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1
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0032471590
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The development of monoclonal antibodies for the therapy of cancer
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This review is an excellent summary of the clinical applications using monoclonal antibodies and recombinant derivatives up to 1998.
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Farah RA, Clinchy B, Herrera L, Vitetta ES The development of monoclonal antibodies for the therapy of cancer. Crit Rev Eukaryot Gene Expr. 8:1998;321-345. This review is an excellent summary of the clinical applications using monoclonal antibodies and recombinant derivatives up to 1998.
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Crit Rev Eukaryot Gene Expr
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, pp. 321-345
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Farah, R.A.1
Clinchy, B.2
Herrera, L.3
Vitetta, E.S.4
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2
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0032146225
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Recombinant antibody fragments
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This review summarises the highlights in recombinant antibody designs in 1997 and early 1998. A comparison with my current review here demonstrates the very rapid progress that has been made in the design and engineering of recombinant antibody fragments throughout 1998 and 1999.
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Hudson PJ Recombinant antibody fragments. Curr Opin Biotechnol. 9:1998;395-402. This review summarises the highlights in recombinant antibody designs in 1997 and early 1998. A comparison with my current review here demonstrates the very rapid progress that has been made in the design and engineering of recombinant antibody fragments throughout 1998 and 1999.
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Curr Opin Biotechnol
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Hudson, P.J.1
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4
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0031785720
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Use of rituximab, the new FDA-approved antibody
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This publication reviews the pharmocokinetics and Phase I and II trials for the first FDA-approved recombinant cancer therapeutic antibody. The antibody was designed as a simple chimaera of mouse V-domains fused to human C-domains. In the pivotal study of Rituximab, an overall response rate of 50% was achieved with median time to progression in responders of 13.2 months. It is a useful reference for initial clinical data using recombinant antibodies and will be followed by many other publications in 1999 describing more detailed clinical trials with 'Rituxan' and other therapeutic recombinant antibodies.
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Leget GA, Czuczman MS Use of rituximab, the new FDA-approved antibody. Curr Opin Oncol. 10:1998;548-551. This publication reviews the pharmocokinetics and Phase I and II trials for the first FDA-approved recombinant cancer therapeutic antibody. The antibody was designed as a simple chimaera of mouse V-domains fused to human C-domains. In the pivotal study of Rituximab, an overall response rate of 50% was achieved with median time to progression in responders of 13.2 months. It is a useful reference for initial clinical data using recombinant antibodies and will be followed by many other publications in 1999 describing more detailed clinical trials with 'Rituxan' and other therapeutic recombinant antibodies.
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(1998)
Curr Opin Oncol
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, pp. 548-551
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Leget, G.A.1
Czuczman, M.S.2
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5
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0032895235
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Trastuzumab, a recombinant DNA-derived humanized monoclonal antibody, a novel agent for the treatment of metastatic breast cancer
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Goldenberg MM Trastuzumab, a recombinant DNA-derived humanized monoclonal antibody, a novel agent for the treatment of metastatic breast cancer. Clin Ther. 21:1999;309-318.
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Clin Ther
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Goldenberg, M.M.1
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0033053528
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Display technologies expand their horizons
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Bradbury A Display technologies expand their horizons. Trends Biotechnol. 17:1999;137-138.
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Trends Biotechnol
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Bradbury, A.1
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8
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0033603596
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A large non-immunized human Fab fragment phage library that permits rapid isolation and kinetic analysis of high affinity antibodies
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This is probably the largest naïve Fab library constructed to date. Refer to World Wide Web sites listed in [82-87] for descriptions of other antibody libraries that are commercially available.
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de Haard HJ, van Neer N, Reurs A, Hufton SE, Roovers RC, Henderikx P, de Bruine AP, Arends JW, Hoogenboom HR A large non-immunized human Fab fragment phage library that permits rapid isolation and kinetic analysis of high affinity antibodies. J Biol Chem. 274:1999;18218-18230. This is probably the largest naïve Fab library constructed to date. Refer to World Wide Web sites listed in [82-87] for descriptions of other antibody libraries that are commercially available.
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J Biol Chem
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De Haard, H.J.1
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Reurs, A.3
Hufton, S.E.4
Roovers, R.C.5
Henderikx, P.6
De Bruine, A.P.7
Arends, J.W.8
Hoogenboom, H.R.9
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9
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0033153570
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Identification of a human anti-CD55 single-chain Fv by subtractive panning of a phage library using tumor and nontumor cell lines
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Ridgway JB, Ng E, Kern JA, Lee J, Brush J, Goddard A, Carter P Identification of a human anti-CD55 single-chain Fv by subtractive panning of a phage library using tumor and nontumor cell lines. Cancer Res. 59:1999;2718-2723.
