메뉴 건너뛰기




Volumn 4, Issue 3, 2015, Pages 197-224

Antibody conjugates: From heterogeneous populations to defined reagents

Author keywords

Antibody conjugates; Bioconjugation; Chemical conjugation; Enzymatic conjugation; Immunoglobulin; Non covalent antibody conjugates

Indexed keywords

ANTIBODY CONJUGATE; BRENTUXIMAB VEDOTIN; CYSTEINE; ENZYME; FORMYLGLYCINE GENERATING ENZYME; GEMTUZUMAB OZOGAMICIN; IBRITUMOMAB TIUXETAN; IODOACETAMIDE; LYSINE; MALEIMIDE; MONOCLONAL ANTIBODY; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; RADIOISOTOPE; SCAFFOLD PROTEIN; SELENOCYSTEINE; SORTASE; TRASTUZUMAB EMTANSINE; TYROSINE; UNCLASSIFIED DRUG;

EID: 85106466647     PISSN: 20734468     EISSN: None     Source Type: Journal    
DOI: 10.3390/antib4030197     Document Type: Review
Times cited : (97)

References (182)
  • 1
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Köhler, G.; Milstein, C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 1975, 256, 495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Köhler, G.1    Milstein, C.2
  • 3
    • 84921345093 scopus 로고    scopus 로고
    • Antibodies to watch in 2015
    • Reichert, J.M. Antibodies to watch in 2015. MAbs 2015, 7, 1-8.
    • (2015) MAbs , vol.7 , pp. 1-8
    • Reichert, J.M.1
  • 4
    • 84892621213 scopus 로고    scopus 로고
    • Antibody-drug conjugates: Present and future
    • Beck, A.; Reichert, J.M. Antibody-drug conjugates: present and future. MAbs 2014, 6, 15-17.
    • (2014) MAbs , vol.6 , pp. 15-17
    • Beck, A.1    Reichert, J.M.2
  • 5
    • 85042577043 scopus 로고    scopus 로고
    • Antibody-drug conjugates: A minireview. The synopsis of two approved medicines
    • Papachristos, A.; Pippa, N.; Demetzos, C.; Sivolapenko, G. Antibody-drug conjugates: A minireview. The synopsis of two approved medicines. Drug Deliv. 2015, 1-5.
    • (2015) Drug Deliv , pp. 1-5
    • Papachristos, A.1    Pippa, N.2    Demetzos, C.3    Sivolapenko, G.4
  • 8
    • 84871362496 scopus 로고    scopus 로고
    • Antibody-drug conjugates for the treatment of cancer
    • Flygare, J.; Pillow, T.; Aristoff, P. Antibody-drug conjugates for the treatment of cancer. Chem. Biol. Drug Des. 2013, 81, 113-121.
    • (2013) Chem. Biol. Drug Des , vol.81 , pp. 113-121
    • Flygare, J.1    Pillow, T.2    Aristoff, P.3
  • 9
    • 84892615120 scopus 로고    scopus 로고
    • Site-specific antibody drug conjugates for cancer therapy
    • Panowski, S.; Bhakta, S.; Raab, H.; Polakis, P.; Junutula, J.R. Site-specific antibody drug conjugates for cancer therapy. MAbs 2013, 6, 34-45.
    • (2013) MAbs , vol.6 , pp. 34-45
    • Panowski, S.1    Bhakta, S.2    Raab, H.3    Polakis, P.4    Junutula, J.R.5
  • 10
    • 81355139629 scopus 로고    scopus 로고
    • Choosing an effective protein bioconjugation strategy
    • Stephanopoulos, N.; Francis, M.B. Choosing an effective protein bioconjugation strategy. Nat. Chem. Biol. 2011, 7, 876-884.
    • (2011) Nat. Chem. Biol , vol.7 , pp. 876-884
    • Stephanopoulos, N.1    Francis, M.B.2
  • 14
    • 84892621003 scopus 로고    scopus 로고
    • Methods for site-specific drug conjugation to antibodies
    • Behrens, C.R.; Liu, B. Methods for site-specific drug conjugation to antibodies. mAbs 2013, 6, 46-53.
    • (2013) mAbs , vol.6 , pp. 46-53
    • Behrens, C.R.1    Liu, B.2
  • 16
    • 84923228905 scopus 로고    scopus 로고
    • Site-specific antibody-drug conjugates: The nexus of bioorthogonal chemistry, protein engineering, and drug development
    • Agarwal, P.; Bertozzi, C.R. Site-specific antibody-drug conjugates: The nexus of bioorthogonal chemistry, protein engineering, and drug development. Bioconjug. Chem. 2015, 26, 176-192.
    • (2015) Bioconjug. Chem , vol.26 , pp. 176-192
    • Agarwal, P.1    Bertozzi, C.R.2
  • 17
    • 84939263374 scopus 로고    scopus 로고
    • Current methods for the synthesis of homogeneous antibody-drug conjugates
    • Sochaj, A.M.; Swiderska, K.W.; Otlewski, J. Current methods for the synthesis of homogeneous antibody-drug conjugates. Biotechnol. Adv. 2015, doi: 10.1016/j.biotechadv.2015.05.001.
    • (2015) Biotechnol. Adv
    • Sochaj, A.M.1    Swiderska, K.W.2    Otlewski, J.3
  • 18
    • 84938679600 scopus 로고    scopus 로고
    • Advances in the development of site-specific antibody-drug conjugation
    • Zhou, Q.; Kim, J. Advances in the development of site-specific antibody-drug conjugation. Anticancer Agents Med. Chem. 2015, 15, 828-836.
    • (2015) Anticancer Agents Med. Chem , vol.15 , pp. 828-836
    • Zhou, Q.1    Kim, J.2
  • 19
    • 84939974152 scopus 로고    scopus 로고
    • Antibody drug conjugates: Design and selection of linker, payload and conjugation chemistry
    • McCombs, J.R.; Owen, S.C. Antibody drug conjugates: Design and selection of linker, payload and conjugation chemistry. AAPS J. 2015, 17, 339-351.
    • (2015) AAPS J , vol.17 , pp. 339-351
    • McCombs, J.R.1    Owen, S.C.2
  • 20
    • 0014890505 scopus 로고
    • Specific chemical modification of proteins
    • Glazer, A.N. Specific chemical modification of proteins. Annu. Rev. Biochem. 1970, 39, 101-130.
    • (1970) Annu. Rev. Biochem , vol.39 , pp. 101-130
    • Glazer, A.N.1
  • 21
    • 0020972604 scopus 로고
    • Preparation of antibody-linked cytotoxic agents
    • Ghose, T.I.; Blair, A.H.; Kulkarni, P.N. Preparation of antibody-linked cytotoxic agents. Methods Enzymol. 1983, 93, 280-333.
    • (1983) Methods Enzymol , vol.93 , pp. 280-333
    • Ghose, T.I.1    Blair, A.H.2    Kulkarni, P.N.3
  • 22
    • 85013795111 scopus 로고    scopus 로고
    • Academic Press: New York, NY, USA
    • Hermanson, G.T. Bioconjugate Techniques; Academic Press: New York, NY, USA, 2008; pp. 1041-1132.
    • (2008) Bioconjugate Techniques , pp. 1041-1132
    • Hermanson, G.T.1
  • 23
    • 44849088699 scopus 로고    scopus 로고
    • Peptide/protein-polymer conjugates: Synthetic strategies and design concepts
    • Gauthier, M.A.; Klok, H.-A. Peptide/protein-polymer conjugates: Synthetic strategies and design concepts. Chem. Commun. (Cambridge, U. K.) 2008, 21, 2591-2611.
    • (2008) Chem. Commun. (Cambridge, U. K.) , vol.21 , pp. 2591-2611
    • Gauthier, M.A.1    Klok, H.-A.2
  • 24
    • 51349122139 scopus 로고    scopus 로고
    • New methods for protein bioconjugation
    • Wiley-VCH Verlag GmbH: Weinheim, Germany
    • Francis, M.B. New methods for protein bioconjugation. In Chemical Biology; Wiley-VCH Verlag GmbH: Weinheim, Germany, 2008; pp. 593-634.
