol.273 , pp. 927-948
    • Al-Lazikani, B.1    Lesk, A.M.2    Chothia, C.3
  • 4
    • 1642307201 scopus 로고    scopus 로고
    • Identification of differences in the specificity-determining residues of antibodies that recognize antigens of different size: implications for the rational design of antibody repertoires
    • Almagro, J. C. (2004). Identification of differences in the specificity-determining residues of antibodies that recognize antigens of different size: implications for the rational design of antibody repertoires. J. Mol. Recognit. 17, 132-143.
    • (2004) J. Mol. Recognit. , vol.17 , pp. 132-143
    • Almagro, J.C.1
  • 6
    • 38449104580 scopus 로고    scopus 로고
    • Humanization of antibodies
    • Almagro, J. C., and Fransson, J. (2008). Humanization of antibodies. Front. Biosci. 13, 1619-1633.
    • (2008) Front. Biosci. , vol.13 , pp. 1619-1633
    • Almagro, J.C.1    Fransson, J.2
  • 7
    • 0007006714 scopus 로고    scopus 로고
    • The differences between the structural repertoires of IGHV germ-line gene segments of mice and humans: implication for the molecular mechanism of the immune response
    • Almagro, J. C., Hernandez I., del Carmen Ramirez, M., and Vargas-Madrazo, E. (1997). The differences between the structural repertoires of IGHV germ-line gene segments of mice and humans: implication for the molecular mechanism of the immune response. Mol. Immunol. 34, 1199-1214.
    • (1997) Mol. Immunol. , vol.34 , pp. 1199-1214
    • Almagro, J.C.1    Hernandez, I.2    del Carmen Ramirez, M.3    Vargas-Madrazo, E.4
  • 8
    • 84858247303 scopus 로고    scopus 로고
    • Characterization of a high-affinity human antibody with a disulfide bridge in the third complementarity-determining region of the heavy chain
    • Almagro, J. C., Raghunathan, G., Beil, E., Janecki, D. J., Chen, Q., Dinh, T., et al. (2012). Characterization of a high-affinity human antibody with a disulfide bridge in the third complementarity-determining region of the heavy chain. J. Mol. Recognit. 25, 125-135.
    • (2012) J. Mol. Recognit. , vol.25 , pp. 125-135
    • Almagro, J.C.1    Raghunathan, G.2    Beil, E.3    Janecki, D.J.4    Chen, Q.5    Dinh, T.6
  • 9
    • 0041646843 scopus 로고
    • Joining of immunoglobulin heavy chain gene segments: implications from a chromosome with evidence of three D-JH fusions
    • Alt, F., and Baltimore, D. (1982). Joining of immunoglobulin heavy chain gene segments: implications from a chromosome with evidence of three D-JH fusions. Proc. Natl. Acad. Sci. U.S.A. 79, 4118-4122.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 4118-4122
    • Alt, F.1    Baltimore, D.2
  • 10
    • 0018654090 scopus 로고
    • Three-dimensional structure of immunoglobulins
    • Amzel, L. M., and Poljak, R. J. (1979). Three-dimensional structure of immunoglobulins. Annu. Rev. Biochem. 48, 961-997.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 961-997
    • Amzel, L.M.1    Poljak, R.J.2
  • 11
    • 0027759586 scopus 로고
    • Selection of human anti-hapten antibodies from semisynthetic libraries
    • Barbas, C. E 3rd., Amberg, W., Simoncsits, A., Jones, T. M., and Lerner, R. A. (1993). Selection of human anti-hapten antibodies from semisynthetic libraries. Gene 137, 57-62.
    • (1993) Gene , vol.137 , pp. 57-62
    • Barbas III, C.E.1    Amberg, W.2    Simoncsits, A.3    Jones, T.M.4    Lerner, R.A.5
  • 12
    • 0026563253 scopus 로고
    • Semisynthetic combinatorial antibody libraries: a chemical solution to the diversity problem
    • Barbas, C. E 3rd., Bain, J. D., Hoekstra, D. M., and Lerner, R. A. (1992). Semisynthetic combinatorial antibody libraries: a chemical solution to the diversity problem. Proc. Natl. Acad. Sci. U.S.A. 89, 4457-4461.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4457-4461
    • Barbas III, C.E.1    Bain, J.D.2    Hoekstra, D.M.3    Lerner, R.A.4
  • 13
    • 41249087476 scopus 로고    scopus 로고
    • Comprehensive analysis of the factors contributing to the stability and solubility of autonomous human VH domains
    • Barthelemy, P. A., Raab, H., Appleton, B. A., Bond, C. J., Wu, P., Wiesmann, C., et al. (2008). Comprehensive analysis of the factors contributing to the stability and solubility of autonomous human VH domains. J. Biol. Chem. 283, 3639-3654.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3639-3654
    • Barthelemy, P.A.1    Raab, H.2    Appleton, B.A.3    Bond, C.J.4    Wu, P.5    Wiesmann, C.6
  • 14
    • 84856185049 scopus 로고    scopus 로고
    • Rep-Seq: uncovering the immunological repertoire through next-generation sequencing
    • Benichou, J., Ben-Hamo, R., Louzoun, Y., and Efroni, S. (2012). Rep-Seq: uncovering the immunological repertoire through next-generation sequencing. Immunology 135, 183-191.
    • (2012) Immunology , vol.135 , pp. 183-191
    • Benichou, J.1    Ben-Hamo, R.2    Louzoun, Y.3    Efroni, S.4
  • 15
    • 0027499308 scopus 로고
    • Passenger transgenes reveal intrinsic specificity of the antibody hypermutation mechanism: clustering, polarity, and specific hot spots
    • Betz, A. G., Rada, C., Pannell, R., Milstein, C., and Neuberger, M. S. (1993). Passenger transgenes reveal intrinsic specificity of the antibody hypermutation mechanism: clustering, polarity, and specific hot spots. Proc. Natl. Acad. Sci. U.S.A. 90, 2385-2388.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2385-2388
    • Betz, A.G.1    Rada, C.2    Pannell, R.3    Milstein, C.4    Neuberger, M.S.5
  • 16
    • 77953591801 scopus 로고    scopus 로고
    • The functional capacity of the natural amino acids for molecular recognition
    • Birtalan, S., Fisher, R. D., and Sidhu ,S.S. (2010). The functional capacity of the natural amino acids for molecular recognition. Mol. Biosyst. 6 1186-1194.
    • (2010) Mol. Biosyst. , vol.6 , pp. 1186-1194
    • Birtalan, S.1    Fisher, R.D.2    Sidhu, S.S.3
  • 17
    • 40849097408 scopus 로고    scopus 로고
    • The intrinsic contributions of tyrosine, serine, glycine and arginine to the affinity and specificity of antibodies
    • Birtalan, S., Zhang, Y., Fellouse, E A., Shao, L., Schaefer, G., and Sidhu, S. S. (2008). The intrinsic contributions of tyrosine, serine, glycine and arginine to the affinity and specificity of antibodies. J. Mol. Biol. 377, 1518-1528.
    • (2008) J. Mol. Biol. , vol.377 , pp. 1518-1528
    • Birtalan, S.1    Zhang, Y.2    Fellouse, E.A.3    Shao, L.4    Schaefer, G.5    Sidhu, S.S.6
  • 18
    • 4143080377 scopus 로고    scopus 로고
    • VH gene segments in the mouse and human genomes
    • Bono, B. D., Madera, M., and Chothia, C. (2004). VH gene segments in the mouse and human genomes. J. Mol. Biol. 342, 131-143.
    • (2004) J. Mol. Biol. , vol.342 , pp. 131-143
    • Bono, B.D.1    Madera, M.2    Chothia, C.3
  • 19
    • 0031826661 scopus 로고    scopus 로고
    • Preparation of phage antibodies to the ED-A domain of human fibronectin
    • Borsi, L., Castellani, P., Allemanni, G., Neri, D., and Zardi, L. (1998). Preparation of phage antibodies to the ED-A domain of human fibronectin. Exp. Cell Res. 240, 244-251.
    • (1998) Exp. Cell Res. , vol.240 , pp. 244-251
    • Borsi, L.1    Castellani, P.2    Allemanni, G.3    Neri, D.4    Zardi, L.5
  • 21
    • 33744811140 scopus 로고    scopus 로고
    • Tumor-targeting properties of novel antibodies specific to the large isoform of tenascin-C
    • Brack, S. S., Silacci, M., Birchler, M., and Neri, D. (2006). Tumor-targeting properties of novel antibodies specific to the large isoform of tenascin-C. Clin. Cancer Res. 12, 3200-3208.
    • (2006) Clin. Cancer Res. , vol.12 , pp. 3200-3208
    • Brack, S.S.1    Silacci, M.2    Birchler, M.3    Neri, D.4
  • 22
    • 77950808409 scopus 로고    scopus 로고
    • The use of phage display in neurobiology
    • Chapter 5, Unit 5
    • Bradbury, A. R. (2010). The use of phage display in neurobiology. Curr. Protoc. Neurosci. Chapter 5, Unit 5. 12.
    • (2010) Curr. Protoc. Neurosci. , pp. 12
    • Bradbury, A.R.1
  • 23
    • 0030772225 scopus 로고    scopus 로고
    • Construction of a semisynthetic antibody library using trinucleotide oligos
    • Braunagel, M., and Little, M. (1997). Construction of a semisynthetic antibody library using trinucleotide oligos. Nucleic Acids Res. 25, 4690-4691.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4690-4691
    • Braunagel, M.1    Little, M.2
  • 24
    • 79953316880 scopus 로고    scopus 로고
    • Comparison of antibody repertoires produced by HIV-1 infection, other chronic and acute infections, and systemic autoimmune disease
    • doi: 10.1371/journal. pone.0016857
    • Breden, F., Lepik, C., Longo, N., Montero, M., Lipsky, P., and Scott, J. (2011). Comparison of antibody repertoires produced by HIV-1 infection, other chronic and acute infections, and systemic autoimmune disease. PLoS ONE 6:e16857. doi: 10.1371/journal. pone.0016857
    • (2011) PLoS ONE , vol.6
    • Breden, F.1    Lepik, C.2    Longo, N.3    Montero, M.4    Lipsky, P.5    Scott, J.6
  • 25
    • 0032525035 scopus 로고    scopus 로고
    • Pairing of variable heavy and variable kappa chains in individual naive and memory B cells
    • Brezinschek, H. P., Foster, S. J., Dorner, T., Brezinschek, R. I., and Lipsky, P. E. (1998). Pairing of variable heavy and variable kappa chains in individual naive and memory B cells. J. Immunol. 160, 4762-4767.
