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Volumn 24, Issue 11, 2013, Pages 1870-1882

Fab-PEG-Fab as a potential antibody mimetic

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANTIBODIES; COVALENT BONDS; DISSOCIATION; SULFUR COMPOUNDS;

EID: 84888580381     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc400246z     Document Type: Article
Times cited : (44)

References (108)
  • 1
    • 0004257938 scopus 로고    scopus 로고
    • pp, Lippincott Williams and Wilkins
    • Paul, W. (2012) Fundamental Immunology, pp 140-142, Lippincott Williams and Wilkins.
    • (2012) Fundamental Immunology , pp. 140-142
    • Paul, W.1
  • 2
    • 0031844118 scopus 로고    scopus 로고
    • Comparison of the conformations of two intact monoclonal antibodies with hinges
    • Harris, L. J., Larson, S. B., Skaletsky, E., and Mcpherson, A. (1998) Comparison of the conformations of two intact monoclonal antibodies with hinges Immunol. Rev. 163, 35-43
    • (1998) Immunol. Rev. , vol.163 , pp. 35-43
    • Harris, L.J.1    Larson, S.B.2    Skaletsky, E.3    Mcpherson, A.4
  • 3
    • 83555173535 scopus 로고    scopus 로고
    • Disulfide scrambling in IgG2monoclonal antibodies: Insights from molecular dynamics simulations
    • Wang, X., Kumar, S., and Singh, S. (2011) Disulfide scrambling in IgG2monoclonal antibodies: Insights from molecular dynamics simulations Pharm. Res. 28, 3128-3143
    • (2011) Pharm. Res. , vol.28 , pp. 3128-3143
    • Wang, X.1    Kumar, S.2    Singh, S.3
  • 8
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger, P. and Hudson, P. J. (2005) Engineered antibody fragments and the rise of single domains Nat. Biotechnol. 23 (9) 1126-1136
    • (2005) Nat. Biotechnol. , vol.23 , Issue.9 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 9
    • 48549107351 scopus 로고    scopus 로고
    • When binding is enough: Nonactivating antibody formats
    • Labrijn, A. F., Aalberse, R. C., and Schuurman, J. (2008) When binding is enough: Nonactivating antibody formats Curr. Opin. Immunol. 20, 479-485
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 479-485
    • Labrijn, A.F.1    Aalberse, R.C.2    Schuurman, J.3
  • 10
    • 64349107630 scopus 로고    scopus 로고
    • Development trends for therapeutic antibody fragments
    • Nelson, A. L. and Reichert, J. M. (2009) Development trends for therapeutic antibody fragments Nat. Biotechnol. 27 (4) 1-7
    • (2009) Nat. Biotechnol. , vol.27 , Issue.4 , pp. 1-7
    • Nelson, A.L.1    Reichert, J.M.2
  • 11
    • 77953653252 scopus 로고    scopus 로고
    • Antibody fragments; Hope and hype
    • Nelson, A. L. (2010) Antibody fragments; Hope and hype mAbs 2 (1) 77-83
    • (2010) MAbs , vol.2 , Issue.1 , pp. 77-83
    • Nelson, A.L.1
  • 12
    • 79955656236 scopus 로고    scopus 로고
    • Fragmentation of monoclonal antibodies
    • Vlasak, J. and Ionescu, R. (2011) Fragmentation of monoclonal antibodies mAbs 3 (3) 253-263
    • (2011) MAbs , vol.3 , Issue.3 , pp. 253-263
    • Vlasak, J.1    Ionescu, R.2
  • 16
    • 33845938292 scopus 로고    scopus 로고
    • PEGylated proteins: Eevaluation of their safety in the absence of definitive metabolism studies
    • Webster, R., Didier, E., Harris, P., Siegel, N., Stadler, J., Tilbury, L., and Smith, D. (2007) PEGylated proteins:evaluation of their safety in the absence of definitive metabolism studies Drug Metab. Dispos. 35 (1) 9-16
    • (2007) Drug Metab. Dispos. , vol.35 , Issue.1 , pp. 9-16
    • Webster, R.1    Didier, E.2    Harris, P.3    Siegel, N.4    Stadler, J.5    Tilbury, L.6    Smith, D.7
  • 17
    • 75749146715 scopus 로고    scopus 로고
    • PEGylated interferons for the treatment of chronic hepatitis C: Pharmacological and clinical differences between PEGinterferon-2a and PEGinterferon-2b
    • Foster, G. R. (2010) PEGylated interferons for the treatment of chronic hepatitis C: Pharmacological and clinical differences between PEGinterferon-2a and PEGinterferon-2b Drugs 70 (2) 147-165
    • (2010) Drugs , vol.70 , Issue.2 , pp. 147-165
    • Foster, G.R.1
  • 20
    • 79958706138 scopus 로고    scopus 로고
    • Preclinical aspects of anti-VEGF agents for the treatment of wet AMD: Ranibizumab and bevacizumab
    • Meyer, C. H. and Holz, F. G. (2011) Preclinical aspects of anti-VEGF agents for the treatment of wet AMD: Ranibizumab and bevacizumab Eye 25 (6) 661-672
    • (2011) Eye , vol.25 , Issue.6 , pp. 661-672
    • Meyer, C.H.1    Holz, F.G.2
  • 21
    • 79960941984 scopus 로고    scopus 로고
    • Expression and distribution of immunoglobulin G and its receptors in an immune privileged site: The eye
