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Volumn 112, Issue 50, 2015, Pages 15354-15359

Augmented binary substitution: Single-pass cdr germlining and stabilization of therapeutic antibodies

Author keywords

Antibody; Humanization; Immunogenicity; Paratope; Plasticity

Indexed keywords

IMMUNOGLOBULIN G; MONOCLONAL ANTIBODY; COMPLEMENTARITY DETERMINING REGION; EPITOPE; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; IMMUNOGLOBULIN VARIABLE REGION; PEPTIDE LIBRARY; TAU PROTEIN;

EID: 84950117303     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1510944112     Document Type: Article
Times cited : (21)

References (66)
  • 1
    • 77957361348 scopus 로고    scopus 로고
    • Development trends for human monoclonal antibody therapeutics
    • Nelson AL, Dhimolea E, Reichert J.M. (2010) Development trends for human monoclonal antibody therapeutics. Nat Rev Drug Discov 9(10):767-774.
    • (2010) Nat Rev Drug Discov , vol.9 , Issue.10 , pp. 767-774
    • Nelson, A.L.1    Dhimolea, E.2    Reichert, J.M.3
  • 2
    • 0034607856 scopus 로고    scopus 로고
    • The rabbit antibody repertoire as a novel source for the generation of therapeutic human antibodies
    • Rader C, et al (2000) The rabbit antibody repertoire as a novel source for the generation of therapeutic human antibodies. J Biol Chem 275(18):13668-13676.
    • (2000) J Biol Chem , vol.275 , Issue.18 , pp. 13668-13676
    • Rader, C.1
  • 3
    • 84871818326 scopus 로고    scopus 로고
    • An ultra-specific avian antibody to phosphorylated tau protein reveals a unique mechanism for phosphoepitope recognition
    • Shih HH, et al (2012) An ultra-specific avian antibody to phosphorylated tau protein reveals a unique mechanism for phosphoepitope recognition. J Biol Chem 287(53):44425-44434.
    • (2012) J Biol Chem , vol.287 , Issue.53 , pp. 44425-44434
    • Shih, H.H.1
  • 4
    • 0021054153 scopus 로고
    • Monoclonal antibody therapeutic trials in seven patients with T-cell lymphoma
    • Miller RA, Oseroff AR, Stratte P.T., Levy R. (1983) Monoclonal antibody therapeutic trials in seven patients with T-cell lymphoma. Blood 62(5):988-995.
    • (1983) Blood , vol.62 , Issue.5 , pp. 988-995
    • Miller, R.A.1    Oseroff, A.R.2    Stratte, P.T.3    Levy, R.4
  • 5
    • 77953658260 scopus 로고    scopus 로고
    • The immunogenicity of humanized and fully human antibodies: Residual immunogenicity resides in the CDR regions
    • Harding FA, Stickler MM, Razo J, DuBridge R.B. (2010) The immunogenicity of humanized and fully human antibodies: Residual immunogenicity resides in the CDR regions. MAbs 2(3):256-265.
    • (2010) MAbs , vol.2 , Issue.3 , pp. 256-265
    • Harding, F.A.1    Stickler, M.M.2    Razo, J.3    DuBridge, R.B.4
  • 6
    • 84888022850 scopus 로고    scopus 로고
    • T-cell dependent immunogenicity of protein therapeutics: Preclinical assessment and mitigation
    • Jawa V, et al (2013) T-cell dependent immunogenicity of protein therapeutics: Preclinical assessment and mitigation. Clin Immunol 149(3):534-555.
    • (2013) Clin Immunol , vol.149 , Issue.3 , pp. 534-555
    • Jawa, V.1
  • 7
    • 0022558297 scopus 로고
    • Replacing the complementarity-determining regions in a human antibody with those from a mouse
    • Jones PT, Dear PH, Foote J, Neuberger M.S., Winter G. (1986) Replacing the complementarity-determining regions in a human antibody with those from a mouse. Nature 321 (6069):522-525.
