메뉴 건너뛰기




Volumn 7, Issue 4, 2010, Pages 461-478

The use of single chain Fv as targeting agents for immunoliposomes: An update on immunoliposomal drugs for cancer treatment

Author keywords

Biodistribution; Cancer; Drug delivery; Fab ; Immunoliposomes; Liposomes; Monoclonal antibodies; Pharmacokinetics; ScFv

Indexed keywords

AMPHOTERICIN B LIPID COMPLEX; CARCINOEMBRYONIC ANTIBODY; CD19 ANTIBODY; CD19 ANTIGEN; CD22 ANTIBODY; CD45 ANTIBODY; CIPROFLOXACIN; CYSTEINE; CYTARABINE; DAUNORUBICIN; DIOLEOYLPHOSPHATIDYLETHANOLAMINE; DOXORUBICIN; FLUIDOSOME TOBRAMYCIN; FOLATE BINDING PROTEIN; HYDRAZIDE; IBRITUMOMAB TIUXETAN; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOLIPOSOME; MACROGOL; MALEIMIDE; MARQIBO; MESOTHELIN ANTIBODY; MONOCLONAL ANTIBODY; NITRILOTRIACETATE NICKEL; OKT 3; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; TOBRAMYCIN; TOPOTECAN; TRASTUZUMAB; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; UNINDEXED DRUG; VINBLASTINE; VINCRISTINE;

EID: 77949900348     PISSN: 17425247     EISSN: None     Source Type: Journal    
DOI: 10.1517/17425240903579963     Document Type: Review
Times cited : (78)

References (165)
  • 1
    • 85012373035 scopus 로고
    • Diffusion of univalent ions across the lamellae of swollen phospholipids
    • Bangham AD, Standish MM, Watkins JC. Diffusion of univalent ions across the lamellae of swollen phospholipids. J Mol Biol 1965;13:238-252
    • (1965) J Mol Biol , vol.13 , pp. 238-252
    • Bangham, A.D.1    Standish, M.M.2    Watkins, J.C.3
  • 2
    • 1642362625 scopus 로고    scopus 로고
    • Drug delivery systems: Entering the mainstream
    • Allen TM, Cullis PR. Drug delivery systems: entering the mainstream. Science 2004;303:1818-1822
    • (2004) Science , vol.303 , pp. 1818-1822
    • Allen, T.M.1    Cullis, P.R.2
  • 3
    • 0028605289 scopus 로고
    • AmBisome targeting to fungal infections
    • Adler-Moore J. AmBisome targeting to fungal infections. Bone Marrow Transplant 1994;14(Suppl 5):S3-7
    • (1994) Bone Marrow Transplant , vol.14 , Issue.SUPPL. 5
    • Adler-Moore, J.1
  • 4
    • 0035282073 scopus 로고    scopus 로고
    • Reduced cardiotoxicity and preserved antitumor efficacy of liposome-encapsulated doxorubicin and cyclophosphamide compared with conventional doxorubicin and cyclophosphamide in a randomized, multicenter trial of metastatic breast cancer
    • Batist G, Ramakrishnan G, Rao CS, et al. Reduced cardiotoxicity and preserved antitumor efficacy of liposome-encapsulated doxorubicin and cyclophosphamide compared with conventional doxorubicin and cyclophosphamide in a randomized, multicenter trial of metastatic breast cancer. J Clin Oncol 2001;19:1444-1454
    • (2001) J Clin Oncol , vol.19 , pp. 1444-1454
    • Batist, G.1    Ramakrishnan, G.2    Rao, C.S.3
  • 5
    • 0031036426 scopus 로고    scopus 로고
    • AIDS-related Kaposi's sarcoma after failure of standard chemotherapy
    • Northfelt DW, Dezube BJ, Thommes JA, et al. Efficacy of pegylated-liposomal doxorubicin in the treatment of
    • (1997) J Clin Oncol , vol.15 , pp. 653-659
    • Northfelt, D.W.1    Dezube, B.J.2    Thommes, J.A.3
  • 6
    • 0027316032 scopus 로고
    • Liposomal daunorubicin treatment of HIV-associated Kaposi's sarcoma
    • Presant CA, Scolaro M, Kennedy P, et al. Liposomal daunorubicin treatment of HIV-associated Kaposi's sarcoma. Lancet 1993;341(8855):1242-1243
    • (1993) Lancet , vol.341 , Issue.8855 , pp. 1242-1243
    • Presant, C.A.1    Scolaro, M.2    Kennedy, P.3
  • 7
    • 0032711629 scopus 로고    scopus 로고
    • A randomized controlled trial comparing intrathecal sustained-release cytarabine (DepoCyt) to intrathecal methotrexate in patients with neoplastic meningitis from solid tumors
    • Glantz MJ, Jaeckle KA, Chamberlain MC, et al. A randomized controlled trial comparing intrathecal sustained-release cytarabine (DepoCyt) to intrathecal methotrexate in patients with neoplastic meningitis from solid tumors. Clin Cancer Res 1999;5:3394-3402
    • (1999) Clin Cancer Res , vol.5 , pp. 3394-3402
    • Glantz, M.J.1    Jaeckle, K.A.2    Chamberlain, M.C.3
  • 8
    • 18144419703 scopus 로고    scopus 로고
    • Liposome-encapsulated vincristine, vinblastine and vinorelbine: A comparative study of drug loading and retention
    • Zhigaltsev IV, Maurer N, Akhong QF, et al. Liposome-encapsulated vincristine, vinblastine and vinorelbine: a comparative study of drug loading and retention. J Control Release 2005;104(1):103-111
    • (2005) J Control Release , vol.104 , Issue.1 , pp. 103-111
    • Zhigaltsev, I.V.1    Maurer, N.2    Akhong, Q.F.3
  • 9
    • 0032781420 scopus 로고    scopus 로고
    • Evaluation of the pulmonary and systemic immunogenicity of Fluidosomes, a fluid liposomal-tobramycin formulation for the treatment of chronic infections in lungs
    • Sachetelli S, Beaulac C, Riffon R, Lagace J. Evaluation of the pulmonary and systemic immunogenicity of Fluidosomes, a fluid liposomal-tobramycin formulation for the treatment of chronic infections in lungs. Biochim Biophys Acta 1999;1428(2-3):334-340
    • (1999) Biochim Biophys Acta , vol.1428 , Issue.2-3 , pp. 334-340
    • Sachetelli, S.1    Beaulac, C.2    Riffon, R.3    Lagace, J.4
  • 10
    • 27644447423 scopus 로고    scopus 로고
    • Spray-freeze-dried liposomal ciprofloxacin powder for inhaled aerosol drug delivery
    • Sweeney LG, Wang Z, Loebenberg R, et al. Spray-freeze-dried liposomal ciprofloxacin powder for inhaled aerosol drug delivery. Int J Pharm 2005;305(1-2):180-185
    • (2005) Int J Pharm , vol.305 , Issue.1-2 , pp. 180-185
    • Sweeney, L.G.1    Wang, Z.2    Loebenberg, R.3
  • 11
    • 10744233861 scopus 로고    scopus 로고
    • Vascular damage and anti-angiogenic effects of tumor vessel-targeted liposomal chemotherapy
    • Pastorino F, Brignole C, Marimpietri D, et al. Vascular damage and anti-angiogenic effects of tumor vessel-targeted liposomal chemotherapy. Cancer Res 2003;63(21):7400-7409
    • (2003) Cancer Res , vol.63 , Issue.21 , pp. 7400-7409
    • Pastorino, F.1    Brignole, C.2    Marimpietri, D.3
  • 12
    • 0028794831 scopus 로고
    • Folate-mediated tumor cell targeting of liposome-entrapped doxorubicin in vitro
    • Lee RJ, Low PS. Folate-mediated tumor cell targeting of liposome-entrapped doxorubicin in vitro. Biochim Biophys Acta 1995;1233:134-144
    • (1995) Biochim Biophys Acta , vol.1233 , pp. 134-144
    • Lee, R.J.1    Low, P.S.2
  • 13
    • 0030983406 scopus 로고    scopus 로고
    • Modulation of doxorubicin resistance in a doxorubicin-resistant human leukaemia cell by an immunoliposome targeting transferrin receptor
    • Suzuki S, Inoue K, Hongoh A, et al. Modulation of doxorubicin resistance in a doxorubicin-resistant human leukaemia cell by an immunoliposome targeting transferrin receptor. Br J Cancer 1997;76(1):83-89
    • (1997) Br J Cancer , vol.76 , Issue.1 , pp. 83-89
    • Suzuki, S.1    Inoue, K.2    Hongoh, A.3
  • 14
    • 0022858683 scopus 로고
    • A new concept for macromolecular therapeutics in cancer chemotherapy; Mechanism of tumoritropic accumulation of proteins and the antitumor agent SMANCS
    • Matsumura Y, Maeda H. A new concept for macromolecular therapeutics in cancer chemotherapy; mechanism of tumoritropic accumulation of proteins and the antitumor agent SMANCS. Cancer Res 1986;46(12 Pt 1):6387-6392
    • (1986) Cancer Res , vol.46 , Issue.12 PART 1 , pp. 6387-6392
    • Matsumura, Y.1    Maeda, H.2
  • 15
    • 0035300546 scopus 로고    scopus 로고
    • Characterization of the effect of hyperthermia on nanoparticle extravasation from tumor vasculature
    • Kong G, Braun RD, Dewhirst MW. Characterization of the effect of hyperthermia on nanoparticle extravasation from tumor vasculature. Cancer Res 2001;61(7):3027-3032
    • (2001) Cancer Res , vol.61 , Issue.7 , pp. 3027-3032
    • Kong, G.1    Braun, R.D.2    Dewhirst, M.W.3
  • 16
    • 0034000453 scopus 로고    scopus 로고
    • Tumor vascular permeability and the EPR effect in macromolecular therapeutics: A review
    • Maeda H, Wu J, Sawa T, et al. Tumor vascular permeability and the EPR effect in macromolecular therapeutics: a review. J Control Release 2000;65:271-284
    • (2000) J Control Release , vol.65 , pp. 271-284
    • Maeda, H.1    Wu, J.2    Sawa, T.3
  • 17
    • 24644437854 scopus 로고    scopus 로고
    • Ligand-targeted liposomes for cancer treatment
    • Sapra P, Tyagi P, Allen TM. Ligand-targeted liposomes for cancer treatment. Curr Drug Deliv 2005;2(4):369-381
    • (2005) Curr Drug Deliv , vol.2 , Issue.4 , pp. 369-381
    • Sapra, P.1    Tyagi, P.2    Allen, T.M.3
  • 18
    • 0036781811 scopus 로고    scopus 로고
    • Ligand-targeted therapeutics in anticancer therapy
    • Allen TM. Ligand-targeted therapeutics in anticancer therapy. Nat Rev Cancer 2002;2(10):750-763
    • (2002) Nat Rev Cancer , vol.2 , Issue.10 , pp. 750-763
    • Allen, T.M.1
  • 19
    • 11144300731 scopus 로고    scopus 로고
    • Future directions of liposome-and immunoliposome-based cancer therapeutics
    • Park JW, Benz CC, Martin FJ. Future directions of liposome-and immunoliposome-based cancer therapeutics. Semin Oncol 2004;31(6 Suppl 13):196-205
    • (2004) Semin Oncol , vol.31 , Issue.6 SUPPL. 13 , pp. 196-205
    • Park, J.W.1    Benz, C.C.2    Martin, F.J.3
  • 20
    • 32544452539 scopus 로고    scopus 로고
    • Immunoliposomes for cancer therapy
    • Kontermann RE. Immunoliposomes for cancer therapy. Curr Opin Mol Ther 2006;8(1):39-45
    • (2006) Curr Opin Mol Ther , vol.8 , Issue.1 , pp. 39-45
    • Kontermann, R.E.1
  • 21
    • 33846889329 scopus 로고    scopus 로고
    • Poly(amino acid)s: Promising enzymatically degradable stealth coatings for liposomes