    • Niu, N., Zhang, J., Sun, Y., Wang, S., Sun, Y., Korteweg, C., Gao, W., and Gu, J. (2010) Expression and distribution of immunoglobulin G and its receptors in an immune privileged site: The eye Cell. Mol. Life Sci. 68 (14) 2481-2492
    • (2010) Cell. Mol. Life Sci. , vol.68 , Issue.14 , pp. 2481-2492
    • Niu, N.1    Zhang, J.2    Sun, Y.3    Wang, S.4    Sun, Y.5    Korteweg, C.6    Gao, W.7    Gu, J.8
  • 24
    • 77649253359 scopus 로고    scopus 로고
    • FcRn receptor-mediated pharmacokinetics of therapeutic IgG in the eye
    • Kim, H., Robinson, S., and Csaky, K. (2009) FcRn receptor-mediated pharmacokinetics of therapeutic IgG in the eye Mol. Vis. 15, 2803-2812
    • (2009) Mol. Vis. , vol.15 , pp. 2803-2812
    • Kim, H.1    Robinson, S.2    Csaky, K.3
  • 26
    • 36549039554 scopus 로고    scopus 로고
    • Pharmacokinetics of intravitreal ranibizumab (Lucentis)
    • Bakri, S. J., Snyder, M., Reid, J., Pulido, J., Ezzat, M., and Singh, R. (2007) Pharmacokinetics of intravitreal ranibizumab (Lucentis) Ophthalmology 114 (12) 2179-2182
    • (2007) Ophthalmology , vol.114 , Issue.12 , pp. 2179-2182
    • Bakri, S.J.1    Snyder, M.2    Reid, J.3    Pulido, J.4    Ezzat, M.5    Singh, R.6
  • 27
    • 84875887676 scopus 로고    scopus 로고
    • Characterization of the long-term pharmacokinetics of bevacizumab following last dose in patients with resected stage II and III carcinoma of the colon
    • Li, J., Gupta, M., Jin, D., Xin, Y., Visich, J., and Allison, D. E. (2012) Characterization of the long-term pharmacokinetics of bevacizumab following last dose in patients with resected stage II and III carcinoma of the colon Cancer Chemother. Pharmacol. 71 (3) 575-580
    • (2012) Cancer Chemother. Pharmacol. , vol.71 , Issue.3 , pp. 575-580
    • Li, J.1    Gupta, M.2    Jin, D.3    Xin, Y.4    Visich, J.5    Allison, D.E.6
  • 28
    • 0035253739 scopus 로고    scopus 로고
    • Phase I safety and pharmacokinetic study of recombinant human anti-vascular endothelial growth factor in patients with advanced cancer
    • Gordon, M. S., Margolin, K., Talpaz, M., Sledge, G. W., Holmgren, E., Benjamin, R., Stalter, S., Shak, S., and Adelman, D. (2001) Phase I safety and pharmacokinetic study of recombinant human anti-vascular endothelial growth factor in patients with advanced cancer J. Clin. Oncol. 19 (3) 843-850
    • (2001) J. Clin. Oncol. , vol.19 , Issue.3 , pp. 843-850
    • Gordon, M.S.1    Margolin, K.2    Talpaz, M.3    Sledge, G.W.4    Holmgren, E.5    Benjamin, R.6    Stalter, S.7    Shak, S.8    Adelman, D.9
  • 29
    • 80053371459 scopus 로고    scopus 로고
    • Intraocular pharmacokinetics after a single intravitreal injection of 1.5 mg versus 3.0 mg of bevacizumab in humans
    • Meyer, C. H., Krohne, T. U., and Holz, F. G. (2011) Intraocular pharmacokinetics after a single intravitreal injection of 1.5 mg versus 3.0 mg of bevacizumab in humans Retina (Philadelphia, Pa) 31 (9) 1877-1884
    • (2011) Retina (Philadelphia, Pa) , vol.31 , Issue.9 , pp. 1877-1884
    • Meyer, C.H.1    Krohne, T.U.2    Holz, F.G.3
  • 30
    • 84866398752 scopus 로고    scopus 로고
    • Intraocular pharmacokinetics of ranibizumab following a single intravitreal injection in humans
    • Krohne, T. U., Liu, Z., Holz, F. G., and Meyer, C. H. (2012) Intraocular pharmacokinetics of ranibizumab following a single intravitreal injection in humans Am. J. Ophthal. 154 (4) 682-686.e2
    • (2012) Am. J. Ophthal. , vol.154 , Issue.4
    • Krohne, T.U.1    Liu, Z.2    Holz, F.G.3    Meyer, C.H.4
  • 31
    • 84875435647 scopus 로고    scopus 로고
    • Pharmacokinetics of ranibizumab in patients with neovascular age-related macular degeneration: A population approach
    • Xu, L., Lu, T., Tuomi, L., Jumbe, N., Lu, J., Eppler, S., Kuebler, P., Damico-Beyer, L. A., and Joshi, A. (2013) Pharmacokinetics of ranibizumab in patients with neovascular age-related macular degeneration: A population approach Invest. Ophthalmol. Vis. Sci. 54 (3) 1616-1624
    • (2013) Invest. Ophthalmol. Vis. Sci. , vol.54 , Issue.3 , pp. 1616-1624
    • Xu, L.1    Lu, T.2    Tuomi, L.3    Jumbe, N.4    Lu, J.5    Eppler, S.6    Kuebler, P.7    Damico-Beyer, L.A.8    Joshi, A.9
  • 33
    • 78650995184 scopus 로고    scopus 로고
    • A kit to prepare 111In-DTPA-trastuzumab (Herceptin) Fab fragments injection under GMP conditions for imaging or radioimmunoguided surgery of HER2-positive breast cancer