    • (1998) J. Immunol. , vol.160 , pp. 4762-4767
    • Brezinschek, H.P.1    Foster, S.J.2    Dorner, T.3    Brezinschek, R.I.4    Lipsky, P.E.5
  • 26
    • 0029802551 scopus 로고    scopus 로고
    • Phage antibodies with pan-species recognition of the oncofoetal angiogenesis marker fibronectin ED-B domain
    • Carnemolla, B., Neri, D., Castellani, P., Leprini, A., Neri, G., Pini, A., et al. (1996). Phage antibodies with pan-species recognition of the oncofoetal angiogenesis marker fibronectin ED-B domain. Int. I Cancer 68, 397-405.
    • (1996) Int. I Cancer , vol.68 , pp. 397-405
    • Carnemolla, B.1    Neri, D.2    Castellani, P.3    Leprini, A.4    Neri, G.5    Pini, A.6
  • 27
    • 79954591066 scopus 로고    scopus 로고
    • Structural repertoire of immunoglobulin λ light chains
    • Chailyan, A., Marcatili, P., Cirillo, D., and Tramontano, A. (2011). Structural repertoire of immunoglobulin λ light chains. Proteins 79, 1513-1524.
    • (2011) Proteins , vol.79 , pp. 1513-1524
    • Chailyan, A.1    Marcatili, P.2    Cirillo, D.3    Tramontano, A.4
  • 28
    • 0023278330 scopus 로고
    • Canonical structures for the hyper-variable regions of immunoglobulins
    • Chothia, C., and Lesk, A. M. (1987). Canonical structures for the hyper-variable regions of immunoglobulins. J. Mol. Biol. 196,901-917.
    • (1987) J. Mol. Biol. , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 31
    • 33745323376 scopus 로고    scopus 로고
    • Trends in antibody sequence changes during the somatic hypermutation process
    • Clark, L. A., Ganesan, S., Papp, S., and Vlijmen, H. W. V (2006). Trends in antibody sequence changes during the somatic hypermutation process. J. Immunol. 177, 333-340.
    • (2006) J. Immunol. , vol.177 , pp. 333-340
    • Clark, L.A.1    Ganesan, S.2    Papp, S.3    Vlijmen, H.W.V.4
  • 32
    • 42449109020 scopus 로고    scopus 로고
    • Synthetic antibody libraries focused towards peptide ligands
    • Cobaugh, C., Almagro, J., Pogson, M., Iverson, B., and Georgiou, G. (2008). Synthetic antibody libraries focused towards peptide ligands. J. Mol. Biol. 378, 622-633.
    • (2008) J. Mol. Biol. , vol.378 , pp. 622-633
    • Cobaugh, C.1    Almagro, J.2    Pogson, M.3    Iverson, B.4    Georgiou, G.5
  • 33
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly, M. L. (1983). Solvent-accessible surfaces of proteins and nucleic acids. Science 221, 709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 34
    • 0028326520 scopus 로고
    • A directory of human germ-line V kappa segments reveals a strong bias in their usage
    • Cox, J. P., Tomlinson, I. M., and Winter, G. (1994). A directory of human germ-line V kappa segments reveals a strong bias in their usage. Eur. I Immunol. 24, 827-836.
    • (1994) Eur. I Immunol. , vol.24 , pp. 827-836
    • Cox, J.P.1    Tomlinson, I.M.2    Winter, G.3
  • 35
    • 79952593462 scopus 로고    scopus 로고
    • B-cell receptor, clini-cal course and prognosis in chronic lymphocytic leukaemia: the grow-ing saga of the IGHV3 subgroup gene usage
    • Dal-Bo, M., Giudice, I. D., Bomben, R., Capello, D., Bertoni, F., Forconi, F., et al. (2011). B-cell receptor, clini-cal course and prognosis in chronic lymphocytic leukaemia: the grow-ing saga of the IGHV3 subgroup gene usage. Br. J. Haematol. 153, 3-14.
    • (2011) Br. J. Haematol. , vol.153 , pp. 3-14
    • Dal-Bo, M.1    Giudice, I.D.2    Bomben, R.3    Capello, D.4    Bertoni, F.5    Forconi, F.6
  • 36
    • 0020977127 scopus 로고
    • Structural basis of antibody function
    • Davies, D. R., and Metzger, H. (1983). Structural basis of antibody function. Annu. Rev. Immunol. 1, 87-117.
    • (1983) Annu. Rev. Immunol. , vol.1 , pp. 87-117
    • Davies, D.R.1    Metzger, H.2
  • 37
    • 0027953603 scopus 로고
    • 'Camelising' human antibody fragments: NMR studies on VH domains
    • Davies, J., and Riechmann, L. (1994). 'Camelising' human antibody fragments: NMR studies on VH domains. FEBS Lett. 339, 285-290.
    • (1994) FEBS Lett , vol.339 , pp. 285-290
    • Davies, J.1    Riechmann, L.2
  • 40
    • 0033593356 scopus 로고    scopus 로고
    • Analysis of heavy and light chain pairings indicates that receptor editing shapes the human antibody repertoire
    • De Wildt, R. M., Hoet, R. M., van Venrooij, W. J., Tomlinson, I. M., and Winter, G. (1999). Analysis of heavy and light chain pairings indicates that receptor editing shapes the human antibody repertoire. J. Mol. Biol. 285, 895-901.
    • (1999) J. Mol. Biol. , vol.285 , pp. 895-901
    • De Wildt, R.M.1    Hoet, R.M.2    van Venrooij, W.J.3    Tomlinson, I.M.4    Winter, G.5
  • 41
    • 0042195979 scopus 로고    scopus 로고
    • Selection and characterization of naturally occurring single-domain (IgNAR) antibody fragments from immunized sharks by phage display
    • Dooley, H., Flajnik, M. F., and Porter, A. J. (2003). Selection and characterization of naturally occurring single-domain (IgNAR) antibody fragments from immunized sharks by phage display. Mol. Immunol. 40, 25-33.
    • (2003) Mol. Immunol. , vol.40 , pp. 25-33
    • Dooley, H.1    Flajnik, M.F.2    Porter, A.J.3
  • 42
    • 0031688707 scopus 로고    scopus 로고
    • Somatic hypermutation of human immunoglobulin heavy chain genes: targeting of RGYW motifs on both DNA strands
    • Dörner, T., Foster, S. J., Farner, N. L., and Lipsky, P. E. (1998). Somatic hypermutation of human immunoglobulin heavy chain genes: targeting of RGYW motifs on both DNA strands. Eur. J. Immunol. 28, 3384-3396.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 3384-3396
    • Dörner, T.1    Foster, S.J.2    Farner, N.L.3    Lipsky, P.E.4
  • 43
    • 0037133506 scopus 로고    scopus 로고
    • Biophysical properties of camelid V (HH) domains compared to those of human V (H)3 domains
    • Ewert, S., Cambillau, C., Conrath, K., and Pluckthun, A. (2002). Biophysical properties of camelid V (HH) domains compared to those of human V (H)3 domains. Biochemistry 41, 3628-3636.
    • (2002) Biochemistry , vol.41 , pp. 3628-3636
    • Ewert, S.1    Cambillau, C.2    Conrath, K.3    Pluckthun, A.4
  • 44
    • 4143110187 scopus 로고    scopus 로고
    • Stability improvement of antibodies for extracellular and intracellular applications: CDR grafting to stable frameworks and structure-based framework engineering
    • Ewert, S., Honegger, A., and Pluckthun, A. (2004). Stability improvement of antibodies for extracellular and intracellular applications: CDR grafting to stable frameworks and structure-based framework engineering. Methods 34, 184-199.
    • (2004) Methods , vol.34 , pp. 184-199
    • Ewert, S.1    Honegger, A.2    Pluckthun, A.3
  • 45
    • 0037227517 scopus 로고    scopus 로고
    • Biophysical properties of human antibody variable domains
    • Ewert, S., Huber, T., Honegger, A., and Pluckthun, A. (2003). Biophysical properties of human antibody variable domains. J. Mol. Biol. 325, 531-553.
    • (2003) J. Mol. Biol. , vol.325 , pp. 531-553
    • Ewert, S.1    Huber, T.2    Honegger, A.3    Pluckthun, A.4
  • 46
    • 0345436074 scopus 로고    scopus 로고
    • Molecular mechanisms and selection influence the generation of the human V lambda J lambda repertoire
    • Farner, N. L., Dorner, T., and Lipsky, P. E. (1999). Molecular mechanisms and selection influence the generation of the human V lambda J lambda repertoire. J. Immunol. 162, 2137-2145.
    • (1999) J. Immunol. , vol.162 , pp. 2137-2145
    • Farner, N.L.1    Dorner, T.2    Lipsky, P.E.3
  • 47
    • 33644783935 scopus 로고    scopus 로고
    • Tyrosine plays a dominant functional role in the paratope of a synthetic antibody derived from a four amino acid code
    • Fellouse, E A., Barthelemy, P. A., Kelley, R. F., and Sidhu, S. S. (2006). Tyrosine plays a dominant functional role in the paratope of a synthetic antibody derived from a four amino acid code. J. Mol. Biol. 357, 100-114.
    • (2006) J. Mol. Biol. , vol.357 , pp. 100-114
    • Fellouse, E.A.1    Barthelemy, P.A.2    Kelley, R.F.3    Sidhu, S.S.4
  • 48
    • 34848848421 scopus 로고    scopus 로고
    • High-throughput generation of synthetic antibodies from highly functional minimalist phage-displayed libraries
    • Fellouse, E A., Esaki, K., Birtalan, S., Raptis, D., Cancasci, V. J., Koide, A., et al. (2007). High-throughput generation of synthetic antibodies from highly functional minimalist phage-displayed libraries. J. Mol. Biol. 373, 924-940.
