References to Primary Literature
- SAMLOFF IM, TAGGART RT, SHIRAISHI T, BRANCH T, REIDWA, HEATH R, LEWIS RW, VALLER MJ, AND KAY J: Slow moving proteinase - isolation, characterization, and immunohistochemical localization in gastric-mucosa. Gastroenterol. (1987) 93: 77–84.
- HIGGINS CF: ABC transporters - from microorganismsto man. Ann. Rev. Cell Biol. (1992) 8: 67–113.
- SPOONER RA, EPENETOS AA: Anticancer antibodies:patent activity in 1993. Exp. Opin Ther. Patents 0990 4(6): 621–627.
- MORRISON SL, JOHNSON MJ, HERZENBERG CA, 01 VT: Chimaeric human antibody molecules: mouse antigen binding domains with human constant region do- mains. Proc. Natl. Acad. Sci. USA (1984) 81: 6851–6855. Reduction of the xenogeneic content of an antibody for clinical administration by fusing murine variable domains to human constant domains. Patients receiving these antibodies should raise an anti-body immune response only to the murine component; this reduced human anti-mouse response should permit repeated administration.
- RIECHMANN L, CLARK M, WALDMANN H, WINTER G:Reshaping human antibodies for therapy. Nature (1988)322: 323–327. This and the following reference describe replacing the CDRs of a human antibody with those from a rodent antibody, thus transferring an antibody specificity raised in rodents to an almost completely human molecule. A very much reduced human anti-mouse response should be generated.
- VERHOEYEN M, MILSTEIN C, WINTER: Reshaping humanantibodies: grafting an anti-lysozyme activity. Science(1988) 239: 1534–1536. See note for reference above.
- BENDIG MM, KETTLEBOROUGH CA, JONES ST, MAEDA H,SALDANHA J: The humanization of mouse monoclonal antibodies by CDR-grafting: examples with anti-viral and anti-tumour cell antibodies. In: Monoclonal Antibod-ies 2: Applications in Clinical Oncology. (Ed) A Epenetos, Chapman and Hall Medical, London pp 119–140 (1992). A general method for obtaining humanised antibodies.
- PADLAN EA: A possible procedure for reducing the immunogenicity of antibody variable domains while preserving their ligand-binding properties. Moi. Immu-not (1991) 28: 489–498. An alternative form of humanisation of antibody fragments that involves replacing amino acid residues on the surface of murine antibody domains with amino acids that are found in similar human molecules.
- HUSTON JS, LEVINSON D, MUDGETT-HUNTER M, TAI M-S,NOVOTNY J, MARGOLIES MN, RIDGE RJ, BRUCCOLERI RE,HABER E, CREA R, OPPERMAN H: Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain F. analog produced in Escberichia coll. Proc. Natl. Acad. Sci. USA (1988) 85: 5879–5883. This and the next reference describe the first single-chain F., mole-cules produced.
- BIRD RE, HARDMAN ICD, JACOBSON JW, JOHNSON S,KAUFMAN BM, LEE S-M: Single chain antigen-bindingproteins. Science (1988) 242: 423–426. See note for reference above.
- CHAUDHARY VK, QUEEN C, JUNGHANS RP, WALDMANNTA, FITZGERALD DJ, PASTAN I: A recombinant immuno-toxin consisting of two antibody variable domains fused to Pseudomonas exotoxin. Nature (1989) 339: 394–396. This describes an early recombinant immunotoxin.
- SAVAGE P, SO A, SPOONER RA, EPENETOS AA: A recom-• binant single chain antibody interleukin-2 fusion pro-tein. Br. J. Cancer (1993) 67: 304–310. This describes an sFv-cytokine fusion.
- PACK P, PLUCKTHUN A: Miniantibodies: use of amphi-pathic helices to produce functional, flexibly linked dimeric F. fragments with high avidity in Esthericbia coil. Biochem. (1992) 31: 1579–1584.
- Cytotoxic drug therapy and inactivation of cytotoxicdrugs. Exp. Opin. Ther. Patents.: (1994) 4(3:) 249–251.
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