    • Scollard, D. A., Chan, C., Holloway, C. M. B., and Reilly, R. M. (2011) A kit to prepare 111In-DTPA-trastuzumab (Herceptin) Fab fragments injection under GMP conditions for imaging or radioimmunoguided surgery of HER2-positive breast cancer Nucl. Med. Biol. 38 (1) 129-136
    • (2011) Nucl. Med. Biol. , vol.38 , Issue.1 , pp. 129-136
    • Scollard, D.A.1    Chan, C.2    Holloway, C.M.B.3    Reilly, R.M.4
  • 34
    • 77953655013 scopus 로고    scopus 로고
    • New methods allowing the detection of protein aggregates, A case study on trastuzumab
    • Demeule, B., Palais, C., Machaidze, G., Gurny, R., and Arvinte, T. (2009) New methods allowing the detection of protein aggregates, A case study on trastuzumab mAbs 1 (2) 142-150
    • (2009) MAbs , vol.1 , Issue.2 , pp. 142-150
    • Demeule, B.1    Palais, C.2    Machaidze, G.3    Gurny, R.4    Arvinte, T.5
  • 35
    • 0026486724 scopus 로고
    • Human monoclonal Fab fragments derived from a combinatorial library bind to respiratory syncytial virus F glycoprotein and neutralizeinfectivity
    • Barbas, C. F., Crowe, J. E., Cababa, J. R. D., Suzanne, T. M. J., Zebedeei, L., Murphy, B. R., Chanock, R. M., and Burton, D. R. (1992) Human monoclonal Fab fragments derived from a combinatorial library bind to respiratory syncytial virus F glycoprotein and neutralizeinfectivity Proc. Natl. Acad. Sci. U.S.A. 89, 10164-10168
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10164-10168
    • Barbas, C.F.1    Crowe, J.E.2    Cababa, J.R.D.3    Suzanne, T.M.J.4    Zebedeei, L.5    Murphy, B.R.6    Chanock, R.M.7    Burton, D.R.8
  • 36
    • 84888604600 scopus 로고    scopus 로고
    • in (Carmen, A. Ed.) p, CRC Press, Taylor & Francis Group.
    • Minor, L. K. (2006) in Drug Discovery Series (Carmen, A., Ed.) p 423, CRC Press, Taylor & Francis Group.
    • (2006) Drug Discovery Series , pp. 423
    • Minor, L.K.1
  • 40
    • 0032701484 scopus 로고    scopus 로고
    • Improving biosensor analysis
    • Myszka, D. G. (1999) Improving biosensor analysis J. Mol. Recognit. 12, 279-284
    • (1999) J. Mol. Recognit. , vol.12 , pp. 279-284
    • Myszka, D.G.1
  • 41
    • 20044375603 scopus 로고    scopus 로고
    • Biological activity of bevacizumab, a humanized anti-VEGF antibody in vitro
    • Wang, Y., Fei, D., Vanderlaan, M., and Song, A. (2004) Biological activity of bevacizumab, a humanized anti-VEGF antibody in vitro Angiogenesis 7 (4) 335-345
    • (2004) Angiogenesis , vol.7 , Issue.4 , pp. 335-345
    • Wang, Y.1    Fei, D.2    Vanderlaan, M.3    Song, A.4
  • 42
    • 78650405941 scopus 로고    scopus 로고
    • In vitro study of thrombin on tubule formation and regulators of angiogenesis
    • Wang, B., Pearson, T., Manning, G., and Donnelly, R. (2010) In vitro study of thrombin on tubule formation and regulators of angiogenesis Clin. Appl. Thromb-Hem. 16 (6) 674-678
    • (2010) Clin. Appl. Thromb-Hem. , vol.16 , Issue.6 , pp. 674-678
    • Wang, B.1    Pearson, T.2    Manning, G.3    Donnelly, R.4
  • 43
    • 33646562554 scopus 로고    scopus 로고
    • Structure-function studies of two synthetic anti-vascular endothelial growth factor fabs and comparison with the Avastin Fab
    • Fuh, G., Wei-Ching, P. W., Mark, L., Chingwei, U., Moffat, V. L., and Wiesmann, C. (2006) Structure-function studies of two synthetic anti-vascular endothelial growth factor fabs and comparison with the Avastin Fab J. Biol. Chem. 281 (10) 6625-6631
    • (2006) J. Biol. Chem. , vol.281 , Issue.10 , pp. 6625-6631
    • Fuh, G.1    Wei-Ching, P.W.2    Mark, L.3    Chingwei, U.4    Moffat, V.L.5    Wiesmann, C.6
  • 44
    • 0010345821 scopus 로고
    • Kinetic and concentration analysis using BIA technology
    • Karlsson, R., Hakan Roos, R., Fagerstam, L., and Persson, B. (1994) Kinetic and concentration analysis using BIA technology Methods 6, 99-110
    • (1994) Methods , vol.6 , pp. 99-110
    • Karlsson, R.1    Hakan Roos, R.2    Fagerstam, L.3    Persson, B.4
  • 45
    • 0030795295 scopus 로고    scopus 로고
    • Reliable determination of binding affinity and kinetics using surface plasmon resonance biosensors
    • Schuck, P. (1997) Reliable determination of binding affinity and kinetics using surface plasmon resonance biosensors Curr. Opin. Biotechnol. 8, 498
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 498
    • Schuck, P.1
  • 46
    • 0031014046 scopus 로고    scopus 로고
    • Kinetic analysis of macro molecular interactions using surface plasmon resonance biosensors
    • Myszka, D. G. (1997) Kinetic analysis of macro molecular interactions using surface plasmon resonance biosensors Curr. Opin. Biotechnol. 8, 50-57