    • (1986) Nature , vol.321 , Issue.6069 , pp. 522-525
    • Jones, P.T.1    Dear, P.H.2    Foote, J.3    Neuberger, M.S.4    Winter, G.5
  • 8
    • 38449104580 scopus 로고    scopus 로고
    • Humanization of antibodies
    • Almagro JC, 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
  • 9
    • 17644378667 scopus 로고    scopus 로고
    • Immunogenicity of engineered antibodies
    • Hwang WY, Foote J. (2005) Immunogenicity of engineered antibodies. Methods 36(1):3-10.
    • (2005) Methods , vol.36 , Issue.1 , pp. 3-10
    • Hwang, W.Y.1    Foote, J.2
  • 10
    • 0030993418 scopus 로고    scopus 로고
    • Antibody humanization using monovalent phage display
    • Baca M, Presta LG, O'Connor SJ, Wells J.A. (1997) Antibody humanization using monovalent phage display. J Biol Chem 272(16):10678-10684.
    • (1997) J Biol Chem , vol.272 , Issue.16 , pp. 10678-10684
    • Baca, M.1    Presta, L.G.2    O'Connor, S.J.3    Wells, J.A.4
  • 11
    • 17644391684 scopus 로고    scopus 로고
    • Antibody humanization by framework shuffling
    • Dall'Acqua WF, et al. (2005) Antibody humanization by framework shuffling. Methods 36(1):43-60.
    • (2005) Methods , vol.36 , Issue.1 , pp. 43-60
    • Dall'Acqua, W.F.1
  • 13
    • 77951762065 scopus 로고    scopus 로고
    • Human framework adaptation of a mouse anti-human IL-13 antibody
    • Fransson J, et al (2010) Human framework adaptation of a mouse anti-human IL-13 antibody. J Mol Biol 398(2):214-231.
    • (2010) J Mol Biol , vol.398 , Issue.2 , pp. 214-231
    • Fransson, J.1
  • 14
    • 84891623854 scopus 로고    scopus 로고
    • Antibody humanization by redesign of complementarity-determining region residues proximate to the acceptor framework
    • Hanf KJ, et al (2014) Antibody humanization by redesign of complementarity-determining region residues proximate to the acceptor framework. Methods 65(1): 68-76.
    • (2014) Methods , vol.65 , Issue.1 , pp. 68-76
    • Hanf, K.J.1
  • 15
    • 34249017414 scopus 로고    scopus 로고
    • A molecular immunology approach to antibody humanization and functional optimization
    • Lazar GA, Desjarlais JR, Jacinto J, Karki S., Hammond P.W. (2007) A molecular immunology approach to antibody humanization and functional optimization. Mol Immunol 44(8):1986-1998.
    • (2007) Mol Immunol , vol.44 , Issue.8 , pp. 1986-1998
    • Lazar, G.A.1    Desjarlais, J.R.2    Jacinto, J.3    Karki, S.4    Hammond, P.W.5
  • 16
    • 0037100379 scopus 로고    scopus 로고
    • "Superhumanized" antibodies: Reduction of immunogenic potential by complementarity-determining region grafting with human germline sequences: Application to an anti-CD28
    • Tan P, et al (2002) "Superhumanized" antibodies: Reduction of immunogenic potential by complementarity-determining region grafting with human germline sequences: Application to an anti-CD28. J Immunol 169(2):1119-1125.
    • (2002) J Immunol , vol.169 , Issue.2 , pp. 1119-1125
    • Tan, P.1
  • 17
    • 0025848797 scopus 로고
    • A possible procedure for reducing the immunogenicity of antibody variable domains while preserving their ligand-binding properties
    • Padlan EA (1991) A possible procedure for reducing the immunogenicity of antibody variable domains while preserving their ligand-binding properties. Mol Immunol 28(4-5):489-498.
    • (1991) Mol Immunol , vol.28 , Issue.4-5 , pp. 489-498
    • Padlan, E.A.1
  • 18
    • 84856794463 scopus 로고    scopus 로고
    • A universal combinatorial design of antibody framework to graft distinct CDR sequences: A bioinformatics approach
    • Haidar JN, et al (2012) A universal combinatorial design of antibody framework to graft distinct CDR sequences: A bioinformatics approach. Proteins 80(3):896-912.