    • (2007) J. Mol. Biol. , vol.373 , pp. 924-940
    • Fellouse, E.A.1    Esaki, K.2    Birtalan, S.3    Raptis, D.4    Cancasci, V.J.5    Koide, A.6
  • 50
    • 4344714933 scopus 로고    scopus 로고
    • Synthetic antibodies from a four-amino-acid code: a dominant role for tyrosine in antigen recognition
    • Fellouse, F. A., Wiesmann, C., and Sidhu, S. S. (2004). Synthetic antibodies from a four-amino-acid code: a dominant role for tyrosine in antigen recognition. Proc. Natl. Acad. Sci. U.S.A. 101, 12467-12472.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12467-12472
    • Fellouse, F.A.1    Wiesmann, C.2    Sidhu, S.S.3
  • 51
    • 77953811009 scopus 로고    scopus 로고
    • Dissection of the IgNAR V domain: molecular scanning and ortho-logue database mining define novel IgNAR hallmarks and affinity maturation mechanisms
    • Fennell, B. J., Darmanin-Sheehan, A., Hufton, S. E., Calabro, V., Wu, L., Muller, M. R., et al. (2010). Dissection of the IgNAR V domain: molecular scanning and ortho-logue database mining define novel IgNAR hallmarks and affinity maturation mechanisms. J. Mol. Biol. 400, 155-170.
    • (2010) J. Mol. Biol. , vol.400 , pp. 155-170
    • Fennell, B.J.1    Darmanin-Sheehan, A.2    Hufton, S.E.3    Calabro, V.4    Wu, L.5    Muller, M.R.6
  • 52
    • 27744525475 scopus 로고    scopus 로고
    • Exploiting the avian immunoglobulin system to simplify the generation of recombinant antibodies to allergenic proteins
    • Finlay, W. J., deVore, N. C., Dobrovolskaia, E. N., Gam, A., Goodyear, C. S., and Slater, J. E. (2005). Exploiting the avian immunoglobulin system to simplify the generation of recombinant antibodies to allergenic proteins. Clin. Exp. Allergy 35, 1040-1048.
    • (2005) Clin. Exp. Allergy , vol.35 , pp. 1040-1048
    • Finlay, W.J.1    deVore, N.C.2    Dobrovolskaia, E.N.3    Gam, A.4    Goodyear, C.S.5    Slater, J.E.6
  • 53
    • 33646594077 scopus 로고    scopus 로고
    • Generation of high-affinity chicken single-chain Fv antibody fragments for measurement of the Pseudonitzschia pungens toxin domoic acid
    • Finlay, W. J., Shaw, I., Reilly, J. P., and Kane, M. (2006). Generation of high-affinity chicken single-chain Fv antibody fragments for measurement of the Pseudonitzschia pungens toxin domoic acid. Appl. Environ. Microbiol. 72, 3343-3349.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 3343-3349
    • Finlay, W.J.1    Shaw, I.2    Reilly, J.P.3    Kane, M.4
  • 54
    • 78651390679 scopus 로고    scopus 로고
    • Sequencing antibody repertoires: the next generation
    • Fischer, N. (2011). Sequencing antibody repertoires: the next generation. MAbs 3, 17-20.
    • (2011) MAbs , vol.3 , pp. 17-20
    • Fischer, N.1
  • 55
    • 77956181220 scopus 로고    scopus 로고
    • Structure of the complex between HER2 and an antibody paratope formed by side chains from tryptophan and serine
    • Fisher, R. D., Ultsch, M., Lingel, A., Schaefer, G., Shao, L., Birtalan, S., et al. (2010). Structure of the complex between HER2 and an antibody paratope formed by side chains from tryptophan and serine. J. Mol. Biol. 402,217-229.
    • (2010) J. Mol. Biol. , vol.402 , pp. 217-229
    • Fisher, R.D.1    Ultsch, M.2    Lingel, A.3    Schaefer, G.4    Shao, L.5    Birtalan, S.6
  • 56
    • 80052341911 scopus 로고    scopus 로고
    • A case of convergence: why did a simple alternative to canonical antibodies arise in sharks and camels?
    • doi: 10.1371/ journal.pbio.1001120
    • Flajnik, M. F., Deschacht, N., and Muyldermans, S. (2011). A case of convergence: why did a simple alternative to canonical antibodies arise in sharks and camels? PLoS Biol. 9:e1001120. doi: 10.1371/ journal.pbio.1001120
    • (2011) PLoS Biol , vol.9
    • Flajnik, M.F.1    Deschacht, N.2    Muyldermans, S.3
  • 57
    • 70350051125 scopus 로고    scopus 로고
    • The generation and selection of single-domain, v region libraries from nurse sharks
    • Flajnik, M. F., and Dooley, H. (2009). The generation and selection of single-domain, v region libraries from nurse sharks. Methods Mol. Biol. 562, 71-82.
    • (2009) Methods Mol. Biol. , vol.562 , pp. 71-82
    • Flajnik, M.F.1    Dooley, H.2
  • 58
    • 0026559783 scopus 로고
    • Antibody framework residues affecting the conformation of the hypervariable loops
    • Foote, J., and Winter, G. (1992). Antibody framework residues affecting the conformation of the hypervariable loops. J. Mol. Biol. 224, 487-499.
    • (1992) J. Mol. Biol. , vol.224 , pp. 487-499
    • Foote, J.1    Winter, G.2
  • 59
    • 33751347582 scopus 로고    scopus 로고
    • Biopharmaceutical drug discovery using novel protein scaffolds
    • Gill, D. S., and Damle, N. K. (2006). Biopharmaceutical drug discovery using novel protein scaffolds. Curr. Opin. Biotechnol. 17, 653-658.
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 653-658
    • Gill, D.S.1    Damle, N.K.2
  • 60
    • 84856483987 scopus 로고    scopus 로고
    • Leveraging SBDD in protein therapeutic development: antibody engineering
    • Gilliland, G., Luo, J., Vafa, O., and Almagro, J. (2012). Leveraging SBDD in protein therapeutic development: antibody engineering. MethodsMol. Biol. 841, 321-349.
    • (2012) MethodsMol. Biol. , vol.841 , pp. 321-349
    • Gilliland, G.1    Luo, J.2    Vafa, O.3    Almagro, J.4
  • 61
    • 73949116413 scopus 로고    scopus 로고
    • Precise determination of the diversity of a combinatorial antibody library gives insight into the human immunoglobulin repertoire
    • Glanville, J., Zhai, W., Berka, J., Telman, D., Huerta, G., Mehta, G. R., et al. (2009). Precise determination of the diversity of a combinatorial antibody library gives insight into the human immunoglobulin repertoire. Proc. Natl. Acad. Sci. U.S.A. 106, 20216-20221.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 20216-20221
    • Glanville, J.1    Zhai, W.2    Berka, J.3    Telman, D.4    Huerta, G.5    Mehta, G.R.6
  • 62
    • 84855849845 scopus 로고    scopus 로고
    • Dual beneficial effect of interloop disulfide bond for single domain antibody fragments
    • Govaert, J., Pellis, M., Deschacht, N., Vincke, C., Conrath, K., Muyldermans, S., et al. (2012). Dual beneficial effect of interloop disulfide bond for single domain antibody fragments. J. Biol. Chem. 287, 1970-1979.
    • (2012) J. Biol. Chem. , vol.287 , pp. 1970-1979
    • Govaert, J.1    Pellis, M.2    Deschacht, N.3    Vincke, C.4    Conrath, K.5    Muyldermans, S.6
  • 63
    • 0027473684 scopus 로고
    • Human anti-self antibodies with high specificity from phage display libraries
    • Griffiths, A. D., Malmqvist, M., Marks, J. D., Bye, J. M., Embleton, M. J., McCafferty, J., et al. (1993). Human anti-self antibodies with high specificity from phage display libraries. EMBOJ. 12,725-734.
    • (1993) EMBOJ , vol.12 , pp. 725-734
    • Griffiths, A.D.1    Malmqvist, M.2    Marks, J.D.3    Bye, J.M.4    Embleton, M.J.5    McCafferty, J.6
  • 64
    • 0028291823 scopus 로고
    • Isolation of high affinity human antibodies directly from large synthetic repertoires
    • Griffiths, A. D., Williams, S. C., Hartley, O., Tomlinson, I. M., Waterhouse, P., Crosby, W. L., et al. (1994). Isolation of high affinity human antibodies directly from large synthetic repertoires. EMBO J. 13, 3245-3260.
    • (1994) EMBO J , vol.13 , pp. 3245-3260
    • Griffiths, A.D.1    Williams, S.C.2    Hartley, O.3    Tomlinson, I.M.4    Waterhouse, P.5    Crosby, W.L.6
  • 65
    • 77954757013 scopus 로고    scopus 로고
    • Stability and CDR composition biases enrich binder functionality landscapes
    • Hackel, B. J., Ackerman, M. E., Howland, S. W., and Wittrup, K. D. (2010). Stability and CDR composition biases enrich binder functionality landscapes. J. Mol. Biol. 401, 84-96.
    • (2010) J. Mol. Biol. , vol.401 , pp. 84-96
    • Hackel, B.J.1    Ackerman, M.E.2    Howland, S.W.3    Wittrup, K.D.4
  • 66
    • 77954626231 scopus 로고    scopus 로고
    • The full amino acid repertoire is superior to serine/tyrosine for selection of high affinity immunoglobulin G binders from the fibronectin scaffold
    • Hackel, B. J., and Wittrup, K. D. (2010). The full amino acid repertoire is superior to serine/tyrosine for selection of high affinity immunoglobulin G binders from the fibronectin scaffold. Protein Eng. Des. Sel. 23, 211-219.
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 211-219
    • Hackel, B.J.1    Wittrup, K.D.2
  • 68
    • 77953658260 scopus 로고    scopus 로고
    • The immunogenicity of humanized and fully human antibodies: residual immunogenicity resides in the CDR regions
    • Harding, E A., Stickler, M. M., Razo, J., and Dubridge, R. B. (2010). The immunogenicity of humanized and fully human antibodies: residual immunogenicity resides in the CDR regions. MAbs 2, 256-265.
    • (2010) MAbs , vol.2 , pp. 256-265
    • Harding, E.A.1    Stickler, M.M.2    Razo, J.3    Dubridge, R.B.4
  • 69
    • 35348819390 scopus 로고    scopus 로고
    • Properties, production, and applications of camelid single-domain antibody fragments
    • Harmsen, M. M., and De Haard, H. J. (2007). Properties, production, and applications of camelid single-domain antibody fragments. Appl. Microbiol. Biotechnol. 77, 13-22.
    • (2007) Appl. Microbiol. Biotechnol. , vol.77 , pp. 13-22
    • Harmsen, M.M.1    De Haard, H.J.2
  • 70
    • 0034524838 scopus 로고    scopus 로고
    • Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence features
    • Harmsen, M. M., Ruuls, R. C., Nijman, I. J., Niewold, T. A., Frenken, L. G., and de Geus, B. (2000). Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence features. Mol. Immunol. 37, 579-590.
