Publikationen

• Friedrich, L., Stangl, S., Hahne, H., Küster, B., Köhler, P., Multhoff G. & Skerra A. (2010) Bacterial production and functional characterization of the Fab fragment of the murine IgG1/{lambda} monoclonal antibody cmHsp70.1, a reagent for tumour diagnostics. Protein Eng Des Sel. [Epub ahead of print]

• Miethke, M. & Skerra, A. (2010) Neutrophil gelatinase-associated lipocalin possesses antimicrobial activity by interfering with L-norepinephrine-mediated bacterial iron acquisition. Antimicrob Agents Chemother. [Epub ahead of print]

• Koch, S., Capaldo, C. T., Samarin, S., Nava, P., Neumaier, I., Skerra, A., Sacks, D. B., Parkos, C. A. & Nusrat, A. (2009) Dkk-1 inhibits intestinal epithelial cell migration by attenuating directional polarization of leading edge cells. Mol Biol Cell. 20(22), 4816-4825.

• Breustedt, D. A., Chatwell, L. & Skerra, A. (2009) A new crystal form of human tear lipocalin reveals high flexibility in the loop region and induced fit in the ligand cavity. Acta Crystallogr D Biol Crystallogr. 65(Pt10), 1118-1125.

• Mills, J. L., Liu, G., Skerra, A. & Szyperski, T. (2009) NMR structure and dynamics of the engineered fluorescein-binding lipocalin FluA reveal rigidification of beta-barrel and variable loops upon enthalpy-driven ligand binding. Biochemistry. 48(31), 7411-7419.

• Gebauer M. & Skerra A. (2009) Engineered protein scaffolds as next-generation antibody therapeutics. Curr Opin Chem Biol. 13(3), 245-255.

• Schönfeld D., Matschiner G., Chatwell L., Trentmann S., Gille H., Hülsmeyer M., Brown N., Kaye P.M., Schlehuber S., Hohlbaum A.M & Skerra A. (2009) An engineered lipocalin specific for CTLA-4 reveals a combining site with structural and conformational features similar to antibodies. Proc. Natl. Acad. Sci. USA, 105, 8198-8203.

• Kim, H. J., Eichinger, A. & Skerra, A. (2009) High-Affinity Recognition of Lanthanide(III) Chelate Complexes by a Reprogrammed Human Lipocalin 2. J. Am. Chem. Soc., 131, 3565-3576.

• Schlapschy, M., Fogarasi, M., Gruber, H., Gresch, O., Schäfer, C., Aguib, Y. & Skerra, A. (2009) Functional humanization of an anti-CD16 Fab fragment: obstacles of switching from murine λ to human λ or κ light chains. Protein Eng. Des. Sel., 22, 175-188.

• Jarchow, S., Lück, C., Görg, A. & Skerra, A. (2008) Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp. Proteomics, 8, 4987-4994.

• Haas, T. & Skerra, A. (2008) Weiße Biotechnologie - Innovationen für die Chemieindustrie. Nachr. Chem. 56, 1028-1031.

• Jäschke, A. & Skerra, A. (2008) Biochemie: mehr Bio oder mehr Chemie? Nachr. Chem. 56, 520-523.

• Schönfeld, D. L., Ravelli, R. B., Mueller, U. & Skerra, A. (2008) The 1.8-Å crystal structure of α1-acid glycoprotein (orosomucoid) solved by UV RIP reveals the broad drug-binding activity of this human plasma lipocalin. J. Mol. Biol. 384, 393-405.

• Krauss, N., Wessner, H., Welfle, K., Welfle, H., Scholz, C., Seifert, M., Zubow, K., Ay, J., Hahn, M., Scheerer, P., Skerra, A. & Höhne, W. (2008) The structure of the anti-c-myc antibody 9E10 Fab fragment/epitope peptide complex reveals a novel binding mode dominated by the heavy chain hypervariable loops. Proteins 73, 552-565.

• Korndörfer, I. P., Kanitz, A., Danzer, J., Zimmer, M., Loessner, M. J. & Skerra, A. Structural analysis of the L-alanoyl-D-glutamate endopeptidase domain of Listeria bacteriophage endolysin Ply500 reveals a new member of the LAS peptidase family. Acta Crystallogr. D 64, 644-650.

• Skerra, A. (2008) Alternative binding proteins: Anticalins - harnessing the structural plasticity of the lipocalin ligand pocket to engineer novel binding activities. FEBS J. 275, 2677-2683.

• Kolmar, H. & Skerra, A. (2008) Alternative binding proteins get mature: rivalling antibodies. FEBS J. 275, 2667.

• Chatwell, L., Illarionova, V., Illarionov, B., Eisenreich, W., Huber, R., Skerra, A., Bacher, A. & Fischer, M. (2008) Structure of lumazine protein, an optical transponder of luminescent bacteria. J. Mol. Biol. 382, 44-55.