    • (2012) Proteins , vol.80 , Issue.3 , pp. 896-912
    • Haidar, J.N.1
  • 19
    • 84874213990 scopus 로고    scopus 로고
    • Natural and man-made V-gene repertoires for antibody discovery
    • Finlay WJ, Almagro J.C. (2012) Natural and man-made V-gene repertoires for antibody discovery. Front Immunol 3:342.
    • (2012) Front Immunol , vol.3 , pp. 342
    • Finlay, W.J.1    Almagro, J.C.2
  • 20
    • 84904420055 scopus 로고    scopus 로고
    • Second antibody modeling assessment (AMA-II)
    • Almagro JC, et al (2014) Second antibody modeling assessment (AMA-II). Proteins 82(8):1553-1562.
    • (2014) Proteins , vol.82 , Issue.8 , pp. 1553-1562
    • Almagro, J.C.1
  • 21
    • 84875169292 scopus 로고    scopus 로고
    • Humanization of antibodies using heavy chain complementarity-determining region 3 grafting coupled with in vitro somatic hypermutation
    • Bowers PM, et al (2013) Humanization of antibodies using heavy chain complementarity-determining region 3 grafting coupled with in vitro somatic hypermutation. J Biol Chem 288(11):7688-7696.
    • (2013) J Biol Chem , vol.288 , Issue.11 , pp. 7688-7696
    • Bowers, P.M.1
  • 22
    • 84880000622 scopus 로고    scopus 로고
    • Mutational analysis of 48G7 reveals that somatic hypermutation affects both antibody stability and binding affinity
    • Sun SB, et al (2013) Mutational analysis of 48G7 reveals that somatic hypermutation affects both antibody stability and binding affinity. J Am Chem Soc 135(27): 9980-9983.
    • (2013) J Am Chem Soc , vol.135 , Issue.27 , pp. 9980-9983
    • Sun, S.B.1
  • 23
    • 79960091033 scopus 로고    scopus 로고
    • Highly specific off-target binding identified and eliminated during the humanization of an antibody against FGF receptor 4
    • Bumbaca D, et al (2011) Highly specific off-target binding identified and eliminated during the humanization of an antibody against FGF receptor 4. MAbs 3(4):376-386.
    • (2011) MAbs , vol.3 , Issue.4 , pp. 376-386
    • Bumbaca, D.1
  • 24
    • 84883865798 scopus 로고    scopus 로고
    • Immunogenicity of mAbs in non-human primates during nonclinical safety assessment
    • van Meer P.J., et al (2013) Immunogenicity of mAbs in non-human primates during nonclinical safety assessment. MAbs 5(5):810-816.
    • (2013) MAbs , vol.5 , Issue.5 , pp. 810-816
    • Van Meer, P.J.1
  • 25
    • 84913540290 scopus 로고    scopus 로고
    • Biosimilars entering the clinic without animal studies. A paradigm shift in the European union
    • van Aerts L.A., De Smet K, Reichmann G, van der Laan JW, Schneider CK (2014) Biosimilars entering the clinic without animal studies. A paradigm shift in the European Union. MAbs 6(5):1155-1162.
    • (2014) MAbs , vol.6 , Issue.5 , pp. 1155-1162
    • Van Aerts, L.A.1    De Smet, K.2    Reichmann, G.3    Van Der Laan, J.W.4    Schneider, C.K.5
  • 26
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An immunologic perspective
    • Rosenberg AS (2006) Effects of protein aggregates: An immunologic perspective. AAPS J 8(3):E501-E507.
    • (2006) AAPS J , vol.8 , Issue.3 , pp. E501-E507
    • Rosenberg, A.S.1
  • 27
    • 84925507517 scopus 로고    scopus 로고
    • Small amounts of sub-visible aggregates enhance the immunogenic potential of monoclonal antibody therapeutics
    • Ahmadi M, et al (2015) Small amounts of sub-visible aggregates enhance the immunogenic potential of monoclonal antibody therapeutics. Pharm Res 32(4): 1383-1394.
    • (2015) Pharm Res , vol.32 , Issue.4 , pp. 1383-1394
    • Ahmadi, M.1
  • 28
    • 64649099284 scopus 로고    scopus 로고
    • Affinity maturation of a humanized rat antibody for anti-RAGE therapy: Comprehensive mutagenesis reveals a high level of mutational plasticity both inside and outside the complementarity-determining regions
    • Finlay WJ, et al (2009) Affinity maturation of a humanized rat antibody for anti-RAGE therapy: Comprehensive mutagenesis reveals a high level of mutational plasticity both inside and outside the complementarity-determining regions. J Mol Biol 388(3):541-558.