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 50-57
    • Myszka, D.G.1
  • 47
    • 0033527584 scopus 로고    scopus 로고
    • Selection and analysis of an optimized anti-VEGF antibody: Crystal structure of an affinity-matured Fab in complex with antigen
    • Chen, Y., Weismann, C., Fun, G., Li, B., Christinger, H. W., Mckay, P., M. De Vos, A., and Lowman, H. B. (1999) Selection and analysis of an optimized anti-VEGF antibody: Crystal structure of an affinity-matured Fab in complex with antigen J. Mol. Biol. 293, 865-881
    • (1999) J. Mol. Biol. , vol.293 , pp. 865-881
    • Chen, Y.1    Weismann, C.2    Fun, G.3    Li, B.4    Christinger, H.W.5    Mckay, P.6    De Vos, A.M.7    Lowman, H.B.8
  • 49
    • 0001303221 scopus 로고
    • Recombination of a mixture of univalent antibody fragments of different specificity
    • Nisonoff, A. and Rivers, M. M. (1961) Recombination of a mixture of univalent antibody fragments of different specificity Arch. Biochem. Biophys. 93, 460-462
    • (1961) Arch. Biochem. Biophys. , vol.93 , pp. 460-462
    • Nisonoff, A.1    Rivers, M.M.2
  • 51
    • 0021860882 scopus 로고
    • Preparation of bispecific antibodies by chemical recombinant of monoclonal immunoglobulin G1 fragments
    • Brennen, M. (1985) Preparation of bispecific antibodies by chemical recombinant of monoclonal immunoglobulin G1 fragments Science 229 (4708) 81-83
    • (1985) Science , vol.229 , Issue.4708 , pp. 81-83
    • Brennen, M.1
  • 53
    • 78649234620 scopus 로고    scopus 로고
    • Synthetic of N-terminally linked protein and peptide dimers by native chemical ligation
    • Xiao, J., B. S. Hamilton, B. S., and Tolbert, T. J. (2010) Synthetic of N-terminally linked protein and peptide dimers by native chemical ligation Bioconjugate Chem. 21, 1943-1947
    • (2010) Bioconjugate Chem. , vol.21 , pp. 1943-1947
    • Xiao, J.1    Hamilton, B.S.2    Tolbert, T.J.3
  • 54
    • 0037428948 scopus 로고    scopus 로고
    • Bispecific antibody conjugates in therapeutics
    • Cao, Y. and Lam, L. (2003) Bispecific antibody conjugates in therapeutics Adv. Drug Delivery Rev. 55 (2) 171-197
    • (2003) Adv. Drug Delivery Rev. , vol.55 , Issue.2 , pp. 171-197
    • Cao, Y.1    Lam, L.2
  • 56
    • 85027955048 scopus 로고    scopus 로고
    • Pharmacokinetic rationale for dosing every 2 weeks versus 4 weeks with intravitreal ranibizumab, bevacizumab, and aflibercept (vascular endothelial growth factor trap-eye)
    • Stewart, M. W., Rosenfeld, P. J., Penha, F. M., Wang, F., Yehoshua, Z., Bueno-Lopez, E., and Lopez, P. F. (2012) Pharmacokinetic rationale for dosing every 2 weeks versus 4 weeks with intravitreal ranibizumab, bevacizumab, and aflibercept (vascular endothelial growth factor trap-eye) Retina 32 (3) 434
    • (2012) Retina , vol.32 , Issue.3 , pp. 434
    • Stewart, M.W.1    Rosenfeld, P.J.2    Penha, F.M.3    Wang, F.4    Yehoshua, Z.5    Bueno-Lopez, E.6    Lopez, P.F.7
  • 57
    • 77949884124 scopus 로고    scopus 로고
    • Importance of neonatal FcR in regulating the serum half-life of therapeutic proteins containing the Fc domain of human IgG1: A comparative study of the affinity of monoclonal antibodies and Fc-fusion proteins to human neonatal FcR
    • Suzuki, T., Ishii-Watabe, A., Tada, M., Kobayashi, T., Kanayasu-Toyoda, T., Kawanishi, T., and Yamaguchi, T. (2010) Importance of neonatal FcR in regulating the serum half-life of therapeutic proteins containing the Fc domain of human IgG1: A comparative study of the affinity of monoclonal antibodies and Fc-fusion proteins to human neonatal FcR J. Immunol. 184 (4) 1968-76
    • (2010) J. Immunol. , vol.184 , Issue.4 , pp. 1968-1976
    • Suzuki, T.1    Ishii-Watabe, A.2    Tada, M.3    Kobayashi, T.4    Kanayasu-Toyoda, T.5    Kawanishi, T.6    Yamaguchi, T.7
  • 58
    • 62549154024 scopus 로고    scopus 로고
    • Abatacept, a novel CD80/86-CD28 T cell co-stimulation modulator, in the treatment of rheumatoid arthritis
    • Korhonen, R. and Moilanen, E. (2009) Abatacept, a novel CD80/86-CD28 T cell co-stimulation modulator, in the treatment of rheumatoid arthritis Basic Clin. Pharmacol. Toxicol. 104 (4) 276-84
    • (2009) Basic Clin. Pharmacol. Toxicol. , vol.104 , Issue.4 , pp. 276-284
    • Korhonen, R.1    Moilanen, E.2
  • 59
    • 79952822776 scopus 로고    scopus 로고
    • The development of romiplostim for patients with immune thrombocytopenia
    • Molineux, G. (2011) The development of romiplostim for patients with immune thrombocytopenia Ann. N.Y. Acad. Sci. 1222, 55-63
