Kortt AA - Search Results

1

Dimeric and trimeric antibodies: high avidity scFvs for cancer targeting.

Kortt AA, Dolezal O, Power BE, Hudson PJ. Kortt AA, et al. Biomol Eng. 2001 Oct 15;18(3):95-108. doi: 10.1016/s1389-0344(01)00090-9. Biomol Eng. 2001. PMID: 11566601 Review.

2

Large-scale bacterial fermentation and isolation of scFv multimers using a heat-inducible bacterial expression vector.

Bayly AM, Kortt AA, Hudson PJ, Power BE. Bayly AM, et al. Among authors: kortt aa. J Immunol Methods. 2002 Apr 1;262(1-2):217-27. doi: 10.1016/s0022-1759(02)00021-2. J Immunol Methods. 2002. PMID: 11983235

3

Single-chain Fv multimers of the anti-neuraminidase antibody NC10: the residue at position 15 in the V(L) domain of the scFv-0 (V(L)-V(H)) molecule is primarily responsible for formation of a tetramer-trimer equilibrium.

Dolezal O, De Gori R, Walter M, Doughty L, Hattarki M, Hudson PJ, Kortt AA. Dolezal O, et al. Among authors: kortt aa. Protein Eng. 2003 Jan;16(1):47-56. doi: 10.1093/proeng/gzg006. Protein Eng. 2003. PMID: 12646692

4

Single-chain Fv fragments of anti-neuraminidase antibody NC10 containing five- and ten-residue linkers form dimers and with zero-residue linker a trimer.

Kortt AA, Lah M, Oddie GW, Gruen CL, Burns JE, Pearce LA, Atwell JL, McCoy AJ, Howlett GJ, Metzger DW, Webster RG, Hudson PJ. Kortt AA, et al. Protein Eng. 1997 Apr;10(4):423-33. doi: 10.1093/protein/10.4.423. Protein Eng. 1997. PMID: 9194168

5

Affinity maturation of recombinant antibodies using E. coli mutator cells.

Irving RA, Kortt AA, Hudson PJ. Irving RA, et al. Among authors: kortt aa. Immunotechnology. 1996 Jun;2(2):127-43. doi: 10.1016/1380-2933(96)00044-9. Immunotechnology. 1996. PMID: 9373321

6

Orientation of antigen binding sites in dimeric and trimeric single chain Fv antibody fragments.

Lawrence LJ, Kortt AA, Iliades P, Tulloch PA, Hudson PJ. Lawrence LJ, et al. Among authors: kortt aa. FEBS Lett. 1998 Apr 3;425(3):479-84. doi: 10.1016/s0014-5793(98)00292-0. FEBS Lett. 1998. PMID: 9563517 Free article.

7

Three-dimensional structures of single-chain Fv-neuraminidase complexes.

Malby RL, McCoy AJ, Kortt AA, Hudson PJ, Colman PM. Malby RL, et al. Among authors: kortt aa. J Mol Biol. 1998 Jun 19;279(4):901-10. doi: 10.1006/jmbi.1998.1794. J Mol Biol. 1998. PMID: 9642070

8

scFv multimers of the anti-neuraminidase antibody NC10: length of the linker between VH and VL domains dictates precisely the transition between diabodies and triabodies.

Atwell JL, Breheney KA, Lawrence LJ, McCoy AJ, Kortt AA, Hudson PJ. Atwell JL, et al. Among authors: kortt aa. Protein Eng. 1999 Jul;12(7):597-604. doi: 10.1093/protein/12.7.597. Protein Eng. 1999. PMID: 10436086

9

High avidity scFv multimers; diabodies and triabodies.

Hudson PJ, Kortt AA. Hudson PJ, et al. Among authors: kortt aa. J Immunol Methods. 1999 Dec 10;231(1-2):177-89. doi: 10.1016/s0022-1759(99)00157-x. J Immunol Methods. 1999. PMID: 10648937 Review.

10

ScFv multimers of the anti-neuraminidase antibody NC10: shortening of the linker in single-chain Fv fragment assembled in V(L) to V(H) orientation drives the formation of dimers, trimers, tetramers and higher molecular mass multimers.

Dolezal O, Pearce LA, Lawrence LJ, McCoy AJ, Hudson PJ, Kortt AA. Dolezal O, et al. Among authors: kortt aa. Protein Eng. 2000 Aug;13(8):565-74. doi: 10.1093/protein/13.8.565. Protein Eng. 2000. PMID: 10964986

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