    • (2009) J Mol Biol , vol.388 , Issue.3 , pp. 541-558
    • Finlay, W.J.1
  • 29
    • 77649270662 scopus 로고    scopus 로고
    • Engineering fully human monoclonal antibodies from murine variable regions
    • Bernett MJ, et al (2010) Engineering fully human monoclonal antibodies from murine variable regions. J Mol Biol 396(5):1474-1490.
    • (2010) J Mol Biol , vol.396 , Issue.5 , pp. 1474-1490
    • Bernett, M.J.1
  • 30
    • 0030580057 scopus 로고    scopus 로고
    • Antibody-antigen interactions: Contact analysis and binding site topography
    • MacCallum RM, Martin AC, Thornton J.M. (1996) Antibody-antigen interactions: Contact analysis and binding site topography. J Mol Biol 262(5):732-745.
    • (1996) J Mol Biol , vol.262 , Issue.5 , pp. 732-745
    • MacCallum, R.M.1    Martin, A.C.2    Thornton, J.M.3
  • 31
    • 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 JC (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(2):132-143.
    • (2004) J Mol Recognit , vol.17 , Issue.2 , pp. 132-143
    • Almagro, J.C.1
  • 32
    • 84863246128 scopus 로고    scopus 로고
    • Antigen-binding site anatomy and somatic mutations in antibodies that recognize different types of antigens
    • Raghunathan G, Smart J, Williams J., Almagro J.C. (2012) Antigen-binding site anatomy and somatic mutations in antibodies that recognize different types of antigens. J Mol Recognit 25(3):103-113.
    • (2012) J Mol Recognit , vol.25 , Issue.3 , pp. 103-113
    • Raghunathan, G.1    Smart, J.2    Williams, J.3    Almagro, J.C.4
  • 33
    • 0036295439 scopus 로고    scopus 로고
    • Comprehensive functional maps of the antigen-binding site of an anti-erbb2 antibody obtained with shotgun scanning mutagenesis
    • Vajdos FF, et al (2002) Comprehensive functional maps of the antigen-binding site of an anti-ErbB2 antibody obtained with shotgun scanning mutagenesis. J Mol Biol 320(2):415-428.
    • (2002) J Mol Biol , vol.320 , Issue.2 , pp. 415-428
    • Vajdos, F.F.1
  • 34
    • 62849095162 scopus 로고    scopus 로고
    • Variants of the antibody herceptin that interact with HER2 and VEGF at the antigen binding site
    • Bostrom J, et al (2009) Variants of the antibody herceptin that interact with HER2 and VEGF at the antigen binding site. Science 323 (5921):1610-1614.
    • (2009) Science , vol.323 , Issue.5921 , pp. 1610-1614
    • Bostrom, J.1
  • 35
    • 79954591066 scopus 로고    scopus 로고
    • Structural repertoire of immunoglobulin À light chains
    • Chailyan A, Marcatili P, Cirillo D., Tramontano A. (2011) Structural repertoire of immunoglobulin À light chains. Proteins 79(5):1513-1524.
    • (2011) Proteins , vol.79 , Issue.5 , pp. 1513-1524
    • Chailyan, A.1    Marcatili, P.2    Cirillo, D.3    Tramontano, A.4
  • 36
    • 79251598995 scopus 로고    scopus 로고
    • A new clustering of antibody CDR loop conformations
    • North B, Lehmann A, Dunbrack R.L., Jr (2011) A new clustering of antibody CDR loop conformations. J Mol Biol 406(2):228-256.
    • (2011) J Mol Biol , vol.406 , Issue.2 , pp. 228-256
    • North, B.1    Lehmann, A.2    Dunbrack, R.L.3
  • 37
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • Chothia C, Lesk A.M. (1987) Canonical structures for the hypervariable regions of immunoglobulins. J Mol Biol 196(4):901-917.