    • (2000) Mol. Immunol. , vol.37 , pp. 579-590
    • Harmsen, M.M.1    Ruuls, R.C.2    Nijman, I.J.3    Niewold, T.A.4    Frenken, L.G.5    de Geus, B.6
  • 71
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and screening recombinant antibody libraries
    • Hoogenboom, H. R. (2005). Selecting and screening recombinant antibody libraries. Nat. Biotechnol. 23, 1105-1116.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1105-1116
    • Hoogenboom, H.R.1
  • 72
    • 0030130977 scopus 로고    scopus 로고
    • Non-stochastic utilization of Ig V region genes in unselected human peripheral B cells
    • Huang, S. C., Jiang, R., Glas, A. M., and Milner, E. C. (1996). Non-stochastic utilization of Ig V region genes in unselected human peripheral B cells. Mol. Immunol. 33, 553-560.
    • (1996) Mol. Immunol. , vol.33 , pp. 553-560
    • Huang, S.C.1    Jiang, R.2    Glas, A.M.3    Milner, E.C.4
  • 73
    • 0031586002 scopus 로고    scopus 로고
    • The creation of diversity in the human immunoglobulin V (lambda) repertoire
    • Ignatovich, O., Tomlinson, I. M., Jones, P. T., and Winter, G. (1997). The creation of diversity in the human immunoglobulin V (lambda) repertoire. J. Mol. Biol. 268, 69-77.
    • (1997) J. Mol. Biol. , vol.268 , pp. 69-77
    • Ignatovich, O.1    Tomlinson, I.M.2    Jones, P.T.3    Winter, G.4
  • 74
    • 33746191445 scopus 로고    scopus 로고
    • Isolation and comparative characterization of Ki-67 equivalent antibodies from the HuCAL phage display library
    • Jarutat, T., Frisch, C., Nickels, C., Merz, H., and Knappik, A. (2006). Isolation and comparative characterization of Ki-67 equivalent antibodies from the HuCAL phage display library. Biol. Chem. 387, 995-1003.
    • (2006) Biol. Chem. , vol.387 , pp. 995-1003
    • Jarutat, T.1    Frisch, C.2    Nickels, C.3    Merz, H.4    Knappik, A.5
  • 75
    • 34250006793 scopus 로고    scopus 로고
    • Selection of vimentin-specific antibodies from the HuCAL phage display library by subtractive panning on formalin-fixed, paraffin-embedded tissue
    • Jarutat, T., Nickels, C., Frisch, C., Stellmacher, F., Hofig, K. P., Knappik, A., et al. (2007). Selection of vimentin-specific antibodies from the HuCAL phage display library by subtractive panning on formalin-fixed, paraffin-embedded tissue. Biol. Chem. 388, 651-658.
    • (2007) Biol. Chem. , vol.388 , pp. 651-658
    • Jarutat, T.1    Nickels, C.2    Frisch, C.3    Stellmacher, F.4    Hofig, K.P.5    Knappik, A.6
  • 77
    • 0037093863 scopus 로고    scopus 로고
    • Heavy chain V region diversity in the duckbilled platypus (Ornithorhynchus anatinus): long and highly variable complementarity-determining region 3 compensates for limited germline diversity
    • Johansson, J., Aveskogh, M., Munday, B., and Hellman, L. (2002). Heavy chain V region diversity in the duckbilled platypus (Ornithorhynchus anatinus): long and highly variable complementarity-determining region 3 compensates for limited germline diversity.J. Immunol. 168, 5155-5162.
    • (2002) J. Immunol. , vol.168 , pp. 5155-5162
    • Johansson, J.1    Aveskogh, M.2    Munday, B.3    Hellman, L.4
  • 78
    • 0022558297 scopus 로고
    • Replacing the complementarity-determining regions in a human antibody with those from a mouse
    • Jones, P. T., Dear, P. H., Foote, J., Neuberger, M. S., and Winter, G. (1986). Replacing the complementarity-determining regions in a human antibody with those from a mouse. Nature 321, 522-525.
    • (1986) Nature , vol.321 , pp. 522-525
    • Jones, P.T.1    Dear, P.H.2    Foote, J.3    Neuberger, M.S.4    Winter, G.5
  • 79
    • 0015247402 scopus 로고
    • Attempts to locate complementarity-determining residues in the variable positions of light and heavy chains
    • Kabat, E. A., and Wu, T. T. (1971). Attempts to locate complementarity-determining residues in the variable positions of light and heavy chains. Ann. N.Y. Acad. Sci. 190,382-393.
    • (1971) Ann. N.Y. Acad. Sci. , vol.190 , pp. 382-393
    • Kabat, E.A.1    Wu, T.T.2
  • 80
    • 0034635335 scopus 로고    scopus 로고
    • Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides
    • Knappik, A., Ge, L., Honegger, A., Pack, P., Fischer, M., Wellnhofer, G., et al. (2000). Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides. J. Mol. Biol. 296, 57-86.
    • (2000) J. Mol. Biol. , vol.296 , pp. 57-86
    • Knappik, A.1    Ge, L.2    Honegger, A.3    Pack, P.4    Fischer, M.5    Wellnhofer, G.6
  • 81
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Köhler, G., and Milstein, C. (1975). Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256, 495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Köhler, G.1    Milstein, C.2
  • 82
    • 65749099472 scopus 로고    scopus 로고
    • The importance of being tyrosine: lessons in molecular recognition from minimalist synthetic binding proteins
    • Koide, S., and Sidhu, S. S. (2009). The importance of being tyrosine: lessons in molecular recognition from minimalist synthetic binding proteins. ACS Chem. Biol. 4, 325-334.
    • (2009) ACS Chem. Biol. , vol.4 , pp. 325-334
    • Koide, S.1    Sidhu, S.S.2
  • 84
    • 33751198274 scopus 로고    scopus 로고
    • Synthetic anti-BR3 antibodies that mimic BAFF binding and target both human and murine B cells
    • Lee, C. V., Hymowitz, S. G., Wallweber, H. J., Gordon, N. C., Billeci, K. L., Tsai, S. P., et al. (2006). Synthetic anti-BR3 antibodies that mimic BAFF binding and target both human and murine B cells. Blood 108,3103-3111.
    • (2006) Blood , vol.108 , pp. 3103-3111
    • Lee, C.V.1    Hymowitz, S.G.2    Wallweber, H.J.3    Gordon, N.C.4    Billeci, K.L.5    Tsai, S.P.6
  • 85
    • 3242760800 scopus 로고    scopus 로고
    • High-affinity human antibodies from phage-displayed synthetic Fab libraries with a single framework scaffold
    • Lee, C. V., Liang, W. C., Dennis, M. S., Eigenbrot, C., Sidhu, S. S., and Fuh, G. (2004). High-affinity human antibodies from phage-displayed synthetic Fab libraries with a single framework scaffold. J. Mol. Biol. 340,1073-1093.
    • (2004) J. Mol. Biol. , vol.340 , pp. 1073-1093
    • Lee, C.V.1    Liang, W.C.2    Dennis, M.S.3    Eigenbrot, C.4    Sidhu, S.S.5    Fuh, G.6
  • 87
    • 79952640176 scopus 로고    scopus 로고
    • Rare antibodies from combinatorial libraries suggests an S O. S. component of the human immunological repertoire
    • Lerner, R. (2011). Rare antibodies from combinatorial libraries suggests an S.O.S. component of the human immunological repertoire. Mol. Biosyst. 7, 1004-1012.
    • (2011) Mol. Biosyst. , vol.7 , pp. 1004-1012
    • Lerner, R.1
  • 88
    • 0348047387 scopus 로고    scopus 로고
    • Cloning of porcine scFv antibodies by phage display and expression in Escherichia coli
    • Li, F., and Aitken, R. (2004). Cloning of porcine scFv antibodies by phage display and expression in Escherichia coli. Vet. Immunol. Immunopathol. 97, 39-51.
    • (2004) Vet. Immunol. Immunopathol. , vol.97 , pp. 39-51
    • Li, F.1    Aitken, R.2
  • 89
    • 0035696023 scopus 로고    scopus 로고
    • Editors and editing of anti-DNA receptors
    • Li, H., Jiang, Y., Prak, E. L., Radic, M., and Weigert, M. (2001). Editors and editing of anti-DNA receptors. Immunity 15, 947-957.
    • (2001) Immunity , vol.15 , pp. 947-957
    • Li, H.1    Jiang, Y.2    Prak, E.L.3    Radic, M.4    Weigert, M.5
  • 90
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte, L. L., Chothia, C., and Janin, J. (1999). The atomic structure of protein-protein recognition sites.J. Mol. Biol. 285, 2177-2198.
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 91
    • 0030580057 scopus 로고    scopus 로고
    • Antibody-antigen interactions: contact analysis and binding site topography
    • MacCallum, R., Martin, A., and Thornton, J. (1996). Antibody-antigen interactions: contact analysis and binding site topography. J. Mol. Biol. 262, 732-745.
    • (1996) J. Mol. Biol. , vol.262 , pp. 732-745
    • MacCallum, R.1    Martin, A.2    Thornton, J.3
  • 92
    • 27644489367 scopus 로고    scopus 로고
    • Immunoglobulin gene diversification
    • Maizels, N. (2005). Immunoglobulin gene diversification. Annu. Rev. Genet. 39, 23-46.
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 23-46
    • Maizels, N.1
  • 93
    • 0033912255 scopus 로고    scopus 로고
    • Bypassing hybridoma technology: HLA-C reactive human single-chain antibody fragments (scFv) derived from a synthetic phage display library (HuCAL) and their potential to discriminate HLA class I specificities
    • Marget, M., Sharma, B. B., Tesar, M., Kretzschmar, T., Jenisch, S., Westphal, E., et al. (2000). Bypassing hybridoma technology: HLA-C reactive human single-chain antibody fragments (scFv) derived from a synthetic phage display library (HuCAL) and their potential to discriminate HLA class I specificities. Tissue Antigens 56, 1-9.
    • (2000) Tissue Antigens , vol.56 , pp. 1-9
    • Marget, M.1    Sharma, B.B.2    Tesar, M.3    Kretzschmar, T.4    Jenisch, S.5    Westphal, E.6
  • 94
  • 95
    • 0030589039 scopus 로고    scopus 로고
    • Structural families in loops of homologous proteins: automatic classification, modelling and application to antibodies
    • Martin, A. C., and Thornton, J. M. (1996). Structural families in loops of homologous proteins: automatic classification, modelling and application to antibodies. J. Mol. Biol. 263,800-815.