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Ridgway, J.B.1
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Carter, P.7
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0032144281
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Model and simulation of multivalent binding to fixed ligands
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Muller KM, Arndt KM, Pluckthun A Model and simulation of multivalent binding to fixed ligands. Anal Biochem. 261:1998;149-157.
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Muller, K.M.1
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0032532015
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Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE, and IgA2, to form small immune complexes: A role for flexibility and geometry
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Roux KH, Strelets L, Brekke OH, Sandlie I, Michaelsen TE Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE, and IgA2, to form small immune complexes: a role for flexibility and geometry. J Immunol. 161:1998;4083-4090.
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J Immunol
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Roux, K.H.1
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12
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0031967887
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Structure of a neutralizing antibody bound monovalently to human rhinovirus 2
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Hewat EA, Marlovits TC, Blaas D Structure of a neutralizing antibody bound monovalently to human rhinovirus 2. J Virol. 72:1998;4396-4402.
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J Virol
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Hewat, E.A.1
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0030806221
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Homodimerization of tumor-reactive monoclonal antibodies markedly increases their ability to induce growth arrest or apoptosis of tumor cells
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Ghetie MA, Podar EM, Ilgen A, Gordon BE, Uhr JW, Vitetta ES Homodimerization of tumor-reactive monoclonal antibodies markedly increases their ability to induce growth arrest or apoptosis of tumor cells. Proc Natl Acad Sci USA. 94:1997;7509-7514.
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Ghetie, M.A.1
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Vitetta, E.S.6
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14
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0032422140
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Pharmacokinetics and biodistribution of genetically-engineered antibodies
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An excellent review describing the practical limitations of large (150 kDa) IgGs resulting from slow clearance from the blood pool, poor diffusion from the vasculature and poor penetration through the tumour mass. Antibody valency and recombinant designs are also reviewed as are factors that are critical for the functional affinity of an antibody for a cell surface antigen or a polymeric antigen.
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Colcher D, Pavlinkova G, Beresford G, Booth BJM, Choudhury A, Batra SK Pharmacokinetics and biodistribution of genetically-engineered antibodies. Q J Nucl Med. 42:1998;225-241. An excellent review describing the practical limitations of large (150 kDa) IgGs resulting from slow clearance from the blood pool, poor diffusion from the vasculature and poor penetration through the tumour mass. Antibody valency and recombinant designs are also reviewed as are factors that are critical for the functional affinity of an antibody for a cell surface antigen or a polymeric antigen.
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Q J Nucl Med
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Colcher, D.1
Pavlinkova, G.2
Beresford, G.3
Booth, B.J.M.4
Choudhury, A.5
Batra, S.K.6
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15
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Dosimetric evaluation and radioimmunotherapy of anti-tumour multivalent Fab fragments
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Casey JL, Pedley RB, King DJ, Green AJ, Yarranton GT, Begent RHJ Dosimetric evaluation and radioimmunotherapy of anti-tumour multivalent Fab fragments. Brit J Cancer. 1999;. in press.
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Casey, J.L.1
Pedley, R.B.2
King, D.J.3
Green, A.J.4
Yarranton, G.T.5
Begent, R.H.J.6
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16
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0032144271
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F(ab')2 molecules made from Escherichia coli produced Fab' with hinge sequences conferring increased serum survival in an animal model
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Humphreys DP, Vetterlein OM, Chapman AP, King DJ, Antoniw P, Suitters AJ, Reeks DG, Parton TA, King LM, Smith BJet al. F(ab')2 molecules made from Escherichia coli produced Fab' with hinge sequences conferring increased serum survival in an animal model. J Immunol Methods. 217:1998;1-10.
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J Immunol Methods
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Humphreys, D.P.1
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King, D.J.4
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Suitters, A.J.6
Reeks, D.G.7
Parton, T.A.8
King, L.M.9
Smith, B.J.10
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17
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0032767275
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ScFv multimers: Length of the linker between VH and VL domains dictates precisely the transition between diabodies and triabodies
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This publication provides the first detailed description of the diabody → triabody transition and explains why scFv trimers are the preferred conformation when very short polypeptide linkers between V-domains prevent diabody formation.