    • (2008) Chemical Biology , pp. 593-634
    • Francis, M.B.1
  • 25
    • 70349917806 scopus 로고    scopus 로고
    • Bioorthogonal chemistry: Fishing for selectivity in a sea of functionality
    • Sletten, E.M.; Bertozzi, C.R. Bioorthogonal chemistry: Fishing for selectivity in a sea of functionality. Angew. Chem. Int. Ed. Engl. 2009, 48, 6974-6998.
    • (2009) Angew. Chem. Int. Ed. Engl , vol.48 , pp. 6974-6998
    • Sletten, E.M.1    Bertozzi, C.R.2
  • 26
    • 0023823192 scopus 로고
    • Determination of the number of e-amino groups available for conjugation of effector molecules to monoclonal antibodies
    • Mueller, B.M.; Wrasidlo, W.A.; Reisfeld, R.A. Determination of the number of e-amino groups available for conjugation of effector molecules to monoclonal antibodies. Hybridoma 1988, 7, 453-456.
    • (1988) Hybridoma , vol.7 , pp. 453-456
    • Mueller, B.M.1    Wrasidlo, W.A.2    Reisfeld, R.A.3
  • 28
    • 77956637683 scopus 로고    scopus 로고
    • Physicochemical stability of the antibody-drug conjugate Trastuzumab-DM1: Changes due to modification and conjugation processes
    • Wakankar, A.A.; Feeney, M.B.; Rivera, J.; Chen, Y.; Kim, M.; Sharma, V.K.; Wang, Y.J. Physicochemical stability of the antibody-drug conjugate Trastuzumab-DM1: Changes due to modification and conjugation processes. Bioconjug. Chem. 2010, 21, 1588-1595.
    • (2010) Bioconjug. Chem , vol.21 , pp. 1588-1595
    • Wakankar, A.A.1    Feeney, M.B.2    Rivera, J.3    Chen, Y.4    Kim, M.5    Sharma, V.K.6    Wang, Y.J.7
  • 29
    • 0030805884 scopus 로고    scopus 로고
    • Calicheamicin derivatives conjugated to monoclonal antibodies: Determination of loading values and distributions by infrared and UV matrix-assisted laser desorption/ionization mass spectrometry and electrospray ionization mass spectrometry
    • Siegel, M.M.; Tabei, K.; Kunz, A.; Hollander, I.J.; Hamann, R.R.; Bell, D.H.; Berkenkamp, S.; Hillenkamp, F. Calicheamicin derivatives conjugated to monoclonal antibodies: determination of loading values and distributions by infrared and UV matrix-assisted laser desorption/ionization mass spectrometry and electrospray ionization mass spectrometry. Anal. Chem. 1997, 69, 2716-2726.
    • (1997) Anal. Chem , vol.69 , pp. 2716-2726
    • Siegel, M.M.1    Tabei, K.2    Kunz, A.3    Hollander, I.J.4    Hamann, R.R.5    Bell, D.H.6    Berkenkamp, S.7    Hillenkamp, F.8
  • 30
    • 0033893747 scopus 로고    scopus 로고
    • Region-selective labeling of antibodies as determined by electrospray ionization-mass spectrometry (ESI-MS)
    • Adamczyk, M.; Gebler, J.; Shreder, K.; Wu, J. Region-selective labeling of antibodies as determined by electrospray ionization-mass spectrometry (ESI-MS). Bioconjug. Chem. 2000, 11, 557-563.
    • (2000) Bioconjug. Chem , vol.11 , pp. 557-563
    • Adamczyk, M.1    Gebler, J.2    Shreder, K.3    Wu, J.4
  • 31
    • 24344456964 scopus 로고    scopus 로고
    • Structural characterization of the maytansinoid-monoclonal antibody immunoconjugate, huN901-DM1, by mass spectrometry
    • Wang, L.; Amphlett, G.; Blattler, W.A.; Lambert, J.M.; Zhang, W. Structural characterization of the maytansinoid-monoclonal antibody immunoconjugate, huN901-DM1, by mass spectrometry. Protein Sci. 2005, 14, 2436-2446.
    • (2005) Protein Sci , vol.14 , pp. 2436-2446
    • Wang, L.1    Amphlett, G.2    Blattler, W.A.3    Lambert, J.M.4    Zhang, W.5
  • 33
    • 84938751906 scopus 로고    scopus 로고
    • Conjugates of small molecule drugs with antibodies and other proteins
    • Feng, Y.; Zhu, Z.; Chen, W.; Prabakaran, P.; Lin, K.; Dimitrov, D. Conjugates of small molecule drugs with antibodies and other proteins. Biomedicines 2014, 2, 1-13.
    • (2014) Biomedicines , vol.2 , pp. 1-13
    • Feng, Y.1    Zhu, Z.2    Chen, W.3    Prabakaran, P.4    Lin, K.5    Dimitrov, D.6
  • 34
    • 84896925253 scopus 로고    scopus 로고
    • Emerging classes of armed antibody therapeutics against cancer
    • Hess, C.; Venetz, D.; Neri, D. Emerging classes of armed antibody therapeutics against cancer. Med. Chem. Commun. 2014, 5, 408-431.
    • (2014) Med. Chem. Commun , vol.5 , pp. 408-431
    • Hess, C.1    Venetz, D.2    Neri, D.3
  • 35
    • 47749144375 scopus 로고    scopus 로고
    • Chances and pitfalls of chemical cross-linking with amine-reactive N-hydroxysuccinimide esters
    • Kalkhof, S.; Sinz, A. Chances and pitfalls of chemical cross-linking with amine-reactive N-hydroxysuccinimide esters. Anal. Bioanal. Chem. 2008, 392, 305-312.
    • (2008) Anal. Bioanal. Chem , vol.392 , pp. 305-312
    • Kalkhof, S.1    Sinz, A.2
  • 36
    • 66249146087 scopus 로고    scopus 로고
    • Chemical cross-linking with NHS esters: A systematic study on amino acid reactivities
    • Madler, S.; Bich, C.; Touboul, D.; Zenobi, R. Chemical cross-linking with NHS esters: A systematic study on amino acid reactivities. J. Mass Spectrom. 2009, 44, 694-706.
    • (2009) J. Mass Spectrom , vol.44 , pp. 694-706
    • Madler, S.1    Bich, C.2    Touboul, D.3    Zenobi, R.4
  • 37
    • 79955606896 scopus 로고    scopus 로고
    • Identification of amino acid residues responsible for the release of free drug from an antibody-drug conjugate utilizing lysine-succinimidyl ester chemistry
    • Chih, H.W.; Gikanga, B.; Yang, Y.; Zhang, B. Identification of amino acid residues responsible for the release of free drug from an antibody-drug conjugate utilizing lysine-succinimidyl ester chemistry. J. Pharm. Sci. 2011, 100, 2518-2525.
    • (2011) J. Pharm. Sci , vol.100 , pp. 2518-2525
    • Chih, H.W.1    Gikanga, B.2    Yang, Y.3    Zhang, B.4
  • 38
    • 0018721964 scopus 로고
    • The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain
    • Goto, Y.; Hamaguchi, K. The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain. J. Biochem. 1979, 86, 1433-1441.
    • (1979) J. Biochem , vol.86 , pp. 1433-1441
    • Goto, Y.1    Hamaguchi, K.2
  • 39
    • 0031575401 scopus 로고    scopus 로고
    • A natural antibody missing a cysteine in VH: Consequences for thermodynamic stability and folding
    • Proba, K.; Honegger, A.; Pluckthun, A. A natural antibody missing a cysteine in VH: consequences for thermodynamic stability and folding. J. Mol. Biol. 1997, 265, 161-172.
    • (1997) J. Mol. Biol , vol.265 , pp. 161-172
    • Proba, K.1    Honegger, A.2    Pluckthun, A.3
  • 42
    • 77953603827 scopus 로고    scopus 로고
    • Ranking the susceptibility of disulfide bonds in human IgG1 antibodies by reduction, differential alkylation, and LC-MS analysis
    • Liu, H.; Chumsae, C.; Gaza-Bulseco, G.; Hurkmans, K.; Radziejewski, C.H. Ranking the susceptibility of disulfide bonds in human IgG1 antibodies by reduction, differential alkylation, and LC-MS analysis. Anal. Chem. 2010, 82, 5219-5226.