    • (1996) J. Mol. Biol. , vol.263 , pp. 800-815
    • Martin, A.C.1    Thornton, J.M.2
  • 96
    • 0035725844 scopus 로고    scopus 로고
    • Nomenclature and overview of the mouse (Mus musculus and Mus sp ) immunoglobulin kappa (IGK) genes
    • Martinez-Jean, C., Folch, G., and Lefranc, M. (2001). Nomenclature and overview of the mouse (Mus musculus and Mus sp.) immunoglobulin kappa (IGK) genes. Exp. Clin. Immunogenet. 18, 255-279.
    • (2001) Exp. Clin. Immunogenet. , vol.18 , pp. 255-279
    • Martinez-Jean, C.1    Folch, G.2    Lefranc, M.3
  • 97
    • 0031775443 scopus 로고    scopus 로고
    • The complete nucleotide sequence of the human immunoglobulin heavy chain variable region locus
    • Matsuda, F., Ishii, K., Bourvagnet, P., Kuma, K., Hayashida, H., Miyata, T., and Honjo, T. (1998). The complete nucleotide sequence of the human immunoglobulin heavy chain variable region locus. J. Exp. Med. 188, 2151-2162.
    • (1998) J. Exp. Med. , vol.188 , pp. 2151-2162
    • Matsuda, F.1    Ishii, K.2    Bourvagnet, P.3    Kuma, K.4    Hayashida, H.5    Miyata, T.6    Honjo, T.7
  • 98
    • 0025226085 scopus 로고
    • Phage antibodies: filamentous phage displaying antibody variable domains
    • McCafferty, J., Griffiths, A. D., Winter, G., and Chiswell, D. J. (1990). Phage antibodies: filamentous phage displaying antibody variable domains. Nature 348, 552-554.
    • (1990) Nature , vol.348 , pp. 552-554
    • McCafferty, J.1    Griffiths, A.D.2    Winter, G.3    Chiswell, D.J.4
  • 99
    • 0025964038 scopus 로고
    • Structure, function and properties of antibody binding sites
    • Mian, I., Bradwell, A., and Olson, A. (1991). Structure, function and properties of antibody binding sites. I Mol. Biol. 217, 133-151.
    • (1991) I Mol. Biol. , vol.217 , pp. 133-151
    • Mian, I.1    Bradwell, A.2    Olson, A.3
  • 100
    • 0032536197 scopus 로고    scopus 로고
    • Conformations of the third hyper-variable region in the VH domain of immunoglobulins
    • Morea, V., Tramontano, A., Rustici, M., Chothia, C., and Lesk, A. M. (1998). Conformations of the third hyper-variable region in the VH domain of immunoglobulins. J. Mol. Biol. 275, 269-294.
    • (1998) J. Mol. Biol. , vol.275 , pp. 269-294
    • Morea, V.1    Tramontano, A.2    Rustici, M.3    Chothia, C.4    Lesk, A.M.5
  • 101
    • 0021716682 scopus 로고
    • Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains
    • Morrison, S. L., Johnson, M. J., Herzenberg, L. A., and Oi, V. T. (1984). Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains. Proc. Natl. Acad. Sci. U.S.A. 81,6851-6855.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 6851-6855
    • Morrison, S.L.1    Johnson, M.J.2    Herzenberg, L.A.3    Oi, V.T.4
  • 103
    • 0033103453 scopus 로고    scopus 로고
    • Unique single-domain antigen binding fragments derived from naturally occurring camel heavy-chain antibodies
    • Muyldermans, S., and Lauwereys, M. (1999). Unique single-domain antigen binding fragments derived from naturally occurring camel heavy-chain antibodies. J. Mol. Recognit. 12, 131-140.
    • (1999) J. Mol. Recognit. , vol.12 , pp. 131-140
    • Muyldermans, S.1    Lauwereys, M.2
  • 104
    • 77957361348 scopus 로고    scopus 로고
    • Development trends for human monoclonal antibody therapeutics
    • Nelson, A., Dhimolea, E., and Reichert, J. (2010). Development trends for human monoclonal antibody therapeutics. Nat. Rev. Drug Discov. 9, 767-774.
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 767-774
    • Nelson, A.1    Dhimolea, E.2    Reichert, J.3
  • 105
    • 0029348652 scopus 로고
    • Engineering recombi-nant antibodies for immunother-apy
    • Neri, D., Petrul, H., and Roncucci, G. (1995). Engineering recombi-nant antibodies for immunother-apy. Cell Biophys. 27, 47-61.
    • (1995) Cell Biophys , vol.27 , pp. 47-61
    • Neri, D.1    Petrul, H.2    Roncucci, G.3
  • 106
    • 0031630685 scopus 로고    scopus 로고
    • Antibodies from phage display libraries as immunochemical reagents
    • Neri, D., Pini, A., and Nissim, A. (1998). Antibodies from phage display libraries as immunochemical reagents. Methods Mol. Biol. 80, 475-500.
    • (1998) Methods Mol. Biol. , vol.80 , pp. 475-500
    • Neri, D.1    Pini, A.2    Nissim, A.3
  • 108
    • 0034755438 scopus 로고    scopus 로고
    • Functional heavy-chain antibodies in Camelidae
    • Nguyen, V. K., Desmyter, A., and Muyldermans, S. (2001). Functional heavy-chain antibodies in Camelidae. Adv. Immunol. 79, 261-296.
    • (2001) Adv. Immunol. , vol.79 , pp. 261-296
    • Nguyen, V.K.1    Desmyter, A.2    Muyldermans, S.3
  • 109
    • 0345425685 scopus 로고    scopus 로고
    • Loss of splice consensus signal is responsible for the removal of the entire C (H)1 domain of the functional camel IGG2A heavy-chain antibodies
    • Nguyen, V. K., Hamers, R., Wyns, L., and Muyldermans, S. (1999). Loss of splice consensus signal is responsible for the removal of the entire C (H)1 domain of the functional camel IGG2A heavy-chain antibodies. Mol. Immunol. 36, 515-524.
    • (1999) Mol. Immunol. , vol.36 , pp. 515-524
    • Nguyen, V.K.1    Hamers, R.2    Wyns, L.3    Muyldermans, S.4
  • 110
    • 0036251627 scopus 로고    scopus 로고
    • Heavy-chain antibodies in Camelidae; a case of evolutionary innovation
    • Nguyen, V. K., Su, C., Muyldermans, S., and van der Loo, W. (2002). Heavy-chain antibodies in Camelidae; a case of evolutionary innovation. Immunogenetics 54, 39-47.
    • (2002) Immunogenetics , vol.54 , pp. 39-47
    • Nguyen, V.K.1    Su, C.2    Muyldermans, S.3    van der Loo, W.4
  • 111
    • 28944441839 scopus 로고    scopus 로고
    • Humanization of chicken monoclonal antibody using phage-display system
    • Nishibori, N., Horiuchi, H., Furusawa, S., and Matsuda, H. (2006). Humanization of chicken monoclonal antibody using phage-display system. Mol. Immunol. 43, 634-642.
    • (2006) Mol. Immunol. , vol.43 , pp. 634-642
    • Nishibori, N.1    Horiuchi, H.2    Furusawa, S.3    Matsuda, H.4
  • 112
    • 34249790004 scopus 로고    scopus 로고
    • Molecular mechanisms of antibody somatic hypermutation
    • Noia, J. D., and Neuberger, M. (2007). Molecular mechanisms of antibody somatic hypermutation. Annu. Rev. Biochem. 76, 1-22.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 1-22
    • Noia, J.D.1    Neuberger, M.2
  • 113
    • 79251598995 scopus 로고    scopus 로고
    • A new clustering of antibody CDR loop conformations
    • North, B., Lehmann, A., and Dunbrack, R. J. (2011). A new clustering of antibody CDR loop conformations. J. Mol. Biol. 406, 228-256.
    • (2011) J. Mol. Biol. , vol.406 , pp. 228-256
    • North, B.1    Lehmann, A.2    Dunbrack, R.J.3
  • 115
    • 33646719897 scopus 로고    scopus 로고
    • Antibodies for proteomic research: comparison of traditional immunization with recombinant antibody technology
    • Ohara, R., Knappik, A., Shimada, K., Frisch, C., Ylera, F., and Koga, H. (2006). Antibodies for proteomic research: comparison of traditional immunization with recombinant antibody technology. Proteomics 6, 2638-2646.
    • (2006) Proteomics , vol.6 , pp. 2638-2646
    • Ohara, R.1    Knappik, A.2    Shimada, K.3    Frisch, C.4    Ylera, F.5    Koga, H.6
  • 116
    • 0017614064 scopus 로고
    • Structural basis for the specificity of antibody-antigen reactions and structural mechanisms for the diversification of antigen-binding specificities
    • Padlan, E. A. (1977). Structural basis for the specificity of antibody-antigen reactions and structural mechanisms for the diversification of antigen-binding specificities. Q. Rev. Biophys. 10, 35-65.
    • (1977) Q. Rev. Biophys. , vol.10 , pp. 35-65
    • Padlan, E.A.1
  • 117
    • 0028289241 scopus 로고
    • Anatomy of the antibody molecule
    • Padlan, E. A. (1994). Anatomy of the antibody molecule. Mol. Immunol. 31, 169-217.
    • (1994) Mol. Immunol. , vol.31 , pp. 169-217
    • Padlan, E.A.1
  • 118
    • 0023969216 scopus 로고
    • Chicken immunoglobulin gamma-heavy chains: limited VH gene repertoire, combinatorial diversification by D gene segments and evolution of the heavy chain locus
    • Parvari, R., Avivi, A., Lentner, F., Ziv, E., Tel-Or, S., Burstein, Y., et al. (1988). Chicken immunoglobulin gamma-heavy chains: limited VH gene repertoire, combinatorial diversification by D gene segments and evolution of the heavy chain locus. EMBOJ. 7, 739-744.
