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Volumn 23, Issue 9, 2005, Pages 1137-1146

Arming antibodies: Prospects and challenges for immunoconjugates

Author keywords

[No Author keywords available]

Indexed keywords

DRUG PRODUCTS; IMMUNOLOGY; MEDICAL APPLICATIONS; MOLECULAR STRUCTURE; ONCOLOGY; RADIOISOTOPES; TISSUE; TOXIC MATERIALS;

EID: 27144550160     PISSN: 10870156     EISSN: 15461696     Source Type: Journal    
DOI: 10.1038/nbt1141     Document Type: Review
Times cited : (928)

References (102)
  • 1
    • 0033853776 scopus 로고    scopus 로고
    • Natural and designer binding sites made by phage display technology
    • Hoogenboom, H.R. & Chames, P. Natural and designer binding sites made by phage display technology. Immunol. Today 21, 371-378 (2000).
    • (2000) Immunol. Today , vol.21 , pp. 371-378
    • Hoogenboom, H.R.1    Chames, P.2
  • 2
    • 3142682191 scopus 로고    scopus 로고
    • Yeast display of antibody fragments: A discovery and characterization platform
    • Feldhaus, M.J. & Siegel, R.W. Yeast display of antibody fragments: a discovery and characterization platform. J. Immunol. Methods 290, 69-80 (2004).
    • (2004) J. Immunol. Methods , vol.290 , pp. 69-80
    • Feldhaus, M.J.1    Siegel, R.W.2
  • 3
    • 3142685154 scopus 로고    scopus 로고
    • In-vitro protein evolution by ribosome display and mRNA display
    • Lipovsek, D. & Pluckthun, A. In-vitro protein evolution by ribosome display and mRNA display. J. Immunol. Methods 290, 51-67 (2004).
    • (2004) J. Immunol. Methods , vol.290 , pp. 51-67
    • Lipovsek, D.1    Pluckthun, A.2
  • 4
    • 0035251462 scopus 로고    scopus 로고
    • Ribosome display and affinity maturation: From antibodies to single V-domains and steps towards cancer therapeutics
    • Irving, R.A., Coia, G., Roberts, A., Nuttall, S.D. & Hudson, P.J. Ribosome display and affinity maturation: from antibodies to single V-domains and steps towards cancer therapeutics. J. Immunol. Methods 248, 31-45 (2001).
    • (2001) J. Immunol. Methods , vol.248 , pp. 31-45
    • Irving, R.A.1    Coia, G.2    Roberts, A.3    Nuttall, S.D.4    Hudson, P.J.5
  • 5
    • 0028222932 scopus 로고
    • Antigen-specific human antibodies from mice comprising four distinct genetic modifications
    • Lonberg, N. et al. Antigen-specific human antibodies from mice comprising four distinct genetic modifications. Nature 368, 856-859 (1994).
    • (1994) Nature , vol.368 , pp. 856-859
    • Lonberg, N.1
  • 6
    • 0027963484 scopus 로고
    • Antigen-specific human monoclonal antibodies from mice engineered with human Ig heavy and light chain YACs
    • Green, L.L. et al. Antigen-specific human monoclonal antibodies from mice engineered with human Ig heavy and light chain YACs. Nat. Genet. 7, 13-21 (1994).
    • (1994) Nat. Genet. , vol.7 , pp. 13-21
    • Green, L.L.1
  • 7
    • 0024986216 scopus 로고
    • Tumor physiology and antibody delivery
    • Jain, R.K. Tumor physiology and antibody delivery. Front. Radiat. Ther. Oncol. 24, 32-46; discussion 64-68 (1990).
    • (1990) Front. Radiat. Ther. Oncol. , vol.24 , pp. 32-46
    • Jain, R.K.1
  • 8
    • 0029114671 scopus 로고
    • Targeting cancer micrometastases with monoclonal antibodies: A binding-site barrier
    • Saga, T. et al. Targeting cancer micrometastases with monoclonal antibodies: a binding-site barrier. Proc. Natl. Acad. Sci. USA 92, 8999-9003 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8999-9003
    • Saga, T.1
  • 9
    • 0036155882 scopus 로고    scopus 로고
    • Impaired surface antigen presentation in tumors: Implications for T cell-based immunotherapy
    • Ruiz-Cabello, F., Cabrera, T., Lopez-Nevot, M.A. & Garrido, F. Impaired surface antigen presentation in tumors: implications for T cell-based immunotherapy. Semin. Cancer Biol. 12, 15-24 (2002).
    • (2002) Semin. Cancer Biol. , vol.12 , pp. 15-24
    • Ruiz-Cabello, F.1    Cabrera, T.2    Lopez-Nevot, M.A.3    Garrido, F.4
  • 10
    • 14844342715 scopus 로고    scopus 로고
    • Tositumomab and (131)I therapy in non-Hodgkin's lymphoma
    • Wahl, R.L. Tositumomab and (131)I therapy in non-Hodgkin's lymphoma. J. Nucl. Med. 46 (Suppl. 1), 128S-140S (2005).
    • (2005) J. Nucl. Med. , vol.46 , Issue.1 SUPPL.
    • Wahl, R.L.1
  • 11
    • 0842324901 scopus 로고    scopus 로고
    • Safety and efficacy of radioimmunotherapy with yttrium 90 ibritumomab tiuxetan (Zevalin)
    • Borghaei, H. & Schilder, R.J. Safety and efficacy of radioimmunotherapy with yttrium 90 ibritumomab tiuxetan (Zevalin). Semin. Nucl. Med. 34, 4-9 (2004).
    • (2004) Semin. Nucl. Med. , vol.34 , pp. 4-9
    • Borghaei, H.1    Schilder, R.J.2
  • 12
    • 13544266555 scopus 로고    scopus 로고
    • CD33-directed therapy with gemtuzumab ozogamicin in acute myeloid leukemia: Progress in understanding cytotoxicity and potential mechanisms of drug resistance
    • Linenberger, M.L. CD33-directed therapy with gemtuzumab ozogamicin in acute myeloid leukemia: progress in understanding cytotoxicity and potential mechanisms of drug resistance. Leukemia 19, 176-182 (2005).