    • (2011) Ann. N.Y. Acad. Sci. , vol.1222 , pp. 55-63
    • Molineux, G.1
  • 60
    • 67649203468 scopus 로고    scopus 로고
    • Advances and challenges in developing cytokine fusion proteins as improved therapeutics
    • Chang, C.-H., Gupta, P., and Goldenberg, D. M. (2009) Advances and challenges in developing cytokine fusion proteins as improved therapeutics Expert Opin. Drug Discovery 4 (2) 181-194
    • (2009) Expert Opin. Drug Discovery , vol.4 , Issue.2 , pp. 181-194
    • Chang, C.-H.1    Gupta, P.2    Goldenberg, D.M.3
  • 61
    • 84857500984 scopus 로고    scopus 로고
    • Selective domain stabilization as a strategy to reduce fusion protein aggregation
    • Cordes, A. A., Platt, C. W., Carpenter, J. F., and Randolph, T. W. (2012) Selective domain stabilization as a strategy to reduce fusion protein aggregation J. Pharm. Sci. 101 (4) 1400-1409
    • (2012) J. Pharm. Sci. , vol.101 , Issue.4 , pp. 1400-1409
    • Cordes, A.A.1    Platt, C.W.2    Carpenter, J.F.3    Randolph, T.W.4
  • 62
    • 33144464467 scopus 로고    scopus 로고
    • Control of protein functional dynamics by peptide linkers
    • Wriggers, W., Chakravarty, S., and Jennings, P. A. (2005) Control of protein functional dynamics by peptide linkers Biopolymers 80 (6) 736-746
    • (2005) Biopolymers , vol.80 , Issue.6 , pp. 736-746
    • Wriggers, W.1    Chakravarty, S.2    Jennings, P.A.3
  • 63
    • 37549068535 scopus 로고    scopus 로고
    • Extended polypeptide linkers establish the spatial architecture of a pyruvate dehydrogenase multienzyme complex
    • Lengyel, J. S., Stott, K. M., Wu, X., Brooks, B. R., Balbo, A., Schuck, P., Perham, R. N., Subramaniam, S., and Milne, J. L. S. (2008) Extended polypeptide linkers establish the spatial architecture of a pyruvate dehydrogenase multienzyme complex Structure 16 (1) 93-103
    • (2008) Structure , vol.16 , Issue.1 , pp. 93-103
    • Lengyel, J.S.1    Stott, K.M.2    Wu, X.3    Brooks, B.R.4    Balbo, A.5    Schuck, P.6    Perham, R.N.7    Subramaniam, S.8    Milne, J.L.S.9
  • 64
    • 79960189344 scopus 로고    scopus 로고
    • Dynamic allostery: Linkers are not merely flexible
    • Ma, B., Tsai, C.-J., HalilogÌlu, T., and Nussinov, R. (2011) Dynamic allostery: Linkers are not merely flexible Structure 19 (7) 907-917
    • (2011) Structure , vol.19 , Issue.7 , pp. 907-917
    • Ma, B.1    Tsai, C.-J.2    Halilogìlu, T.3    Nussinov, R.4
  • 65
    • 0035184008 scopus 로고    scopus 로고
    • Stable linker peptides for a cellulose-binding domain-lipase fusion protein expressed in Pichia pastoris
    • Gustavsson, M., Lehtiö, J., Denman, S., Teeri, T. T., Hult, K., and Martinelle, M. (2001) Stable linker peptides for a cellulose-binding domain-lipase fusion protein expressed in Pichia pastoris Protein Eng. 14 (9) 711-715
    • (2001) Protein Eng. , vol.14 , Issue.9 , pp. 711-715
    • Gustavsson, M.1    Lehtiö, J.2    Denman, S.3    Teeri, T.T.4    Hult, K.5    Martinelle, M.6
  • 66
    • 0034788744 scopus 로고    scopus 로고
    • Design of the linkers which effectively separate domains of a bifunctional fusion protein
    • Arai, R., Ueda, H., Kitayama, A., Kamiya, N., and Nagamune, T. (2001) Design of the linkers which effectively separate domains of a bifunctional fusion protein Protein Eng. 14 (8) 529-532
    • (2001) Protein Eng. , vol.14 , Issue.8 , pp. 529-532
    • Arai, R.1    Ueda, H.2    Kitayama, A.3    Kamiya, N.4    Nagamune, T.5
  • 67
    • 4143137525 scopus 로고    scopus 로고
    • Effect of linker sequences between the antibody variable domains on the formation, stability and biological activity of a bispecific tandem diabody
    • Le Gall, F., Reusch, U., Little, M., and Kipriyanov, S. M. (2004) Effect of linker sequences between the antibody variable domains on the formation, stability and biological activity of a bispecific tandem diabody Protein Eng. Des. Sel. 17 (4) 357-366
    • (2004) Protein Eng. Des. Sel. , vol.17 , Issue.4 , pp. 357-366
    • Le Gall, F.1    Reusch, U.2    Little, M.3    Kipriyanov, S.M.4
  • 68
    • 33749850258 scopus 로고    scopus 로고
    • Effects of interlinker sequences on the biological properties of bispecific single-chain antibodies
    • Fang, M. (2003) Effects of interlinker sequences on the biological properties of bispecific single-chain antibodies Chin. Sci. Bull. 48 (21) 2277
    • (2003) Chin. Sci. Bull. , vol.48 , Issue.21 , pp. 2277
    • Fang, M.1
  • 69
    • 70350622968 scopus 로고    scopus 로고
    • Design and optimization of a linker for fusion protein construction