    • (2010) Anal. Chem , vol.82 , pp. 5219-5226
    • Liu, H.1    Chumsae, C.2    Gaza-Bulseco, G.3    Hurkmans, K.4    Radziejewski, C.H.5
  • 46
    • 84922713475 scopus 로고    scopus 로고
    • Cysteine-selective reactions for antibody conjugation
    • Cal, P.M.; Bernardes, G.J.; Gois, P.M. Cysteine-selective reactions for antibody conjugation. Angew. Chem. Int. Ed. Engl. 2014, 53, 10585-10587.
    • (2014) Angew. Chem. Int. Ed. Engl , vol.53 , pp. 10585-10587
    • Cal, P.M.1    Bernardes, G.J.2    Gois, P.M.3
  • 47
    • 84906345897 scopus 로고    scopus 로고
    • Improving the serum stability of sitespecific antibody conjugates with sulfone linkers
    • Patterson, J.T.; Asano, S.; Li, X.; Rader, C.; Barbas, C.F. Improving the serum stability of sitespecific antibody conjugates with sulfone linkers. Bioconjug. Chem. 2014, 25, 1402-1407.
    • (2014) Bioconjug. Chem , vol.25 , pp. 1402-1407
    • Patterson, J.T.1    Asano, S.2    Li, X.3    Rader, C.4    Barbas, C.F.5
  • 49
    • 84930652377 scopus 로고    scopus 로고
    • In vitro and In vivo evaluation of cysteine rebridged trastuzumab-MMAE antibody drug conjugates with defined drug-to-antibody ratios
    • Bryant, P.; Pabst, M.; Badescu, G.; Bird, M.; McDowell, W.; Jamieson, E.; Swierkosz, J.; Jurlewicz, K.; Tommasi, R.; Henseleit, K.; et al. In vitro and In vivo evaluation of cysteine rebridged trastuzumab-MMAE antibody drug conjugates with defined drug-to-antibody ratios. Mol. Pharm. 2015, 12, 1872-1879.
    • (2015) Mol. Pharm , vol.12 , pp. 1872-1879
    • Bryant, P.1    Pabst, M.2    Badescu, G.3    Bird, M.4    McDowell, W.5    Jamieson, E.6    Swierkosz, J.7    Jurlewicz, K.8    Tommasi, R.9    Henseleit, K.10
  • 52
    • 84926284885 scopus 로고    scopus 로고
    • A plug-andplay approach to antibody-based therapeutics via a chemoselective dual click strategy
    • Maruani, A.; Smith, M.E.; Miranda, E.; Chester, K.A.; Chudasama, V.; Caddick, S. A plug-andplay approach to antibody-based therapeutics via a chemoselective dual click strategy. Nat. Commun. 2015, 6, 6645.
    • (2015) Nat. Commun , vol.6 , pp. 6645
    • Maruani, A.1    Smith, M.E.2    Miranda, E.3    Chester, K.A.4    Chudasama, V.5    Caddick, S.6
  • 56
    • 84934438721 scopus 로고    scopus 로고
    • Engineering THIOMABs for site-specific conjugation of thiolreactive linkers
    • Ducry, L., Ed.; Humana Press: New York, NJ, USA
    • Bhakta, S.; Raab, H.; Junutula, J. Engineering THIOMABs for site-specific conjugation of thiolreactive linkers. In Antibody-Drug Conjugates; Ducry, L., Ed.; Humana Press: New York, NJ, USA, 2013; Volume 1045, pp. 189-203.
    • (2013) Antibody-Drug Conjugates , vol.1045 , pp. 189-203
    • Bhakta, S.1    Raab, H.2    Junutula, J.3
  • 60
    • 0027529320 scopus 로고
    • A genetically engineered human IgG with limited flexibility fully initiates cytolysis via complement
    • Shopes, B. A genetically engineered human IgG with limited flexibility fully initiates cytolysis via complement. Mol. Immunol. 1993, 30, 603-609.
    • (1993) Mol. Immunol , vol.30 , pp. 603-609
    • Shopes, B.1
  • 61
    • 80054828086 scopus 로고    scopus 로고
    • Tunable degradation of maleimide-thiol adducts in reducing environments
    • Baldwin, A.D.; Kiick, K.L. Tunable degradation of maleimide-thiol adducts in reducing environments. Bioconjug. Chem. 2011, 22, 1946-1953.
    • (2011) Bioconjug. Chem , vol.22 , pp. 1946-1953
    • Baldwin, A.D.1    Kiick, K.L.2
  • 64
    • 72449121780 scopus 로고    scopus 로고
    • Molecularly defined antibody conjugation through a selenocysteine interface
    • Hofer, T.; Skeffington, L.R.; Chapman, C.M.; Rader, C. Molecularly defined antibody conjugation through a selenocysteine interface. Biochemistry 2009, 48, 12047-12057.
    • (2009) Biochemistry , vol.48 , pp. 12047-12057
    • Hofer, T.1    Skeffington, L.R.2    Chapman, C.M.3    Rader, C.4
  • 65
    • 50449091735 scopus 로고    scopus 로고
    • An engineered selenocysteine defines a unique class of antibody derivatives
    • Hofer, T.; Thomas, J.D.; Burke, T.R., Jr.; Rader, C. An engineered selenocysteine defines a unique class of antibody derivatives. Proc. Natl. Acad. Sci. USA 2008, 105, 12451-12456.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 12451-12456
    • Hofer, T.1    Thomas, J.D.2    Burke, T.R.3    Rader, C.4
  • 66
    • 84891626541 scopus 로고    scopus 로고
    • Antibody conjugation via one and two C-terminal selenocysteines
    • Li, X.; Yang, J.; Rader, C. Antibody conjugation via one and two C-terminal selenocysteines. Methods (San Diego, Calif.) 2014, 65, 133-138.
    • (2014) Methods (San Diego, Calif.) , vol.65 , pp. 133-138
    • Li, X.1    Yang, J.2    Rader, C.3
  • 67
    • 76149123221 scopus 로고    scopus 로고
    • 3rd. Tyrosine bioconjugation through aqueous ene-type reactions: A click-like reaction for tyrosine
    • Ban, H.; Gavrilyuk, J.; Barbas, C.F., 3rd. Tyrosine bioconjugation through aqueous ene-type reactions: a click-like reaction for tyrosine. J. Am. Chem. Soc. 2010, 132, 1523-1525.
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 1523-1525
    • Ban, H.1    Gavrilyuk, J.2    Barbas, C.F.3
  • 68
    • 84876470762 scopus 로고    scopus 로고
    • Facile and stabile linkages through tyrosine: Bioconjugation strategies with the tyrosine-click reaction
    • Ban, H.; Nagano, M.; Gavrilyuk, J.; Hakamata, W.; Inokuma, T.; Barbas, C. Facile and stabile linkages through tyrosine: Bioconjugation strategies with the tyrosine-click reaction. Bioconjug. Chem. 2013, 24, 520-532.
    • (2013) Bioconjug. Chem , vol.24 , pp. 520-532
    • Ban, H.1    Nagano, M.2    Gavrilyuk, J.3    Hakamata, W.4    Inokuma, T.5    Barbas, C.6
  • 69
    • 84871307240 scopus 로고    scopus 로고
    • Formylbenzene diazonium hexafluorophosphate reagent for tyrosine-selective modification of proteins and the introduction of a bioorthogonal aldehyde
    • Gavrilyuk, J.; Ban, H.; Nagano, M.; Hakamata, W.; Barbas, C. Formylbenzene diazonium hexafluorophosphate reagent for tyrosine-selective modification of proteins and the introduction of a bioorthogonal aldehyde. Bioconjug. Chem. 2012, 23, 2321-2328.
    • (2012) Bioconjug. Chem , vol.23 , pp. 2321-2328
    • Gavrilyuk, J.1    Ban, H.2    Nagano, M.3    Hakamata, W.4    Barbas, C.5
  • 71
    • 84906724230 scopus 로고    scopus 로고
    • Unnatural amino acids in novel antibody conjugates
    • Hallam, T.J.; Smider, V.V. Unnatural amino acids in novel antibody conjugates. Future Med. Chem. 2014, 6, 1309-1324.
    • (2014) Future Med. Chem , vol.6 , pp. 1309-1324
    • Hallam, T.J.1    Smider, V.V.2
  • 72
    • 62649104324 scopus 로고    scopus 로고
    • Expanding the genetic code for biological studies
    • Wang, Q.; Parrish, A.R.; Wang, L. Expanding the genetic code for biological studies. Chem. Biol. 2009, 16, 323-336.