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Atwell J, Breheney KA, Lawrence LJ, McCoy AJ, Kortt AA, Hudson PJ ScFv multimers: length of the linker between VH and VL domains dictates precisely the transition between diabodies and triabodies. Protein Eng. 12:1999;597-604. This publication provides the first detailed description of the diabody → triabody transition and explains why scFv trimers are the preferred conformation when very short polypeptide linkers between V-domains prevent diabody formation.
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Protein Eng
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Atwell, J.1
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Hudson, P.J.6
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18
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0032801102
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Di-, tri- And tetrameric single chain Fv antibody fragments against human CD19: Effect of valency on binding
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LeGall F, Kipriyanov SM, Moldenhauer G, Little M Di-, tri- and tetrameric single chain Fv antibody fragments against human CD19: effect of valency on binding. FEBS Lett. 453:1999;164-168.
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Legall, F.1
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0033046339
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Binding characteristics and tumor targeting of a covalently linked divalent CC49 single-chain antibody
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Beresford GW, Pavlinkova G, Booth BJ, Batra SK, Colcher D Binding characteristics and tumor targeting of a covalently linked divalent CC49 single-chain antibody. Int J Cancer. 81:1999;911-917.
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Beresford, G.W.1
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20
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0032478777
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Orientation of antigen binding sites in dimeric and trimeric single chain Fv antibody fragments
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Lawrence LJ, Kortt AA, Iliades P, Tulloch PA, Hudson PJ Orientation of antigen binding sites in dimeric and trimeric single chain Fv antibody fragments. FEBS Lett. 425:1998;479-484.
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Lawrence, L.J.1
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21
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0032006660
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Increased affinity leads to improved selective tumor delivery of single-chain Fv antibodies
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Adams GP, Schier R, Marshall K, Wolf EJ, McCall AM, Marks JD, Weiner LM Increased affinity leads to improved selective tumor delivery of single-chain Fv antibodies. Cancer Res. 58:1998;485-490.
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Adams, G.P.1
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Weiner, L.M.7
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22
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Prolonged in vivo tumor retention of a human diabody targeting the extracellular domain of human HER2/neu
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This phage-selected and affinity-matured recombinant antibody may be the world's first phage-engineered scFv in clinical trials. There is an excellent discussion of multivalent antibody design and an explanation of the functional affinity (avidity) gains that are made via apparently reduced off-rates, which result from both multiple binding and rebinding to the target antigens.
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Adams GP, Schier R, McCall AM, Crawford RS, Wolf EJ, Weiner LM, Marks JD Prolonged in vivo tumor retention of a human diabody targeting the extracellular domain of human HER2/neu. Brit J Cancer. 77:1998;1405-1412. This phage-selected and affinity-matured recombinant antibody may be the world's first phage-engineered scFv in clinical trials. There is an excellent discussion of multivalent antibody design and an explanation of the functional affinity (avidity) gains that are made via apparently reduced off-rates, which result from both multiple binding and rebinding to the target antigens.
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Brit J Cancer
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Adams, G.P.1
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Weiner, L.M.6
Marks, J.D.7
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23
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Increased binding affinity and valence of recombinant antibody fragments lead to improved targeting of tumoral angiogenesis
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Viti F, Tarli L, Giovannoni L, Zardi L, Neri D Increased binding affinity and valence of recombinant antibody fragments lead to improved targeting of tumoral angiogenesis. Cancer Res. 59:1999;347-352.
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Anti-carcinoembryonic antigen (CEA) diabody for rapid tumor targeting and imaging
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Wu AM, Williams LE, Zieran L, Padma A, Sherman M, Bebb GG, Odom-Maryon T, Wong JYC, Shively JE, Raubitschek AA Anti-carcinoembryonic antigen (CEA) diabody for rapid tumor targeting and imaging. Tumour Targeting. 4:1999;47-54.
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Minibody: A novel engineered anti-carcinoembryonic antigen antibody fragment (single-chain Fv-CH3) which exhibits rapid, high-level targeting of xenografts
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Hu S, Shively L, Raubitschek A, Sherman M, Williams LE, Wong JY, Shively JE, Wu AM Minibody: a novel engineered anti-carcinoembryonic antigen antibody fragment (single-chain Fv-CH3) which exhibits rapid, high-level targeting of xenografts. Cancer Res. 56:1996;3055-3061.