    • (2005) Leukemia , vol.19 , pp. 176-182
    • Linenberger, M.L.1
  • 14
    • 0033791994 scopus 로고    scopus 로고
    • Designer genes: Recombinant antibody fragments for biological imaging
    • Wu, A.M. & Yazaki, P.J. Designer genes: recombinant antibody fragments for biological imaging. Q. J. Nucl. Med. 44, 268-283 (2000).
    • (2000) Q. J. Nucl. Med. , vol.44 , pp. 268-283
    • Wu, A.M.1    Yazaki, P.J.2
  • 15
    • 15944388634 scopus 로고    scopus 로고
    • Engineered single chain antibody fragments for radioimmunotherapy
    • Hulahov, A. & Chester, K.A. Engineered single chain antibody fragments for radioimmunotherapy. Q. J. Nucl. Med. Mol. Imaging 48, 279-288 (2004).
    • (2004) Q. J. Nucl. Med. Mol. Imaging , vol.48 , pp. 279-288
    • Hulahov, A.1    Chester, K.A.2
  • 16
    • 0035874887 scopus 로고    scopus 로고
    • High affinity restricts the localization and tumor penetration of single-chain Fv antibody molecules
    • Adams, G.P. et al. High affinity restricts the localization and tumor penetration of single-chain Fv antibody molecules. Cancer Res. 61, 4750-4755 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 4750-4755
    • Adams, G.P.1
  • 17
    • 0035077938 scopus 로고    scopus 로고
    • Tumor targeting of radiometal labeled anti-CEA recombinant T84.66 diabody and T84.66 minibody: Comparison to radioiodinated fragments
    • Yazaki, P.J. et al. Tumor targeting of radiometal labeled anti-CEA recombinant T84.66 diabody and T84.66 minibody: comparison to radioiodinated fragments. Bioconjug. Chem. 12, 220-228 (2001).
    • (2001) Bioconjug. Chem. , vol.12 , pp. 220-228
    • Yazaki, P.J.1
  • 18
    • 0036837633 scopus 로고    scopus 로고
    • Selective targeting of tumoral vasculature: Comparison of different formats of an antibody (L19) to the ED-B domain of fibronectin
    • Borsi, L. et al. Selective targeting of tumoral vasculature: comparison of different formats of an antibody (L19) to the ED-B domain of fibronectin. Int. J. Cancer 102, 75-85 (2002).
    • (2002) Int. J. Cancer , vol.102 , pp. 75-85
    • Borsi, L.1
  • 19
    • 0028850319 scopus 로고
    • Biological properties of chimeric domain-deleted anticarcinoma immunoglobulins
    • Slavin-Chiorini, D.C. et al. Biological properties of chimeric domain-deleted anticarcinoma immunoglobulins. Cancer Res. (Suppl.) 55, 5957s-5967s (1995).
    • (1995) Cancer Res. (Suppl.) , vol.55
    • Slavin-Chiorini, D.C.1
  • 20
    • 19944430279 scopus 로고    scopus 로고
    • Tailoring the pharmacokinetics and positron emission tomography imaging properties of anti-carcinoembryonic antigen single-chain Fv-Fc antibody fragments
    • Kenanova, V. et al. Tailoring the pharmacokinetics and positron emission tomography imaging properties of anti-carcinoembryonic antigen single-chain Fv-Fc antibody fragments. Cancer Res. 65, 622-631 (2005).
    • (2005) Cancer Res. , vol.65 , pp. 622-631
    • Kenanova, V.1
  • 21
    • 0842263617 scopus 로고    scopus 로고
    • Production of soluble ScFvs with C-terminal-free thiol for site-specific conjugation or stable dimeric ScFvs on demand
    • Albrecht, H. et al. Production of soluble ScFvs with C-terminal-free thiol for site-specific conjugation or stable dimeric ScFvs on demand. Bioconjug. Chem. 15, 16-26 (2004).
    • (2004) Bioconjug. Chem. , vol.15 , pp. 16-26
    • Albrecht, H.1
  • 22
    • 12344336363 scopus 로고    scopus 로고
    • Characterization of site-specific ScFv PEGylation for tumor-targeting pharmaceuticals
    • Natarajan, A., Xiong, C.Y., Albrecht, H., DeNardo, G.L. & DeNardo, S.J. Characterization of site-specific ScFv PEGylation for tumor-targeting pharmaceuticals. Bioconjug. Chem. 16, 113-121 (2005).
    • (2005) Bioconjug. Chem. , vol.16 , pp. 113-121
    • Natarajan, A.1    Xiong, C.Y.2    Albrecht, H.3    DeNardo, G.L.4    DeNardo, S.J.5
  • 23
    • 0036737972 scopus 로고    scopus 로고
    • Reduction of kidney uptake in radiometal labeled peptide linkers conjugated to recombinant antibody fragments. Site-specific conjugation of DOTA-peptides to a Cys-diabody
    • Li, L. et al. Reduction of kidney uptake in radiometal labeled peptide linkers conjugated to recombinant antibody fragments. Site-specific conjugation of DOTA-peptides to a Cys-diabody. Bioconjug. Chem. 13, 985-995 (2002).
    • (2002) Bioconjug. Chem. , vol.13 , pp. 985-995
    • Li, L.1
  • 24
    • 0842313257 scopus 로고    scopus 로고
    • Covalent disulfide-linked anti-CEA diabody allows site-specific conjugation and radiolabeling for tumor targeting applications
    • Olafsen, T. et al. Covalent disulfide-linked anti-CEA diabody allows site-specific conjugation and radiolabeling for tumor targeting applications. Protein Eng. Des. Sel. 17, 21-27 (2004).
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 21-27
    • Olafsen, T.1
  • 25
    • 0032884409 scopus 로고    scopus 로고
    • Stable one-step technetium-99m labeling of His-tagged recombinant proteins with a novel Tc(I)-carbonyl complex
    • Waibel, R. et al. Stable one-step technetium-99m labeling of His-tagged recombinant proteins with a novel Tc(I)-carbonyl complex. Nat. Biotechnol. 17, 897-901 (1999).
    • (1999) Nat. Biotechnol. , vol.17 , pp. 897-901
    • Waibel, R.1
  • 27
    • 1542681650 scopus 로고    scopus 로고
    • (124)I-labeled engineered anti-CEA minibodies and diabodies allow high-contrast, antigen-specific small-animal PET imaging of xenografts in athymic mice
    • Sundaresan, G. et al. (124)I-labeled engineered anti-CEA minibodies and diabodies allow high-contrast, antigen-specific small-animal PET imaging of xenografts in athymic mice. J. Nucl. Med. 44, 1962-1969 (2003).