    • Zhang, J., Yun, J., Shang, Z., Zhang, X., and Pan, B. (2009) Design and optimization of a linker for fusion protein construction Prog. Nat. Sci. 19 (10) 1197-1200
    • (2009) Prog. Nat. Sci. , vol.19 , Issue.10 , pp. 1197-1200
    • Zhang, J.1    Yun, J.2    Shang, Z.3    Zhang, X.4    Pan, B.5
  • 70
    • 79953812851 scopus 로고    scopus 로고
    • Effects of receptor binding on plasma half-life of bifunctional transferrin fusion proteins
    • Chen, X., Lee, H. F., Zaro, J. L., and Shen, W. C. (2011) Effects of receptor binding on plasma half-life of bifunctional transferrin fusion proteins Mol. Pharmaceutics 8 (2) 457-465
    • (2011) Mol. Pharmaceutics , vol.8 , Issue.2 , pp. 457-465
    • Chen, X.1    Lee, H.F.2    Zaro, J.L.3    Shen, W.C.4
  • 71
    • 84863005606 scopus 로고    scopus 로고
    • Towards a universal disulphide stabilised single chain Fv format: Importance of interchain disulphide bond location and vL-vH orientation
    • Weatherill, E. E., Cain, K. L., Heywood, S. P., Compson, J. E., Heads, J. T., Adams, R., and Humphreys, D. P. (2012) Towards a universal disulphide stabilised single chain Fv format: Importance of interchain disulphide bond location and vL-vH orientation Protein Eng. Des. Sel. 25 (7) 321-329
    • (2012) Protein Eng. Des. Sel. , vol.25 , Issue.7 , pp. 321-329
    • Weatherill, E.E.1    Cain, K.L.2    Heywood, S.P.3    Compson, J.E.4    Heads, J.T.5    Adams, R.6    Humphreys, D.P.7
  • 74
    • 84861610591 scopus 로고    scopus 로고
    • Immunocytokines: A novel class of potent armed antibodies
    • Pasche, N. and Neri, D. (2012) Immunocytokines: A novel class of potent armed antibodies Drug Discovery Today 17 (11-12) 583-590
    • (2012) Drug Discovery Today , vol.17 , Issue.1112 , pp. 583-590
    • Pasche, N.1    Neri, D.2
  • 75
    • 84858257263 scopus 로고    scopus 로고
    • Dual targeting strategies with bispecific antibodies
    • Kontemann, R. (2012) Dual targeting strategies with bispecific antibodies mAbs 4 (2) 182-197
    • (2012) MAbs , vol.4 , Issue.2 , pp. 182-197
    • Kontemann, R.1
  • 76
    • 34248382009 scopus 로고    scopus 로고
    • Bispecific antibodies: Molecules that enable novel therapeutic strategies
    • Fischer, N. and Leger, O. (2007) Bispecific antibodies: Molecules that enable novel therapeutic strategies Pathobiology 74 (1) 3-14
    • (2007) Pathobiology , vol.74 , Issue.1 , pp. 3-14
    • Fischer, N.1    Leger, O.2
  • 78
    • 84867702136 scopus 로고    scopus 로고
    • Novel protein scaffolds as emerging therapeutic proteins: From discovery to clinical proof-of-concept
    • Wurch, T., Pierré, A., and Depil, S. (2012) Novel protein scaffolds as emerging therapeutic proteins: From discovery to clinical proof-of-concept Trends Biotechnol. 30 (11) 575-582
    • (2012) Trends Biotechnol. , vol.30 , Issue.11 , pp. 575-582
    • Wurch, T.1    Pierré, A.2    Depil, S.3
  • 79
    • 84863303532 scopus 로고    scopus 로고
    • Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements
    • Huang, C.-J., Lin, H., and Yang, X. (2012) Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements J. Ind. Microbiol. Biotechnol. 39 (3) 383-399
    • (2012) J. Ind. Microbiol. Biotechnol. , vol.39 , Issue.3 , pp. 383-399
    • Huang, C.-J.1    Lin, H.2    Yang, X.3
  • 80
    • 0032531947 scopus 로고    scopus 로고
    • Spanning binding sites on allosteric proteins with polymer-linked ligand dimers
    • Kramer, R. H. and Karpen, J. W. (1998) Spanning binding sites on allosteric proteins with polymer-linked ligand dimers Nature 395 (6703) 710-713
    • (1998) Nature , vol.395 , Issue.6703 , pp. 710-713
    • Kramer, R.H.1    Karpen, J.W.2
  • 81
    • 81555196349 scopus 로고    scopus 로고
    • Conformational analysis of bivalent estrogen receptor ligands: From intramolecular to intermolecular binding
    • Shan, M., Bujotzek, A., Abendroth, F., Wellner, A., Gust, R., Seitz, O., Weber, M., and Haag, R. (2011) Conformational analysis of bivalent estrogen receptor ligands: From intramolecular to intermolecular binding ChemBioChem 12 (17) 2587-2598
    • (2011) ChemBioChem , vol.12 , Issue.17 , pp. 2587-2598
    • Shan, M.1    Bujotzek, A.2    Abendroth, F.3    Wellner, A.4    Gust, R.5    Seitz, O.6    Weber, M.7    Haag, R.8
  • 83
    • 38349128433 scopus 로고    scopus 로고
    • Binding mechanisms of PEGylated ligands reveal multiple effects of the PEG scaffold
    • Das, R., Baird, E., Allen, S., Baird, B., Holowka, D., and Goldstein, B. (2008) Binding mechanisms of PEGylated ligands reveal multiple effects of the PEG scaffold Biochemistry 47 (3) 1017-1030