    • Romberg B, Metselaar JM, Baranyi L, et al. Poly(amino acid)s: promising enzymatically degradable stealth coatings for liposomes. Int J Pharm 2007;331(2):186-189
    • (2007) Int J Pharm , vol.331 , Issue.2 , pp. 186-189
    • Romberg, B.1    Metselaar, J.M.2    Baranyi, L.3
  • 22
    • 0026352832 scopus 로고
    • Sterically stabilized liposomes: Improvements in pharmacokinetics and antitumor therapeutic efficacy
    • Papahadjopoulos D, Allen TM, Gabizon A, et al. Sterically stabilized liposomes: improvements in pharmacokinetics and antitumor therapeutic efficacy. Proc Natl Acad Sci USA 1991;88(24):11460-11464
    • (1991) Proc Natl Acad Sci USA , vol.88 , Issue.24 , pp. 11460-11464
    • Papahadjopoulos, D.1    Allen, T.M.2    Gabizon, A.3
  • 23
    • 0028349925 scopus 로고
    • Prolonged circulation time and enhanced accumulation in malignant exudates of doxorubicin encapsulated in polyethylene-glycol coated liposomes
    • Gabizon A, Catane R, Uziely B, et al. Prolonged circulation time and enhanced accumulation in malignant exudates of doxorubicin encapsulated in polyethylene-glycol coated liposomes. Cancer Res 1994;54:987-992
    • (1994) Cancer Res , vol.54 , pp. 987-992
    • Gabizon, A.1    Catane, R.2    Uziely, B.3
  • 24
    • 33750715718 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of lipidic nano-particles in cancer
    • Allen TM, Cheng WW, Hare JI, Laginha KM. Pharmacokinetics and pharmacodynamics of lipidic nano-particles in cancer. Anticancer Agents Med Chem 2006;6(6):513-523
    • (2006) Anticancer Agents Med Chem , vol.6 , Issue.6 , pp. 513-523
    • Allen, T.M.1    Cheng, W.W.2    Hare, J.I.3    Laginha, K.M.4
  • 25
    • 2442551191 scopus 로고    scopus 로고
    • Drug release rate influences the pharmacokinetics, biodistribution, therapeutic activity, and toxicity of pegylated liposomal doxorubicin formulations in murine breast cancer
    • Charrois GJR, Allen TM. Drug release rate influences the pharmacokinetics, biodistribution, therapeutic activity, and toxicity of pegylated liposomal doxorubicin formulations in murine breast cancer. Biochim Biophys Acta 2004;1663(1-2):167-177
    • (2004) Biochim Biophys Acta , vol.1663 , Issue.1-2 , pp. 167-177
    • Charrois, G.J.R.1    Allen, T.M.2
  • 26
    • 18244362593 scopus 로고    scopus 로고
    • Anti-CD19-targeted liposomal doxorubicin improves the therapeutic efficacy in murine B-cell lymphoma and ameliorates the toxicity of liposomes with varying drug release rates
    • Allen TM, Mumbengegwi DR, Charrois GJ. Anti-CD19-targeted liposomal doxorubicin improves the therapeutic efficacy in murine B-cell lymphoma and ameliorates the toxicity of liposomes with varying drug release rates. Clin Cancer Res 2005;11:3567-3573
    • (2005) Clin Cancer Res , vol.11 , pp. 3567-3573
    • Allen, T.M.1    Mumbengegwi, D.R.2    Charrois, G.J.3
  • 27
    • 33646707051 scopus 로고    scopus 로고
    • Therapeutically optimized rates of drug release can be achieved by varying the drug-to-lipid ratio in liposomal vincristine formulations
    • Johnston MJ, Semple SC, Klimuk SK, et al. Therapeutically optimized rates of drug release can be achieved by varying the drug-to-lipid ratio in liposomal vincristine formulations. Biochim Biophys Acta 2006;1758(1):55-64
    • (2006) Biochim Biophys Acta , vol.1758 , Issue.1 , pp. 55-64
    • Johnston, M.J.1    Semple, S.C.2    Klimuk, S.K.3
  • 28
    • 0037115543 scopus 로고    scopus 로고
    • Internalizing antibodies are necessary for improved therapeutic efficacy of antibody-targeted liposomal drugs
    • Sapra P, Allen TM. Internalizing antibodies are necessary for improved therapeutic efficacy of antibody-targeted liposomal drugs. Cancer Res 2002;62(24):7190-7194
    • (2002) Cancer Res , vol.62 , Issue.24 , pp. 7190-7194
    • Sapra, P.1    Allen, T.M.2
  • 29
    • 33746172167 scopus 로고    scopus 로고
    • Antibody targeting of long-circulating lipidic nanoparticles does not increase tumor localization but does increase internalization in animal models
    • Kirpotin DB, Drummond DC, Shao Y, et al. Antibody targeting of long-circulating lipidic nanoparticles does not increase tumor localization but does increase internalization in animal models. Cancer Res 2006;66(13):6732-6740
    • (2006) Cancer Res , vol.66 , Issue.13 , pp. 6732-6740
    • Kirpotin, D.B.1    Drummond, D.C.2    Shao, Y.3
  • 30
    • 35848955441 scopus 로고    scopus 로고
    • Anti-CD166 single chain antibody-mediated intracellular delivery of liposomal drugs to prostate cancer cells
    • Roth A, Drummond DC, Conrad F, et al. Anti-CD166 single chain antibody-mediated intracellular delivery of liposomal drugs to prostate cancer cells. Mol Cancer Ther 2007;6(10):2737-2746
    • (2007) Mol Cancer Ther , vol.6 , Issue.10 , pp. 2737-2746
    • Roth, A.1    Drummond, D.C.2    Conrad, F.3
  • 31
    • 33750552967 scopus 로고    scopus 로고
    • Targeting liposomal chemotherapy via both tumor cell-specific and tumor vasculature-specific ligands potentiates therapeutic efficacy
    • Pastorino F, Brignole C, Di Paolo D, et al. Targeting liposomal chemotherapy via both tumor cell-specific and tumor vasculature-specific ligands potentiates therapeutic efficacy. Cancer Res 2006;66(20):10073-10082
    • (2006) Cancer Res , vol.66 , Issue.20 , pp. 10073-10082
    • Pastorino, F.1    Brignole, C.2    Di Paolo, D.3
  • 32
    • 58149350356 scopus 로고    scopus 로고
    • Enhanced antitumor efficacy of clinical-grade vasculature-targeted liposomal doxorubicin
    • Pastorino F, Di Paolo D, Piccardi F, et al. Enhanced antitumor efficacy of clinical-grade vasculature-targeted liposomal doxorubicin. Clin Cancer Res 2008;14(22):7320-7329
    • (2008) Clin Cancer Res , vol.14 , Issue.22 , pp. 7320-7329
    • Pastorino, F.1    Di Paolo, D.2    Piccardi, F.3
  • 33
    • 0036554863 scopus 로고    scopus 로고
    • Anti-HER2 immunoliposomes: Enhanced efficacy attributable to targeted delivery
    • Park JW, Hong K, Kirpotin DB, et al. Anti-HER2 immunoliposomes: Enhanced efficacy attributable to targeted delivery. Clin Cancer Res 2002;8(4):1172-1181
    • (2002) Clin Cancer Res , vol.8 , Issue.4 , pp. 1172-1181
    • Park, J.W.1    Hong, K.2    Kirpotin, D.B.3
  • 34
    • 35648943224 scopus 로고    scopus 로고
    • Effects on hepatocellular carcinoma of doxorubicin-loaded immunoliposomes designed to target the VEGFR-2
    • Roth P, Hammer C, Piguet AC, et al. Effects on hepatocellular carcinoma of doxorubicin-loaded immunoliposomes designed to target the VEGFR-2. J Drug Target 2007;15(9):623-631
    • (2007) J Drug Target , vol.15 , Issue.9 , pp. 623-631
    • Roth, P.1    Hammer, C.2    Piguet, A.C.3
  • 35
    • 1842478453 scopus 로고    scopus 로고
    • Improved outcome when B-cell lymphoma is treated with combinations of immunoliposomal anticancer drugs targeted to both the CD19 and CD20 epitopes
    • Sapra P, Allen TM. Improved outcome when B-cell lymphoma is treated with combinations of immunoliposomal anticancer drugs targeted to both the CD19 and CD20 epitopes. Clin Cancer Res 2004;10(7):2530-2537
    • (2004) Clin Cancer Res , vol.10 , Issue.7 , pp. 2530-2537
    • Sapra, P.1    Allen, T.M.2
  • 36
    • 34248172836 scopus 로고    scopus 로고
    • In vitro efficacy of a sterically stabilized immunoliposomes targeted to membrane type 1 matrix metalloproteinase (MT1-MMP)
    • Atobe K, Ishida T, Ishida E, et al. In vitro efficacy of a sterically stabilized immunoliposomes targeted to membrane type 1 matrix metalloproteinase (MT1-MMP). Biol Pharm Bull 2007;30(5):972-978
    • (2007) Biol Pharm Bull , vol.30 , Issue.5 , pp. 972-978
    • Atobe, K.1    Ishida, T.2    Ishida, E.3
  • 37
    • 33845679807 scopus 로고    scopus 로고
    • Surface-modified LPD nanoparticles for tumor targeting
    • Li SD, Huang L. Surface-modified LPD nanoparticles for tumor targeting. Ann NY Acad Sci 2006;1082:1-8
    • (2006) Ann NY Acad Sci , vol.1082 , pp. 1-8
    • Li, S.D.1    Huang, L.2
  • 38
    • 67651183769 scopus 로고    scopus 로고
    • Folate-mediated intracellular drug delivery increases the anticancer efficacy of nanoparticulate formulation of arsenic trioxide
    • Chen H, Ahn R, Van den Bossche J, et al. Folate-mediated intracellular drug delivery increases the anticancer efficacy of nanoparticulate formulation of arsenic trioxide. Mol Cancer Ther 2009;8(7):1955-1963
    • (2009) Mol Cancer Ther , vol.8 , Issue.7 , pp. 1955-1963
    • Chen, H.1    Ahn, R.2    Van Den Bossche, J.3
  • 39
    • 36049008819 scopus 로고    scopus 로고
    • Effective anti-tumor activity of oxaliplatin encapsulated in transferrin-PEG-liposome
    • Suzuki R, Takizawa T, Kuwata Y, et al. Effective anti-tumor activity of oxaliplatin encapsulated in transferrin-PEG-liposome. Int J Pharm 2008;346(1-2):143-150
    • (2008) Int J Pharm , vol.346 , Issue.1-2 , pp. 143-150
    • Suzuki, R.1    Takizawa, T.2    Kuwata, Y.3
  • 40
    • 0036928350 scopus 로고    scopus 로고
    • Rituximab-mediated sensitization of B-non-Hodgkin's lymphoma (NHL) to cytotoxicity induced by paclitaxel, gemcitabine, and vinorelbine
    • Emmanouilides C, Jazirehi AR, Bonavida B. Rituximab-mediated sensitization of B-non-Hodgkin's lymphoma (NHL) to cytotoxicity induced by paclitaxel, gemcitabine, and vinorelbine. Cancer Biother Radiopharm 2002;17(6):621-630
    • (2002) Cancer Biother Radiopharm , vol.17 , Issue.6 , pp. 621-630
    • Emmanouilides, C.1    Jazirehi, A.R.2    Bonavida, B.3
  • 41
    • 16444363534 scopus 로고    scopus 로고
    • Cellular and molecular signal transduction pathways modulated by rituximab (rituxan, anti-CD20 mAb) in non-Hodgkin's lymphoma: Implications in chemosensitization and therapeutic intervention