    • (2003) J. Nucl. Med. , vol.44 , pp. 1962-1969
    • Sundaresan, G.1
  • 28
    • 13944266719 scopus 로고    scopus 로고
    • Quantitative immuno-positron emission tomography imaging of HER2-positive tumor xenografts with an iodine-124 labeled anti-HER2 diabody
    • Robinson, M.K. et al. Quantitative immuno-positron emission tomography imaging of HER2-positive tumor xenografts with an iodine-124 labeled anti-HER2 diabody. Cancer Res. 65, 1471-1478 (2005).
    • (2005) Cancer Res. , vol.65 , pp. 1471-1478
    • Robinson, M.K.1
  • 29
    • 4143058066 scopus 로고    scopus 로고
    • Characterization of engineered anti-p185HER-2 (scFv-CH3)2 antibody fragments (minibodies) for tumor targeting
    • Olafsen, T. et al. Characterization of engineered anti-p185HER-2 (scFv-CH3)2 antibody fragments (minibodies) for tumor targeting. Protein Eng. Des. Sel. 17, 315-323 (2004).
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 315-323
    • Olafsen, T.1
  • 30
    • 21344437728 scopus 로고    scopus 로고
    • Optimizing radiolabeled engineered anti-p185HER2 antibody fragments for in vivo imaging
    • Olafsen, T. et al. Optimizing radiolabeled engineered anti-p185HER2 antibody fragments for in vivo imaging. Cancer Res. 65, 5907-5916 (2005).
    • (2005) Cancer Res. , vol.65 , pp. 5907-5916
    • Olafsen, T.1
  • 31
    • 2542643923 scopus 로고    scopus 로고
    • Imaging the pharmacodynamics of HER2 degradation in response to Hsp90 inhibitors
    • Smith-Jones, P.M. et al. Imaging the pharmacodynamics of HER2 degradation in response to Hsp90 inhibitors. Nat. Biotechnol. 22, 701-706 (2004).
    • (2004) Nat. Biotechnol. , vol.22 , pp. 701-706
    • Smith-Jones, P.M.1
  • 32
    • 9544250404 scopus 로고    scopus 로고
    • Clinical evidence of efficient tumor targeting based on single-chain Fv antibody selected from a combinatorial library
    • Begent, R.H.J. et al. Clinical evidence of efficient tumor targeting based on single-chain Fv antibody selected from a combinatorial library. Nat. Med. 2, 979-984 (1996).
    • (1996) Nat. Med. , vol.2 , pp. 979-984
    • Begent, R.H.J.1
  • 33
    • 0031456426 scopus 로고    scopus 로고
    • Single chain antigen binding protein (sFv CC49) - First human studies in colorectal carcinoma metastatic to liver
    • Larson, S.M. et al. Single chain antigen binding protein (sFv CC49) - First human studies in colorectal carcinoma metastatic to liver. Cancer 80 (Suppl.), 2458-2468 (1997).
    • (1997) Cancer , vol.80 , Issue.SUPPL. , pp. 2458-2468
    • Larson, S.M.1
  • 34
    • 0037314650 scopus 로고    scopus 로고
    • Immunoscintigraphic detection of the ED-B domain of fibronectin, a marker of angiogenesis, in patients with cancer
    • Santimaria, M. et al. Immunoscintigraphic detection of the ED-B domain of fibronectin, a marker of angiogenesis, in patients with cancer. Clin. Cancer Res. 9, 571-579 (2003).
    • (2003) Clin. Cancer Res. , vol.9 , pp. 571-579
    • Santimaria, M.1
  • 35
    • 4143080306 scopus 로고    scopus 로고
    • Pilot trial evaluating an 123l-labeled 80-kilodalton engineered anticarcinoembryonic antigen antibody fragment (cT84.66 minibody) in patients with colorectal cancer
    • Wong, J.Y. et al. Pilot trial evaluating an 123l-labeled 80-kilodalton engineered anticarcinoembryonic antigen antibody fragment (cT84.66 minibody) in patients with colorectal cancer. Clin. Cancer Res. 10, 5014-5021 (2004).
    • (2004) Clin. Cancer Res. , vol.10 , pp. 5014-5021
    • Wong, J.Y.1
  • 36
    • 0034180952 scopus 로고    scopus 로고
    • Delivery of the α-emitting radioisotope bismuth-213 to solid tumors via single-chain Fv and diabody molecules
    • Adams, G. et al. Delivery of the α-emitting radioisotope bismuth-213 to solid tumors via single-chain Fv and diabody molecules. Nucl. Med. Biol. 27, 339-346 (2000).
    • (2000) Nucl. Med. Biol. , vol.27 , pp. 339-346
    • Adams, G.1
  • 37
    • 4344681476 scopus 로고    scopus 로고
    • A single treatment of yttrium-90-labeled CHX-A"-C6.5 diabody inhibits the growth of established human tumor xenografts in immunodeficient mice
    • Adams, G.P. et al. A single treatment of yttrium-90-labeled CHX-A"-C6.5 diabody inhibits the growth of established human tumor xenografts in immunodeficient mice. Cancer Res. 64, 6200-6206 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 6200-6206
    • Adams, G.P.1
  • 38
    • 14844343723 scopus 로고    scopus 로고
    • Perspectives on cancer therapy with radiolabeled monoclonal antibodies
    • Sharkey, R.M. & Goldenberg, D.M. Perspectives on cancer therapy with radiolabeled monoclonal antibodies. J. Nucl. Med. 46 (Suppl. 1), 115S-127S (2005).
    • (2005) J. Nucl. Med. , vol.46 , Issue.1 SUPPL.
    • Sharkey, R.M.1    Goldenberg, D.M.2
  • 39
    • 14844359240 scopus 로고    scopus 로고
    • Current status of therapy of solid tumors
    • Jhanwar, Y.S. & Divgi, C. Current status of therapy of solid tumors. J. Nucl. Med. 46 (Suppl. 1), 141S-150S (2005).
    • (2005) J. Nucl. Med. , vol.46 , Issue.1 SUPPL.