    • (2009) Chem. Biol , vol.16 , pp. 323-336
    • Wang, Q.1    Parrish, A.R.2    Wang, L.3
  • 73
    • 84878842686 scopus 로고    scopus 로고
    • Protein conjugation with genetically encoded unnatural amino acids
    • Kim, C.H.; Axup, J.Y.; Schultz, P.G. Protein conjugation with genetically encoded unnatural amino acids. Curr. Opin. Chem. Biol. 2013, 17, 412-419.
    • (2013) Curr. Opin. Chem. Biol , vol.17 , pp. 412-419
    • Kim, C.H.1    Axup, J.Y.2    Schultz, P.G.3
  • 76
    • 0014688965 scopus 로고
    • Conformational studies of immunoglobulin G and its subunits by the methods of hydrogen-deuterium exchange and infrared spectroscopy
    • Abaturov, L.V.; Nezlin, R.S.; Vengerova, T.I.; Varshavsky, J.M. Conformational studies of immunoglobulin G and its subunits by the methods of hydrogen-deuterium exchange and infrared spectroscopy. Biochim. Biophys. Acta 1969, 194, 386-396.
    • (1969) Biochim. Biophys. Acta , vol.194 , pp. 386-396
    • Abaturov, L.V.1    Nezlin, R.S.2    Vengerova, T.I.3    Varshavsky, J.M.4
  • 77
    • 0026332693 scopus 로고
    • Temperature and pH dependence of immunoglobulin G conformation
    • Calmettes, P.; Cser, L.; Rajnavolgyi, E. Temperature and pH dependence of immunoglobulin G conformation. Arch. Biochem. Biophys. 1991, 291, 277-283.
    • (1991) Arch. Biochem. Biophys , vol.291 , pp. 277-283
    • Calmettes, P.1    Cser, L.2    Rajnavolgyi, E.3
  • 78
    • 33847059215 scopus 로고    scopus 로고
    • Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies
    • Ejima, D.; Tsumoto, K.; Fukada, H.; Yumioka, R.; Nagase, K.; Arakawa, T.; Philo, J.S. Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies. Proteins 2007, 66, 954-962.
    • (2007) Proteins , vol.66 , pp. 954-962
    • Ejima, D.1    Tsumoto, K.2    Fukada, H.3    Yumioka, R.4    Nagase, K.5    Arakawa, T.6    Philo, J.S.7
  • 79
    • 84863249248 scopus 로고    scopus 로고
    • Aglycosylated antibodies and antibody fragments produced in a scalable in vitro transcription-translation system
    • Yin, G.; Garces, E.D.; Yang, J.; Zhang, J.; Tran, C.; Steiner, A.R.; Roos, C.; Bajad, S.; Hudak, S.; Penta, K.; et al. Aglycosylated antibodies and antibody fragments produced in a scalable in vitro transcription-translation system. MAbs 2012, 4, 217-225.
    • (2012) MAbs , vol.4 , pp. 217-225
    • Yin, G.1    Garces, E.D.2    Yang, J.3    Zhang, J.4    Tran, C.5    Steiner, A.R.6    Roos, C.7    Bajad, S.8    Hudak, S.9    Penta, K.10
  • 80
    • 84857440637 scopus 로고    scopus 로고
    • High-yield cell-free protein synthesis for site-specific incorporation of unnatural amino acids at two sites
    • Ozawa, K.; Loscha, K.V.; Kuppan, K.V.; Loh, C.T.; Dixon, N.E.; Otting, G. High-yield cell-free protein synthesis for site-specific incorporation of unnatural amino acids at two sites. Biochem. Biophys. Res. Commun. 2012, 418, 652-656.
    • (2012) Biochem. Biophys. Res. Commun , vol.418 , pp. 652-656
    • Ozawa, K.1    Loscha, K.V.2    Kuppan, K.V.3    Loh, C.T.4    Dixon, N.E.5    Otting, G.6
  • 81
    • 84894033400 scopus 로고    scopus 로고
    • Synthesis of 2.3 mg/ml of protein with an all Escherichia coli cell-free transcription-translation system
    • Caschera, F.; Noireaux, V. Synthesis of 2.3 mg/ml of protein with an all Escherichia coli cell-free transcription-translation system. Biochimie 2014, 99, 162-168.
    • (2014) Biochimie , vol.99 , pp. 162-168
    • Caschera, F.1    Noireaux, V.2
  • 82
    • 84987619011 scopus 로고    scopus 로고
    • Non-standard amino acid incorporation into proteins using Escherichia coli cell-free protein synthesis
    • Hong, S.H.; Kwon, Y.-C.C.; Jewett, M.C. Non-standard amino acid incorporation into proteins using Escherichia coli cell-free protein synthesis. Front. Chem. 2014, 2, 34.
    • (2014) Front. Chem , vol.2 , pp. 34
    • Hong, S.H.1    Kwon, Y.-C.C.2    Jewett, M.C.3
  • 84
    • 0021752522 scopus 로고
    • A novel procedure for labeling immunoglobulins by conjugation to oligosaccharide moieties
    • O'Shannessy, D.J.; Dobersen, M.J.; Quarles, R.H. A novel procedure for labeling immunoglobulins by conjugation to oligosaccharide moieties. Immunol. Lett. 1984, 8, 273-277.
    • (1984) Immunol. Lett , vol.8 , pp. 273-277
    • O'Shannessy, D.J.1    Dobersen, M.J.2    Quarles, R.H.3
  • 85
    • 0024439981 scopus 로고
    • Synthesis of methotrexate-antibody conjugates by regiospecific coupling and assessment of drug and antitumor activities
    • Kralovec, J.; Spencer, G.; Blair, A.H.; Mammen, M.; Singh, M.; Ghose, T. Synthesis of methotrexate-antibody conjugates by regiospecific coupling and assessment of drug and antitumor activities. J. Med. Chem. 1989, 32, 2426-2431.
    • (1989) J. Med. Chem , vol.32 , pp. 2426-2431
    • Kralovec, J.1    Spencer, G.2    Blair, A.H.3    Mammen, M.4    Singh, M.5    Ghose, T.6
  • 87
    • 0025318641 scopus 로고
    • Antitumor activity of L/1C2-4-desacetylvinblastine-3-carboxhydrazide immunoconjugate in xenografts
    • Johnson, D.A.; Baker, A.L.; Laguzza, B.C.; Fix, D.V.; Gutowski, M.C. Antitumor activity of L/1C2-4-desacetylvinblastine-3-carboxhydrazide immunoconjugate in xenografts. Cancer Res. 1990, 50, 1790-1794.
    • (1990) Cancer Res , vol.50 , pp. 1790-1794
    • Johnson, D.A.1    Baker, A.L.2    Laguzza, B.C.3    Fix, D.V.4    Gutowski, M.C.5
  • 88
    • 84862557056 scopus 로고    scopus 로고
    • Fucose-specific conjugation of hydrazide derivatives to a vascular-targeting monoclonal antibody in IgG format
    • Zuberbühler, K.; Casi, G.; Bernardes, G.J.; Neri, D. Fucose-specific conjugation of hydrazide derivatives to a vascular-targeting monoclonal antibody in IgG format. Chem. Commun. (Camb.) 2012, 48, 7100-7102.
    • (2012) Chem. Commun. (Camb.) , vol.48 , pp. 7100-7102
    • Zuberbühler, K.1    Casi, G.2    Bernardes, G.J.3    Neri, D.4
  • 89
    • 0027301165 scopus 로고
    • A new method of technetium-99m labeling of monoclonal antibodies through sugar residues. A study with TAG-72 specific CC-49 antibody
    • Ranadive, G.N.; Rosenzweig, H.S.; Epperly, M.W.; Seskey, T.; Bloomer, W.D. A new method of technetium-99m labeling of monoclonal antibodies through sugar residues. A study with TAG-72 specific CC-49 antibody. Nucl. Med. Biol. 1993, 20, 719-726.
    • (1993) Nucl. Med. Biol , vol.20 , pp. 719-726
    • Ranadive, G.N.1    Rosenzweig, H.S.2    Epperly, M.W.3    Seskey, T.4    Bloomer, W.D.5
  • 91
    • 0028500134 scopus 로고
    • Fc site-specific labeling of immunoglobulins with calf intestinal alkaline phosphatase
    • Husain, M.; Bieniarz, C. Fc site-specific labeling of immunoglobulins with calf intestinal alkaline phosphatase. Bioconjug. Chem. 1994, 5, 482-490.