    • (2008) Biochemistry , vol.47 , Issue.3 , pp. 1017-1030
    • Das, R.1    Baird, E.2    Allen, S.3    Baird, B.4    Holowka, D.5    Goldstein, B.6
  • 85
    • 37249071981 scopus 로고    scopus 로고
    • Development of anti-MUC1 di-scFvs for molecular targeting of epithelial cancers, such as breast and prostate cancers
    • Albrecht, H., Denardo, G. L., and Denardo, S. J. (2007) Development of anti-MUC1 di-scFvs for molecular targeting of epithelial cancers, such as breast and prostate cancers Q. J. Nucl. Med. Mol. Imaging 51 (4) 304-313
    • (2007) Q. J. Nucl. Med. Mol. Imaging , vol.51 , Issue.4 , pp. 304-313
    • Albrecht, H.1    Denardo, G.L.2    Denardo, S.J.3
  • 86
    • 40249100759 scopus 로고    scopus 로고
    • End-functionalized polymers: Versatile building blocks for soft materials
    • Lo Verso, F. and Likos, C. N. (2008) End-functionalized polymers: Versatile building blocks for soft materials Polymer 49 (6) 1425-1434
    • (2008) Polymer , vol.49 , Issue.6 , pp. 1425-1434
    • Lo Verso, F.1    Likos, C.N.2
  • 87
    • 0029246884 scopus 로고
    • Associating polymers: Equilibrium and linear viscoelasticity
    • Semenov, A. N., Joanny, J. F., and Khokhlov, A. R. (1995) Associating polymers: Equilibrium and linear viscoelasticity Macromolecules 28 (4) 1066-1075
    • (1995) Macromolecules , vol.28 , Issue.4 , pp. 1066-1075
    • Semenov, A.N.1    Joanny, J.F.2    Khokhlov, A.R.3
  • 88
    • 77957918000 scopus 로고    scopus 로고
    • Modeling the adsorption behavior of linear end-functionalized poly(ethylene glycol) on an ionic substrate by a coarse-grained Monte Carlo approach
    • Elli, S., Eusebio, L., Gronchi, P., Ganazzoli, F., and Goisis, M. (2010) Modeling the adsorption behavior of linear end-functionalized poly(ethylene glycol) on an ionic substrate by a coarse-grained Monte Carlo approach Langmuir 26 (20) 15814-15823
    • (2010) Langmuir , vol.26 , Issue.20 , pp. 15814-15823
    • Elli, S.1    Eusebio, L.2    Gronchi, P.3    Ganazzoli, F.4    Goisis, M.5
  • 89
    • 9244221679 scopus 로고    scopus 로고
    • Prediction of the viscosity radius and the size exclusion chromatography behavior of PEGylated proteins
    • Fee, C. and Van Alstine, J. (2004) Prediction of the viscosity radius and the size exclusion chromatography behavior of PEGylated proteins Bioconjugate Chem. 15 (6) 1304-1313
    • (2004) Bioconjugate Chem. , vol.15 , Issue.6 , pp. 1304-1313
    • Fee, C.1    Van Alstine, J.2
  • 90
    • 49249103016 scopus 로고    scopus 로고
    • Effect of PEGylation on the solution conformation of antibody fragments
    • Lu, Y., Harding, S. E., Turner, A., Smith, B., and Athwal, D. S. (2008) Effect of PEGylation on the solution conformation of antibody fragments J. Pharm. Sci. 97 (6) 2062-2079
    • (2008) J. Pharm. Sci. , vol.97 , Issue.6 , pp. 2062-2079
    • Lu, Y.1    Harding, S.E.2    Turner, A.3    Smith, B.4    Athwal, D.S.5
  • 91
    • 46849122649 scopus 로고    scopus 로고
    • Exploring the energy landscape of antibody-antigen complexes: Protein dynamics, flexibility, and molecular recognition
    • Thielges, M. C., Zimmermann, J. R., Yu, W., Oda, M., and Romesberg, F. E. (2008) Exploring the energy landscape of antibody-antigen complexes: Protein dynamics, flexibility, and molecular recognition Biochemistry 47 (27) 7237-7247
    • (2008) Biochemistry , vol.47 , Issue.27 , pp. 7237-7247
    • Thielges, M.C.1    Zimmermann, J.R.2    Yu, W.3    Oda, M.4    Romesberg, F.E.5
  • 92
    • 27544496736 scopus 로고    scopus 로고
    • Protein PEGylation decreases observed target association rates via a dual blocking mechanism
    • Kubetzko, S., Sarkar, C. A., and Plückthun, A. (2005) Protein PEGylation decreases observed target association rates via a dual blocking mechanism Mol. Pharmacol. 68 (5) 1439-1454
    • (2005) Mol. Pharmacol. , vol.68 , Issue.5 , pp. 1439-1454
    • Kubetzko, S.1    Sarkar, C.A.2    Plückthun, A.3
  • 95
    • 77956309074 scopus 로고    scopus 로고
    • Long-lasting target binding and rebinding as mechanisms to prolong in vivo drug action
    • Vauquelin, G. and Charlton, S. J. (2010) Long-lasting target binding and rebinding as mechanisms to prolong in vivo drug action Br. J. Pharmacol. 161 (3) 488-508
    • (2010) Br. J. Pharmacol. , vol.161 , Issue.3 , pp. 488-508
    • Vauquelin, G.1    Charlton, S.J.2
  • 96
    • 77954544788 scopus 로고    scopus 로고
    • Thermodynamics of multivalent interactions: Influence of the linker