    • (1988) EMBOJ , vol.7 , pp. 739-744
    • Parvari, R.1    Avivi, A.2    Lentner, F.3    Ziv, E.4    Tel-Or, S.5    Burstein, Y.6
  • 119
    • 0025208320 scopus 로고
    • Somatic diversification of chicken immunoglobulin light chains by point mutations
    • Parvari, R., Ziv, E., Lantner, F., Heller, D., and Schechter, I. (1990). Somatic diversification of chicken immunoglobulin light chains by point mutations. Proc. Natl. Acad. Sci. U.S.A. 87, 3072-3076.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 3072-3076
    • Parvari, R.1    Ziv, E.2    Lantner, F.3    Heller, D.4    Schechter, I.5
  • 120
    • 0023065569 scopus 로고
    • A few germline genes encode the variable regions of chicken immunoglobulin light and gamma-heavy chains
    • Parvari, R., Ziv, E., Lantner, F., Tel-Or, S., Burstein, Y., and Schechter, I. (1987a). A few germline genes encode the variable regions of chicken immunoglobulin light and gamma-heavy chains. Prog. Clin. Biol. Res. 238, 15-26.
    • (1987) Prog. Clin. Biol. Res. , vol.238 , pp. 15-26
    • Parvari, R.1    Ziv, E.2    Lantner, F.3    Tel-Or, S.4    Burstein, Y.5    Schechter, I.6
  • 121
    • 0023083818 scopus 로고
    • Analyses of chicken immunoglobulin light chain cDNA clones indicate a few germline V lambda genes and allotypes of the C lambda locus
    • Parvari, R., Ziv, E., Lentner, F., Tel-Or, S., Burstein, Y., and Schechter, I. (1987b). Analyses of chicken immunoglobulin light chain cDNA clones indicate a few germline V lambda genes and allotypes of the C lambda locus. EMBO J. 6, 97-102.
    • (1987) EMBO J , vol.6 , pp. 97-102
    • Parvari, R.1    Ziv, E.2    Lentner, F.3    Tel-Or, S.4    Burstein, Y.5    Schechter, I.6
  • 122
    • 33344476078 scopus 로고    scopus 로고
    • A focused antibody library for improved hapten recognition
    • Persson, H., Lantto, J., and Ohlin, M. (2006). A focused antibody library for improved hapten recognition. J. Mol. Biol. 357, 607-620.
    • (2006) J. Mol. Biol. , vol.357 , pp. 607-620
    • Persson, H.1    Lantto, J.2    Ohlin, M.3
  • 124
    • 77953457663 scopus 로고    scopus 로고
    • In vitro affinity maturation of HuCAL antibodies: complementarity determining region exchange and RapMAT technology
    • Prassler, J., Steidl, S., and Urlinger, S. (2009). In vitro affinity maturation of HuCAL antibodies: complementarity determining region exchange and RapMAT technology. Immunotherapy 1, 571-583.
    • (2009) Immunotherapy , vol.1 , pp. 571-583
    • Prassler, J.1    Steidl, S.2    Urlinger, S.3
  • 125
    • 80053303946 scopus 로고    scopus 로고
    • HuCAL PLATINUM, a synthetic Fab library optimized for sequence diversity and superior performance in mammalian expression systems
    • Prassler, J., Thiel, S., Pracht, C., Polzer, A., Peters, S., Bauer, M., et al. (2011). HuCAL PLATINUM, a synthetic Fab library optimized for sequence diversity and superior performance in mammalian expression systems. J. Mol. Biol. 413, 261-278.
    • (2011) J. Mol. Biol. , vol.413 , pp. 261-278
    • Prassler, J.1    Thiel, S.2    Pracht, C.3    Polzer, A.4    Peters, S.5    Bauer, M.6
  • 126
    • 0031014034 scopus 로고    scopus 로고
    • Molecular mechanisms governing reading frame choice of immunoglobulin diversity genes
    • Raaphorst, F. M., Raman, C. S., Nall, B. T., and Teale, J. M. (1997). Molecular mechanisms governing reading frame choice of immunoglobulin diversity genes. Immunol. Today 18, 37-43.
    • (1997) Immunol. Today , vol.18 , pp. 37-43
    • Raaphorst, F.M.1    Raman, C.S.2    Nall, B.T.3    Teale, J.M.4
  • 127
    • 0032127804 scopus 로고    scopus 로고
    • Hot spot focusing of somatic hyper-mutation in MSH2-deficient mice suggests two stages of mutational targeting
    • Rada, C., Ehrenstein, M. R., Neuberger, M. S., and Milstein, C. (1998). Hot spot focusing of somatic hyper-mutation in MSH2-deficient mice suggests two stages of mutational targeting. Immunity 9, 135-141.
    • (1998) Immunity , vol.9 , pp. 135-141
    • Rada, C.1    Ehrenstein, M.R.2    Neuberger, M.S.3    Milstein, C.4
  • 128
    • 0034607856 scopus 로고    scopus 로고
    • The rabbit antibody repertoire as a novel source for the generation of therapeutic human antibodies
    • Rader, C., Ritter, G., Nathan, S., Elia, M., Gout, I., Jungbluth, A. A., et al. (2000). The rabbit antibody repertoire as a novel source for the generation of therapeutic human antibodies. J. Biol Chem. 275,13668-13676.
    • (2000) J. Biol Chem. , vol.275 , pp. 13668-13676
    • Rader, C.1    Ritter, G.2    Nathan, S.3    Elia, M.4    Gout, I.5    Jungbluth, A.A.6
  • 129
    • 84863246128 scopus 로고    scopus 로고
    • Antigen-binding site anatomy and somaticmutations in antibodies that recognize different types of antigens
    • Ragunathan, G., Smart, J., Williams, J., and Almagro, J. (2012). Antigen-binding site anatomy and somaticmutations in antibodies that recognize different types of antigens. J. Mol. Recognit. 25, 103-113.
    • (2012) J. Mol. Recognit. , vol.25 , pp. 103-113
    • Ragunathan, G.1    Smart, J.2    Williams, J.3    Almagro, J.4
  • 130
    • 0023510298 scopus 로고
    • Evolutionary and somatic selection of the antibody repertoire in the mouse
    • Rajewsky, K., Förster, I., and Cumano, A. (1987). Evolutionary and somatic selection of the antibody repertoire in the mouse. Science 238, 1088-1094.
    • (1987) Science , vol.238 , pp. 1088-1094
    • Rajewsky, K.1    Förster, I.2    Cumano, A.3
  • 131
    • 0035889578 scopus 로고    scopus 로고
    • Analysis of antibodies of known structure suggests a lack of correspondence between the residues in contact with the antigen and those modified by somatic hypermutation
    • Ramirez-Benitez, M. C., and Almagro, J. C. (2001). Analysis of antibodies of known structure suggests a lack of correspondence between the residues in contact with the antigen and those modified by somatic hypermutation. Proteins 45, 199-206.
    • (2001) Proteins , vol.45 , pp. 199-206
    • Ramirez-Benitez, M.C.1    Almagro, J.C.2
  • 132
    • 26044467886 scopus 로고    scopus 로고
    • Antibodies, immunoglobulin genes and the bursa of Fabricius in chicken B cell development
    • Ratcliffe, M. J. (2006). Antibodies, immunoglobulin genes and the bursa of Fabricius in chicken B cell development. Dev. Comp. Immunol. 30, 101-118.
    • (2006) Dev. Comp. Immunol. , vol.30 , pp. 101-118
    • Ratcliffe, M.J.1
  • 133
    • 84860896956 scopus 로고    scopus 로고
    • Marketed therapeutic antibodies compendium
    • Reichert, J. (2012). Marketed therapeutic antibodies compendium. MAbs 4,413-415.
    • (2012) MAbs , vol.4 , pp. 413-415
    • Reichert, J.1
  • 134
    • 0021957934 scopus 로고
    • A single rearrangement event generates most of the chicken immunoglobulin light chain diversity
    • Reynaud, C. A., Anquez, V., Dahan, A., and Weill, J. C. (1985). A single rearrangement event generates most of the chicken immunoglobulin light chain diversity. Cell 40, 283-291.
    • (1985) Cell , vol.40 , pp. 283-291
    • Reynaud, C.A.1    Anquez, V.2    Dahan, A.3    Weill, J.C.4
  • 135
    • 0023652339 scopus 로고
    • A hyperconversion mechanism generates the chicken light chain preim-mune repertoire
    • Reynaud, C. A., Anquez, V., Grimal, H., and Weill, J. C. (1987). A hyperconversion mechanism generates the chicken light chain preim-mune repertoire. Cell 48, 379-388.
    • (1987) Cell , vol.48 , pp. 379-388
    • Reynaud, C.A.1    Anquez, V.2    Grimal, H.3    Weill, J.C.4
  • 136
    • 0026002863 scopus 로고
    • The chicken D locus and its contribution to the immunoglobulin heavy chain repertoire
    • Reynaud, C. A., Anquez, V., and Weill, J. C. (1991). The chicken D locus and its contribution to the immunoglobulin heavy chain repertoire. Eur. J. Immunol. 21, 2661-2670.
    • (1991) Eur. J. Immunol. , vol.21 , pp. 2661-2670
    • Reynaud, C.A.1    Anquez, V.2    Weill, J.C.3
  • 137
    • 0024443875 scopus 로고
    • Somatic hyperconversion diversifies the single Vh gene of the chicken with a high incidence in the D region
    • Reynaud, C. A., Dahan, A., Anquez, V., and Weill, J. C. (1989). Somatic hyperconversion diversifies the single Vh gene of the chicken with a high incidence in the D region. Cell 59, 171-183.
    • (1989) Cell , vol.59 , pp. 171-183
    • Reynaud, C.A.1    Dahan, A.2    Anquez, V.3    Weill, J.C.4
  • 138
    • 0020790142 scopus 로고
    • Complete sequence of a chicken lambda light chain immunoglobulin derived from the nucleotide sequence of its mRNA
    • Reynaud, C. A., Dahan, A., and Weill, J. C. (1983). Complete sequence of a chicken lambda light chain immunoglobulin derived from the nucleotide sequence of its mRNA. Proc. Natl. Acad. Sci. U.S.A. 80, 4099-4103.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 4099-4103
    • Reynaud, C.A.1    Dahan, A.2    Weill, J.C.3
  • 139
    • 0033544535 scopus 로고    scopus 로고
    • Single domain antibodies: comparison of camel VH and camelised human VH domains
    • Riechmann, L., and Muyldermans, S. (1999). Single domain antibodies: comparison of camel VH and camelised human VH domains. J.Immunol. Methods 231, 25-38.