    • Jazirehi AR, Bonavida B. Cellular and molecular signal transduction pathways modulated by rituximab (rituxan, anti-CD20 mAb) in non-Hodgkin's lymphoma: implications in chemosensitization and therapeutic intervention. Oncogene 2005;24(13):2121-2143
    • (2005) Oncogene , vol.24 , Issue.13 , pp. 2121-2143
    • Jazirehi, A.R.1    Bonavida, B.2
  • 42
    • 24144455629 scopus 로고    scopus 로고
    • Pharmacokinetics and concentration-effect relationships of therapeutic monoclonal antibodies and fusion proteins
    • Ternant D, Paintaud G. Pharmacokinetics and concentration-effect relationships of therapeutic monoclonal antibodies and fusion proteins. Expert Opin Biol Ther 2005;5(Suppl 1):S37-47
    • (2005) Expert Opin Biol Ther , vol.5 , Issue.SUPPL. 1
    • Ternant, D.1    Paintaud, G.2
  • 43
    • 0018923144 scopus 로고
    • Mast cell membrane antigens and Fc receptors in anaphylaxis. II. Functionally distinct receptors for IgG and for IgE on mouse mast cells
    • Daeron M, Prouvost-Danon A, Voisin GA. Mast cell membrane antigens and Fc receptors in anaphylaxis. II. Functionally distinct receptors for IgG and for IgE on mouse mast cells. Cell Immunol 1980;49(1):178-189
    • (1980) Cell Immunol , vol.49 , Issue.1 , pp. 178-189
    • Daeron, M.1    Prouvost-Danon, A.2    Voisin, G.A.3
  • 44
    • 0032851961 scopus 로고    scopus 로고
    • Nonclinical studies addressing the mechanism of action of trastuzumab (Herceptin)
    • Sliwkowski MX, Lofgren JA, Lewis GD, et al. Nonclinical studies addressing the mechanism of action of trastuzumab (Herceptin). Semin Oncol 1999;26(4 Suppl 12):60-70
    • (1999) Semin Oncol , vol.26 , Issue.4 SUPPL. 12 , pp. 60-70
    • Sliwkowski, M.X.1    Lofgren, J.A.2    Lewis, G.D.3
  • 45
    • 0038347495 scopus 로고    scopus 로고
    • Renaissance of cancer therapeutic antibodies
    • Glennie MJ, van de Winkel JG. Renaissance of cancer therapeutic antibodies. Drug Discov Today 2003;8(11):503-510
    • (2003) Drug Discov Today , vol.8 , Issue.11 , pp. 503-510
    • Glennie, M.J.1    Van De Winkel, J.G.2
  • 46
    • 0346880530 scopus 로고    scopus 로고
    • Clonal analysis of a human antimouse antibody (HAMA) response
    • Thorpe SJ, Turner C, Heath A, et al. Clonal analysis of a human antimouse antibody (HAMA) response. Scand J Immunol 2003;57(1):85-92
    • (2003) Scand J Immunol , vol.57 , Issue.1 , pp. 85-92
    • Thorpe, S.J.1    Turner, C.2    Heath, A.3
  • 47
    • 27144449009 scopus 로고    scopus 로고
    • Monoclonal antibody therapy of cancer
    • Adams GP, Weiner LM. Monoclonal antibody therapy of cancer. Nat Biotechnol 2005;23(9):1147-1157
    • (2005) Nat Biotechnol , vol.23 , Issue.9 , pp. 1147-1157
    • Adams, G.P.1    Weiner, L.M.2
  • 48
    • 17644386490 scopus 로고    scopus 로고
    • Development of humanized antibodies as cancer therapeutics
    • Qu Z, Griffiths GL, Wegener WA, et al. Development of humanized antibodies as cancer therapeutics. Methods 2005;36(1):84-95
    • (2005) Methods , vol.36 , Issue.1 , pp. 84-95
    • Qu, Z.1    Griffiths, G.L.2    Wegener, W.A.3
  • 49
    • 0021716682 scopus 로고
    • Chimeric human antibody molecules: Mouse antigen-binding domains with human constant region domains
    • Morrison SL, Johnson MJ, Herzenberg LA, Oi VT. Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains. Proc Natl Acad Sci USA 1984;81(21):6851-6855
    • (1984) Proc Natl Acad Sci USA , vol.81 , Issue.21 , pp. 6851-6855
    • Morrison, S.L.1    Johnson, M.J.2    Herzenberg, L.A.3    Oi, V.T.4
  • 50
    • 0022558297 scopus 로고
    • Replacing the complementarity-determining regions in a human antibody with those from a mouse
    • Jones PT, Dear PH, Foote J, et al. Replacing the complementarity- determining regions in a human antibody with those from a mouse. Nature 1986;321(6069):522-525
    • (1986) Nature , vol.321 , Issue.6069 , pp. 522-525
    • Jones, P.T.1    Dear, P.H.2    Foote, J.3
  • 51
    • 73349104417 scopus 로고    scopus 로고
    • A human monoclonal antibody drug and target discovery platform for B-cell chronic lymphocytic leukemia based on allogeneic hematopoietic stem cell transplantation and phage display
    • Baskar S, Suschak JM, Samija I, et al. A human monoclonal antibody drug and target discovery platform for B-cell chronic lymphocytic leukemia based on allogeneic hematopoietic stem cell transplantation and phage display. Blood 2009;114(20):4494-4502
    • (2009) Blood , vol.114 , Issue.20 , pp. 4494-4502
    • Baskar, S.1    Suschak, J.M.2    Samija, I.3
  • 52
    • 33747788413 scopus 로고    scopus 로고
    • High levels of human anti-human antibodies to adalimumab in a patient not responding to adalimumab treatment
    • Bartelds GM, Wolbink GJ, Stapel S, et al. High levels of human anti-human antibodies to adalimumab in a patient not responding to adalimumab treatment. Ann Rheum Dis 2006;65(9):1249-1250
    • (2006) Ann Rheum Dis , vol.65 , Issue.9 , pp. 1249-1250
    • Bartelds, G.M.1    Wolbink, G.J.2    Stapel, S.3
  • 53
    • 34548192177 scopus 로고    scopus 로고
    • Decreased clinical response to infliximab in ankylosing spondylitis is correlated with anti-infliximab formation
    • de Vries MK, Wolbink GJ, Stapel SO, et al. Decreased clinical response to infliximab in ankylosing spondylitis is correlated with anti-infliximab formation. Ann Rheum Dis 2007;66(9):1252-1254
    • (2007) Ann Rheum Dis , vol.66 , Issue.9 , pp. 1252-1254
    • De Vries, M.K.1    Wolbink, G.J.2    Stapel, S.O.3
  • 54
    • 77949848609 scopus 로고    scopus 로고
    • Anti-infliximab and anti-adalimumab antibodies in relation to response to adalimumab in infliximab switchers and anti-TNF naive patients: A cohort study
    • [Epub ahead of print]
    • Bartelds GM, Wijbrandts CA, Nurmohamed MT, et al. Anti-infliximab and anti-adalimumab antibodies in relation to response to adalimumab in infliximab switchers and anti-TNF naive patients: a cohort study. Ann Rheum Dis 2009 [Epub ahead of print]
    • (2009) Ann Rheum Dis
    • Bartelds, G.M.1    Wijbrandts, C.A.2    Nurmohamed, M.T.3
  • 55
    • 38549093524 scopus 로고    scopus 로고
    • Targeted delivery of anti-CD19 liposomal doxorubicin in B-cell lymphoma: A comparison of whole monoclonal antibody, Fab' fragments and single chain Fv
    • Cheng WW, Allen TM. Targeted delivery of anti-CD19 liposomal doxorubicin in B-cell lymphoma: a comparison of whole monoclonal antibody, Fab' fragments and single chain Fv. J Control Release 2008;126(1):50-58
    • (2008) J Control Release , vol.126 , Issue.1 , pp. 50-58
    • Cheng, W.W.1    Allen, T.M.2
  • 56
    • 0031022084 scopus 로고    scopus 로고
    • High level production of soluble single chain antibodies in small-scale Escherichia coli cultures
    • Kipriyanov SM, Moldenhauer G, Little M. High level production of soluble single chain antibodies in small-scale Escherichia coli cultures. J Immunol Methods 1997; 200(1-2):69-77
    • (1997) J Immunol Methods , vol.200 , Issue.1-2 , pp. 69-77
    • Kipriyanov, S.M.1    Moldenhauer, G.2    Little, M.3
  • 57
    • 0036900866 scopus 로고    scopus 로고
    • Antibody manufacture in transgenic animals and comparisons with other systems
    • Houdebine LM. Antibody manufacture in transgenic animals and comparisons with other systems. Curr Opin Biotechnol 2002;13(6):625-629
    • (2002) Curr Opin Biotechnol , vol.13 , Issue.6 , pp. 625-629
    • Houdebine, L.M.1
  • 58
    • 0034285785 scopus 로고    scopus 로고
    • Phage display of antibody fragments
    • Pini A, Bracci L. Phage display of antibody fragments. Curr Protein Pept Sci 2000;1(2):155-169
    • (2000) Curr Protein Pept Sci , vol.1 , Issue.2 , pp. 155-169
    • Pini, A.1    Bracci, L.2
  • 59
    • 0031035521 scopus 로고    scopus 로고
    • Specific detection of his-tagged proteins with recombinant anti-His tag scFv-phosphatase or scFv-phage fusions
    • Lindner P, Bauer K, Krebber A, et al. Specific detection of his-tagged proteins with recombinant anti-His tag scFv-phosphatase or scFv-phage fusions. Biotechniques 1997;22(1):140-149
    • (1997) Biotechniques , vol.22 , Issue.1 , pp. 140-149
    • Lindner, P.1    Bauer, K.2    Krebber, A.3
  • 60
    • 0035545989 scopus 로고    scopus 로고
    • Effects of humanization and gene shuffling on immunogenicity and antigen binding of anti-TAG-72 single-chain Fvs
    • Pavlinkova G, Colcher D, Booth BJ, et al. Effects of humanization and gene shuffling on immunogenicity and antigen binding of anti-TAG-72 single-chain Fvs. Int J Cancer 2001;94:717-726
    • (2001) Int J Cancer , vol.94 , pp. 717-726
    • Pavlinkova, G.1    Colcher, D.2    Booth, B.J.3
  • 61
    • 0042838162 scopus 로고    scopus 로고
    • Humanization of predicted T-cell epitopes reduces the immunogenicity of chimeric antibodies: New evidence supporting a simple method
    • Roque-Navarro L, Mateo C, Lombardero J, et al. Humanization of predicted T-cell epitopes reduces the immunogenicity of chimeric antibodies: new evidence supporting a simple method. Hybrid Hybridomics 2003;22(4):245-257
    • (2003) Hybrid Hybridomics , vol.22 , Issue.4 , pp. 245-257
    • Roque-Navarro, L.1    Mateo, C.2    Lombardero, J.3
  • 62
    • 1042290308 scopus 로고    scopus 로고
    • Improved therapeutic responses in a xenograft model of human B-lymphoma (Namalwa) for liposomal vincristine versus liposomal doxorubicin targeted via anti-CD19 IgG2a or Fab' fragments
    • Sapra P, Moase EH, Ma J, Allen TM. Improved therapeutic responses in a xenograft model of human B-lymphoma (Namalwa) for liposomal vincristine versus liposomal doxorubicin targeted via anti-CD19 IgG2a or Fab' fragments. Clin Cancer Res 2004;10(3):1100-1111