    • (1994) Bioconjug. Chem , vol.5 , pp. 482-490
    • Husain, M.1    Bieniarz, C.2
  • 92
    • 4244025108 scopus 로고    scopus 로고
    • Synthesis and characterization of positively charged tPA as a prodrug using heparin/protamine-based drug delivery system
    • Liang, J.F.; Li, Y.T.; Connell, M.E.; Yang, V.C. Synthesis and characterization of positively charged tPA as a prodrug using heparin/protamine-based drug delivery system. AAPS PharmSci 2000, 2, E7.
    • (2000) AAPS PharmSci , vol.2
    • Liang, J.F.1    Li, Y.T.2    Connell, M.E.3    Yang, V.C.4
  • 93
    • 0035858295 scopus 로고    scopus 로고
    • ATTEMPTS: A heparin/protamine-based prodrug approach for delivery of thrombolytic drugs
    • Liang, J.F.; Park, Y.J.; Song, H.; Li, Y.T.; Yang, V.C. ATTEMPTS: a heparin/protamine-based prodrug approach for delivery of thrombolytic drugs. J. Control. Release 2001, 72, 145-156.
    • (2001) J. Control. Release , vol.72 , pp. 145-156
    • Liang, J.F.1    Park, Y.J.2    Song, H.3    Li, Y.T.4    Yang, V.C.5
  • 94
    • 0037428958 scopus 로고    scopus 로고
    • ATTEMPTS: A heparin/protamine-based triggered release system for the delivery of enzyme drugs without associated side-effects
    • Park, Y.-J.; Liang, J.-F.; Song, H.; Li, Y.T.; Naik, S.; Yang, V.C. ATTEMPTS: A heparin/protamine-based triggered release system for the delivery of enzyme drugs without associated side-effects. Adv. Drug Deliv. Rev. 2003, 55, 251-265.
    • (2003) Adv. Drug Deliv. Rev , vol.55 , pp. 251-265
    • Park, Y.-J.1    Liang, J.-F.2    Song, H.3    Li, Y.T.4    Naik, S.5    Yang, V.C.6
  • 95
    • 84860914656 scopus 로고    scopus 로고
    • Galactosylation variations in marketed therapeutic antibodies
    • Raju, T.S.; Jordan, R.E. Galactosylation variations in marketed therapeutic antibodies. MAbs 2012, 4, 385-391.
    • (2012) MAbs , vol.4 , pp. 385-391
    • Raju, T.S.1    Jordan, R.E.2
  • 97
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • Jefferis, R. Glycosylation of recombinant antibody therapeutics. Biotechnol. Prog. 2005, 21, 11-16.
    • (2005) Biotechnol. Prog , vol.21 , pp. 11-16
    • Jefferis, R.1
  • 99
    • 0028855916 scopus 로고
    • Studies on the rate and control of antibody oxidation by periodate
    • Wolfe, C.A.; Hage, D.S. Studies on the rate and control of antibody oxidation by periodate. Anal. Biochem. 1995, 231, 123-130.
    • (1995) Anal. Biochem , vol.231 , pp. 123-130
    • Wolfe, C.A.1    Hage, D.S.2
  • 100
    • 0031282160 scopus 로고    scopus 로고
    • Development of a kinetic model to describe the effective rate of antibody oxidation by periodate
    • Hage, D.S.; Wolfe, C.A.; Oates, M.R. Development of a kinetic model to describe the effective rate of antibody oxidation by periodate. Bioconjug. Chem. 1997, 8, 914-920.
    • (1997) Bioconjug. Chem , vol.8 , pp. 914-920
    • Hage, D.S.1    Wolfe, C.A.2    Oates, M.R.3
  • 101
    • 0025345823 scopus 로고
    • Enzymic oxidation of monoclonal antibodies by soluble and immobilized bifunctional enzyme complexes
    • Solomon, B.; Koppel, R.; Schwartz, F.; Fleminger, G. Enzymic oxidation of monoclonal antibodies by soluble and immobilized bifunctional enzyme complexes. J. Chromatogr. A 1990, 510, 321-329.
    • (1990) J. Chromatogr. A , vol.510 , pp. 321-329
    • Solomon, B.1    Koppel, R.2    Schwartz, F.3    Fleminger, G.4
  • 103
    • 84903715027 scopus 로고    scopus 로고
    • Preparation of well-defined antibody-drug conjugates through glycan remodeling and strain-promoted azide-alkyne cycloadditions
    • Li, X.; Fang, T.; Boons, G.J. Preparation of well-defined antibody-drug conjugates through glycan remodeling and strain-promoted azide-alkyne cycloadditions. Angew. Chem. Int. Ed. Engl. 2014, 53, 7179-7182.
    • (2014) Angew. Chem. Int. Ed. Engl , vol.53 , pp. 7179-7182
    • Li, X.1    Fang, T.2    Boons, G.J.3
  • 105
    • 67649206319 scopus 로고    scopus 로고
    • Site specific conjugation of fluoroprobes to the remodeled Fc N-glycans of monoclonal antibodies using mutant glycosyltransferases: Application for cell surface antigen detection
    • Boeggeman, E.; Ramakrishnan, B.; Pasek, M.; Manzoni, M.; Puri, A.; Loomis, K.H.; Waybright, T.J.; Qasba, P.K. Site specific conjugation of fluoroprobes to the remodeled Fc N-glycans of monoclonal antibodies using mutant glycosyltransferases: Application for cell surface antigen detection. Bioconjug. Chem. 2009, 20, 1228-1236.
    • (2009) Bioconjug. Chem , vol.20 , pp. 1228-1236
    • Boeggeman, E.1    Ramakrishnan, B.2    Pasek, M.3    Manzoni, M.4    Puri, A.5    Loomis, K.H.6    Waybright, T.J.7    Qasba, P.K.8
  • 106
    • 84879364396 scopus 로고    scopus 로고
    • An enzymemediated methodology for the site-specific radiolabeling of antibodies based on catalyst-free click chemistry
    • Zeglis, B.M.; Davis, C.B.; Aggeler, R.; Kang, H.-C.; Chen, A.; Agnew, B.; Lewis, J.S. An enzymemediated methodology for the site-specific radiolabeling of antibodies based on catalyst-free click chemistry. Bioconjug. Chem. 2013, 42, 1057-1067.
    • (2013) Bioconjug. Chem , vol.42 , pp. 1057-1067
    • Zeglis, B.M.1    Davis, C.B.2    Aggeler, R.3    Kang, H.-C.4    Chen, A.5    Agnew, B.6    Lewis, J.S.7
  • 107
    • 84918536144 scopus 로고    scopus 로고
    • Chemoenzymatic strategy for the synthesis of site-specifically labeled immunoconjugates for multimodal PET and optical imaging
    • Zeglis, B.M.; Davis, C.B.; Abdel-Atti, D.; Carlin, S.D.; Chen, A.; Aggeler, R.; Agnew, B.J.; Lewis, J.S. Chemoenzymatic strategy for the synthesis of site-specifically labeled immunoconjugates for multimodal PET and optical imaging. Bioconjug. Chem. 2014, 25, 2123-2128.
    • (2014) Bioconjug. Chem , vol.25 , pp. 2123-2128
    • Zeglis, B.M.1    Davis, C.B.2    Abdel-Atti, D.3    Carlin, S.D.4    Chen, A.5    Aggeler, R.6    Agnew, B.J.7    Lewis, J.S.8
  • 109
    • 84945366854 scopus 로고    scopus 로고
    • Chemoenzymatic conjugation of toxic payloads to the globally conserved N-glycan of native mAbs provides homogeneous and highly efficacious antibody-drug conjugates
    • van Geel, R.; Wijdeven, M.A.; Heesbeen, R.; Verkade, J.M.; Wasiel, A.A.; van Berkel, S.S.; van Delft, F.L. Chemoenzymatic conjugation of toxic payloads to the globally conserved N-glycan of native mAbs provides homogeneous and highly efficacious antibody-drug conjugates. Bioconjug. Chem. 2015, doi: 10.1021/acs.bioconjchem.5b00224.