    • Jhanwar, Y.S.1    Divgi, C.2
  • 40
    • 0347995052 scopus 로고    scopus 로고
    • Y-anti-carcinoembryonic antigen chimeric T84.66 radioimmunotherapy with 5-fluorouracil in patients with metastatic colorectal cancer
    • Y-anti-carcinoembryonic antigen chimeric T84.66 radioimmunotherapy with 5-fluorouracil in patients with metastatic colorectal cancer. Clin. Cancer Res. 9, 5842-5852 (2003).
    • (2003) Clin. Cancer Res. , vol.9 , pp. 5842-5852
    • Wong, J.Y.1
  • 41
    • 19644379671 scopus 로고    scopus 로고
    • Y-labeled humanized anti-CEA monoclonal antibody with doxorubicin and peripheral blood stem cell rescue in advanced medullary thyroid cancer
    • Y-labeled humanized anti-CEA monoclonal antibody with doxorubicin and peripheral blood stem cell rescue in advanced medullary thyroid cancer. J. Nucl. Med. 46, 620-633 (2005).
    • (2005) J. Nucl. Med. , vol.46 , pp. 620-633
    • Sharkey, R.M.1
  • 42
    • 0033180164 scopus 로고    scopus 로고
    • Receptor-mediated and enzyme-dependent targeting of cytotoxic anticancer drugs
    • Dubowchik, G.M. & Walker, M.A. Receptor-mediated and enzyme-dependent targeting of cytotoxic anticancer drugs. Pharmacol. Ther. 83, 67-123 (1999).
    • (1999) Pharmacol. Ther. , vol.83 , pp. 67-123
    • Dubowchik, G.M.1    Walker, M.A.2
  • 43
    • 0042787657 scopus 로고    scopus 로고
    • Progress in immunoconjugate cancer therapeutics
    • Payne, G. Progress in immunoconjugate cancer therapeutics. Cancer Cell 3, 207-212 (2003).
    • (2003) Cancer Cell , vol.3 , pp. 207-212
    • Payne, G.1
  • 44
    • 0027218284 scopus 로고
    • Cure of xenografted human carcinomas by BR96-doxorubicin immunoconjugates
    • Trail, P.A. et al. Cure of xenografted human carcinomas by BR96-doxorubicin immunoconjugates. Science 261, 212-215 (1993).
    • (1993) Science , vol.261 , pp. 212-215
    • Trail, P.A.1
  • 45
    • 0030923296 scopus 로고    scopus 로고
    • Disposition of conjugate-bound and free doxorubicin in tumor-bearing mice following administration of a BR96-doxorubicin immunoconjugate (BMS 182248)
    • Mosure, K.W., Henderson, A.J., Klunk, L.J. & Knipe, J.O. Disposition of conjugate-bound and free doxorubicin in tumor-bearing mice following administration of a BR96-doxorubicin immunoconjugate (BMS 182248). Cancer Chemother. Pharmacol. 40, 251-258 (1997).
    • (1997) Cancer Chemother. Pharmacol. , vol.40 , pp. 251-258
    • Mosure, K.W.1    Henderson, A.J.2    Klunk, L.J.3    Knipe, J.O.4
  • 46
    • 0034077405 scopus 로고    scopus 로고
    • Phase I trial of the anti-Lewis Y drug immunoconjugate BR96-doxorubicin in patients with Lewis Y-expressing epithelial tumors
    • Saleh, M.N. et al. Phase I trial of the anti-Lewis Y drug immunoconjugate BR96-doxorubicin in patients with Lewis Y-expressing epithelial tumors. J. Clin. Oncol. 18, 2282-2292 (2000).
    • (2000) J. Clin. Oncol. , vol.18 , pp. 2282-2292
    • Saleh, M.N.1
  • 47
    • 0037440038 scopus 로고    scopus 로고
    • Cantuzumab mertansine, a maytansinoid immunoconjugate directed to the CanAg antigen: A phase I, pharmacokinetic, and biologic correlative study
    • Tolcher, A.W. et al. Cantuzumab mertansine, a maytansinoid immunoconjugate directed to the CanAg antigen: a phase I, pharmacokinetic, and biologic correlative study. J. Clin. Oncol. 21, 211-222 (2003).
    • (2003) J. Clin. Oncol. , vol.21 , pp. 211-222
    • Tolcher, A.W.1
  • 48
    • 0346333230 scopus 로고    scopus 로고
    • Cure of SCID mice bearing human B-lymphoma xenografts by an anti-CD74 antibody-anthracycline drug conjugate
    • Griffiths, G.L. et al. Cure of SCID mice bearing human B-lymphoma xenografts by an anti-CD74 antibody-anthracycline drug conjugate. Clin. Cancer Res. 9, 6567-6571 (2003).
    • (2003) Clin. Cancer Res. , vol.9 , pp. 6567-6571
    • Griffiths, G.L.1
  • 49
    • 0042303836 scopus 로고    scopus 로고
    • Antibody-targeted chemotherapy with immunoconjugates of calicheamicin
    • Damle, N.K. & Frost, P. Antibody-targeted chemotherapy with immunoconjugates of calicheamicin. Curr. Opin. Pharmacol. 3, 386-390 (2003).
    • (2003) Curr. Opin. Pharmacol. , vol.3 , pp. 386-390
    • Damle, N.K.1    Frost, P.2
  • 50
    • 4544350808 scopus 로고    scopus 로고
    • Tumour-targeted chemotherapy with immunoconjugates of calicheamicin
    • Damle, N.K. Tumour-targeted chemotherapy with immunoconjugates of calicheamicin. Expert Opin. Biol. Ther. 4, 1445-1452 (2004).
    • (2004) Expert Opin. Biol. Ther. , vol.4 , pp. 1445-1452
    • Damle, N.K.1
  • 51
    • 0036007598 scopus 로고    scopus 로고
    • An anti-CD33 antibody-calicheamicin conjugate for treatment of acute myeloid leukemia. Choice of linker
    • Hamann, P. R. et al. An anti-CD33 antibody-calicheamicin conjugate for treatment of acute myeloid leukemia. Choice of linker. Bioconjug. Chem. 13, 40-46 (2002).
    • (2002) Bioconjug. Chem. , vol.13 , pp. 40-46
    • Hamann, P.R.1
  • 52
    • 0036007596 scopus 로고    scopus 로고
    • Gemtuzumab ozogamicin, a potent and selective anti-CD33 antibody-calicheamicin conjugate for treatment of acute myeloid leukemia
    • Hamann, P.R. et al. Gemtuzumab ozogamicin, a potent and selective anti-CD33 antibody-calicheamicin conjugate for treatment of acute myeloid leukemia. Bioconjug. Chem. 13, 47-58 (2002).
