Helix-stabilized Fv (hsFv) antibody fragments: substituting the constant domains of a Fab fragment for a heterodimeric coiled-coil domain.
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A. Plückthun | K. Arndt | K. Müller | A Plückthun | K M Müller | K M Arndt
[1] A. Plückthun,et al. Yet another numbering scheme for immunoglobulin variable domains: an automatic modeling and analysis tool. , 2001, Journal of molecular biology.
[2] A. Plückthun,et al. Stability engineering of antibody single-chain Fv fragments. , 2001, Journal of molecular biology.
[3] K. Tsumoto,et al. Functional construction of the anti-mucin core protein (MUC1) antibody MUSE11 variable regions in a bacterial expression system. , 2000, Journal of biochemistry.
[4] A. Plückthun,et al. A heterodimeric coiled-coil peptide pair selected in vivo from a designed library-versus-library ensemble. , 2000, Journal of molecular biology.
[5] A. Plückthun,et al. Domain interactions in antibody Fv and scFv fragments: effects on unfolding kinetics and equilibria , 1999, FEBS letters.
[6] H. Bosshard,et al. Extremely fast folding of a very stable leucine zipper with a strengthened hydrophobic core and lacking electrostatic interactions between helices. , 1999, Biochemistry.
[7] A. Plückthun,et al. Factors influencing the dimer to monomer transition of an antibody single-chain Fv fragment. , 1998, Biochemistry.
[8] A. Plückthun,et al. A dimeric bispecific miniantibody combines two specificities with avidity , 1998, FEBS letters.
[9] A. Plückthun,et al. The first constant domain (CH1 and CL) of an antibody used as heterodimerization domain for bispecific miniantibodies , 1998, FEBS letters.
[10] A. Plückthun,et al. New protein engineering approaches to multivalent and bispecific antibody fragments. , 1997, Immunotechnology : an international journal of immunological engineering.
[11] Tobin R. Sosnick,et al. The role of helix formation in the folding of a fully α‐helical coiled coil , 1996 .
[12] T. Logtenberg,et al. Leucine Zipper Dimerized Bivalent and Bispecific scFv Antibodies from a Semi-synthetic Antibody Phage Display Library (*) , 1996, The Journal of Biological Chemistry.
[13] E. Voss,et al. Comparative Properties of the Single Chain Antibody and Fv Derivatives of mAb 4-4-20 , 1996, The Journal of Biological Chemistry.
[14] J. Baenziger,et al. Thermal stabilization of a single‐chain Fv antibody fragment by introduction of a disulphide bond , 1995, FEBS letters.
[15] A. Baici,et al. Kinetics of folding of leucine zipper domains. , 1995, Biochemistry.
[16] M. Polymenis,et al. Domain interactions and antigen binding of recombinant anti-Z-DNA antibody variable domains. The role of heavy and light chains measured by surface plasmon resonance. , 1995, Journal of immunology.
[17] A. Plückthun,et al. Tetravalent miniantibodies with high avidity assembling in Escherichia coli. , 1995, Journal of molecular biology.
[18] R. Raag,et al. Single‐chain Fvs , 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[19] A. Plückthun,et al. An improved affinity tag based on the FLAG peptide for the detection and purification of recombinant antibody fragments. , 1994, BioTechniques.
[20] A. Lawson,et al. Multimerization behaviour of single chain Fv variants for the tumour-binding antibody B72.3. , 1994, Protein engineering.
[21] M. Whitlow,et al. Multivalent Fvs: characterization of single-chain Fv oligomers and preparation of a bispecific Fv. , 1994, Protein engineering.
[22] R. Webster,et al. Recombinant anti-sialidase single-chain variable fragment antibody. Characterization, formation of dimer and higher-molecular-mass multimers and the solution of the crystal structure of the single-chain variable fragment/sialidase complex. , 1994, European journal of biochemistry.
[23] R. Raag,et al. Crystallization of single-chain Fv proteins. , 1993, Journal of molecular biology.
[24] R L Stanfield,et al. Major antigen-induced domain rearrangements in an antibody. , 1993, Structure.