    • (1987) J Mol Biol , vol.196 , Issue.4 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 38
    • 0030589039 scopus 로고    scopus 로고
    • Structural families in loops of homologous proteins: Automatic classification, modelling and application to antibodies
    • Martin AC, Thornton J.M. (1996) Structural families in loops of homologous proteins: Automatic classification, modelling and application to antibodies. J Mol Biol 263(5): 800-815.
    • (1996) J Mol Biol , vol.263 , Issue.5 , pp. 800-815
    • Martin, A.C.1    Thornton, J.M.2
  • 39
    • 84869840045 scopus 로고    scopus 로고
    • A strategy for risk mitigation of antibodies with fast clearance
    • Hötzel I., et al (2012) A strategy for risk mitigation of antibodies with fast clearance. MAbs 4(6):753-760.
    • (2012) MAbs , vol.4 , Issue.6 , pp. 753-760
    • Hötzel, I.1
  • 40
    • 77951212654 scopus 로고    scopus 로고
    • Correlation of pharmacodynamic activity, pharmacokinetics, and anti-product antibody responses to anti-IL-21R antibody therapeutics following IV administration to cynomolgus monkeys
    • Vugmeyster Y, et al (2010) Correlation of pharmacodynamic activity, pharmacokinetics, and anti-product antibody responses to anti-IL-21R antibody therapeutics following IV administration to cynomolgus monkeys. J Transl Med 8:41.
    • (2010) J Transl Med , vol.8 , pp. 41
    • Vugmeyster, Y.1
  • 41
    • 84874562364 scopus 로고    scopus 로고
    • Identification and multidimensional optimization of an asymmetric bispecific IgG antibody mimicking the function of factor VIII cofactor activity
    • Sampei Z, et al (2013) Identification and multidimensional optimization of an asymmetric bispecific IgG antibody mimicking the function of factor VIII cofactor activity. PLoS One 8(2):e57479.
    • (2013) PLoS One , vol.8 , Issue.2
    • Sampei, Z.1
  • 42
    • 84913525345 scopus 로고    scopus 로고
    • Framework selection can influence pharmacokinetics of a humanized therapeutic antibody through differences in molecule charge
    • Li B, et al (2014) Framework selection can influence pharmacokinetics of a humanized therapeutic antibody through differences in molecule charge. MAbs 6(5): 1255-1264.
    • (2014) MAbs , vol.6 , Issue.5 , pp. 1255-1264
    • Li, B.1
  • 43
    • 20444363121 scopus 로고    scopus 로고
    • Ultra-potent antibodies against respiratory syncytial virus: Effects of binding kinetics and binding valence on viral neutralization
    • Wu H, et al (2005) Ultra-potent antibodies against respiratory syncytial virus: Effects of binding kinetics and binding valence on viral neutralization. J Mol Biol 350(1): 126-144.
    • (2005) J Mol Biol , vol.350 , Issue.1 , pp. 126-144
    • Wu, H.1
  • 45
    • 0028049374 scopus 로고
    • Humanization of murine monoclonal antibodies through variable domain resurfacing
    • Roguska MA, et al (1994) Humanization of murine monoclonal antibodies through variable domain resurfacing. Proc Natl Acad Sci USA 91(3):969-973.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.3 , pp. 969-973
    • Roguska, M.A.1
  • 46
    • 84879835707 scopus 로고    scopus 로고
    • Monoclonal antibody humanness score and its applications
    • Gao SH, Huang K, Tu H., Adler A.S. (2013) Monoclonal antibody humanness score and its applications. BMC Biotechnol 13:55.
    • (2013) BMC Biotechnol , vol.13 , pp. 55
    • Gao, S.H.1    Huang, K.2    Tu, H.3    Adler, A.S.4
  • 47
    • 77649272592 scopus 로고    scopus 로고
    • The humanness of macaque antibody sequences
    • Thullier P, Huish O, Pelat T., Martin A.C. (2010) The humanness of macaque antibody sequences. J Mol Biol 396(5):1439-1450.
    • (2010) J Mol Biol , vol.396 , Issue.5 , pp. 1439-1450
    • Thullier, P.1    Huish, O.2    Pelat, T.3    Martin, A.C.4
  • 48
    • 34248170673 scopus 로고    scopus 로고
    • Analyzing the "degree of humanness" of antibody sequences
    • Abhinandan KR, Martin A.C. (2007) Analyzing the "degree of humanness" of antibody sequences. J Mol Biol 369(3):852-862.