    • (2002) Bioconjug. Chem. , vol.13 , pp. 47-58
    • Hamann, P.R.1
  • 53
    • 0034900174 scopus 로고    scopus 로고
    • Approval summary: Gemtuzumab ozogamicin in relapsed acute myeloid leukemia
    • Bross, P.F. et al. Approval summary: gemtuzumab ozogamicin in relapsed acute myeloid leukemia. Clin. Cancer Res. 7, 1490-1496 (2001).
    • (2001) Clin. Cancer Res. , vol.7 , pp. 1490-1496
    • Bross, P.F.1
  • 54
    • 0033151526 scopus 로고    scopus 로고
    • Selective ablation of acute myeloid leukemia using antibody-targeted chemotherapy: A phase I study of an anti-CD33 calicheamicin immunoconjugate
    • Sievers, E.L. et al. Selective ablation of acute myeloid leukemia using antibody-targeted chemotherapy: a phase I study of an anti-CD33 calicheamicin immunoconjugate. Blood 93, 3678-3684 (1999).
    • (1999) Blood , vol.93 , pp. 3678-3684
    • Sievers, E.L.1
  • 55
    • 0034753903 scopus 로고    scopus 로고
    • Mylotarg: Antibody-targeted chemotherapy comes of age
    • Sievers, E.L. & Linenberger, M. Mylotarg: antibody-targeted chemotherapy comes of age. Curr. Opin. Oncol. 13, 522-527 (2001).
    • (2001) Curr. Opin. Oncol. , vol.13 , pp. 522-527
    • Sievers, E.L.1    Linenberger, M.2
  • 56
    • 0035878068 scopus 로고    scopus 로고
    • Mylotarg (gemtuzumab ozogamicin) therapy is associated with hepatic venoocclusive disease in patients who have not received stem cell transplantation
    • Giles, F.J. et al. Mylotarg (gemtuzumab ozogamicin) therapy is associated with hepatic venoocclusive disease in patients who have not received stem cell transplantation. Cancer 92, 406-413 (2001).
    • (2001) Cancer , vol.92 , pp. 406-413
    • Giles, F.J.1
  • 57
    • 10744229449 scopus 로고    scopus 로고
    • Antibody-targeted chemotherapy with CMC-544: A CD22-targeted immunoconjugate of calicheamicin for the treatment of B-lymphoid malignancies
    • DiJoseph, J.F. et al. Antibody-targeted chemotherapy with CMC-544: a CD22-targeted immunoconjugate of calicheamicin for the treatment of B-lymphoid malignancies. Blood 103, 1807-1814 (2004).
    • (2004) Blood , vol.103 , pp. 1807-1814
    • DiJoseph, J.F.1
  • 58
    • 19944426031 scopus 로고    scopus 로고
    • Antibody-targeted chemotherapy of B-cell lymphoma using calicheamicin conjugated to murine or humanized antibody against CD22
    • DiJoseph, J.F. et al. Antibody-targeted chemotherapy of B-cell lymphoma using calicheamicin conjugated to murine or humanized antibody against CD22. Cancer Immunol. Immunother. 54, 11-24 (2005).
    • (2005) Cancer Immunol. Immunother. , vol.54 , pp. 11-24
    • DiJoseph, J.F.1
  • 59
    • 3042770596 scopus 로고    scopus 로고
    • Antibody-targeted chemotherapy with the calicheamicin conjugate hu3S193-N-acetyl gamma calicheamicin dimethyl hydrazide targets Lewis(y) and eliminates Lewis(y-positive) human carcinoma cells and xenografts
    • Boghaert, E.R. et al. Antibody-targeted chemotherapy with the calicheamicin conjugate hu3S193-N-acetyl gamma calicheamicin dimethyl hydrazide targets Lewis(y) and eliminates Lewis(y-positive) human carcinoma cells and xenografts. Clin. Cancer Res. 10, 4538-4549 (2004).
    • (2004) Clin. Cancer Res. , vol.10 , pp. 4538-4549
    • Boghaert, E.R.1
  • 60
    • 0035883042 scopus 로고    scopus 로고
    • Multidrug-resistance phenotype and clinical responses to gemtuzumab ozogamicin
    • Linenberger, M.L. et al. Multidrug-resistance phenotype and clinical responses to gemtuzumab ozogamicin. Blood 98, 988-994 (2001).
    • (2001) Blood , vol.98 , pp. 988-994
    • Linenberger, M.L.1
  • 61
    • 20144375952 scopus 로고    scopus 로고
    • An anti-MUC1 antibody-calicheamicin conjugate for treatment of solid tumors. Choice of linker and overcoming drug resistance
    • Hamann, P.R. et al. An anti-MUC1 antibody-calicheamicin conjugate for treatment of solid tumors. Choice of linker and overcoming drug resistance. Bioconjug. Chem. 16, 346-353 (2005).
    • (2005) Bioconjug. Chem. , vol.16 , pp. 346-353
    • Hamann, P.R.1
  • 62
    • 0027156735 scopus 로고
    • Immunotoxins: Magic bullets or misguided missiles?
    • Vitetta, E.S., Thorpe, P.E. & Uhr, J.W. Immunotoxins: magic bullets or misguided missiles? Immunol. Today 14, 252-259 (1993).
    • (1993) Immunol. Today , vol.14 , pp. 252-259
    • Vitetta, E.S.1    Thorpe, P.E.2    Uhr, J.W.3
  • 63
    • 0023689869 scopus 로고
    • Improved antitumor effects of immunotoxins prepared with deglycosylated ricin A-chain and hindered disulfide linkages
    • Thorpe, P.E. et al. Improved antitumor effects of immunotoxins prepared with deglycosylated ricin A-chain and hindered disulfide linkages. Cancer Res. 48, 6396-6403 (1988).
    • (1988) Cancer Res. , vol.48 , pp. 6396-6403
    • Thorpe, P.E.1
  • 64
    • 11344280534 scopus 로고    scopus 로고
    • Technology evaluation: Cantuzumab mertansine, ImmunoGen
    • Smith, S.V. Technology evaluation: cantuzumab mertansine, ImmunoGen. Curr. Opin. Mol. Ther. 6, 666-674 (2004).