    • (2004) Clin Cancer Res , vol.10 , Issue.3 , pp. 1100-1111
    • Sapra, P.1    Moase, E.H.2    Ma, J.3    Allen, T.M.4
  • 63
    • 0027630475 scopus 로고
    • Synthesis of end-group functionalized polyethylene glycol-lipid conjugates for preparation of polymer-grafted liposomes
    • Zalipsky S. Synthesis of end-group functionalized polyethylene glycol-lipid conjugates for preparation of polymer-grafted liposomes. Bioconjugate Chem 1993;4:296-299
    • (1993) Bioconjugate Chem , vol.4 , pp. 296-299
    • Zalipsky, S.1
  • 64
    • 0029120094 scopus 로고
    • A new strategy for attachment of antibodies to sterically stabilized liposomes resulting in efficient targeting to cancer cells
    • Allen TM, Brandeis E, Hansen CB, et al. A new strategy for attachment of antibodies to sterically stabilized liposomes resulting in efficient targeting to cancer cells. Biochim Biophys Acta 1995;1237:99-108
    • (1995) Biochim Biophys Acta , vol.1237 , pp. 99-108
    • Allen, T.M.1    Brandeis, E.2    Hansen, C.B.3
  • 65
    • 0031021149 scopus 로고    scopus 로고
    • Sterically stabilized anti-HER2 immunoliposomes: Design and targeting to human breast cancer cells in vitro
    • Kirpotin D, Park JW, Hong K, et al. Sterically stabilized anti-HER2 immunoliposomes: design and targeting to human breast cancer cells in vitro. Biochemistry 1997;36:66-75
    • (1997) Biochemistry , vol.36 , pp. 66-75
    • Kirpotin, D.1    Park, J.W.2    Hong, K.3
  • 66
    • 0032946945 scopus 로고    scopus 로고
    • Targetability of novel immunoliposomes prepared by a new antibody conjugation technique
    • Bendas G, Krause A, Bakowsky U, et al. Targetability of novel immunoliposomes prepared by a new antibody conjugation technique. Int J Pharmaceutics 1999;181(1):79-93
    • (1999) Int J Pharmaceutics , vol.181 , Issue.1 , pp. 79-93
    • Bendas, G.1    Krause, A.2    Bakowsky, U.3
  • 67
    • 0035795123 scopus 로고    scopus 로고
    • P-Nitrophenylcarbonyl-PEG-PE-liposomes: Fast and simple attachment of specific ligands, including monoclonal antibodies, to distal ends of PEG chains via p-nitrophenylcarbonyl groups
    • Torchilin VP, Levchenko TS, Lukyanov AN, et al. p-Nitrophenylcarbonyl- PEG-PE-liposomes: fast and simple attachment of specific ligands, including monoclonal antibodies, to distal ends of PEG chains via p-nitrophenylcarbonyl groups. Biochim Biophys Acta 2001;1511:397-411
    • (2001) Biochim Biophys Acta , vol.1511 , pp. 397-411
    • Torchilin, V.P.1    Levchenko, T.S.2    Lukyanov, A.N.3
  • 68
    • 0037731636 scopus 로고    scopus 로고
    • Epidermal growth factor receptor (EGFR)-targeted immunoliposomes mediate specific and efficient drug delivery to EGFR-and EGFRvIII-overexpressing tumor cells
    • Mamot C, Drummond DC, Greiser U, et al. Epidermal growth factor receptor (EGFR)-targeted immunoliposomes mediate specific and efficient drug delivery to EGFR-and EGFRvIII-overexpressing tumor cells. Cancer Res 2003;63(12):3154-3161
    • (2003) Cancer Res , vol.63 , Issue.12 , pp. 3154-3161
    • Mamot, C.1    Drummond, D.C.2    Greiser, U.3
  • 69
    • 0037224431 scopus 로고    scopus 로고
    • Doxorubicin-loaded Fab' fragments of anti-disialoganglioside immunoliposomes selectively inhibit the growth and dissemination of human neuroblastoma in nude mice
    • Pastorino F, Brignole C, Marimpietri D, et al. Doxorubicin-loaded Fab' fragments of anti-disialoganglioside immunoliposomes selectively inhibit the growth and dissemination of human neuroblastoma in nude mice. Cancer Res 2003;63(1):86-92
    • (2003) Cancer Res , vol.63 , Issue.1 , pp. 86-92
    • Pastorino, F.1    Brignole, C.2    Marimpietri, D.3
  • 70
    • 33646062270 scopus 로고    scopus 로고
    • Isolation and characterization of a scFv antibody specific for tumor endothelial marker 1 (TEM1), a new reagent for targeted tumor therapy
    • Marty C, Langer-Machova Z, Sigrist S, et al. Isolation and characterization of a scFv antibody specific for tumor endothelial marker 1 (TEM1), a new reagent for targeted tumor therapy. Cancer Lett 2006;235(2):298-308
    • (2006) Cancer Lett , vol.235 , Issue.2 , pp. 298-308
    • Marty, C.1    Langer-Machova, Z.2    Sigrist, S.3
  • 71
    • 33845519894 scopus 로고    scopus 로고
    • Expression and purification of two anti-CD19 single chain Fv fragments for targeting of liposomes to CD19-expressing cells
    • Cheng WW, Das D, Suresh M, Allen TM. Expression and purification of two anti-CD19 single chain Fv fragments for targeting of liposomes to CD19-expressing cells. Biochim Biophys Acta 2007;1768(1):21-29
    • (2007) Biochim Biophys Acta , vol.1768 , Issue.1 , pp. 21-29
    • Cheng, W.W.1    Das, D.2    Suresh, M.3    Allen, T.M.4
  • 72
    • 38949108975 scopus 로고    scopus 로고
    • Novel single-chain Fv' formats for the generation of immunoliposomes by site-directed coupling
    • Messerschmidt SK, Kolbe A, Muller D, et al. Novel single-chain Fv' formats for the generation of immunoliposomes by site-directed coupling. Bioconjug Chem 2008;19(1):362-369
    • (2008) Bioconjug Chem , vol.19 , Issue.1 , pp. 362-369
    • Messerschmidt, S.K.1    Kolbe, A.2    Muller, D.3
  • 74
    • 0028884966 scopus 로고
    • Attachment of antibodies to sterically stabilized liposomes: Evaluation, comparison and optimization of coupling procedures
    • Hansen CB, Kao GY, Moase EH, et al. Attachment of antibodies to sterically stabilized liposomes: evaluation, comparison and optimization of coupling procedures. Biochim Biophys Acta 1995;1239:133-144
    • (1995) Biochim Biophys Acta , vol.1239 , pp. 133-144
    • Hansen, C.B.1    Kao, G.Y.2    Moase, E.H.3
  • 75
    • 34247607115 scopus 로고    scopus 로고
    • Construction of anti-EGFR immunoliposomes via folate-folate binding protein affinity
    • Pan X, Lee RJ. Construction of anti-EGFR immunoliposomes via folate-folate binding protein affinity. Int J Pharm 2007;336(2):276-283
    • (2007) Int J Pharm , vol.336 , Issue.2 , pp. 276-283
    • Pan, X.1    Lee, R.J.2
  • 76
    • 30644469546 scopus 로고    scopus 로고
    • Generation of immunoliposomes using recombinant single-chain Fv fragments bound to Ni-NTA-liposomes
    • Ruger R, Muller D, Fahr A, Kontermann RE. Generation of immunoliposomes using recombinant single-chain Fv fragments bound to Ni-NTA-liposomes. J Drug Target 2005;13(7):399-406
    • (2005) J Drug Target , vol.13 , Issue.7 , pp. 399-406
    • Ruger, R.1    Muller, D.2    Fahr, A.3    Kontermann, R.E.4
  • 77
    • 33750104153 scopus 로고    scopus 로고
    • In vitro characterization of binding and stability of single-chain Fv Ni-NTA-liposomes
    • Ruger R, Muller D, Fahr A, Kontermann RE. In vitro characterization of binding and stability of single-chain Fv Ni-NTA-liposomes. J Drug Target 2006;14(8):576-582
    • (2006) J Drug Target , vol.14 , Issue.8 , pp. 576-582
    • Ruger, R.1    Muller, D.2    Fahr, A.3    Kontermann, R.E.4
  • 78
    • 0032858556 scopus 로고    scopus 로고
    • A combinatorial approach to producing sterically stabilized (Stealth) immunoliposomal drugs
    • Ishida T, Iden DL, Allen TM. A combinatorial approach to producing sterically stabilized (Stealth) immunoliposomal drugs. FEBS Lett 1999;460(1):129-133
    • (1999) FEBS Lett , vol.460 , Issue.1 , pp. 129-133
    • Ishida, T.1    Iden, D.L.2    Allen, T.M.3
  • 79
    • 0035817346 scopus 로고    scopus 로고
    • In vitro and in vivo comparison of immunoliposomes made by conventional coupling techniques with those made by a new post-insertion technique
    • Iden DL, Allen TM. In vitro and in vivo comparison of immunoliposomes made by conventional coupling techniques with those made by a new post-insertion technique. Biochim Biophys Acta 2001;1513(2):207-216
    • (2001) Biochim Biophys Acta , vol.1513 , Issue.2 , pp. 207-216
    • Iden, D.L.1    Allen, T.M.2
  • 80
    • 0036200912 scopus 로고    scopus 로고
    • Use of the post-insertion technique to insert peptide ligands into pre-formed Stealth liposomes with retention of binding activity and cytotoxicity
    • Moreira JN, Ishida T, Gaspar R, Allen TM. Use of the post-insertion technique to insert peptide ligands into pre-formed Stealth liposomes with retention of binding activity and cytotoxicity. Pharm Res 2002;19(3):265-269
    • (2002) Pharm Res , vol.19 , Issue.3 , pp. 265-269
    • Moreira, J.N.1    Ishida, T.2    Gaspar, R.3    Allen, T.M.4
  • 81
    • 13544268486 scopus 로고    scopus 로고
    • Preclinical Manufacture of an Anti-HER2 scFv-PEG-DSPE, Liposome-Inserting conjugate.1. Gram-Scale Production and Purification
    • Nellis DF, Ekstrom DL, Kirpotin DB, et al. Preclinical Manufacture of an Anti-HER2 scFv-PEG-DSPE, Liposome-Inserting conjugate. 1. Gram-Scale Production and Purification. Biotechnol Prog 2005;21(1):205-220
    • (2005) Biotechnol Prog , Issue.21 , pp. 205-220
    • Nellis, D.F.1    Ekstrom, D.L.2    Kirpotin, D.B.3
  • 82
    • 13544251524 scopus 로고    scopus 로고
    • Preclinical manufacture of anti-HER2 liposome-inserting, scFv-PEG-lipid conjugate. 2. Conjugate micelle identity, purity, stability, and potency analysis
    • Nellis DF, Giardina SL, Janini GM, et al. Preclinical manufacture of anti-HER2 liposome-inserting, scFv-PEG-lipid conjugate. 2. Conjugate micelle identity, purity, stability, and potency analysis. Biotechnol Prog 2005;21(1):221-232
    • (2005) Biotechnol Prog , Issue.21 , pp. 221-232
    • Nellis, D.F.1    Giardina, S.L.2    Janini, G.M.3
  • 83
    • 0034214039 scopus 로고    scopus 로고
    • Selective targeting of immunoliposomal doxorubicin against human multiple myeloma in vitro and ex vivo
