|
[1] Perez H L, Cardarelli P M, Deshpande S, et al. Antibody-drug conjugates: current status and future directions. Drug Discov Today, 2013 Nov 15.
[Epub ahead of print].
[2] FDA. FDA news release: Pfizer voluntarily withdraws cancer treatment Mylotarg from U.S. market 2010,(http://www.fda.gov/%20NewsEvents/Newsroom/PressAnnouncements/ucm216448.htm).
[3] FDA. FDA news release: FDA approves Adcetris to treat two types of lymphoma.2011, (http://www.fda.gov/NewsEvents/Newsroom/PressAnnouncements/ucm268781.htm).
[4] FDA. FDA news release: FDA approves new treatment for late-stage breast cancer. 2013,(http://www.fda.gov/newsevents/newsroom/pressannouncements/ucm340704.htm).
[5] Gerber H P, Koehn F E, Abraham R T. The antibody-drug conjugate: an enabling modality for natural product-based cancer therapeutics. Nat Prod Rep, 2013, 30 (5):625-639.
[6] Beck A, Reichert J M. Antibody-drug conjugates: Present and future. MAbs, 2014, 6 (1): 15-17.
[7] Wahl A F, Klussman K, Thompson J D, et al. The anti-CD30 monoclonal antibody SGN-30 promotes growth arrest and DNA fragmentation in vitro and affects antitumor activity in models of Hodgkin's disease. Cancer Res, 2002, 62 (13): 3736-3742.
[8] Slamon D J, Clark G M, Wong S G, et al. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science, 1987, 235(4785):177-182.
[9] Thurber G M, Schmidt M M, Wittrup K D. Antibody tumor penetration: transport opposed by systemic and antigen-mediated clearance. Adv Drug Deliv Rev, 2008,60 (12): 1421-1434.
[10] Junttila T T, Li G, Parsons K, et al. Trastuzumab-DM1 (T-DM1) retains all the mechanisms of action of trastuzumab and efficiently inhibits growth of lapatinib insensitive breast cancer. Breast Cancer Res Treat, 2011, 128 (2):347-356.
[11] McDonagh C F, Kim K M, Turcott E, et al. Engineered anti-CD70 antibody-drug conjugate with increased therapeutic index. Mol Cancer Ther, 2008, 7(9):2913-2923.
[12] DiJoseph J F, Doughr M M, Kalyandrug L B, et al. Antitumor efficacy of a combination of CMC-544 (inotuzumab ozogamicin), a CD22-targeted cytotoxic immunoconjugate of calicheamicin, and rituximab against non-Hodgkin's B-cell lymphoma. Clin Cancer Res, 2006, 12(1):242-249.
[13] Ricart A D. Antibody-drug conjugates of calicheamicin derivative: gemtuzumab ozogamicin and inotuzumab ozogamicin. Clin Cancer Res, 2011, 17 (20): 6417-6427.
[14] DiJoseph J F, Armellino D C, Boghaert E R, et al. Antibody-targeted chemotherapy with CMC-544: a CD22-targeted immunoconjugate of calicheamicin for the treatment of B-lymphoid malignancies. Blood, 2004, 103(5): 1807-1817.
[15] Senter P D, Sievers E L. The discovery and development of brentuximab vedotin for use in relapsed Hodgkin lymphoma and systemic anaplastic large cell lymphoma. Nat Biotechnol, 2012, 30(7):631-637.
[16] Lewis Philips G D, Li G, Dugger D L, et al. Targeting HER2-positive breast cancer with transtuzumab-DM1, an antibody-cytotoxic drug conjugate. Cancer Res, 2008, 68(22):9280-9290.
[17] Alley S C, Benjamin D R, Jeffrey S C, et al. Contribution of linker stability to the activities of anticancer immunoconjugates. Bioconjug Chem, 2008, 19(3):759-765.
[18] Wang L, Amphlett G, Blattler W A, et al. Structural characterization of the maytansinoid-monoclonal antibody immunoconjugate, huN901-DM1, by mass spectrometry. Protein Sci, 2005, 14(9):2436-2446.
[19] Hamblett K J, Senter P D, Chace D F, et al. Effects of drug loading on the antitumor activity of a monoclonal antibody drug conjugate. Clin Cancer Res, 2004,10(20):7063-7070.
[20] Junutula J R, Raab H, Clark S, et al. Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index. Nat Biotechnol, 2008, 26(8):925-932.
[21] Axup J Y, Baijuri K M, Ritland M, et al. Synthesis of site-specific antibody-drug conjugates using unnatural amino acids. Proc Natl Acad Sci U S A, 2012, 109(40): 16101-16106.
[22] Hofer T, Skeffington L R, Chapman C M, et al. Molecularly defined antibody conjugation through a selenocysteine interface. Biochemistry, 2009,48(50):12047-12057.
[23] Stro P P, Liu S H, Dorywalska M, et al. Location matters: site of conjugation modulates stability and pharmacokinetics of antibody drug conjugates. Chem Biol, 2013, 20(2): 161-167.
[24] Senter P D. Potent antibody drug conjugates for cancer therapy. Curr Opin Chem Biol, 2009, 13(3):235-244.
[25] Trail P A, Willner D, Lasch S J, et al. Cure of xenografted human carcinomas by BR96-doxorubicin immunoconjugates. Science, 1993, 261(5118):212-215.
[26] Saleh M N, Sugarman S, Murray J, 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, 2000, 18(11):2282-2292.
[27] Casi G, Neri D. Antibody-drug conjugates: basic concepts, examples and future perspectives. J Control Release, 2012, 161(2):422-428.