    • (2007) J Mol Biol , vol.369 , Issue.3 , pp. 852-862
    • Abhinandan, K.R.1    Martin, A.C.2
  • 49
    • 84883856643 scopus 로고    scopus 로고
    • Developability studies before initiation of process development: Improving manufacturability of monoclonal antibodies
    • Yang X, et al (2013) Developability studies before initiation of process development: Improving manufacturability of monoclonal antibodies. MAbs 5(5):787-794.
    • (2013) MAbs , vol.5 , Issue.5 , pp. 787-794
    • Yang, X.1
  • 50
    • 84900864804 scopus 로고    scopus 로고
    • Modern therapeutic antibody drug discovery technologies
    • Strohl WR (2014) Modern therapeutic antibody drug discovery technologies. Curr Drug Discov Technol 11(1):1-2.
    • (2014) Curr Drug Discov Technol , vol.11 , Issue.1 , pp. 1-2
    • Strohl, W.R.1
  • 51
    • 70450081797 scopus 로고    scopus 로고
    • Review: To what extent are T cells tolerant to immunoglobulin variable regions?
    • Bogen B, Ruffini P. (2009) Review: To what extent are T cells tolerant to immunoglobulin variable regions? Scand J Immunol 70(6):526-530.
    • (2009) Scand J Immunol , vol.70 , Issue.6 , pp. 526-530
    • Bogen, B.1    Ruffini, P.2
  • 52
    • 84943659439 scopus 로고    scopus 로고
    • Poor correlation between T-cell activation assays and HLA-DR binding prediction algorithms in an immunogenic fragment of pseudomonas exotoxin A
    • Mazor R, Tai CH, Lee B, Pastan I. (2015) Poor correlation between T-cell activation assays and HLA-DR binding prediction algorithms in an immunogenic fragment of Pseudomonas exotoxin A. J Immunol Methods 425:10-20.
    • (2015) J Immunol Methods , vol.425 , pp. 10-20
    • Mazor, R.1    Tai, C.H.2    Lee, B.3    Pastan, I.4
  • 53
    • 0032555214 scopus 로고    scopus 로고
    • A phage display approach for rapid antibody humanization: Designed combinatorial V gene libraries
    • Rader C, Cheresh DA, Barbas C.F., 3rd (1998) A phage display approach for rapid antibody humanization: Designed combinatorial V gene libraries. Proc Natl Acad Sci USA 95(15):8910-8915.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.15 , pp. 8910-8915
    • Rader, C.1    Cheresh, D.A.2    Barbas, C.F.3
  • 54
    • 84930932414 scopus 로고    scopus 로고
    • Humanization of a phosphothreonine peptide-specific chicken antibody by combinatorial library optimization of the phosphoepitope-binding motif
    • Baek DS, Kim Y.S. (2015) Humanization of a phosphothreonine peptide-specific chicken antibody by combinatorial library optimization of the phosphoepitope-binding motif. Biochem Biophys Res Commun 463(3):414-420.
    • (2015) Biochem Biophys Res Commun , vol.463 , Issue.3 , pp. 414-420
    • Baek, D.S.1    Kim, Y.S.2
  • 55
    • 84860389579 scopus 로고    scopus 로고
    • High-throughput measurement, correlation analysis, and Machine-learning predictions for pH and thermal stabilities of pfizer-generated antibodies
    • King AC, et al (2011) High-throughput measurement, correlation analysis, and machine-learning predictions for pH and thermal stabilities of Pfizer-generated antibodies. Protein Sci 20(9):1546-1557.
    • (2011) Protein Sci , vol.20 , Issue.9 , pp. 1546-1557
    • King, A.C.1
  • 56
    • 0037227517 scopus 로고    scopus 로고
    • Biophysical properties of human antibody variable domains
    • Ewert S, Huber T, Honegger A., Plückthun A (2003) Biophysical properties of human antibody variable domains. J Mol Biol 325(3):531-553.