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Wu, A.M.8
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26
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0031733034
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IgM secretory tailpiece drives multimerisation of bivalent scFv fragments in eukaryotic cells
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Olafsen T, Rasmussen IB, Norderhaug L, Bruland OS, Sandlie I IgM secretory tailpiece drives multimerisation of bivalent scFv fragments in eukaryotic cells. Immunotechnology. 4:1998;141-153.
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0032891911
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Charge-modified single chain antibody constructs of monoclonal antibody CC49: Generation, characterization, pharmacokinetics, and biodistribution analysis
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Pavlinkova G, Beresford G, Booth BJ, Batra SK, Colcher D Charge-modified single chain antibody constructs of monoclonal antibody CC49: generation, characterization, pharmacokinetics, and biodistribution analysis. Nucl Med Biol. 26:1999;27-34.
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0032944094
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Chemical design of radiolabeled antibody fragments for low renal radioactivity levels
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Arano Y, Fujioka Y, Akizawa H, Ono M, Uehara T, Wakisaka K, Nakayama M, Sakahara H, Konishi J, Saji H Chemical design of radiolabeled antibody fragments for low renal radioactivity levels. Cancer Res. 59:1999;128-134.
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Chapman AP, Antoni P, Spitali M, West S, Stephens S, King DJ Therapeutic antibody fragments with prolonged in vivo half-lives. Nat Biotechnol. 17:1999;780-783.
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0032941030
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Tumor targeting with newly designed biparatopic antibodies directed against two different epitopes of the carcinoembryonic antigen (CEA)
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This paper describes the design of high-avidity antibodies by targeting two adjacent epitopes on a single target antigen. These 'biparatopic' antibodies are similar to 'CRAbs', the chelating recombinant antibodies described in [31]. High avidity will require that both arms bind simultaneously without a significant loss of entropy.
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Robert B, Dorvillius M, Buchegger F, Garambois V, Mani JC, Pugnieres M, Mach JP, Pelegrin A Tumor targeting with newly designed biparatopic antibodies directed against two different epitopes of the carcinoembryonic antigen (CEA). Int J Cancer. 81:1999;285-291. This paper describes the design of high-avidity antibodies by targeting two adjacent epitopes on a single target antigen. These 'biparatopic' antibodies are similar to 'CRAbs', the chelating recombinant antibodies described in [31]. High avidity will require that both arms bind simultaneously without a significant loss of entropy.
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Int J Cancer
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CD3xCD19 bispecific antibodies and CD28 bivalent antibodies enhance T-cell reactivity against autologous leukemic cells in pediatric B-ALL bone marrow
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Manzke O, Berthold F, Huebel K, Tesch H, Diehl V, Bohlen H CD3xCD19 bispecific antibodies and CD28 bivalent antibodies enhance T-cell reactivity against autologous leukemic cells in pediatric B-ALL bone marrow. Int J Cancer. 80:1999;715-722.
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A phase I study of a HER2/neu bispecific antibody with granulocyte-colony-stimulating factor in patients with metastatic breast cancer that overexpresses HER2/neu
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Pullarkat V, Deo Y, Link J, Spears L, Marty V, Curnow R, Groshen S, Gee C, Weber JS A phase I study of a HER2/neu bispecific antibody with granulocyte-colony-stimulating factor in patients with metastatic breast cancer that overexpresses HER2/neu. Cancer Immunol Immunother. 48:1999;9-21.
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Differential susceptibility of primary and established human glioma cells to adenovirus infection: Targeting via the epidermal growth factor receptor achieves fiber receptor-independent gene transfer
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Miller CR, Buchsbaum DJ, Reynolds PN, Douglas JT, Gillespie GY, Mayo MS, Raben D, Curiel DT Differential susceptibility of primary and established human glioma cells to adenovirus infection: targeting via the epidermal growth factor receptor achieves fiber receptor-independent gene transfer. Cancer Res. 58:1998;5738-5748.
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Bartlett JS, Kleinschmidt J, Boucher RC, Samulski RJ Targeted adeno-associated virus vector transduction of nonpermissive cells mediated by a bispecific F(ab'gamma)2 antibody. Nat Biotechnol. 17:1999;181-186.
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Kraeber-Bodere F, Faibre-Chauvet A, Sai-Maurel C, Gautherot E, Fiche M, Campion L, Le Boterff J, Barbet J, Chatal JF, Thedrez P Bispecific antibody and bivalent hapten radioimmunotherapy in CEA-producing medullary thyroid cancer xenograft. J Nucl Med. 40:1999;198-204.
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