[25] I. Pastan,et al. A recombinant immunotoxin containing a disulfide-stabilized Fv fragment. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[26] T Prospero,et al. "Diabodies": small bivalent and bispecific antibody fragments. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[27] J. Bye,et al. Human anti‐self antibodies with high specificity from phage display libraries. , 1993, The EMBO journal.
[28] A. Plückthun. Mono‐ and Bivalent Antibody Fragments Produced in Escherichia coli: Engineering, Folding and Antigen Binding , 1992, Immunological reviews.
[29] M. Wittekind,et al. Production of stable anti-digoxin Fv in Escherichia coli. , 1992, Molecular immunology.
[30] A. Plückthun,et al. Miniantibodies: use of amphipathic helices to produce functional, flexibly linked dimeric FV fragments with high avidity in Escherichia coli. , 1992, Biochemistry.
[31] A. Plückthun,et al. Secretion and in vivo folding of the Fab fragment of the antibody McPC603 in Escherichia coli: influence of disulphides and cis-prolines. , 1991, Protein engineering.
[32] D. Givol,et al. The minimal antigen-binding fragment of antibodies--Fv fragment. , 1991, Molecular immunology.
[33] K. D. Hardman,et al. Conformational stability, folding, and ligand-binding affinity of single-chain Fv immunoglobulin fragments expressed in Escherichia coli. , 1991, Biochemistry.
[34] A. Plückthun,et al. The Functional Expression of Antibody Fv Fragments in Ischhuchia coli: Improved Vectors and a Generally Applicable Purification Technique , 1991, Bio/Technology.
[35] K. D. Hardman,et al. Immunological and structural characterization of a high affinity anti-fluorescein single-chain antibody. , 1990, Journal of Biological Chemistry.
[36] T. N. Bhat,et al. Small rearrangements in structures of Fv and Fab fragments of antibody D 1.3 on antigen binding , 1990, Nature.
[37] R. Glockshuber,et al. A comparison of strategies to stabilize immunoglobulin Fv-fragments. , 1990, Biochemistry.
[38] P. V. von Hippel,et al. Calculation of protein extinction coefficients from amino acid sequence data. , 1989, Analytical biochemistry.
[39] K. D. Hardman,et al. Single-chain antigen-binding proteins. , 1988, Science.
[40] R. Bruccoleri,et al. Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli. , 1988, Proceedings of the National Academy of Sciences of the United States of America.
[41] A. Plückthun,et al. Assembly of a functional immunoglobulin Fv fragment in Escherichia coli. , 1988, Science.
[42] Y. Satow,et al. Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A. , 1985, Journal of molecular biology.
[43] K. J. Dorrington,et al. Equilibrium and kinetic aspects of the interaction of isolated variable and constant domains of light chain with the Fd' fragment of immunoglobulin G. , 1979, Biochemistry.
[44] Bigelow Cc,et al. Equilibrium and kinetic aspects of subunit association in immunoglobulin G , 1974 .
[45] K. Arndt,et al. A dimeric bispeci¢c miniantibody combines two speci¢cities with avidity , 1998 .
[46] K. Arndt,et al. The ¢ rst constant domain ( C H 1 and C L ) of an antibody used as heterodimerization domain for bispeci ¢ c miniantibodies , 1998 .
[47] W. DeGrado,et al. The role of helix formation in the folding of a fully alpha-helical coiled coil. , 1996, Proteins.
[48] A. Plückthun,et al. Engineered turns of a recombinant antibody improve its in vivo folding. , 1995, Protein engineering.
[49] Y. Arata. Nuclear magnetic resonance studies of antibody-antigen interactions. , 1991, Ciba Foundation symposium.
[50] A. Plückthun,et al. Expression of functional antibody Fv and Fab fragments in Escherichia coli. , 1989, Methods in enzymology.
[51] L. Hood,et al. The generation of diversity in phosphorylcholine-binding antibodies. , 1984, Advances in immunology.
[52] C. Bigelow,et al. Equilibrium and kinetic aspects of subunit association in immunoglobulin G. , 1974, Biochemistry.