    • (2003) J Mol Biol , vol.325 , Issue.3 , pp. 531-553
    • Ewert, S.1    Huber, T.2    Honegger, A.3    Plückthun, A.4
  • 57
    • 0034635335 scopus 로고    scopus 로고
    • Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides
    • Knappik A, et al (2000) Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides. J Mol Biol 296(1):57-86.
    • (2000) J Mol Biol , vol.296 , Issue.1 , pp. 57-86
    • Knappik, A.1
  • 58
    • 84877583398 scopus 로고    scopus 로고
    • Comprehensive interrogation of a Minimalist synthetic CDR-H3 library and its ability to generate antibodies with therapeutic potential
    • Mahon CM, et al (2013) Comprehensive interrogation of a minimalist synthetic CDR-H3 library and its ability to generate antibodies with therapeutic potential. J Mol Biol 425(10):1712-1730.
    • (2013) J Mol Biol , vol.425 , Issue.10 , pp. 1712-1730
    • Mahon, C.M.1
  • 59
    • 80053303946 scopus 로고    scopus 로고
    • HuCAL PLATINUM, a synthetic fab library optimized for sequence diversity and superior performance in Mammalian expression systems
    • Prassler J, et al (2011) HuCAL PLATINUM, a synthetic Fab library optimized for sequence diversity and superior performance in mammalian expression systems. J Mol Biol 413(1):261-278.
    • (2011) J Mol Biol , vol.413 , Issue.1 , pp. 261-278
    • Prassler, J.1
  • 60
    • 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, 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(2):385-396.
    • (2010) J Mol Biol , vol.397 , Issue.2 , pp. 385-396
    • Shi, L.1
  • 61
    • 84877897559 scopus 로고    scopus 로고
    • A fully synthetic human fab antibody library based on fixed VH/ VL framework pairings with favorable biophysical properties
    • Tiller T, et al (2013) A fully synthetic human Fab antibody library based on fixed VH/ VL framework pairings with favorable biophysical properties. MAbs 5(3):445-470.
    • (2013) MAbs , vol.5 , Issue.3 , pp. 445-470
    • Tiller, T.1
  • 62
    • 77957355961 scopus 로고    scopus 로고
    • Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation
    • Mouquet H, et al (2010) Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation. Nature 467 (7315):591-595.
    • (2010) Nature , vol.467 , Issue.7315 , pp. 591-595
    • Mouquet, H.1
  • 63
    • 43749107283 scopus 로고    scopus 로고
    • Comparative protein structure modeling using modeller
    • Chapter 5:Unit 5 6
    • Eswar N, et al (2006) Comparative protein structure modeling using Modeller. Curr Protocols Bioinformatics Chapter 5:Unit 5 6.
    • (2006) Curr Protocols Bioinformatics
    • Eswar, N.1
  • 64
    • 0032210911 scopus 로고    scopus 로고
    • Prediction of well-conserved HIV-1 ligands using a matrix-based algorithm, EpiMatrix
    • Schafer JR, Jesdale BM, George J.A., Kouttab NM, De Groot AS (1998) Prediction of well-conserved HIV-1 ligands using a matrix-based algorithm, EpiMatrix. Vaccine 16(19):1880-1884.
    • (1998) Vaccine , vol.16 , Issue.19 , pp. 1880-1884
    • Schafer, J.R.1    Jesdale, B.M.2    George, J.A.3    Kouttab, N.M.4    De Groot, A.S.5
  • 65
    • 0032055915 scopus 로고    scopus 로고
    • Several common HLA-DR types share largely overlapping peptide binding repertoires
    • Southwood S, et al (1998) Several common HLA-DR types share largely overlapping peptide binding repertoires. J Immunol 160(7):3363-3373.
    • (1998) J Immunol , vol.160 , Issue.7 , pp. 3363-3373
    • Southwood, S.1
  • 66
    • 34249010944 scopus 로고    scopus 로고
    • Clinical validation of the "in silico" prediction of immunogenicity of a human recombinant therapeutic protein
    • Koren E, et al (2007) Clinical validation of the "in silico" prediction of immunogenicity of a human recombinant therapeutic protein. Clin Immunol 124(1):26-32.
    • (2007) Clin Immunol , vol.124 , Issue.1 , pp. 26-32
    • Koren, E.1


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