    • Lopes de Menezes DE, Pilarski LM, Belch AR, Allen TM. Selective targeting of immunoliposomal doxorubicin against human multiple myeloma in vitro and ex vivo. Biochim Biophys Acta 2000;1466(1-2):205-220
    • (2000) Biochim Biophys Acta , vol.1466 , Issue.1-2 , pp. 205-220
    • Lopes De Menezes, D.E.1    Pilarski, L.M.2    Belch, A.R.3    Allen, T.M.4
  • 85
    • 29244489232 scopus 로고    scopus 로고
    • Epidermal growth factor receptor-targeted immunoliposomes significantly enhance the efficacy of multiple anticancer drugs in vivo
    • Mamot C, Drummond DC, Noble CO, et al. Epidermal growth factor receptor-targeted immunoliposomes significantly enhance the efficacy of multiple anticancer drugs in vivo. Cancer Res 2005;65(24):11631-11638
    • (2005) Cancer Res , vol.65 , Issue.24 , pp. 11631-11638
    • Mamot, C.1    Drummond, D.C.2    Noble, C.O.3
  • 86
    • 68149159236 scopus 로고    scopus 로고
    • Characterization of highly stable liposomal and immunoliposomal formulations of vincristine and vinblastine
    • Noble CO, Guo Z, Hayes ME, et al. Characterization of highly stable liposomal and immunoliposomal formulations of vincristine and vinblastine. Cancer Chemother Pharmacol 2009;64(4):741-751
    • (2009) Cancer Chemother Pharmacol , vol.64 , Issue.4 , pp. 741-751
    • Noble, C.O.1    Guo, Z.2    Hayes, M.E.3
  • 87
    • 0037427945 scopus 로고    scopus 로고
    • The influence of repeated injections on pharmacokinetics and biodistribution of different types of sterically stabilized immunoliposomes
    • Bendas G, Rothe U, Scherphof GL, Kamps JA. The influence of repeated injections on pharmacokinetics and biodistribution of different types of sterically stabilized immunoliposomes. Biochim Biophys Acta 2003;1609(1):63-70
    • (2003) Biochim Biophys Acta , vol.1609 , Issue.1 , pp. 63-70
    • Bendas, G.1    Rothe, U.2    Scherphof, G.L.3    Kamps, J.A.4
  • 88
    • 40849138014 scopus 로고    scopus 로고
    • Accelerated blood clearance (ABC) phenomenon upon repeated injection of PEGylated liposomes
    • Ishida T, Kiwada H. Accelerated blood clearance (ABC) phenomenon upon repeated injection of PEGylated liposomes. Int J Pharm 2008;354(1-2):56-62
    • (2008) Int J Pharm , vol.354 , Issue.1-2 , pp. 56-62
    • Ishida, T.1    Kiwada, H.2
  • 89
    • 34248589255 scopus 로고    scopus 로고
    • Anti-PEG IgM elicited by injection of liposomes is involved in the enhanced blood clearance of a subsequent dose of PEGylated liposomes
    • Wang X, Ishida T, Kiwada H. Anti-PEG IgM elicited by injection of liposomes is involved in the enhanced blood clearance of a subsequent dose of PEGylated liposomes. J Control Release 2007;119(2):236-244
    • (2007) J Control Release , vol.119 , Issue.2 , pp. 236-244
    • Wang, X.1    Ishida, T.2    Kiwada, H.3
  • 90
    • 0029828939 scopus 로고    scopus 로고
    • Targeting of Stealth liposomes to erB-2 (Her/2) receptor: In vitro and in vivo studies
    • Goren D, Horowitz AT, Zalipsky S, et al. Targeting of Stealth liposomes to erB-2 (Her/2) receptor: in vitro and in vivo studies. Br J Cancer 1996;74:1749-1756
    • (1996) Br J Cancer , vol.74 , pp. 1749-1756
    • Goren, D.1    Horowitz, A.T.2    Zalipsky, S.3
  • 91
    • 0023668196 scopus 로고
    • The role of multivalency in antibody mediated liposome targeting
    • Houck KS, Huang L. The role of multivalency in antibody mediated liposome targeting. Biochem Biophys Res Commun 1987;145(3):1205-1210
    • (1987) Biochem Biophys Res Commun , vol.145 , Issue.3 , pp. 1205-1210
    • Houck, K.S.1    Huang, L.2
  • 92
    • 0030876540 scopus 로고    scopus 로고
    • Immunoliposomes bearing polyethyleneglycol-coupled Fab' fragment show prolonged circulation time and high extravasation into targeted solid tumors in vivo
    • Maruyama K, Takahashi N, Tagawa T, et al. Immunoliposomes bearing polyethyleneglycol-coupled Fab' fragment show prolonged circulation time and high extravasation into targeted solid tumors in vivo. FEBS Lett 1997;413(1):177-180
    • (1997) FEBS Lett , vol.413 , Issue.1 , pp. 177-180
    • Maruyama, K.1    Takahashi, N.2    Tagawa, T.3
  • 93
    • 34447499944 scopus 로고    scopus 로고
    • Single-chain Fv immunoliposomes for the targeting of fibroblast activation protein-expressing tumor stromal cells
    • Baum P, Muller D, Ruger R, Kontermann RE. Single-chain Fv immunoliposomes for the targeting of fibroblast activation protein-expressing tumor stromal cells. J Drug Target 2007;15(6):399-406
    • (2007) J Drug Target , vol.15 , Issue.6 , pp. 399-406
    • Baum, P.1    Muller, D.2    Ruger, R.3    Kontermann, R.E.4
  • 94
    • 41649103030 scopus 로고    scopus 로고
    • Targeted drug delivery to mesothelioma cells using functionally selected internalizing human single-chain antibodies
    • An F, Drummond DC, Wilson S, et al. Targeted drug delivery to mesothelioma cells using functionally selected internalizing human single-chain antibodies. Mol Cancer Ther 2008;7(3):569-578
    • (2008) Mol Cancer Ther , vol.7 , Issue.3 , pp. 569-578
    • An, F.1    Drummond, D.C.2    Wilson, S.3
  • 95
    • 67349253388 scopus 로고    scopus 로고
    • Targeted lipid-coated nanoparticles: Delivery of tumor necrosis factor-functionalized particles to tumor cells
    • Messerschmidt SK, Musyanovych A, Altvater M, et al. Targeted lipid-coated nanoparticles: delivery of tumor necrosis factor-functionalized particles to tumor cells. J Control Release 2009;137(1):69-77
    • (2009) J Control Release , vol.137 , Issue.1 , pp. 69-77
    • Messerschmidt, S.K.1    Musyanovych, A.2    Altvater, M.3
  • 96
    • 0033571383 scopus 로고    scopus 로고
    • High thermal stability is essential for tumor targeting of antibody fragments: Engineering of a humanized anti-epithelial glycoprotein-2 (epithelial cell adhesion molecule) single-chain Fv fragment
    • Willuda J, Honegger A, Waibel R, et al. High thermal stability is essential for tumor targeting of antibody fragments: engineering of a humanized anti-epithelial glycoprotein-2 (epithelial cell adhesion molecule) single-chain Fv fragment. Cancer Res 1999;59(22):5758-5767
    • (1999) Cancer Res , vol.59 , Issue.22 , pp. 5758-5767
    • Willuda, J.1    Honegger, A.2    Waibel, R.3
  • 97
    • 0038423087 scopus 로고    scopus 로고
    • Correlation between in vitro stability and in vivo performance of anti-GCN4 intrabodies as cytoplasmic inhibitors
    • Worn A, Auf der Maur A, Escher D, et al. Correlation between in vitro stability and in vivo performance of anti-GCN4 intrabodies as cytoplasmic inhibitors. J Biol Chem 2000;275(4):2795-2803
    • (2000) J Biol Chem , vol.275 , Issue.4 , pp. 2795-2803
    • Worn, A.1    Auf Der Maur, A.2    Escher, D.3
  • 98
    • 0037031314 scopus 로고    scopus 로고
    • Four-state equilibrium unfolding of an scFv antibody fragment
    • Pedroso I, Irun MP, Machicado C, Sancho J. Four-state equilibrium unfolding of an scFv antibody fragment. Biochemistry 2002;41(31):9873-9884
    • (2002) Biochemistry , vol.41 , Issue.31 , pp. 9873-9884
    • Pedroso, I.1    Irun, M.P.2    MacHicado, C.3    Sancho, J.4
  • 99
    • 12944308809 scopus 로고    scopus 로고
    • Selecting for antibody scFv fragments with improved stability using phage display with denaturation under reducing conditions
    • Brockmann EC, Cooper M, Stromsten N, et al. Selecting for antibody scFv fragments with improved stability using phage display with denaturation under reducing conditions. J Immunol Methods 2005;296(1-2):159-170
    • (2005) J Immunol Methods , vol.296 , Issue.1-2 , pp. 159-170
    • Brockmann, E.C.1    Cooper, M.2    Stromsten, N.3
  • 100
    • 0033926329 scopus 로고    scopus 로고
    • Directed evolution of a stable scaffold for T-cell receptor engineering
    • Shusta EV, Holler PD, Kieke MC, et al. Directed evolution of a stable scaffold for T-cell receptor engineering. Nat Biotechnol 2000;18(7):754-759
    • (2000) Nat Biotechnol , vol.18 , Issue.7 , pp. 754-759
    • Shusta, E.V.1    Holler, P.D.2    Kieke, M.C.3
  • 101
    • 0030916353 scopus 로고    scopus 로고
    • Two amino acid mutations in an anti-human CD3 single chain Fv antibody fragment that affect the yield on bacterial secretion but not the affinity
    • Kipriyanov SM, Moldenhauer G, Martin AC, et al. Two amino acid mutations in an anti-human CD3 single chain Fv antibody fragment that affect the yield on bacterial secretion but not the affinity. Protein Eng 1997;10(4):445-453
    • (1997) Protein Eng , vol.10 , Issue.4 , pp. 445-453
    • Kipriyanov, S.M.1    Moldenhauer, G.2    Martin, A.C.3
  • 102
    • 0035793208 scopus 로고    scopus 로고
    • Stability engineering of antibody single-chain Fv fragments
    • Worn A, Pluckthun A. Stability engineering of antibody single-chain Fv fragments. J Mol Biol 2001;305(5):989-1010
    • (2001) J Mol Biol , vol.305 , Issue.5 , pp. 989-1010
    • Worn, A.1    Pluckthun, A.2
  • 103
    • 0040964401 scopus 로고    scopus 로고
    • Different equilibrium stability behavior of ScFv fragments: Identification, classification, and improvement by protein engineering
    • Worn A, Pluckthun A. Different equilibrium stability behavior of ScFv fragments: identification, classification, and improvement by protein engineering. Biochemistry 1999;38(27):8739-8750
    • (1999) Biochemistry , vol.38 , Issue.27 , pp. 8739-8750
    • Worn, A.1    Pluckthun, A.2
  • 104
    • 10044240322 scopus 로고    scopus 로고
    • Antigen binding and stability properties of non-covalently linked anti-CD22 single-chain Fv dimers
    • Arndt MA, Krauss J, Rybak SM. Antigen binding and stability properties of non-covalently linked anti-CD22 single-chain Fv dimers. FEBS Lett 2004;578(3):257-261
    • (2004) FEBS Lett , vol.578 , Issue.3 , pp. 257-261