• Bourquin, C., van der Haar, M. E., Anz, D., Sandholzer, N., Neumaier, I., Endres, S., Skerra, A., Schwab, M. E. & Linington, C. (2008) DNA vaccination efficiently induces antibodies to Nogo-A and does not exacerbate experimental autoimmune encephalomyelitis. Eur. J. Pharmacol. 588, 99-105.

• Wiedersich, J., Köhler, S., Skerra, A. [Corresponding Author] & Friedrich, J. (2008) Temperature and pressure dependence of protein stability: the engineered fluorescein-binding lipocalin FluA shows an elliptic phase diagram. Proc. Natl. Acad. Sci. USA 105, 5756-5761.

• Chatwell, L., Holla, A., Kaufer, B.B. & Skerra, A. (2008) The carbohydrate recognition domain of Langerin reveals high structural similarity with the one of DC-SIGN but an additional,calcium-independent sugar-binding site. Mol. Immunol. 45, 1981-1994.

• Eichinger, A., Nasreen, A., Kim, H.J. & Skerra, A. (2007) Structural insight into the dual ligand specificity and mode of high density lipoprotein association of apolipoprotein D. J Biol Chem 282, 31068-31075.

• Skerra, A. (2007) Alternative non-antibody scaffolds for molecular recognition. Curr Opin Biotechnol 18, 295-304

• Skerra, A. (2007) Anticalins as alternative binding proteins for therapeutic use. Curr Opin Mol Ther 9, 336-344

• Korndörfer, I. P., Brueckner, F. & Skerra, A. (2007) The crystal structure of the human (S100A8/S100A9)(2) heterotetramer, calprotectin, illustrates how conformational changes of interacting a-helices can determine specific association of two EF-hand proteins. J Mol Biol 370, 887-898.

• Hohlbaum, A.M. and Skerra, A. (2007) Anticalins: the lipocalin family as a novel protein scaffold for the development of next-generation immunotherapies. Expert Rev Clin Immunol 3, 491-501. 

• Schlapschy, M., Theobald, I., Mack, H., Schottelius, M., Wester, H. J. & Skerra, A. (2007) Fusion of a recombinant antibody fragment with a homo-amino-acid polymer: effects on biophysical properties and prolonged plasma half-life. Protein Eng Des Sel 20, 273-284.     

• Zander, H., Hettich, E., Greiff, K., Chatwell, L. & Skerra, A. (2007) Biochemical characterization of the recombinant human Nogo-A ectodomain. FEBS J 274, 2603-2613.

• Zander, H., Reineke, U., Schneider-Mergener, J. & Skerra, A. (2007) Epitope mapping of the neuronal growth inhibitor Nogo-A for the Nogo receptor and the cognate monoclonal antibody IN-1 by means of the SPOT technique. J Mol Recognit 20, 185-196.

• Schmidt, T. G. and Skerra, A. (2007) The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins. Nat Protoc 2, 1528-1535.

• Taussig, M. J., Stoevesandt, O., Borrebaeck, C. A., Bradbury, A. R., Cahill, D., Cambillau, C., de Daruvar, A., Dübel, S., Eichler, J., Frank, R., Gibson, T. J., Gloriam, D., Gold, L., Herberg, F. W., Hermjakob, H., Hoheisel, J. D., Joos, T. O., Kallioniemi, O., Koegll, M., Konthur, Z., Korn, B., Kremmer, E., Krobitsch, S., Landegren, U., van der Maarel, S., McCafferty, J., Muyldermans, S., Nygren, P. A., Palcy, S., Plückthun, A., Polic, B., Przybylski, M., Saviranta, P., Sawyer, A., Sherman, D. J., Skerra, A., Templin, M., Ueffing, M. & Uhlen, M. (2007) ProteomeBinders: planning a European resource of affinity reagents for analysis of the human proteome. Nat Methods 4, 13-17.

• Korndörfer, I. P., Danzer, J., Schmelcher, M., Zimmer, M., Skerra, A. & Loessner, M. J. (2006) The crystal structure of the bacteriophage PSA endolysin reveals a unique fold responsible for specific recognition of Listeria cell walls. J Mol Biol 364, 678-689.

• Breustedt, D. A., Schönfeld, D. L. & Skerra, A. (2006) Comparative ligand-binding analysis of ten human lipocalins. Biochim Biophys Acta 1764, 161-173.

• Nasreen, A., Vogt, M., Kim, H. J., Eichinger, A. & Skerra, A. (2006) Solubility engineering and crystallization of human apolipoprotein D. Protein Sci 15, 190-199.

• Schlapschy, M., Grimm, S. & Skerra, A. (2006) A system for concomitant overexpression of four periplasmic folding catalysts to improve secretory protein production in Escherichia coli. Protein Eng Des Sel 19, 385-390.