    • Kane, R. S. (2010) Thermodynamics of multivalent interactions: Influence of the linker Langmuir 26 (11) 8636-8640
    • (2010) Langmuir , vol.26 , Issue.11 , pp. 8636-8640
    • Kane, R.S.1
  • 97
    • 33846809157 scopus 로고    scopus 로고
    • Dependence of effective molarity on linker length for an intramolecular protein-ligand system
    • Krishnamurthy, V. M., Semetey, V., Bracher, P. J., Shen, N., and Whitesides, G. M. (2007) Dependence of effective molarity on linker length for an intramolecular protein-ligand system J. Am. Chem. Soc. 129 (5) 1312-1320
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.5 , pp. 1312-1320
    • Krishnamurthy, V.M.1    Semetey, V.2    Bracher, P.J.3    Shen, N.4    Whitesides, G.M.5
  • 98
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks, W. P. (1981) On the attribution and additivity of binding energies Proc. Natl. Acad. Sci. U.S.A. 78 (7) 4046-4050
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , Issue.7 , pp. 4046-4050
    • Jencks, W.P.1
  • 99
    • 84875459594 scopus 로고    scopus 로고
    • Exploring avidity: Understanding the potential gains in functional affinity and target residence time of bivalent and heterobivalent ligands
    • Vauquelin, G. and Charlton, S. J. (2013) Exploring avidity: Understanding the potential gains in functional affinity and target residence time of bivalent and heterobivalent ligands Br. J. Pharmacol. 168 (8) 1771-1785
    • (2013) Br. J. Pharmacol. , vol.168 , Issue.8 , pp. 1771-1785
    • Vauquelin, G.1    Charlton, S.J.2
  • 100
    • 80052462704 scopus 로고    scopus 로고
    • Conformational adaptation in drug-target interactions and residence time
    • Copeland, R. A. (2011) Conformational adaptation in drug-target interactions and residence time Future Med. Chem. 3 (12) 1491-1501
    • (2011) Future Med. Chem. , vol.3 , Issue.12 , pp. 1491-1501
    • Copeland, R.A.1
  • 101
    • 84877785836 scopus 로고    scopus 로고
    • A comprehensive analysis of the influence of drug binding kinetics on drug action at molecular and systems levels
    • Yin, N., Pei, J., and Lai, L. (2013) A comprehensive analysis of the influence of drug binding kinetics on drug action at molecular and systems levels Mol. BioSyst. 9 (6) 1381-1389
    • (2013) Mol. BioSyst. , vol.9 , Issue.6 , pp. 1381-1389
    • Yin, N.1    Pei, J.2    Lai, L.3
  • 103
    • 57049085220 scopus 로고    scopus 로고
    • Effects of linker length and flexibility on multivalent targeting
    • Shewmake, T. A., Solis, F. J., Gillies, R. J., and Caplan, M. R. (2008) Effects of linker length and flexibility on multivalent targeting Biomacromolecules 9 (11) 3057-3064
    • (2008) Biomacromolecules , vol.9 , Issue.11 , pp. 3057-3064
    • Shewmake, T.A.1    Solis, F.J.2    Gillies, R.J.3    Caplan, M.R.4
  • 104
    • 0037079187 scopus 로고    scopus 로고
    • Intramolecular complexation in aqueous solutions of an end-capped poly(ethylene glycol)
    • Cojocariu, G. and Natansohn, A. (2002) Intramolecular complexation in aqueous solutions of an end-capped poly(ethylene glycol) J. Phys. Chem. B 106 (45) 11737-11745
    • (2002) J. Phys. Chem. B , vol.106 , Issue.45 , pp. 11737-11745
    • Cojocariu, G.1    Natansohn, A.2
  • 105
    • 84857763275 scopus 로고    scopus 로고
    • Influence of spacer-receptor interactions on the stability of bivalent ligand-receptor complexes
    • Numata, J., Juneja, A., Diestler, D. J., and Knapp, E. W. (2012) Influence of spacer-receptor interactions on the stability of bivalent ligand-receptor complexes J. Phys. Chem. B 116 (8) 2595-2604
    • (2012) J. Phys. Chem. B , vol.116 , Issue.8 , pp. 2595-2604
    • Numata, J.1    Juneja, A.2    Diestler, D.J.3    Knapp, E.W.4
  • 107
    • 59349115572 scopus 로고    scopus 로고
    • No effect of covalently linked poly (ethylene glycol) chains on protein internal dynamics
    • Gonnelli, M. and Strambini, G. B. (2009) No effect of covalently linked poly (ethylene glycol) chains on protein internal dynamics BBA-Proteins and Proteomics 1794, 569-576
    • (2009) BBA-Proteins and Proteomics , vol.1794 , pp. 569-576
    • Gonnelli, M.1    Strambini, G.B.2
  • 108
    • 84864843664 scopus 로고    scopus 로고
    • Quantifying the rebinding effect in multivalent chemical ligand-receptor systems
    • Weber, M., Bujotzek, A., and Haag, R. (2012) Quantifying the rebinding effect in multivalent chemical ligand-receptor systems J. Chem. Phys. 137 (5) 054111
    • (2012) J. Chem. Phys. , vol.137 , Issue.5 , pp. 054111
    • Weber, M.1    Bujotzek, A.2    Haag, R.3


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