    • (2015) Bioconjug. Chem
    • van Geel, R.1    Wijdeven, M.A.2    Heesbeen, R.3    Verkade, J.M.4    Wasiel, A.A.5    van Berkel, S.S.6    van Delft, F.L.7
  • 111
    • 84918825382 scopus 로고    scopus 로고
    • IgG subclasses and allotypes: From structure to effector functions
    • Vidarsson, G.; Dekkers, G.; Rispens, T. IgG subclasses and allotypes: From structure to effector functions. Front. Immunol. 2014, 5, 520.
    • (2014) Front. Immunol , vol.5 , pp. 520
    • Vidarsson, G.1    Dekkers, G.2    Rispens, T.3
  • 112
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold, J.N.; Wormald, M.R.; Sim, R.B.; Rudd, P.M.; Dwek, R.A. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 2007, 25, 21-50.
    • (2007) Annu. Rev. Immunol , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 113
    • 84910647104 scopus 로고    scopus 로고
    • Immunoglobulin G (IgG) Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes
    • Bondt, A.; Rombouts, Y.; Selman, M.H.; Hensbergen, P.J.; Reiding, K.R.; Hazes, J.M.; Dolhain, R.J.; Wuhrer, M. Immunoglobulin G (IgG) Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes. Mol. Cell. Proteomics 2014, 13, 3029-3039.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 3029-3039
    • Bondt, A.1    Rombouts, Y.2    Selman, M.H.3    Hensbergen, P.J.4    Reiding, K.R.5    Hazes, J.M.6    Dolhain, R.J.7    Wuhrer, M.8
  • 114
    • 34248587082 scopus 로고    scopus 로고
    • Regioselective labeling of antibodies through N-terminal transamination
    • Scheck, R.A.; Francis, M.B. Regioselective labeling of antibodies through N-terminal transamination. ACS Chem. Biol. 2007, 2, 247-251.
    • (2007) ACS Chem. Biol , vol.2 , pp. 247-251
    • Scheck, R.A.1    Francis, M.B.2
  • 117
    • 78649810925 scopus 로고    scopus 로고
    • Chemoenzymatic methods for site-specific protein modification
    • Rabuka, D. Chemoenzymatic methods for site-specific protein modification. Curr. Opin. Chem. Biol. 2010, 14, 790-796.
    • (2010) Curr. Opin. Chem. Biol , vol.14 , pp. 790-796
    • Rabuka, D.1
  • 118
    • 84883183094 scopus 로고    scopus 로고
    • Enzymatic labeling of proteins: Techniques and approaches
    • Rashidian, M.; Dozier, J.; Distefano, M. Enzymatic labeling of proteins: techniques and approaches. Bioconjug. Chem. 2013, 24, 1277-1294.
    • (2013) Bioconjug. Chem , vol.24 , pp. 1277-1294
    • Rashidian, M.1    Dozier, J.2    Distefano, M.3
  • 119
    • 34249076359 scopus 로고    scopus 로고
    • Introducing genetically encoded aldehydes into proteins
    • Carrico, I.S.; Carlson, B.L.; Bertozzi, C.R. Introducing genetically encoded aldehydes into proteins. Nat. Chem. Biol. 2007, 3, 321-322.
    • (2007) Nat. Chem. Biol , vol.3 , pp. 321-322
    • Carrico, I.S.1    Carlson, B.L.2    Bertozzi, C.R.3
  • 120
    • 62549121136 scopus 로고    scopus 로고
    • Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag
    • Wu, P.; Shui, W.; Carlson, B.L.; Hu, N.; Rabuka, D.; Lee, J.; Bertozzi, C.R. Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag. Proc. Natl. Acad. Sci. USA 2009, 106, 3000-3005.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3000-3005
    • Wu, P.1    Shui, W.2    Carlson, B.L.3    Hu, N.4    Rabuka, D.5    Lee, J.6    Bertozzi, C.R.7
  • 121
    • 84861034877 scopus 로고    scopus 로고
    • Site-specific chemical protein conjugation using genetically encoded aldehyde tags
    • Rabuka, D.; Rush, J.; deHart, G.; Wu, P.; Bertozzi, C. Site-specific chemical protein conjugation using genetically encoded aldehyde tags. Nat. Protoc. 2012, 7, 1052-1119.
    • (2012) Nat. Protoc , vol.7 , pp. 1052-1119
    • Rabuka, D.1    Rush, J.2    deHart, G.3    Wu, P.4    Bertozzi, C.5
  • 122
  • 124
    • 33947664974 scopus 로고    scopus 로고
    • Sortase A as a novel molecular "stapler" for sequence-specific protein conjugation
    • Parthasarathy, R.; Subramanian, S.; Boder, E.T. Sortase A as a novel molecular "stapler" for sequence-specific protein conjugation. Bioconjug. Chem. 2007, 18, 469-476.
    • (2007) Bioconjug. Chem , vol.18 , pp. 469-476
    • Parthasarathy, R.1    Subramanian, S.2    Boder, E.T.3
  • 126
    • 84903708926 scopus 로고    scopus 로고
    • Sortagging: A robust and efficient chemoenzymatic ligation strategy
    • Ritzefeld, M. Sortagging: A robust and efficient chemoenzymatic ligation strategy. Chemistry 2014, 20, 8516-8529.
    • (2014) Chemistry , vol.20 , pp. 8516-8529
    • Ritzefeld, M.1
  • 128
    • 84872871265 scopus 로고    scopus 로고
    • Sortasemediated modification of aDEC205 affords optimization of antigen presentation and immunization against a set of viral epitopes
    • Swee, L.K.; Guimaraes, C.P.; Sehrawat, S.; Spooner, E.; Barrasa, M.I.; Ploegh, H.L. Sortasemediated modification of aDEC205 affords optimization of antigen presentation and immunization against a set of viral epitopes. Proc. Natl. Acad. Sci. USA 2013, 110, 1428-1433.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 1428-1433
    • Swee, L.K.1    Guimaraes, C.P.2    Sehrawat, S.3    Spooner, E.4    Barrasa, M.I.5    Ploegh, H.L.6
  • 130
    • 84922706942 scopus 로고    scopus 로고
    • A noncanonical function of sortase enables sitespecific conjugation of small molecules to lysine residues in proteins
    • Bellucci, J.J.; Bhattacharyya, J.; Chilkoti, A. A noncanonical function of sortase enables sitespecific conjugation of small molecules to lysine residues in proteins. Angew. Chem. Int. Ed. Engl. 2014, 54, 441-445.
    • (2014) Angew. Chem. Int. Ed. Engl , vol.54 , pp. 441-445
    • Bellucci, J.J.1    Bhattacharyya, J.2    Chilkoti, A.3
  • 132
    • 51249102955 scopus 로고    scopus 로고
    • Novel applications for microbial transglutaminase beyond food processing
    • Zhu, Y.; Tramper, J. Novel applications for microbial transglutaminase beyond food processing. Trends Biotechnol. 2008, 26, 559-565.
    • (2008) Trends Biotechnol , vol.26 , pp. 559-565
    • Zhu, Y.1    Tramper, J.2
  • 133
    • 84901052647 scopus 로고    scopus 로고
    • Versatility of microbial transglutaminase
    • Strop, P. Versatility of microbial transglutaminase. Bioconjug. Chem. 2014, 25, 855-862.
    • (2014) Bioconjug. Chem , vol.25 , pp. 855-862
    • Strop, P.1
  • 134
    • 0034705643 scopus 로고    scopus 로고
    • Use of microbial transglutaminase for the enzymatic biotinylation of antibodies
    • Josten, A.; Haalck, L.; Spener, F.; Meusel, M. Use of microbial transglutaminase for the enzymatic biotinylation of antibodies. J. Immunol. Methods 2000, 240, 47-54.
    • (2000) J. Immunol. Methods , vol.240 , pp. 47-54
    • Josten, A.1    Haalck, L.2    Spener, F.3    Meusel, M.4
  • 135
    • 38949104404 scopus 로고    scopus 로고
    • Modification of different IgG1 antibodies via glutamine and lysine using bacterial and human tissue transglutaminase
    • Mindt, T.L.; Jungi, V.; Wyss, S.; Friedli, A.; Pla, G.; Novak-Hofer, I.; Grünberg, J.; Schibli, R. Modification of different IgG1 antibodies via glutamine and lysine using bacterial and human tissue transglutaminase. Bioconjug. Chem. 2008, 19, 271-278.