    • (2004) Curr. Opin. Mol. Ther. , vol.6 , pp. 666-674
    • Smith, S.V.1
  • 65
    • 1342287215 scopus 로고    scopus 로고
    • Pharmacokinetics and biodistribution of the antitumor immunoconjugate, cantuzumab mertansine (huC242-DM1), and its two components in mice
    • Xie, H., Audette, C., Hoffee, M., Lambert, J.M. & Blattler, W.A. Pharmacokinetics and biodistribution of the antitumor immunoconjugate, cantuzumab mertansine (huC242-DM1), and its two components in mice. J. Pharmacol. Exp. Ther. 308, 1073-1082 (2004).
    • (2004) J. Pharmacol. Exp. Ther. , vol.308 , pp. 1073-1082
    • Xie, H.1    Audette, C.2    Hoffee, M.3    Lambert, J.M.4    Blattler, W.A.5
  • 66
    • 27144516130 scopus 로고    scopus 로고
    • HuC242-DM4, an antibody-maytansinoid conjugate with superior preclinical activity in human CanAg-positive tumor xenograft models in SCID mice
    • Abstract of a paper presented, Anaheim, CA, 16-20 April
    • Lutz, R.L. et al. HuC242-DM4, an antibody-maytansinoid conjugate with superior preclinical activity in human CanAg-positive tumor xenograft models in SCID mice. Abstract of a paper presented at the 96th annual meeting of the American Association for Cancer Research, Anaheim, CA, 16-20 April 2005.
    • (2005) 96th Annual Meeting of the American Association for Cancer Research
    • Lutz, R.L.1
  • 67
    • 42549101120 scopus 로고    scopus 로고
    • Phase II trial of BB-10901 (huN901-DM1) given weekly for four consecutive weeks every 6 weeks in patients with relapsed SCLC and CD56-positive small cell carcinoma
    • Abstract of a paper presented, Orlando, FL, 13-17 May
    • Fosella, F.V. et al. Phase II trial of BB-10901 (huN901-DM1) given weekly for four consecutive weeks every 6 weeks in patients with relapsed SCLC and CD56-positive small cell carcinoma. Abstract of a paper presented at the 41st annual meeting of the American Society of Clinical Oncology, Orlando, FL, 13-17 May 2005.
    • (2005) 41st Annual Meeting of the American Society of Clinical Oncology
    • Fosella, F.V.1
  • 68
    • 9444223279 scopus 로고    scopus 로고
    • + multiple myeloma cells
    • + multiple myeloma cells. Blood 104, 3688-3696 (2004).
    • (2004) Blood , vol.104 , pp. 3688-3696
    • Tassone, P.1
  • 69
    • 7444263583 scopus 로고    scopus 로고
    • A prostate-specific membrane antigen-targeted monoclonal antibody-chemotherapeutic conjugate designed for the treatment of prostate cancer
    • Henry, M.D. et al. A prostate-specific membrane antigen-targeted monoclonal antibody-chemotherapeutic conjugate designed for the treatment of prostate cancer. Cancer Res. 64, 7995-8001 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 7995-8001
    • Henry, M.D.1
  • 70
    • 0032402354 scopus 로고    scopus 로고
    • Cathepsin B-sensitive dipeptide prodrugs. 1. A model study of structural requirements for efficient release of doxorubicin
    • Dubowchik, G.M. & Firestone, R.A. Cathepsin B-sensitive dipeptide prodrugs. 1. A model study of structural requirements for efficient release of doxorubicin. Bioorg. Med. Chem. Lett. 8, 3341-3346 (1998).
    • (1998) Bioorg. Med. Chem. Lett. , vol.8 , pp. 3341-3346
    • Dubowchik, G.M.1    Firestone, R.A.2
  • 71
    • 0032402572 scopus 로고    scopus 로고
    • Cathepsin B-sensitive dipeptide prodrugs. 2. Models of anticancer drugs paclitaxel (Taxol), mitomycin C and doxorubicin
    • Dubowchik, G.M., Mosure, K., Knipe, J.O. & Firestone, R.A. Cathepsin B-sensitive dipeptide prodrugs. 2. Models of anticancer drugs paclitaxel (Taxol), mitomycin C and doxorubicin. Bioorg. Med. Chem. Lett. 8, 3347-3352 (1998).
    • (1998) Bioorg. Med. Chem. Lett. , vol.8 , pp. 3347-3352
    • Dubowchik, G.M.1    Mosure, K.2    Knipe, J.O.3    Firestone, R.A.4
  • 72
    • 0036074253 scopus 로고    scopus 로고
    • Cathepsin B-labile dipeptide linkers for lysosomal release of doxorubicin from internalizing immunoconjugates: Model studies of enzymatic drug release and antigen-specific in vitro anticancer activity
    • Dubowchik, G.M. et al. Cathepsin B-labile dipeptide linkers for lysosomal release of doxorubicin from internalizing immunoconjugates: model studies of enzymatic drug release and antigen-specific in vitro anticancer activity. Bioconjug. Chem. 13, 855-869 (2002).
    • (2002) Bioconjug. Chem. , vol.13 , pp. 855-869
    • Dubowchik, G.M.1
  • 74
    • 3142682236 scopus 로고    scopus 로고
    • Monoclonal antibody mediated intracellular targeting of tallysomycin S(10b)
    • Walker, M.A. et al. Monoclonal antibody mediated intracellular targeting of tallysomycin S(10b). Bioorg. Med. Chem. Lett. 14, 4323-4327 (2004).
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 4323-4327
    • Walker, M.A.1
  • 75
    • 10744222473 scopus 로고    scopus 로고
    • Development of potent monoclonal antibody auristatin conjugates for cancer therapy
    • Doronina, S.O. et al. Development of potent monoclonal antibody auristatin conjugates for cancer therapy. Nat. Biotechnol. 21, 778-784 (2003).
    • (2003) Nat. Biotechnol. , vol.21 , pp. 778-784
    • Doronina, S.O.1
  • 76
    • 0042738861 scopus 로고    scopus 로고
    • cAC10-vcMMAE, an anti-CD30-monomethyl auristatin E conjugate with potent and selective antitumor activity
    • Francisco, J.A. et al. cAC10-vcMMAE, an anti-CD30-monomethyl auristatin E conjugate with potent and selective antitumor activity. Blood 102, 1458-1465 (2003).