[28] Alley S C, Okeley N M, Senter P D. Antibody-drug conjugates: targeted drug delivery for cancer. Curr Opin Chem Biol, 2010, 14(4):529-537.
[29] Teicher B A, Chari R V. Antibody conjugate therapeutics: challenges and potential. Clin Cancer Res, 2011, 17(20): 6389-6397.
[30] Hartley J A. The development of pyrrolobenzodiazepines as antitumour agents. Expert Opin Investig Drugs, 2011, 20(6): 733-744.
[31] Nguyen V T, Giannoni F, Dubois M F, et al. In vivo degradation of RNA polymerase II largest subunit triggered by alpha-amanitin. Nucleic Acids Res, 1996, 24(15):2924-2929.
[32] Magdalan J, Ostrowska A, Piotrowska A, et al. alpha-Amanitin induced apoptosis in primary cultured dog hepatocytes. Folia Histochem Cytobiol, 2010,48(1):58-62.
[33] Moldenhauer G, Salnikov A V, Luttgau S, et al. Therapeutic potential of amanitin-conjugated anti-epithelial cell adhesion molecule monoclonal antibody against pancreatic carcinoma. J Natl Cancer Inst, 2012, 104(8): 622-634.
[34] Sun M M, Beam K S, Cerveny C G, et al. Reduction-alkylation strategies for the modification of specific monoclonal antibody disulfides. Bioconjugate Chem, 2005,16 (5):1282-1290.
[35] McDonagh C F, Turcott E, Westendorf L, et al. Engineered antibody-drug conjugates with defined sites and stoichiometries of drug attachment. Protein Eng Des Sel, 2006, 19(7):299-307.
[36] Erickson H K, Park P U, Widdison W C, et al. Antibody-maytansinoid conjugates are activated in targeted cancer cells by lysosomal degradation and linker-dependent intracellular processing. Cancer Res, 2006, 66(8):4426-4433.
[37] Junutula J R, Raab H, Clark S, et al. Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index. Nat Biotechnol, 2008, 26(8):925-932.
[38] Fleming M S, Zhang W, Lambert J M,et al. A reversed-phase high-performance liquid chromatography method for analysis of monoclonal antibody-maytansinoid immunoconjugates. Anal Biochem, 2005, 340(2):272-278.
[39] Francisco J A, Cerveny C G, Meyer D L, et al. cAC10-Val-CitMMAE, an anti-CD30- monomethyl auristatin E conjugate with potent and selective anti-tumor activity. Blood, 2003, 102(4):1458-1465.
[40] Doronina S O, Mendelsohn B A, Bovee T D, et al. Enhance activity of monomethylauristatin F through monoclonal antibody delivery: effect of linker technology on efficacy and toxicity. Bioconjug Chem, 2006, 17(1):114-124.
[41] Laguzza B C, Nichols C L, Briggs S L, et al. New antitumor monoclonal antibody-vinca conjugates LY203725 and related compounds: design, preparation, and representative in vivo activity. J Med Chem, 1989, 32(3):548-555.
[42] Phillips G D L, Li G, Dugger D L, et al. Targeting HER2-positive breast cancer with trastuzumab-DM1, an antibody-cytotoxic drug conjugate. Cancer Res, 2008, 68(22):9280-9290.
[43] Sanderson R J, Hering M A, James S F, et al. In vivo drug-linker stability of anti-CD30 dipeptide-linked auristatin immunoconjugate. Clin Cancer Res, 2005, 11(2 Pt 1):843-852.
[44] Xu K, Saad O, Baudys J, et al. Bioanalytical strategies for antibody drug conjugate (ADC) biopharmaceutical development: characterization of trastuzumab-MCC-DM1 in plasma by affinity mass spectrometry. J Am Soc Mass Spec, 2007, 18(5): S11-S15.
[45] Valliere-Douglass J F, McFee W A, Salas-Solano O. Native intact mass determination of antibodies conjugated with monomethyl auristatin E and F at interchain cysteine residues. Anal Chem, 2012, 84(6):2843-2849.
[46] Hamblett K J, Senter P D, Chace D F, et al. Effects of drug loading on the anti-tumor activity of a monoclonal antibody drug conjugate. Clin Cancer Res, 2004, 10(20):7063-7070.
[47] Siegel M M, Hollander I J, Hamann P R, et al. Matrix-assisted UV-laser desorption/ionization mass spectrometric analysis of monoclonal antibodies for the determination of carbohydrate, conjugated chelator, and conjugated drug content. Anal Chem, 1991, 63(21):2470-2481.
[48] Gazzano-Santoro H, Ralph P, Ryskamp T C, et al. A non-radioactive complementdependent cytotoxicity assay for anti-CD20 monoclonal antibody. J Immunol Methods, 1997, 202(2): 163-171.
[49] Ferrone S, Cooper N R, Pellegrino M A, et al. The lymphocytotoxic reaction: the mechanism of rabbit complement action. J Immunol, 1971, 107(4):939-947.
[50] Sharkey R M, Govindan S V, Cardillo T M, et al. Epratuzumab-SN-38: a new antibody-drug conjugate for the therapy of hematologic malignancies. Mol Cancer Ther, 2012, 11(1):224-234.
[51] 高凯, 徐志凯, 任跃明, 等. 关于我国药典单克隆抗体类生物治疗药物总论的思考. 中国生物工程杂志, 2014, 34(1):127-134. Gao K, Xu Z K, Ren Y M, et al. Points to consider for the general monograph of monoclonal antibody based biotherapeutics in Chinese Pharamacopeia. China Biotechnology, 2014, 34(1): 127-134.
|