    • Arndt, M.A.1    Krauss, J.2    Rybak, S.M.3
  • 106
    • 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(2):161-172
    • (1997) J Mol Biol , vol.265 , Issue.2 , pp. 161-172
    • Proba, K.1    Honegger, A.2    Pluckthun, A.3
  • 107
    • 0026572809 scopus 로고
    • The disulfide bonds in antibody variable domains: Effects on stability, folding in vitro, and functional expression in Escherichia coli
    • Glockshuber R, Schmidt T, Pluckthun A. The disulfide bonds in antibody variable domains: effects on stability, folding in vitro, and functional expression in Escherichia coli. Biochemistry 1992;31(5):1270-1279
    • (1992) Biochemistry , vol.31 , Issue.5 , pp. 1270-1279
    • Glockshuber, R.1    Schmidt, T.2    Pluckthun, A.3
  • 108
    • 0344813702 scopus 로고    scopus 로고
    • Antibody scFv fragments without disulfide bonds made by molecular evolution
    • Proba K, Worn A, Honegger A, Pluckthun A. Antibody scFv fragments without disulfide bonds made by molecular evolution. J Mol Biol 1998;275(2):245-253
    • (1998) J Mol Biol , vol.275 , Issue.2 , pp. 245-253
    • Proba, K.1    Worn, A.2    Honegger, A.3    Pluckthun, A.4
  • 109
    • 0032524034 scopus 로고    scopus 로고
    • An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly
    • Worn A, Pluckthun A. An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly. FEBS Lett 1998;427(3):357-361
    • (1998) FEBS Lett , vol.427 , Issue.3 , pp. 357-361
    • Worn, A.1    Pluckthun, A.2
  • 110
    • 66949126546 scopus 로고    scopus 로고
    • Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli
    • de Marco A. Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli. Microb Cell Fact 2009;8:26-43
    • (2009) Microb Cell Fact , vol.8 , pp. 26-43
    • De Marco, A.1
  • 111
    • 0028216376 scopus 로고
    • Engineering interchain disulfide bonds into conserved framework regions of Fv fragments: Improved biochemical characteristics of recombinant immunotoxins containing disulfide-stabilized Fv
    • Reiter Y, Brinkmann U, Webber KO, et al. Engineering interchain disulfide bonds into conserved framework regions of Fv fragments: improved biochemical characteristics of recombinant immunotoxins containing disulfide-stabilized Fv. Protein Eng 1994;7(5):697-704
    • (1994) Protein Eng , vol.7 , Issue.5 , pp. 697-704
    • Reiter, Y.1    Brinkmann, U.2    Webber, K.O.3
  • 112
    • 0029554780 scopus 로고
    • Disulfide stabilization of antibody Fv: Computer predictions and experimental evaluation
    • Reiter Y, Brinkmann U, Jung SH, et al. Disulfide stabilization of antibody Fv: computer predictions and experimental evaluation. Protein Eng 1995;8(12):1323-1331
    • (1995) Protein Eng , vol.8 , Issue.12 , pp. 1323-1331
    • Reiter, Y.1    Brinkmann, U.2    Jung, S.H.3
  • 113
    • 0032568591 scopus 로고    scopus 로고
    • Optimizing the stability of single-chain proteins by linker length and composition mutagenesis
    • Robinson CR, Sauer RT. Optimizing the stability of single-chain proteins by linker length and composition mutagenesis. Proc Natl Acad Sci USA 1998;95(11):5929-5934
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.11 , pp. 5929-5934
    • Robinson, C.R.1    Sauer, R.T.2
  • 114
    • 40849104794 scopus 로고    scopus 로고
    • Humanization of a highly stable single-chain antibody by structure-based antigen-binding site grafting
    • Villani ME, Morea V, Consalvi V, et al. Humanization of a highly stable single-chain antibody by structure-based antigen-binding site grafting. Mol Immunol 2008;45(9):2474-2485
    • (2008) Mol Immunol , vol.45 , Issue.9 , pp. 2474-2485
    • Villani, M.E.1    Morea, V.2    Consalvi, V.3
  • 115
    • 33748809530 scopus 로고    scopus 로고
    • The change of the scFv into the Fab format improves the stability and in vivo toxin neutralization capacity of recombinant antibodies
    • Quintero-Hernandez V, Juarez-Gonzalez VR, Ortiz-Leon M, et al. The change of the scFv into the Fab format improves the stability and in vivo toxin neutralization capacity of recombinant antibodies. Mol Immunol 2007;44(6):1307-1315
    • (2007) Mol Immunol , vol.44 , Issue.6 , pp. 1307-1315
    • Quintero-Hernandez, V.1    Juarez-Gonzalez, V.R.2    Ortiz-Leon, M.3
  • 116
    • 13844296953 scopus 로고    scopus 로고
    • Directed evolution, phage display and combination of evolved mutants: A strategy to recover the neutralization properties of the scFv version of BCF2 a neutralizing monoclonal antibody specific to scorpion toxin Cn2
    • Juarez-Gonzalez VR, Riano-Umbarila L, Quintero-Hernandez V, et al. Directed evolution, phage display and combination of evolved mutants: a strategy to recover the neutralization properties of the scFv version of BCF2 a neutralizing monoclonal antibody specific to scorpion toxin Cn2. J Mol Biol 2005;346(5):1287-1297
    • (2005) J Mol Biol , vol.346 , Issue.5 , pp. 1287-1297
    • Juarez-Gonzalez, V.R.1    Riano-Umbarila, L.2    Quintero-Hernandez, V.3
  • 117
    • 33847226329 scopus 로고    scopus 로고
    • Characterization of antibodies in single-chain format against the E7 oncoprotein of the human papillomavirus type 16 and their improvement by mutagenesis
    • Dona MG, Giorgi C, Accardi L. Characterization of antibodies in single-chain format against the E7 oncoprotein of the human papillomavirus type 16 and their improvement by mutagenesis. BMC Cancer 2007;7:25-38
    • (2007) BMC Cancer , vol.7 , pp. 25-38
    • Dona, M.G.1    Giorgi, C.2    Accardi, L.3
  • 118
    • 60749090900 scopus 로고    scopus 로고
    • Stabilization and humanization of a single-chain Fv antibody fragment specific for human lymphocyte antigen CD19 by designed point mutations and CDR-grafting onto a human framework
    • Kugler M, Stein C, Schwenkert M, et al. Stabilization and humanization of a single-chain Fv antibody fragment specific for human lymphocyte antigen CD19 by designed point mutations and CDR-grafting onto a human framework. Protein Eng Des Sel 2009;22(3):135-147
    • (2009) Protein Eng des Sel , vol.22 , Issue.3 , pp. 135-147
    • Kugler, M.1    Stein, C.2    Schwenkert, M.3
  • 119
    • 0027615741 scopus 로고
    • High-level expression, purification, and renaturation of recombinant murine interleukin-2 from Escherichia coli
    • Guisez Y, Demolder J, Mertens N, et al. High-level expression, purification, and renaturation of recombinant murine interleukin-2 from Escherichia coli. Protein Expr Purif 1993;4(3):240-246
    • (1993) Protein Expr Purif , vol.4 , Issue.3 , pp. 240-246
    • Guisez, Y.1    Demolder, J.2    Mertens, N.3
  • 120
    • 0028371793 scopus 로고
    • Refolding and characterization of human recombinant heparin-binding neurite-promoting factor
    • Seddon AP, Hulmes JD, Decker MM, et al. Refolding and characterization of human recombinant heparin-binding neurite-promoting factor. Protein Expr Purif 1994;5(1):14-21
    • (1994) Protein Expr Purif , vol.5 , Issue.1 , pp. 14-21
    • Seddon, A.P.1    Hulmes, J.D.2    Decker, M.M.3
  • 121
    • 0037007446 scopus 로고    scopus 로고
    • A kinetic trap is an intrinsic feature in the folding pathway of single-chain Fv fragments
    • Hoyer M. RK, Pluckthun A. A kinetic trap is an intrinsic feature in the folding pathway of single-chain Fv fragments. Biophys Chem 2002;96(2-3):273-284
    • (2002) Biophys Chem , vol.96 , Issue.2-3 , pp. 273-284
    • Hoyer, M.1    Pluckthun, A.2
  • 122
    • 3943101478 scopus 로고    scopus 로고
    • Radiolabelling of glycosylated MFE-23: CPG2 fusion protein (MFECP1) with 99mTc for quantitation of tumour antibody-enzyme localisation in antibody-directed enzyme pro-drug therapy (ADEPT)
    • Francis RJ, Mather SJ, Chester K, et al. Radiolabelling of glycosylated MFE-23: CPG2 fusion protein (MFECP1) with 99mTc for quantitation of tumour antibody-enzyme localisation in antibody-directed enzyme pro-drug therapy (ADEPT). Eur J Nucl Med Mol Imaging 2004;31(8):1090-1096
    • (2004) Eur J Nucl Med Mol Imaging , vol.31 , Issue.8 , pp. 1090-1096
    • Francis, R.J.1    Mather, S.J.2    Chester, K.3
  • 123
    • 33645731077 scopus 로고    scopus 로고
    • A genetically engineered anti-CD45 single-chain antibody-streptavidin fusion protein for pretargeted radioimmunotherapy of hematologic malignancies
    • Lin Y, Pagel JM, Axworthy D, et al. A genetically engineered anti-CD45 single-chain antibody-streptavidin fusion protein for pretargeted radioimmunotherapy of hematologic malignancies. Cancer Res 2006;66(7):3884-3892
    • (2006) Cancer Res , vol.66 , Issue.7 , pp. 3884-3892
    • Lin, Y.1    Pagel, J.M.2    Axworthy, D.3
  • 124
    • 0034074997 scopus 로고    scopus 로고
    • Divalent forms of CC49 single-chain antibody constructs in Pichia pastoris: Expression, purification, and characterization
    • Goel A, Beresford GW, Colcher D, et al. Divalent forms of CC49 single-chain antibody constructs in Pichia pastoris: expression, purification, and characterization. J Biochem 2000;127(5):829-836
    • (2000) J Biochem , vol.127 , Issue.5 , pp. 829-836
    • Goel, A.1    Beresford, G.W.2    Colcher, D.3
  • 125
    • 13844310366 scopus 로고    scopus 로고
    • The in vivo characteristics of genetically engineered divalent and tetravalent single-chain antibody constructs
    • Wittel UA, Jain M, Goel A, et al. The in vivo characteristics of genetically engineered divalent and tetravalent single-chain antibody constructs. Nucl Med Biol 2005;32(2):157-164
    • (2005) Nucl Med Biol , vol.32 , Issue.2 , pp. 157-164
    • Wittel, U.A.1    Jain, M.2    Goel, A.3
  • 126
    • 11844286302 scopus 로고    scopus 로고
    • Comparative evaluation of two purification methods of anti-CD19-c-myc-His(6)-Cys scFv