    • (2003) Blood , vol.102 , pp. 1458-1465
    • Francisco, J.A.1
  • 77
    • 0036795186 scopus 로고    scopus 로고
    • Phase II study of dolastatin-10 as first-line treatment for advanced colorectal cancer
    • Saad, E.D. et al. Phase II study of dolastatin-10 as first-line treatment for advanced colorectal cancer. Am. J. Clin. Oncol. 25, 451-453 (2002).
    • (2002) Am. J. Clin. Oncol. , vol.25 , pp. 451-453
    • Saad, E.D.1
  • 78
    • 6044223544 scopus 로고    scopus 로고
    • Effects of drug loading on the antitumor activity of a monoclonal antibody drug conjugate
    • Hamblett, K.J. et al. Effects of drug loading on the antitumor activity of a monoclonal antibody drug conjugate. Clin. Cancer Res. 10, 7063-7070 (2004).
    • (2004) Clin. Cancer Res. , vol.10 , pp. 7063-7070
    • Hamblett, K.J.1
  • 79
    • 9744243565 scopus 로고    scopus 로고
    • Efficient elimination of B-lineage lymphomas by anti-CD20-auristatin conjugates
    • Law, C.L. et al. Efficient elimination of B-lineage lymphomas by anti-CD20-auristatin conjugates. Clin. Cancer Res. 10, 7842-7851 (2004).
    • (2004) Clin. Cancer Res. , vol.10 , pp. 7842-7851
    • Law, C.L.1
  • 80
    • 0141569732 scopus 로고    scopus 로고
    • Conditionally cleavable radioimmunoconjugates: A novel approach for the release of radioisotopes from radioimmunoconjugates
    • Beeson, C. et al. Conditionally cleavable radioimmunoconjugates: a novel approach for the release of radioisotopes from radioimmunoconjugates. Bioconjug. Chem. 14, 927-933 (2003).
    • (2003) Bioconjug. Chem. , vol.14 , pp. 927-933
    • Beeson, C.1
  • 81
    • 0032408581 scopus 로고    scopus 로고
    • Strategies to reduce renal radioactivity levels of antibody fragments
    • Arano, Y. Strategies to reduce renal radioactivity levels of antibody fragments. Q. J. Nucl. Med. 42, 262-270 (1998).
    • (1998) Q. J. Nucl. Med. , vol.42 , pp. 262-270
    • Arano, Y.1
  • 82
    • 0026926542 scopus 로고
    • Influence of a peptide linker on biodistribution and metabolism of antibody-conjugated benzyl-EDTA. Comparison of enzymatic digestion in vitro and in vivo
    • Studer, M., Kroger, L.A., DeNardo, S.J., Kukis, D.L. & Meares, C.F. Influence of a peptide linker on biodistribution and metabolism of antibody-conjugated benzyl-EDTA. Comparison of enzymatic digestion in vitro and in vivo. Bioconjug. Chem. 3, 424-429 (1992).
    • (1992) Bioconjug. Chem. , vol.3 , pp. 424-429
    • Studer, M.1    Kroger, L.A.2    DeNardo, S.J.3    Kukis, D.L.4    Meares, C.F.5
  • 83
    • 0042242752 scopus 로고    scopus 로고
    • 111In-MN14 using an avidin-affinity column in rats
    • 111In-MN14 using an avidin-affinity column in rats. Cancer Biother. Radiopharm. 18, 365-375 (2003).
    • (2003) Cancer Biother. Radiopharm. , vol.18 , pp. 365-375
    • Wang, Z.1
  • 84
    • 0023841413 scopus 로고
    • Pre-targeted immunoscintigraphy of murine tumors with indium-111-labeled bifunctional haptens
    • Goodwin, D.A., Meares, C.F., McCall, M.J., McTigue, M. & Chaovapong, W. Pre-targeted immunoscintigraphy of murine tumors with indium-111-labeled bifunctional haptens. J. Nucl. Med. 29, 226-234 (1988).
    • (1988) J. Nucl. Med. , vol.29 , pp. 226-234
    • Goodwin, D.A.1    Meares, C.F.2    McCall, M.J.3    McTigue, M.4    Chaovapong, W.5
  • 85
    • 26444440483 scopus 로고    scopus 로고
    • Improving the delivery of radionuclides for imaging and therapy of cancer using pretargeting methods
    • in the press
    • Sharkey, R.M. et al. Improving the delivery of radionuclides for imaging and therapy of cancer using pretargeting methods. Clin. Cancer Res. (in the press) (2005).
    • (2005) Clin. Cancer Res.
    • Sharkey, R.M.1
  • 86
    • 18544410002 scopus 로고    scopus 로고
    • Pretargeted radioimmunotherapy (PRITTM) for treatment of non-Hodgkin's lymphoma (NHL): Initial phase I/II study results
    • Weiden, P.L. et al. Pretargeted radioimmunotherapy (PRITTM) for treatment of non-Hodgkin's lymphoma (NHL): initial phase I/II study results. Canc. Biother. Radiopharm. 15, 15-29 (2000).
    • (2000) Canc. Biother. Radiopharm. , vol.15 , pp. 15-29
    • Weiden, P.L.1
  • 87
    • 0024395317 scopus 로고
    • In vitro and in vivo targeting of radiolabeled monovalent and divalent haptens with dual specificity monoclonal antibody conjugates: Enhanced divalent hapten affinity for cell-bound antibody conjugate
    • Le Doussal, J.M., Martin, M., Gautherot, E., Delaage, M. & Barbet, J. In vitro and in vivo targeting of radiolabeled monovalent and divalent haptens with dual specificity monoclonal antibody conjugates: enhanced divalent hapten affinity for cell-bound antibody conjugate. J. Nucl. Med. 30, 1358-1366 (1989).
    • (1989) J. Nucl. Med. , vol.30 , pp. 1358-1366
    • Le Doussal, J.M.1    Martin, M.2    Gautherot, E.3    Delaage, M.4    Barbet, J.5
  • 88
    • 0034814422 scopus 로고    scopus 로고
    • Pretargeting with amplification using polymeric peptide nucleic acid
    • Wang, Y. et al. Pretargeting with amplification using polymeric peptide nucleic acid. Bioconjug. Chem. 12, 807-816 (2001).