    • (2008) Bioconjug. Chem , vol.19 , pp. 271-278
    • Mindt, T.L.1    Jungi, V.2    Wyss, S.3    Friedli, A.4    Pla, G.5    Novak-Hofer, I.6    Grünberg, J.7    Schibli, R.8
  • 138
  • 142
    • 0013992053 scopus 로고
    • Protein A from S. Aureus
    • Forsgren, A.; Sjöquist, J. Protein A from S. Aureus. J. Immunol. 1966, 97, 822-827.
    • (1966) J. Immunol , vol.97 , pp. 822-827
    • Forsgren, A.1    Sjöquist, J.2
  • 143
    • 0020011459 scopus 로고
    • Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by Streptococci and Pneumonococci
    • Frank, J.D., Henry, G.K., Eds.; Academic Press: New York, NJ, USA
    • Iangone, J.J. Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by Streptococci and Pneumonococci. In Advances in Immunology; Frank, J.D., Henry, G.K., Eds.; Academic Press: New York, NJ, USA, 1982; Volume 32, pp. 157-252.
    • (1982) Advances in Immunology , vol.32 , pp. 157-252
    • Iangone, J.J.1
  • 144
    • 57749173811 scopus 로고    scopus 로고
    • Specific protein delivery to target cells by antibody-displaying bionanocapsules
    • Kurata, N.; Shishido, T.; Muraoka, M.; Tanaka, T.; Ogino, C.; Fukuda, H.; Kondo, A. Specific protein delivery to target cells by antibody-displaying bionanocapsules. J. Biochem. 2008, 144, 701-707.
    • (2008) J. Biochem , vol.144 , pp. 701-707
    • Kurata, N.1    Shishido, T.2    Muraoka, M.3    Tanaka, T.4    Ogino, C.5    Fukuda, H.6    Kondo, A.7
  • 145
    • 80053093214 scopus 로고    scopus 로고
    • Fluorophorelabeled nanocapsules displaying IgG Fc-binding domains for the simultaneous detection of multiple antigens
    • Iijima, M.; Matsuzaki, T.; Yoshimoto, N.; Niimi, T.; Tanizawa, K.; Kuroda, S.I. Fluorophorelabeled nanocapsules displaying IgG Fc-binding domains for the simultaneous detection of multiple antigens. Biomaterials 2011, 32, 9011-9031.
    • (2011) Biomaterials , vol.32 , pp. 9011-9031
    • Iijima, M.1    Matsuzaki, T.2    Yoshimoto, N.3    Niimi, T.4    Tanizawa, K.5    Kuroda, S.I.6
  • 146
    • 78650307772 scopus 로고    scopus 로고
    • Nanocapsules incorporating IgG Fc-binding domain derived from Staphylococcus aureus protein A for displaying IgGs on immunosensor chips
    • Iijima, M.; Kadoya, H.; Hatahira, S.; Hiramatsu, S.; Jung, G.; Martin, A.; Quinn, J.; Jung, J.; Jeong, S.-Y.; Choi, E.; et al. Nanocapsules incorporating IgG Fc-binding domain derived from Staphylococcus aureus protein A for displaying IgGs on immunosensor chips. Biomaterials 2011, 32, 1455-1519.
    • (2011) Biomaterials , vol.32 , pp. 1455-1519
    • Iijima, M.1    Kadoya, H.2    Hatahira, S.3    Hiramatsu, S.4    Jung, G.5    Martin, A.6    Quinn, J.7    Jung, J.8    Jeong, S.-Y.9    Choi, E.10
  • 147
    • 84869200028 scopus 로고    scopus 로고
    • Nano-visualization of orientedimmobilized IgGs on immunosensors by high-speed atomic force microscopy
    • Iijima, M.; Somiya, M.; Yoshimoto, N.; Niimi, T.; Kuroda, S.I. Nano-visualization of orientedimmobilized IgGs on immunosensors by high-speed atomic force microscopy. Sci. Rep. 2012, 2, 790.
    • (2012) Sci. Rep , vol.2 , pp. 790
    • Iijima, M.1    Somiya, M.2    Yoshimoto, N.3    Niimi, T.4    Kuroda, S.I.5
  • 149
    • 33947310214 scopus 로고    scopus 로고
    • Antibody internalization studied using a novel IgG binding toxin fusion
    • Mazor, Y.; Barnea, I.; Keydar, I.; Benhar, I. Antibody internalization studied using a novel IgG binding toxin fusion. J. Immunol. Methods 2007, 321, 41-59.
    • (2007) J. Immunol. Methods , vol.321 , pp. 41-59
    • Mazor, Y.1    Barnea, I.2    Keydar, I.3    Benhar, I.4
  • 150
    • 34648828858 scopus 로고    scopus 로고
    • chFRP5-ZZ-PE38, a large IgG-toxin immunoconjugate outperforms the corresponding smaller FRP5(Fv)-ETA immunotoxin in eradicating ErbB2- expressing tumor xenografts
    • Mazor, Y.; Noy, R.; Wels, W.S.; Benhar, I. chFRP5-ZZ-PE38, a large IgG-toxin immunoconjugate outperforms the corresponding smaller FRP5(Fv)-ETA immunotoxin in eradicating ErbB2- expressing tumor xenografts. Cancer Lett. 2007, 257, 124-135.
    • (2007) Cancer Lett , vol.257 , pp. 124-135
    • Mazor, Y.1    Noy, R.2    Wels, W.S.3    Benhar, I.4
  • 151
    • 79952294364 scopus 로고    scopus 로고
    • An immunoconjugate of anti-CD24 and Pseudomonas exotoxin selectively kills human colorectal tumors in mice
    • Shapira, S.; Shapira, A.; Starr, A.; Kazanov, D.; Kraus, S.; Benhar, I.; Arber, N. An immunoconjugate of anti-CD24 and Pseudomonas exotoxin selectively kills human colorectal tumors in mice. Gastroenterology 2011, 140, 935-946.
    • (2011) Gastroenterology , vol.140 , pp. 935-946
    • Shapira, S.1    Shapira, A.2    Starr, A.3    Kazanov, D.4    Kraus, S.5    Benhar, I.6    Arber, N.7
  • 152
    • 84880699883 scopus 로고    scopus 로고
    • Targeting EGFR-positive cancer cells with cetuximab-ZZ-PE38: Results of in vitro and in vivo studies
    • Barnea, I.; Ben-Yosef, R.; Karaush, V.; Benhar, I.; Vexler, A. Targeting EGFR-positive cancer cells with cetuximab-ZZ-PE38: Results of in vitro and in vivo studies. Head Neck 2013, 35, 1171-1177.
    • (2013) Head Neck , vol.35 , pp. 1171-1177
    • Barnea, I.1    Ben-Yosef, R.2    Karaush, V.3    Benhar, I.4    Vexler, A.5
  • 153
    • 78650363751 scopus 로고    scopus 로고
    • Enzyme-mediated site-specific antibody-protein modification using a ZZ domain as a linker
    • Sakamoto, T.; Sawamoto, S.; Tanaka, T.; Fukuda, H.; Kondo, A. Enzyme-mediated site-specific antibody-protein modification using a ZZ domain as a linker. Bioconjug. Chem. 2010, 21, 2227-2233.
    • (2010) Bioconjug. Chem , vol.21 , pp. 2227-2233
    • Sakamoto, T.1    Sawamoto, S.2    Tanaka, T.3    Fukuda, H.4    Kondo, A.5
  • 154
    • 84555195107 scopus 로고    scopus 로고
    • Covalent immunoglobulin labeling through a photoactivable synthetic Z domain
    • Konrad, A.; Karlstrom, A.E.; Hober, S. Covalent immunoglobulin labeling through a photoactivable synthetic Z domain. Bioconjug. Chem. 2011, 22, 2395-2403.
    • (2011) Bioconjug. Chem , vol.22 , pp. 2395-2403
    • Konrad, A.1    Karlstrom, A.E.2    Hober, S.3
  • 155
    • 84873724699 scopus 로고    scopus 로고
    • Tailor-making a protein a-derived domain for efficient site-specific photocoupling to Fc of mouse IgG1
    • Yu, F.; Järver, P.; Nygren, P.-Å.Å. Tailor-making a protein a-derived domain for efficient site-specific photocoupling to Fc of mouse IgG1. PLoS One 2013, 8, e56597:11.