    • Das D, Allen TM, Suresh MR. Comparative evaluation of two purification methods of anti-CD19-c-myc-His(6)-Cys scFv. Protein Expr Purif 2005;39(2):199-208
    • (2005) Protein Expr Purif , Issue.39 , pp. 199-208
    • Das, D.1    Allen, T.M.2    Suresh, M.R.3
  • 127
    • 27144550160 scopus 로고    scopus 로고
    • Arming antibodies: Prospects and challenges for immunoconjugates
    • Wu AM, Senter PD. Arming antibodies: prospects and challenges for immunoconjugates. Nat Biotechnol 2005;23(9):1137-1146
    • (2005) Nat Biotechnol , vol.23 , Issue.9 , pp. 1137-1146
    • Wu, A.M.1    Senter, P.D.2
  • 128
    • 33751259946 scopus 로고    scopus 로고
    • A phase i study of single administration of antibody-directed enzyme prodrug therapy with the recombinant anti-carcinoembryonic antigen antibody-enzyme fusion protein MFECP1 and a bis-iodo phenol mustard prodrug
    • Mayer A, Francis RJ, Sharma SK, et al. A phase I study of single administration of antibody-directed enzyme prodrug therapy with the recombinant anti-carcinoembryonic antigen antibody-enzyme fusion protein MFECP1 and a bis-iodo phenol mustard prodrug. Clin Cancer Res 2006;12(21):6509-6516
    • (2006) Clin Cancer Res , vol.12 , Issue.21 , pp. 6509-6516
    • Mayer, A.1    Francis, R.J.2    Sharma, S.K.3
  • 129
    • 14644426573 scopus 로고    scopus 로고
    • HA22 (R490A) is a recombinant immunotoxin with increased antitumor activity without an increase in animal toxicity
    • Bang S, Nagata S, Onda M, et al. HA22 (R490A) is a recombinant immunotoxin with increased antitumor activity without an increase in animal toxicity. Clin Cancer Res 2005;11(4):1545-1550
    • (2005) Clin Cancer Res , vol.11 , Issue.4 , pp. 1545-1550
    • Bang, S.1    Nagata, S.2    Onda, M.3
  • 130
    • 34347325240 scopus 로고    scopus 로고
    • Releasable PEGylation of mesothelin targeted immunotoxin SS1P achieves single dosage complete regression of a human carcinoma in mice
    • Filpula D, Yang K, Basu A, et al. Releasable PEGylation of mesothelin targeted immunotoxin SS1P achieves single dosage complete regression of a human carcinoma in mice. Bioconjug Chem 2007;18(3):773-784
    • (2007) Bioconjug Chem , vol.18 , Issue.3 , pp. 773-784
    • Filpula, D.1    Yang, K.2    Basu, A.3
  • 131
    • 21844470230 scopus 로고    scopus 로고
    • Flow cytometric immunophenotyping including Bcl-2 detection on fine needle aspirates in the diagnosis of reactive lymphadenopathy and non-Hodgkin's lymphoma
    • Laane E, Tani E, Bjorklund E, et al. Flow cytometric immunophenotyping including Bcl-2 detection on fine needle aspirates in the diagnosis of reactive lymphadenopathy and non-Hodgkin's lymphoma. Cytometry B Clin Cytom 2005;64(1):34-42
    • (2005) Cytometry B Clin Cytom , vol.64 , Issue.1 , pp. 34-42
    • Laane, E.1    Tani, E.2    Bjorklund, E.3
  • 132
    • 19444362857 scopus 로고    scopus 로고
    • Liposomes targeted via two different antibodies: Assay, B-cell binding and cytotoxicity
    • Laginha K, Mumbengegwi D, Allen T. Liposomes targeted via two different antibodies: assay, B-cell binding and cytotoxicity. Biochim Biophys Acta 2005;1711(1):25-32
    • (2005) Biochim Biophys Acta , vol.1711 , Issue.1 , pp. 25-32
    • Laginha, K.1    Mumbengegwi, D.2    Allen, T.3
  • 133
    • 0036177919 scopus 로고    scopus 로고
    • Rituximab: Mechanism of action and resistance
    • Maloney DG, Smith B, Rose A. Rituximab: mechanism of action and resistance. Semin Oncol 2002;29(1 Suppl 2):2-9
    • (2002) Semin Oncol , vol.29 , Issue.1 SUPPL. 2 , pp. 2-9
    • Maloney, D.G.1    Smith, B.2    Rose, A.3
  • 134
    • 0642312825 scopus 로고    scopus 로고
    • Rituximab (monoclonal anti-CD20 antibody): Mechanisms of action and resistance
    • Smith MR. Rituximab (monoclonal anti-CD20 antibody): mechanisms of action and resistance. Oncogene 2003;22(47):7359-73568
    • (2003) Oncogene , vol.22 , Issue.47 , pp. 7359-73568
    • Smith, M.R.1
  • 135
    • 0242492546 scopus 로고    scopus 로고
    • Transient down-modulation of CD20 by rituximab in patients with chronic lymphocytic leukemia
    • Jilani I, O'Brien S, Manshuri T, et al. Transient down-modulation of CD20 by rituximab in patients with chronic lymphocytic leukemia. Blood 2003;102(10):3514-3520
    • (2003) Blood , vol.102 , Issue.10 , pp. 3514-3520
    • Jilani, I.1    O'Brien, S.2    Manshuri, T.3
  • 136
    • 34248584099 scopus 로고    scopus 로고
    • Bcl-2 expression in rituximab refractory cutaneous B-cell lymphoma
    • Wobser M, Voigt H, Eggert AO, et al. Bcl-2 expression in rituximab refractory cutaneous B-cell lymphoma. Br J Cancer 2007;96(10):1540-1543
    • (2007) Br J Cancer , vol.96 , Issue.10 , pp. 1540-1543
    • Wobser, M.1    Voigt, H.2    Eggert, A.O.3
  • 137
    • 0037142184 scopus 로고    scopus 로고
    • Rat Muc4 (sialomucin complex) reduces binding of anti-ErbB2 antibodies to tumor cell surfaces, a potential mechanism for herceptin resistance
    • Price-Schiavi SA, Jepson S, Li P, et al. Rat Muc4 (sialomucin complex) reduces binding of anti-ErbB2 antibodies to tumor cell surfaces, a potential mechanism for herceptin resistance. Int J Cancer 2002;99(6):783-791
    • (2002) Int J Cancer , vol.99 , Issue.6 , pp. 783-791
    • Price-Schiavi, S.A.1    Jepson, S.2    Li, P.3
  • 138
    • 12544250996 scopus 로고    scopus 로고
    • Decreased accessibility and lack of activation of ErbB2 in JIMT-1, a herceptin-resistant, MUC4-expressing breast cancer cell line
    • Nagy P, Friedlander E, Tanner M, et al. Decreased accessibility and lack of activation of ErbB2 in JIMT-1, a herceptin-resistant, MUC4-expressing breast cancer cell line. Cancer Res 2005;65(2):473-482
    • (2005) Cancer Res , vol.65 , Issue.2 , pp. 473-482
    • Nagy, P.1    Friedlander, E.2    Tanner, M.3
  • 139
    • 77949885376 scopus 로고    scopus 로고
    • Combination targeting of immunoliposomal therapeutics in a murine model of B-Cell lymphoma. 36th Annual Meeting & Exposition of the Controlled Release Society
    • Moase EA, Allen TM. Combination targeting of immunoliposomal therapeutics in a murine model of B-Cell lymphoma. 36th Annual Meeting & Exposition of the Controlled Release Society. Copenhagen, Denmark; 2009
    • (2009) Copenhagen Denmark;
    • Moase, E.A.1    Allen, T.M.2
  • 140
    • 77949883574 scopus 로고    scopus 로고
    • Combined Anti-vasculature and Anti-tumor Targeting in the Treatment of Metastatic Breast Cancer. 36th Annual Meeting & Exposition of the Controlled Release Society
    • Hare JIM, Moase EA, Allen TM. Combined Anti-vasculature and Anti-tumor Targeting in the Treatment of Metastatic Breast Cancer. 36th Annual Meeting & Exposition of the Controlled Release Society. Copenhagen, Denmark; 2009
    • (2009) Copenhagen Denmark;
    • Hare, J.I.M.1    Moase, E.A.2    Allen, T.M.3
  • 141
    • 0842333135 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of doxorubicin and vincristine coencapsulated within liposomes through use of transition metal ion complexation and pH gradient loading
    • Abraham SA, McKenzie C, Masin D, et al. In vitro and in vivo characterization of doxorubicin and vincristine coencapsulated within liposomes through use of transition metal ion complexation and pH gradient loading. Clin Cancer Res 2004;10(2):728-738
    • (2004) Clin Cancer Res , vol.10 , Issue.2 , pp. 728-738
    • Abraham, S.A.1    McKenzie, C.2    Masin, D.3
  • 142
    • 33748326024 scopus 로고    scopus 로고
    • Ratiometric dosing of anticancer drug combinations: Controlling drug ratios after systemic administration regulates therapeutic activity in tumor-bearing mice
    • Mayer LD, Harasym TO, Tardi PG, et al. Ratiometric dosing of anticancer drug combinations: controlling drug ratios after systemic administration regulates therapeutic activity in tumor-bearing mice. Mol Cancer Ther 2006;5(7):1854-1863
    • (2006) Mol Cancer Ther , vol.5 , Issue.7 , pp. 1854-1863
    • Mayer, L.D.1    Harasym, T.O.2    Tardi, P.G.3
  • 143
    • 33847049076 scopus 로고    scopus 로고
    • Coencapsulation of irinotecan and floxuridine into low cholesterol-containing liposomes that coordinate drug release in vivo
    • Tardi PG, Gallagher RC, Johnstone S, et al. Coencapsulation of irinotecan and floxuridine into low cholesterol-containing liposomes that coordinate drug release in vivo. Biochim Biophys Acta 2007;1768(3):678-687
    • (2007) Biochim Biophys Acta , vol.1768 , Issue.3 , pp. 678-687
    • Tardi, P.G.1    Gallagher, R.C.2    Johnstone, S.3
  • 144
    • 0028803894 scopus 로고
    • In vitro liposome mediated DNA transfection of epithelial cell lines using the cationic liposome Dc Chol/Dope
    • Caplen NJ, Kinrade E, Sorgi F, et al. In vitro liposome mediated DNA transfection of epithelial cell lines using the cationic liposome Dc Chol/Dope. Gene Ther 1995;2(9):603-613
    • (1995) Gene Ther , vol.2 , Issue.9 , pp. 603-613
    • Caplen, N.J.1    Kinrade, E.2    Sorgi, F.3
  • 145
    • 0345059269 scopus 로고    scopus 로고
    • Gene delivery mediated by cationic liposomes: From biophysical aspects to enhancement of transfection
    • de Lima MC, Simoes S, Pires P, et al. Gene delivery mediated by cationic liposomes: from biophysical aspects to enhancement of transfection. Mol Membr Biol 1999;16(1):103-109
    • (1999) Mol Membr Biol , vol.16 , Issue.1 , pp. 103-109
    • De Lima, M.C.1    Simoes, S.2    Pires, P.3
  • 146
    • 0035575844 scopus 로고    scopus 로고
    • Targeted delivery and triggered release of liposomal doxorubicin enhances cytotoxicity against human B lymphoma cells
    • Ishida T, Kirchmeier MJ, Moase EH, et al. Targeted delivery and triggered release of liposomal doxorubicin enhances cytotoxicity against human B lymphoma cells. Biochim Biophys Acta 2001;1515:144-158