    • (1999) J.Immunol. Methods , vol.231 , pp. 25-38
    • Riechmann, L.1    Muyldermans, S.2
  • 140
    • 39149087988 scopus 로고    scopus 로고
    • The human combinatorial antibody library HuCAL GOLD combines diversification of all six CDRs according to the natural immune system with a novel display method for efficient selection of high-affinity antibodies
    • Rothe, C., Urlinger, S., Lohning, C., Prassler, J., Stark, Y., Jager, U., et al. (2008). The human combinatorial antibody library HuCAL GOLD combines diversification of all six CDRs according to the natural immune system with a novel display method for efficient selection of high-affinity antibodies. J. Mol. Biol. 376, 1182-1200.
    • (2008) J. Mol. Biol. , vol.376 , pp. 1182-1200
    • Rothe, C.1    Urlinger, S.2    Lohning, C.3    Prassler, J.4    Stark, Y.5    Jager, U.6
  • 141
    • 0025781883 scopus 로고
    • Multiple mechanisms participate in the generation of diversity of human H chain CDR3 regions
    • Sanz, I. (1991). Multiple mechanisms participate in the generation of diversity of human H chain CDR3 regions. J. Immunol. 147, 1720-1729.
    • (1991) J. Immunol. , vol.147 , pp. 1720-1729
    • Sanz, I.1
  • 142
    • 17944380435 scopus 로고    scopus 로고
    • Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design
    • Saphire, E., Parren, P., Pantophlet, R., Zwick, M., Morris, G., Rudd, P., et al. (2001). Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design. Science 293, 1155-1159.
    • (2001) Science , vol.293 , pp. 1155-1159
    • Saphire, E.1    Parren, P.2    Pantophlet, R.3    Zwick, M.4    Morris, G.5    Rudd, P.6
  • 143
    • 0032586844 scopus 로고    scopus 로고
    • Characteristics of the immunoglobulin Vkappa genes, pseudogenes, relics and orphons in the mouse genome
    • Schäble, K., Thiebe, R., Bensch, A., Brensing-Küppers, J., Heim, V., Kirschbaum, T., et al. (1999). Characteristics of the immunoglobulin Vkappa genes, pseudogenes, relics and orphons in the mouse genome. Eur. J. Immunol. 29, 2082-2086.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 2082-2086
    • Schäble, K.1    Thiebe, R.2    Bensch, A.3    Brensing-Küppers, J.4    Heim, V.5    Kirschbaum, T.6
  • 144
    • 0028177722 scopus 로고
    • The human immunoglobulin kappa locus: pseudogenes, unique and repetitive sequences
    • Schäble, K., Thiebe, R., Flügel, A., Meindl, A., and Zachau, H. (1994). The human immunoglobulin kappa locus: pseudogenes, unique and repetitive sequences. Biol. Chem. Hoppe Seyler. 375, 189-199.
    • (1994) Biol. Chem. Hoppe Seyler. , vol.375 , pp. 189-199
    • Schäble, K.1    Thiebe, R.2    Flügel, A.3    Meindl, A.4    Zachau, H.5
  • 145
    • 26044480339 scopus 로고    scopus 로고
    • Similarity and divergence in the development and expression of the mouse and human antibody repertoires
    • Schroeder, H. W Jr. (2006). Similarity and divergence in the development and expression of the mouse and human antibody repertoires. Dev. Comp. Immunol. 30, 119-135.
    • (2006) Dev. Comp. Immunol. , vol.30 , pp. 119-135
    • Schroeder Jr., H.W.1
  • 146
    • 0023525849 scopus 로고
    • Early restriction of the human antibody repertoire
    • Schroeder, H. W Jr., Hillson, J. L., and Perlmutter, R. M. (1987). Early restriction of the human antibody repertoire. Science 238, 791-793.
    • (1987) Science , vol.238 , pp. 791-793
    • Schroeder, H.1    Hillson Jr., W.2    Perlmutter, J.L.R.M.3
  • 148
    • 0032147138 scopus 로고    scopus 로고
    • Regulation of the antibody repertoire through control of HCDR3 diversity
    • Schroeder, H. W. Jr., Ippolito, G. C., and Shiokawa, S. (1998). Regulation of the antibody repertoire through control of HCDR3 diversity. Vaccine 16, 1383-1390.
    • (1998) Vaccine , vol.16 , pp. 1383-1390
    • Schroeder Jr., H.W.1    Ippolito, G.C.2    Shiokawa, S.3
  • 150
    • 77349120461 scopus 로고    scopus 로고
    • De novo selection of high-affinity antibodies from synthetic fab libraries displayed on phage as pIX fusion proteins
    • Shi, L., Wheeler, J. C., Sweet, R. W., Lu, J., Luo, J., Tornetta, M., et al. (2010). De novo selection of high-affinity antibodies from synthetic fab libraries displayed on phage as pIX fusion proteins. J. Mol. Biol. 397,385-396.
    • (2010) J. Mol. Biol. , vol.397 , pp. 385-396
    • Shi, L.1    Wheeler, J.C.2    Sweet, R.W.3    Lu, J.4    Luo, J.5    Tornetta, M.6
  • 151
    • 0030577371 scopus 로고    scopus 로고
    • Structural classification of CDR-H3 in antibodies
    • Shirai, H., Kidera, A., and Nakamura, H. (1996). Structural classification of CDR-H3 in antibodies. FEBS Lett. 399, 1-8.
    • (1996) FEBS Lett , vol.399 , pp. 1-8
    • Shirai, H.1    Kidera, A.2    Nakamura, H.3
  • 152
    • 33751080719 scopus 로고    scopus 로고
    • Synthetic therapeutic antibodies
    • Sidhu, S. S., and Fellouse, F. A. (2006). Synthetic therapeutic antibodies. Nat. Chem. Biol. 2, 682-688.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 682-688
    • Sidhu, S.S.1    Fellouse, F.A.2
  • 153
    • 1842609526 scopus 로고    scopus 로고
    • Phage-displayed antibody libraries of synthetic heavy chain complementarity determining regions
    • Sidhu, S. S., Li, B., Chen, Y., Fellouse, F. A., Eigenbrot, C., and Fuh, G. (2004). Phage-displayed antibody libraries of synthetic heavy chain complementarity determining regions. J. Mol. Biol. 338, 299-310.
    • (2004) J. Mol. Biol. , vol.338 , pp. 299-310
    • Sidhu, S.S.1    Li, B.2    Chen, Y.3    Fellouse, F.A.4    Eigenbrot, C.5    Fuh, G.6
  • 154
    • 33748762207 scopus 로고    scopus 로고
    • Human monoclonal antibodies to domain C of tenascin-C selectively target solid tumors in vivo
    • Silacci, M., Brack, S. S., Spath, N., Buck, A., Hillinger, S., Arni, S., et al. (2006). Human monoclonal antibodies to domain C of tenascin-C selectively target solid tumors in vivo. Protein Eng. Des. Sel. 19, 471-478.
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 471-478
    • Silacci, M.1    Brack, S.S.2    Spath, N.3    Buck, A.4    Hillinger, S.5    Arni, S.6
  • 155
    • 20644469912 scopus 로고    scopus 로고
    • Design, construction, and characterization of a large synthetic human antibody phage display library
    • Silacci, M., Brack, S., Schirru, G., Marlind, J., Ettorre, A., Merlo, A., et al. (2005). Design, construction, and characterization of a large synthetic human antibody phage display library. Proteomics 5, 2340-2350.
    • (2005) Proteomics , vol.5 , pp. 2340-2350
    • Silacci, M.1    Brack, S.2    Schirru, G.3    Marlind, J.4    Ettorre, A.5    Merlo, A.6
  • 156
    • 0031572510 scopus 로고    scopus 로고
    • Bovine IgG repertoire is dominated by a single diversified VH gene family
    • Sinclair, M. C., Gilchrist, J., and Aitken, R. (1997). Bovine IgG repertoire is dominated by a single diversified VH gene family. J. Immunol. 159, 3883-3889.
    • (1997) J. Immunol. , vol.159 , pp. 3883-3889
    • Sinclair, M.C.1    Gilchrist, J.2    Aitken, R.3
  • 157
    • 0021818675 scopus 로고
    • Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface
    • Smith, G. P. (1985). Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228, 1315-1317.
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 158
    • 4544250973 scopus 로고    scopus 로고
    • Crystal structure of a shark single-domain antibody V region in complex with lysozyme
    • Stanfield, R. L., Dooley, H., Flajnik, M. E, and Wilson, I. A. (2004). Crystal structure of a shark single-domain antibody V region in complex with lysozyme. Science 305, 1770-1773.
    • (2004) Science , vol.305 , pp. 1770-1773
    • Stanfield, R.L.1    Dooley, H.2    Flajnik, M.E.3    Wilson, I.A.4
  • 159
    • 33847103076 scopus 로고    scopus 로고
    • Maturation of shark single-domain (IgNAR) antibodies: evidence for induced-fit binding
    • Stanfield, R. L., Dooley, H., Verdino, P., Flajnik, M. F., and Wilson, I. A. (2007). Maturation of shark single-domain (IgNAR) antibodies: evidence for induced-fit binding. J. Mol. Biol. 367, 358-372.
    • (2007) J. Mol. Biol. , vol.367 , pp. 358-372
    • Stanfield, R.L.1    Dooley, H.2    Verdino, P.3    Flajnik, M.F.4    Wilson, I.A.5
  • 161
    • 0029162562 scopus 로고
    • Comprehensive pharmacokinetics of a humanized antibody and analysis of residual anti-idiotypic responses
    • Stephens, S., Emtage, S., Vetterlein, O., Chaplin, L., Bebbington, C., Nesbitt, A., et al. (1995). Comprehensive pharmacokinetics of a humanized antibody and analysis of residual anti-idiotypic responses. Immunology 85, 668-674.
    • (1995) Immunology , vol.85 , pp. 668-674
    • Stephens, S.1    Emtage, S.2    Vetterlein, O.3    Chaplin, L.4    Bebbington, C.5    Nesbitt, A.6
  • 163
    • 0029159770 scopus 로고
    • The structural repertoire of the human V kappa domain
    • Tomlinson, I. M., Cox, J. P., Herardi, G. E., Lesk, A. M., and Chothia, C. (1995). The structural repertoire of the human V kappa domain. EMBO J. 14, 4628-4638.