    • (2013) PLoS One , vol.8 , pp. 11
    • Yu, F.1    Järver, P.2    Nygren, P.-Å.Å.3
  • 156
    • 84896512087 scopus 로고    scopus 로고
    • Site-specific photoconjugation of antibodies using chemically synthesized IgG-binding domains
    • Perols, A.; Karlström, A.E. Site-specific photoconjugation of antibodies using chemically synthesized IgG-binding domains. Bioconjug. Chem. 2014, 25, 481-488.
    • (2014) Bioconjug. Chem , vol.25 , pp. 481-488
    • Perols, A.1    Karlström, A.E.2
  • 157
    • 84927519653 scopus 로고    scopus 로고
    • Optimization of photoactive protein Z for fast and efficient site-specific conjugation of native IgG
    • Hui, J.Z.; Tsourkas, A. Optimization of photoactive protein Z for fast and efficient site-specific conjugation of native IgG. Bioconjug. Chem. 2014, 25, 1709-1719.
    • (2014) Bioconjug. Chem , vol.25 , pp. 1709-1719
    • Hui, J.Z.1    Tsourkas, A.2
  • 158
    • 61449147053 scopus 로고    scopus 로고
    • Photoactivable antibody binding protein: Site-selective and covalent coupling of antibody
    • Jung, Y.; Lee, J.M.; Kim, J.W.; Yoon, J.; Cho, H.; Chung, B.H. Photoactivable antibody binding protein: site-selective and covalent coupling of antibody. Anal. Chem. 2009, 81, 936-942.
    • (2009) Anal. Chem , vol.81 , pp. 936-942
    • Jung, Y.1    Lee, J.M.2    Kim, J.W.3    Yoon, J.4    Cho, H.5    Chung, B.H.6
  • 161
    • 0034428231 scopus 로고    scopus 로고
    • Site-specific photobiotinylation of antibodies, light chains, and immunoglobulin fragments
    • Pavlinkova, G.; Lou, D.; Kohler, H. Site-specific photobiotinylation of antibodies, light chains, and immunoglobulin fragments. Methods 2000, 22, 44-48.
    • (2000) Methods , vol.22 , pp. 44-48
    • Pavlinkova, G.1    Lou, D.2    Kohler, H.3
  • 163
    • 84904421553 scopus 로고    scopus 로고
    • Conjugation of a reactive thiol at the nucleotide binding site for site-specific antibody functionalization
    • Alves, N.J.; Mustafaoglu, N.; Bilgicer, B. Conjugation of a reactive thiol at the nucleotide binding site for site-specific antibody functionalization. Bioconjug. Chem. 2014, 25, 1198-1202.
    • (2014) Bioconjug. Chem , vol.25 , pp. 1198-1202
    • Alves, N.J.1    Mustafaoglu, N.2    Bilgicer, B.3
  • 164
    • 0029590066 scopus 로고
    • Efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes
    • Wagner, J.; Lerner, R.; Barbas, C. Efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes. Science 1995, 270, 1797-1800.
    • (1995) Science , vol.270 , pp. 1797-1800
    • Wagner, J.1    Lerner, R.2    Barbas, C.3
  • 166
    • 0033550282 scopus 로고    scopus 로고
    • Catalytic single-chain antibodies possessing ß-lactamase activity selected from a phage displayed combinatorial library using a mechanismbased inhibitor
    • Tanaka, F.; Almer, H.; Lerner, R.A.; Barbas, C.F. Catalytic single-chain antibodies possessing ß-lactamase activity selected from a phage displayed combinatorial library using a mechanismbased inhibitor. Tetrahedron Lett. 1999, 40, 8063-8066.
    • (1999) Tetrahedron Lett , vol.40 , pp. 8063-8066
    • Tanaka, F.1    Almer, H.2    Lerner, R.A.3    Barbas, C.F.4
  • 167
    • 0036837384 scopus 로고    scopus 로고
    • Reactive immunization: A unique approach to catalytic antibodies
    • Tanaka, F.; Barbas, C. Reactive immunization: A unique approach to catalytic antibodies. J. Immunol. Methods 2002, 269, 67-79.
    • (2002) J. Immunol. Methods , vol.269 , pp. 67-79
    • Tanaka, F.1    Barbas, C.2
  • 168
    • 34347272702 scopus 로고    scopus 로고
    • 3rd. Preparation of integrin alpha(v)beta3-targeting Ab 38C2 constructs
    • Sinha, S.C.; Das, S.; Li, L.S.; Lerner, R.A.; Barbas, C.F., 3rd. Preparation of integrin alpha(v)beta3-targeting Ab 38C2 constructs. Nat. Protoc. 2007, 2, 449-456.
    • (2007) Nat. Protoc , vol.2 , pp. 449-456
    • Sinha, S.C.1    Das, S.2    Li, L.S.3    Lerner, R.A.4    Barbas, C.F.5
  • 170
    • 84896544472 scopus 로고    scopus 로고
    • Chemically programmed antibodies
    • Rader, C. Chemically programmed antibodies. Trends Biotechnol. 2014, 32, 186-197.
    • (2014) Trends Biotechnol , vol.32 , pp. 186-197
    • Rader, C.1
  • 171
    • 0038641840 scopus 로고    scopus 로고
    • Chemically programmed monoclonal antibodies for cancer therapy: Adaptor immunotherapy based on a covalent antibody catalyst
    • Rader, C.; Sinha, S.; Popkov, M.; Lerner, R.; Barbas, C. Chemically programmed monoclonal antibodies for cancer therapy: adaptor immunotherapy based on a covalent antibody catalyst. Proc. Natl. Acad. Sci. USA 2003, 100, 5396-5400.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5396-5400
    • Rader, C.1    Sinha, S.2    Popkov, M.3    Lerner, R.4    Barbas, C.5
  • 173
    • 67650908912 scopus 로고    scopus 로고
    • Selective activity against proliferating tumor endothelial cells by CVX-22, a thrombospondin-1 mimetic CovX-Body
    • Coronella, J.; Li, L.; Johnson, K.; Pirie-Shepherd, S.; Roxas, G.; Levin, N. Selective activity against proliferating tumor endothelial cells by CVX-22, a thrombospondin-1 mimetic CovX-Body. Anticancer Res. 2009, 29, 2243-2252.
    • (2009) Anticancer Res , vol.29 , pp. 2243-2252
    • Coronella, J.1    Li, L.2    Johnson, K.3    Pirie-Shepherd, S.4    Roxas, G.5    Levin, N.6
  • 177
    • 84873382943 scopus 로고    scopus 로고
    • Synthesis and evaluation of the aldolase antibody-derived chemical-antibodies targeting alpha5beta1 integrin
    • Goswami, R.K.; Liu, Y.; Liu, C.; Lerner, R.A.; Sinha, S.C. Synthesis and evaluation of the aldolase antibody-derived chemical-antibodies targeting alpha5beta1 integrin. Mol. Pharm. 2013, 10, 538-543.
    • (2013) Mol. Pharm , vol.10 , pp. 538-543
    • Goswami, R.K.1    Liu, Y.2    Liu, C.3    Lerner, R.A.4    Sinha, S.C.5
  • 178
    • 84936804307 scopus 로고    scopus 로고
    • Chemically programmed bispecific antibody targeting legumain protease and alphavbeta3 integrin mediates strong antitumor effects
    • Liu, Y.; Goswami, R.K.; Liu, C.; Sinha, S.C. Chemically programmed bispecific antibody targeting legumain protease and alphavbeta3 integrin mediates strong antitumor effects. Mol. Pharm. 2015, 12, 2544-2550.
    • (2015) Mol. Pharm , vol.12 , pp. 2544-2550
    • Liu, Y.1    Goswami, R.K.2    Liu, C.3    Sinha, S.C.4
  • 179
  • 180
    • 84867214330 scopus 로고    scopus 로고
    • 3rd. A chemically programmed antibody is a long-lasting and potent inhibitor of influenza neuraminidase
    • Hayakawa, M.; Toda, N.; Carrillo, N.; Thornburg, N.J.; Crowe, J.E., Jr.; Barbas, C.F., 3rd. A chemically programmed antibody is a long-lasting and potent inhibitor of influenza neuraminidase. ChemBioChem 2012, 13, 2191-2195.
    • (2012) ChemBioChem , vol.13 , pp. 2191-2195
    • Hayakawa, M.1    Toda, N.2    Carrillo, N.3    Thornburg, N.J.4    Crowe, J.E.5    Barbas, C.F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.