    • (2001) Bioconjug. Chem. , vol.12 , pp. 807-816
    • Wang, Y.1
  • 89
    • 3242734128 scopus 로고    scopus 로고
    • Amplification targeting: A modified pretargeting approach with potential for signal amplification - Proof of a concept
    • He, J. et al. Amplification targeting: a modified pretargeting approach with potential for signal amplification - proof of a concept. J. Nucl. Med. 45, 1087-1095 (2004).
    • (2004) J. Nucl. Med. , vol.45 , pp. 1087-1095
    • He, J.1
  • 90
    • 0028889940 scopus 로고
    • Bifunctional and multimeric complexes of streptavidin fused to single chain antibodies (scFv)
    • Dübel, S. et al. Bifunctional and multimeric complexes of streptavidin fused to single chain antibodies (scFv). J. Immunol. Methods 178, 201-209 (1995).
    • (1995) J. Immunol. Methods , vol.178 , pp. 201-209
    • Dübel, S.1
  • 91
    • 0034541209 scopus 로고    scopus 로고
    • A tetravalent single-chain antibody-streptavidin fusion protein for pretargeted lymphoma therapy
    • Schultz, J. et al. A tetravalent single-chain antibody-streptavidin fusion protein for pretargeted lymphoma therapy. Cancer Res. 60, 6663-6669 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 6663-6669
    • Schultz, J.1
  • 92
    • 0035707709 scopus 로고    scopus 로고
    • Preclinical evaluation of a humanized NR-LU-10 antibody-streptavidin fusion protein for pretargeted cancer therapy
    • Goshorn, S. et al. Preclinical evaluation of a humanized NR-LU-10 antibody-streptavidin fusion protein for pretargeted cancer therapy. Cancer Biother. Radiopharm. 16, 109-123 (2001).
    • (2001) Cancer Biother. Radiopharm. , vol.16 , pp. 109-123
    • Goshorn, S.1
  • 93
    • 3042796950 scopus 로고    scopus 로고
    • Phase 1 trial of a novel anti-CD20 fusion protein in pretargeted radioimmunotherapy for B-cell non-Hodgkin lymphoma
    • Forera, A. et al. Phase 1 trial of a novel anti-CD20 fusion protein in pretargeted radioimmunotherapy for B-cell non-Hodgkin lymphoma. Blood 104, 227-236 (2004).
    • (2004) Blood , vol.104 , pp. 227-236
    • Forera, A.1
  • 94
    • 26444530095 scopus 로고    scopus 로고
    • Pretargeting of CEA-expressing cancers with a trivalent bispecific fusion protein produced in myeloma cells
    • in the press
    • Rossi, E.A. et al. Pretargeting of CEA-expressing cancers with a trivalent bispecific fusion protein produced in myeloma cells. Clin. Cancer Res. (in the press) (2005).
    • (2005) Clin. Cancer Res.
    • Rossi, E.A.1
  • 95
    • 0035980983 scopus 로고    scopus 로고
    • Selective activation of anticancer prodrugs by monoclonal antibody-enzyme conjugates
    • Senter, P.D. & Springer, C.J. Selective activation of anticancer prodrugs by monoclonal antibody-enzyme conjugates. Adv. Drug Deliv. Rev. 53, 247-264 (2001).
    • (2001) Adv. Drug Deliv. Rev. , vol.53 , pp. 247-264
    • Senter, P.D.1    Springer, C.J.2
  • 97
    • 0031194865 scopus 로고    scopus 로고
    • Construction, expression, and activities of L49-sFv-beta-lactamase, a single-chain antibody fusion protein for anticancer prodrug activation
    • Siemers, N.O. et al. Construction, expression, and activities of L49-sFv-beta-lactamase, a single-chain antibody fusion protein for anticancer prodrug activation. Bioconjug. Chem. 8, 510-519 (1997).
    • (1997) Bioconjug. Chem. , vol.8 , pp. 510-519
    • Siemers, N.O.1
  • 98
    • 10644228142 scopus 로고    scopus 로고
    • Efficient cancer therapy with a nanobody-based conjugate
    • Cortez-Retamozo, V. et al., Efficient cancer therapy with a nanobody-based conjugate. Canc. Res. 64, 2853-2857 (2004)
    • (2004) Canc. Res. , vol.64 , pp. 2853-2857
    • Cortez-Retamozo, V.1
  • 99
    • 0033983443 scopus 로고    scopus 로고
    • Catalytic activity of an in vivo tumor targeted anti-CEA scFv::carboxypeptidase G2 fusion protein
    • Bhatia, J. et al. Catalytic activity of an in vivo tumor targeted anti-CEA scFv::carboxypeptidase G2 fusion protein. Int. J. Cancer 85, 571-577 (2000).
    • (2000) Int. J. Cancer , vol.85 , pp. 571-577
    • Bhatia, J.1
  • 100
    • 18544390790 scopus 로고    scopus 로고
    • A phase I trial of antibody directed enzyme prodrug therapy (ADEPT) in patients with advanced colorectal carcinoma or other CEA producing tumours
    • Francis, R.J. et al. A phase I trial of antibody directed enzyme prodrug therapy (ADEPT) in patients with advanced colorectal carcinoma or other CEA producing tumours. Br. J. Cancer 87, 600-607 (2002).
    • (2002) Br. J. Cancer , vol.87 , pp. 600-607
    • Francis, R.J.1
  • 101
    • 3042784498 scopus 로고    scopus 로고
    • Modifying an immunogenic epitope on a therapeutic protein: A step towards an improved system for antibody-directed enzyme prodrug therapy (ADEPT)
    • Mayer, A. et al. Modifying an immunogenic epitope on a therapeutic protein: a step towards an improved system for antibody-directed enzyme prodrug therapy (ADEPT). Br. J. Cancer 90, 2402-2410 (2004).
    • (2004) Br. J. Cancer , vol.90 , pp. 2402-2410
    • Mayer, A.1
  • 102
    • 18844371189 scopus 로고    scopus 로고
    • Generation of an intensely potent anthracycline by a monoclonal antibody-beta-galactosidase conjugate
    • Torgov, M.Y., Alley, S.C., Cerveny, C.G., Farquhar, D. & Senter, P.D. Generation of an intensely potent anthracycline by a monoclonal antibody-beta-galactosidase conjugate. Bioconjug. Chem. 16, 717-721 (2005).
    • (2005) Bioconjug. Chem. , vol.16 , pp. 717-721
    • Torgov, M.Y.1    Alley, S.C.2    Cerveny, C.G.3    Farquhar, D.4    Senter, P.D.5


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