    • (1995) EMBO J , vol.14 , pp. 4628-4638
    • Tomlinson, I.M.1    Cox, J.P.2    Herardi, G.E.3    Lesk, A.M.4    Chothia, C.5
  • 165
    • 0026785856 scopus 로고
    • The repertoire of human germline VH sequences reveals about fifty groups of VH segments with different hypervariable loops
    • Tomlinson, I. M., Walter, G., Marks, J. D., Llewelyn, M. B., and Winter, G. (1992). The repertoire of human germline VH sequences reveals about fifty groups of VH segments with different hypervariable loops. J. Mol. Biol. 227, 776-798.
    • (1992) J. Mol. Biol. , vol.227 , pp. 776-798
    • Tomlinson, I.M.1    Walter, G.2    Marks, J.D.3    Llewelyn, M.B.4    Winter, G.5
  • 166
    • 0020534965 scopus 로고
    • Somatic generation of antibody diversity
    • Tonegawa, S. (1983). Somatic generation of antibody diversity. Nature 14,575-581.
    • (1983) Nature , vol.14 , pp. 575-581
    • Tonegawa, S.1
  • 168
    • 77249133143 scopus 로고    scopus 로고
    • Orally administered L. lactis secreting an anti-TNF Nanobody demonstrate efficacy in chronic colitis
    • Vandenbroucke, K., de Haard, H., Beirnaert, E., Dreier, T., Lauwereys, M., Huyck, L., et al. (2010). Orally administered L. lactis secreting an anti-TNF Nanobody demonstrate efficacy in chronic colitis. Mucosal Immunol. 3, 49-56.
    • (2010) Mucosal Immunol , vol.3 , pp. 49-56
    • Vandenbroucke, K.1    de Haard, H.2    Beirnaert, E.3    Dreier, T.4    Lauwereys, M.5    Huyck, L.6
  • 169
    • 0029610794 scopus 로고
    • Canonical structure repertoire of the antigen-binding site of immunoglobulins suggests strong geometrical restrictions associated to the mechanism of immune recognition
    • Vargas-Madrazo, E., Lara-Ochoa, E, and Almagro, J. C. (1995). Canonical structure repertoire of the antigen-binding site of immunoglobulins suggests strong geometrical restrictions associated to the mechanism of immune recognition. J. Mol. Biol. 254, 497-504.
    • (1995) J. Mol. Biol. , vol.254 , pp. 497-504
    • Vargas-Madrazo, E.1    Lara-Ochoa, E.2    Almagro, J.C.3
  • 170
    • 0028559783 scopus 로고
    • Trinucleotide phosphoramidites: ideal reagents for the synthesis of mixed oligonucleotides for random mutagenesis
    • Virnekas, B., Ge, L., Pluckthun, A., Schneider, K. C., Wellnhofer, G., and Moroney, S. E. (1994). Trinucleotide phosphoramidites: ideal reagents for the synthesis of mixed oligonucleotides for random mutagenesis. Nucleic Acids Res. 22, 5600-5607.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5600-5607
    • Virnekas, B.1    Ge, L.2    Pluckthun, A.3    Schneider, K.C.4    Wellnhofer, G.5    Moroney, S.E.6
  • 171
    • 0033819491 scopus 로고    scopus 로고
    • Design and use of phage display libraries for the selection of antibodies and enzymes
    • Viti, F., Nilsson, F., Demartis, S., Huber, A., and Neri, D. (2000). Design and use of phage display libraries for the selection of antibodies and enzymes. Meth. Enzymol. 326, 480-505.
    • (2000) Meth. Enzymol. , vol.326 , pp. 480-505
    • Viti, F.1    Nilsson, F.2    Demartis, S.3    Huber, A.4    Neri, D.5
  • 172
    • 0026589924 scopus 로고
    • Early B-cell development in chickens, sheep and rabbits
    • Weill, J. C., and Reynaud, C. A. (1992). Early B-cell development in chickens, sheep and rabbits. Curr. Opin. Immunol. 4, 177-180.
    • (1992) Curr. Opin. Immunol. , vol.4 , pp. 177-180
    • Weill, J.C.1    Reynaud, C.A.2
  • 173
    • 65649122270 scopus 로고    scopus 로고
    • High-throughput sequencing of the zebrafish antibody repertoire
    • Weinstein, J., Jiang, N., White, R. R., Fisher, D., and Quake, S. (2009). High-throughput sequencing of the zebrafish antibody repertoire. Science 324, 807-810.
    • (2009) Science , vol.324 , pp. 807-810
    • Weinstein, J.1    Jiang, N.2    White, R.R.3    Fisher, D.4    Quake, S.5
  • 174
    • 68349117269 scopus 로고    scopus 로고
    • Single domain antibodies: promising experimental and therapeutic tools in infection and immunity
    • Wesolowski, J., Alzogaray, V., Reyelt, J., Unger, M., Juarez, K., Urrutia, M., et al. (2009). Single domain antibodies: promising experimental and therapeutic tools in infection and immunity. Med. Microbiol. Immunol. 198, 157-174.
    • (2009) Med. Microbiol. Immunol. , vol.198 , pp. 157-174
    • Wesolowski, J.1    Alzogaray, V.2    Reyelt, J.3    Unger, M.4    Juarez, K.5    Urrutia, M.6
  • 175
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily-domains for cell surface recognition
    • Williams, A., and Barclay, A. (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.1    Barclay, A.2
  • 176
    • 0028606741 scopus 로고
    • Antibody-antigen interactions: new structures and new con-formational changes
    • Wilson, I. A., and Stanfield, R. L. (1994). Antibody-antigen interactions: new structures and new con-formational 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
  • 177
    • 0031983725 scopus 로고    scopus 로고
    • Somatic hypermutation introduces insertions and deletions into immunoglobulin V genes
    • Wilson, P. C., Bouteiller, O. D., Liu, Y.-J., Potter, K., Banchereau, J., Capra, J. D., et al. (1998). Somatic hypermutation introduces insertions and deletions into immunoglobulin V genes. J. Exp. Med. 187, 59-70.
    • (1998) J. Exp. Med. , vol.187 , pp. 59-70
    • Wilson, P.C.1    Bouteiller, O.D.2    Liu, Y.-J.3    Potter, K.4    Banchereau, J.5    Capra, J.D.6
  • 178
    • 79551493763 scopus 로고    scopus 로고
    • Effects of somatic mutations on CDR loop flexibility during affinity maturation
    • Wong, S. E., Sellers, B. D., and Jacobson, M. P. (2011). Effects of somatic mutations on CDR loop flexibility during affinity maturation. Proteins 79, 821-829.
    • (2011) Proteins , vol.79 , pp. 821-829
    • Wong, S.E.1    Sellers, B.D.2    Jacobson, M.P.3
  • 179
    • 84855361545 scopus 로고    scopus 로고
    • Fundamental characteristics of the immunoglobulin VH repertoire of chickens in comparison with those of humans, mice, and camelids
    • Wu, L., Oficjalska, K., Lambert, M., Fennell, B. J., Darmanin-Sheehan, A., Ni Shuilleabhain, D., et al. (2011). Fundamental characteristics of the immunoglobulin VH repertoire of chickens in comparison with those of humans, mice, and camelids.J. Immunol. 188, 322-333.
    • (2011) J. Immunol. , vol.188 , pp. 322-333
    • Wu, L.1    Oficjalska, K.2    Lambert, M.3    Fennell, B.J.4    Darmanin-Sheehan, A.5    Ni Shuilleabhain, D.6
  • 180
    • 0027212854 scopus 로고
    • Length distribution of CDRH3 in antibodies
    • Wu, T., Johnson, G., and Kabat, E. (1993). Length distribution of CDRH3 in antibodies. Proteins 16, 1-7.
    • (1993) Proteins , vol.16 , pp. 1-7
    • Wu, T.1    Johnson, G.2    Kabat, E.3
  • 181
    • 0014828908 scopus 로고
    • An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity
    • Wu, T. T., and Kabat, E. A. (1970). An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity. J. Exp. Med. 132, 211-250.
    • (1970) J. Exp. Med. , vol.132 , pp. 211-250
    • Wu, T.T.1    Kabat, E.A.2
  • 182
    • 0030210311 scopus 로고    scopus 로고
    • Chicken monoclonal antibody isolated by a phage display system
    • Yamanaka, H. I., Inoue, T., and Ikeda-Tanaka, O. (1996). Chicken monoclonal antibody isolated by a phage display system. J. Immunol. 157, 1156-1162.
    • (1996) J. Immunol. , vol.157 , pp. 1156-1162
    • Yamanaka, H.I.1    Inoue, T.2    Ikeda-Tanaka, O.3
  • 183
    • 0242551578 scopus 로고    scopus 로고
    • Expressed murine and human CDR-H3 intervals of equal length exhibit distinct repertoires that differ in their amino acid composition and predicted range of structures
    • Zemlin, M., Klinger, M., Link, J., Zemlin, C., Bauer, K., Engler, J. A., et al. (2003). Expressed murine and human CDR-H3 intervals of equal length exhibit distinct repertoires that differ in their amino acid composition and predicted range of structures. J. Mol. Biol. 334, 733-749.
    • (2003) J. Mol. Biol. , vol.334 , pp. 733-749
    • Zemlin, M.1    Klinger, M.2    Link, J.3    Zemlin, C.4    Bauer, K.5    Engler, J.A.6
  • 184
  • 185
    • 72949120359 scopus 로고    scopus 로고
    • A germline knowledge based computational approach for determining antibody complementarity determining regions
    • Zhao, S., and Lu, J. (2010). A germline knowledge based computational approach for determining antibody complementarity determining regions. Mol. Immunol. 47, 694-700.
    • (2010) Mol. Immunol. , vol.47 , pp. 694-700
    • Zhao, S.1    Lu, J.2
  • 186
    • 84455161936 scopus 로고    scopus 로고
    • Biased use of the IGHV4 family and evidence for antigen selection in Chlamydophila psittaci-negative ocular adnexal extranodal marginal zone lymphomas
    • doi: 10.1371/journal. pone.0029114
    • Zhu, D., Lossos, C., Chapman-Fredricks, J., Matthews, J., Ikpatt, O., Ruiz, P., et al. (2011). Biased use of the IGHV4 family and evidence for antigen selection in Chlamydophila psittaci-negative ocular adnexal extranodal marginal zone lymphomas. PLoS ONE 6:e29114. doi: 10.1371/journal. pone.0029114
    • (2011) PLoS ONE , vol.6
    • Zhu, D.1    Lossos, C.2    Chapman-Fredricks, J.3    Matthews, J.4    Ikpatt, O.5    Ruiz, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.