    • (2001) Biochim Biophys Acta , vol.1515 , pp. 144-158
    • Ishida, T.1    Kirchmeier, M.J.2    Moase, E.H.3
  • 147
    • 2442421428 scopus 로고    scopus 로고
    • Transferrin-modified liposomes equipped with a pH-sensitive fusogenic peptide: An artificial viral-like delivery system
    • Kakudo T, Chaki S, Futaki S, et al. Transferrin-modified liposomes equipped with a pH-sensitive fusogenic peptide: an artificial viral-like delivery system. Biochemistry 2004;43(19):5618-5628
    • (2004) Biochemistry , vol.43 , Issue.19 , pp. 5618-5628
    • Kakudo, T.1    Chaki, S.2    Futaki, S.3
  • 148
    • 0030591442 scopus 로고    scopus 로고
    • Liposomes with detachable polymer coating: Destabilization and fusion of dioleoylphosphatidylethanolamine vesicles triggered by cleavage of surface-grafted poly(ethylene glycol)
    • Kirpotin D, Hong K, Mullah N, et al. Liposomes with detachable polymer coating: destabilization and fusion of dioleoylphosphatidylethanolamine vesicles triggered by cleavage of surface-grafted poly(ethylene glycol). FEBS Lett 1996;388:115-118
    • (1996) FEBS Lett , vol.388 , pp. 115-118
    • Kirpotin, D.1    Hong, K.2    Mullah, N.3
  • 149
    • 0035902477 scopus 로고    scopus 로고
    • TAT peptide on the surface of liposomes affords their efficient intracellular delivery even at low temperature and in the presence of metabolic inhibitors
    • Torchilin VP, Rammohan R, Weissig V, Levchenko TS. TAT peptide on the surface of liposomes affords their efficient intracellular delivery even at low temperature and in the presence of metabolic inhibitors. Proc Natl Acad Sci USA 2001;98(15):8786-8791
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.15 , pp. 8786-8791
    • Torchilin, V.P.1    Rammohan, R.2    Weissig, V.3    Levchenko, T.S.4
  • 150
    • 0344873301 scopus 로고    scopus 로고
    • Pharmaco attributes of dioleoylphosphatidylethanolamine/ cholesterylhemisuccinate liposomes containing different types of cleavable lipopolymers
    • Zhang JX, Zalipsky S, Mullah N, et al. Pharmaco attributes of dioleoylphosphatidylethanolamine/ cholesterylhemisuccinate liposomes containing different types of cleavable lipopolymers. Pharmacol Res 2004;49:185-198
    • (2004) Pharmacol Res , vol.49 , pp. 185-198
    • Zhang, J.X.1    Zalipsky, S.2    Mullah, N.3
  • 151
    • 61849136126 scopus 로고    scopus 로고
    • Cytoplasmic delivery of liposomal contents mediated by an acid-labile cholesterol-vinyl ether-PEG conjugate
    • Boomer JA, Qualls MM, Inerowicz HD, et al. Cytoplasmic delivery of liposomal contents mediated by an acid-labile cholesterol-vinyl ether-PEG conjugate. Bioconjug Chem 2009;20(1):47-59
    • (2009) Bioconjug Chem , vol.20 , Issue.1 , pp. 47-59
    • Boomer, J.A.1    Qualls, M.M.2    Inerowicz, H.D.3
  • 152
    • 0033638578 scopus 로고    scopus 로고
    • Bispecific mAb aided liposomal drug delivery
    • Cao Y, Suresh MR. Bispecific mAb aided liposomal drug delivery. J Drug Target 2000;8(4):257-266
    • (2000) J Drug Target , vol.8 , Issue.4 , pp. 257-266
    • Cao, Y.1    Suresh, M.R.2
  • 153
    • 11144356521 scopus 로고    scopus 로고
    • A recombinant bispecific single-chain Fv antibody against HLA class II and FcgammaRIII (CD16) triggers effective lysis of lymphoma cells
    • Bruenke J, Fischer B, Barbin K, et al. A recombinant bispecific single-chain Fv antibody against HLA class II and FcgammaRIII (CD16) triggers effective lysis of lymphoma cells. Br J Haematol 2004;125(2):167-179
    • (2004) Br J Haematol , vol.125 , Issue.2 , pp. 167-179
    • Bruenke, J.1    Fischer, B.2    Barbin, K.3
  • 154
    • 85026147994 scopus 로고    scopus 로고
    • A novel CD19-directed recombinant bispecific antibody derivative with enhanced immune effector functions for human leukemic cells
    • Kellner C, Bruenke J, Stieglmaier J, et al. A novel CD19-directed recombinant bispecific antibody derivative with enhanced immune effector functions for human leukemic cells. J Immunother 2008;31(9):871-884
    • (2008) J Immunother , vol.31 , Issue.9 , pp. 871-884
    • Kellner, C.1    Bruenke, J.2    Stieglmaier, J.3
  • 155
    • 67549102111 scopus 로고    scopus 로고
    • Genetic alteration of a bispecific ligand-directed toxin targeting human CD19 and CD22 receptors resulting in improved efficacy against systemic B cell malignancy
    • Vallera DA, Chen H, Sicheneder AR, et al. Genetic alteration of a bispecific ligand-directed toxin targeting human CD19 and CD22 receptors resulting in improved efficacy against systemic B cell malignancy. Leuk Res 2009;33(9):1233-1242
    • (2009) Leuk Res , vol.33 , Issue.9 , pp. 1233-1242
    • Vallera, D.A.1    Chen, H.2    Sicheneder, A.R.3
  • 156
    • 8044237717 scopus 로고    scopus 로고
    • High volumetric yields of functional dimeric miniantibodies in Escherichia coli, using an optimized expression vector and high-cell-density fermentation under non-limited growth conditions
    • Horn U, Strittmatter W, Krebber A, et al. High volumetric yields of functional dimeric miniantibodies in Escherichia coli, using an optimized expression vector and high-cell-density fermentation under non-limited growth conditions. Appl Microbiol Biotechnol 1996;46(5-6):524-532
    • (1996) Appl Microbiol Biotechnol , vol.46 , Issue.5-6 , pp. 524-532
    • Horn, U.1    Strittmatter, W.2    Krebber, A.3
  • 157
    • 33646089874 scopus 로고    scopus 로고
    • Codon optimization, expression, and characterization of an internalizing anti-ErbB2 single-chain antibody in Pichia pastoris
    • Hu S, Li L, Qiao J, et al. Codon optimization, expression, and characterization of an internalizing anti-ErbB2 single-chain antibody in Pichia pastoris. Protein Expr Purif 2006;47(1):249-257
    • (2006) Protein Expr Purif , vol.47 , Issue.1 , pp. 249-257
    • Hu, S.1    Li, L.2    Qiao, J.3
  • 158
    • 58149293161 scopus 로고    scopus 로고
    • Efficient production of single-chain Fv antibody possessing rare codon linkers in fed-batch fermentation
    • Kumada Y, Sakan Y, Kajihara H, et al. Efficient production of single-chain Fv antibody possessing rare codon linkers in fed-batch fermentation. J Biosci Bioeng 2009;107(1):73-77
    • (2009) J Biosci Bioeng , vol.107 , Issue.1 , pp. 73-77
    • Kumada, Y.1    Sakan, Y.2    Kajihara, H.3
  • 159
    • 33845957062 scopus 로고    scopus 로고
    • Optimisation of production of a domoic acid-binding scFv antibody fragment in Escherichia coli using molecular chaperones and functional immobilisation on a mesoporous silicate support
    • Hu X, O'Hara L, White S, et al. Optimisation of production of a domoic acid-binding scFv antibody fragment in Escherichia coli using molecular chaperones and functional immobilisation on a mesoporous silicate support. Protein Expr Purif 2007;52(1):194-201
    • (2007) Protein Expr Purif , vol.52 , Issue.1 , pp. 194-201
    • Hu, X.1    O'Hara, L.2    White, S.3
  • 160
    • 23844516816 scopus 로고    scopus 로고
    • A universal strategy for stable intracellular antibodies
    • Shaki-Loewenstein S, Zfania R, Hyland S, et al. A universal strategy for stable intracellular antibodies. J Immunol Methods 2005;303(1-2):19-39
    • (2005) J Immunol Methods , vol.303 , Issue.1-2 , pp. 19-39
    • Shaki-Loewenstein, S.1    Zfania, R.2    Hyland, S.3
  • 161
    • 33644759558 scopus 로고    scopus 로고
    • Thioredoxin fusions increase folding of single chain Fv antibodies in the cytoplasm of Escherichia coli: Evidence that chaperone activity is the prime effect of thioredoxin
    • Jurado P, de Lorenzo V, Fernandez LA. Thioredoxin fusions increase folding of single chain Fv antibodies in the cytoplasm of Escherichia coli: evidence that chaperone activity is the prime effect of thioredoxin. J Mol Biol 2006;357(1):49-61
    • (2006) J Mol Biol , vol.357 , Issue.1 , pp. 49-61
    • Jurado, P.1    De Lorenzo, V.2    Fernandez, L.A.3
  • 162
    • 77949894368 scopus 로고    scopus 로고
    • Functional expression of single-chain Fv antibody in the cytoplasm of Escherichia coli by thioredoxin fusion and co-expression of molecular chaperones
    • [Epub ahead of print]
    • Sonoda H, Kumada Y, Katsuda T, Yamaji H. Functional expression of single-chain Fv antibody in the cytoplasm of Escherichia coli by thioredoxin fusion and co-expression of molecular chaperones. Protein Expr Purif 2009 [Epub ahead of print]
    • (2009) Protein Expr Purif
    • Sonoda, H.1    Kumada, Y.2    Katsuda, T.3    Yamaji, H.4
  • 163
    • 0344549167 scopus 로고    scopus 로고
    • The hierarchy of mutations influencing the folding of antibody domains in Escherichia coli
    • Wall JG, Pluckthun A. The hierarchy of mutations influencing the folding of antibody domains in Escherichia coli. Protein Eng 1999;12(7):605-611
    • (1999) Protein Eng , vol.12 , Issue.7 , pp. 605-611
    • Wall, J.G.1    Pluckthun, A.2
  • 164
    • 1542321146 scopus 로고    scopus 로고
    • Prospects for molecular farming in the green alga Chlamydomonas
    • Franklin SE, Mayfield SP. Prospects for molecular farming in the green alga Chlamydomonas. Curr Opin Plant Biol 2004;7(2):159-165
    • (2004) Curr Opin Plant Biol , vol.7 , Issue.2 , pp. 159-165
    • Franklin, S.E.1    Mayfield, S.P.2
  • 165
    • 30544435865 scopus 로고    scopus 로고
    • Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli
    • Zhang G, Brokx S, Weiner JH. Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli. Nat Biotechnol 2006;24(1):100-104
    • (2006) Nat Biotechnol , vol.24 , Issue.1 , pp. 100-104
    • Zhang, G.1    Brokx, S.2    Weiner, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.