• Breustedt, D. A., Korndörfer, I. P., Redl, B. & Skerra, A. (2005) The 1.8-A crystal structure of human tear lipocalin reveals an extended branched cavity with capacity for multiple ligands. J Biol Chem 280, 484-493.

• Marget, M., Bohlsen, D., Davarnia, P., Yoo-Ott, K., Kabelitz, D., Skerra, A. & Steinmann, J. (2005) A HLA-Cw6 specific single-chain antibody fragment (scFv) recognizing a natural killer cell receptor epitope. Mol Immunol 42, 643-649.

• Schlehuber, S. & Skerra, A. (2005) Anticalins as an alternative to antibody technology. Expert Opin Biol Ther 5, 1453-1462.

• Schlehuber, S. & Skerra, A.(2005) Anticalins in drug development. BioDrugs 19, 279-288.

• Schlehuber, S. & Skerra, A. (2005) Lipocalins in drug discovery: from natural ligand-binding proteins to "anticalins". Drug Discov Today 10, 23-33.

• Vopel, S., Mühlbach, H. & Skerra, A. (2005) Rational engineering of a fluorescein-binding anticalin for improved ligand affinity. Biol Chem 386, 1097-1104.

• Korndörfer, I. P., Dommel, M. K. & Skerra, A. (2004) Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture. Nat Struct Mol Biol 11, 1015-1020.

• Lewinska, M., Seitz, C., Skerra, A. & Schmidtchen, F. P. (2004) A novel method for the N-terminal modification of native proteins. Bioconjug Chem 15, 231-234.

• Nygren, P. A. & Skerra, A. (2004) Binding proteins from alternative scaffolds. J Immunol Methods. 290, 3-28.

• Schlapschy, M., Gruber, H., Gresch, O., Schafer, C., Renner, C., Pfreundschuh, M. & Skerra, A. (2004) Functional humanization of an anti-CD30 Fab fragment for the immunotherapy of Hodgkin's lymphoma using an in vitro evolution approach. Protein Eng Des Sel. 17, 847-860.

• Schlapschy, M., Dommel, M. K., Hadian, K., Fogarasi, M., Körndorfer, I. P. & Skerra, A. (2004) The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical and preliminary crystallographic characterization. Biol Chem. 385, 137-143.

• Vogt, M. & Skerra, A. (2004) Construction of an artificial receptor protein ("anticalin") based on the human apolipoprotein D. Chembiochem 5, 191-199.

• Breithaupt, C., Schubart, A., Zander, H., Skerra, A., Huber, R., Linington, C. & Jacob, U. (2003) Structural insights into the antigenicity of myelin oligodendrocyte glycoprotein. Proc Natl Acad Sci U S A 100, 9446-9451.

• Korndörfer, I. P., Beste, G. & Skerra, A. (2003) Crystallographic analysis of an "anticalin" with tailored specificity for fluorescein reveals high structural plasticity of the lipocalin loop region. Proteins 53, 121-129.

• Korndörfer, I. P., Schlehuber, S. & Skerra, A. (2003) Structural mechanism of specific ligand recognition by a lipocalin tailored for the complexation of digoxigenin. J Mol Biol. 320, 385-396.

• Liu, G., Mills, J. L., Hess, T. A., Kim, S., Skalicky, J. J., Sukumaran, D. K., Kupce, E., Skerra, A. & Szyperski, T. (2003) Resonance assignments for the 21 kDa engineered fluorescein-binding lipocalin FluA. J Biomol NMR. 27, 187-188.

• Skerra, A. (2003) Imitating the humoral immune response. Curr Opin Chem Biol 7, 683-693.

• Skerra, A. (2003) Das Strep-tag als molekulares Werkzeug zur Hochdurchsatz-Proteinreinigung in der Proteomforschung. Biospektrum 9, 189-192.

• Fiedler, M., Horn, C., Bandtlow, C., Schwab, M. E. & Skerra, A. (2002) An engineered IN-1 F(ab) fragment with improved affinity for the Nogo-A axonal growth inhibitor permits immunochemical detection and shows enhanced neutralizing activity. Protein Eng 15, 931-941.

• Götz, M., Hess, S., Beste, G., Skerra, A. & Michel-Beyerle, M. E. (2002) Ultrafast electron transfer in the complex between fluorescein and a cognate engineered lipocalin protein, a so-called anticalin. Biochemistry 41, 4156-4164.

• Korndörfer, I. P. & Skerra, A. (2002) Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site. Protein Sci 11, 883-893.

• Kramer, K., Fiedler, M., Skerra, A. & Hock, B. (2002) A generic strategy for subcloning antibody variable regions from the scFv phage display vector pCANTAB 5 E into pASK85 permits the economical production of F(ab) fragments and leads to improved recombinant immunoglobulin stability. Biosens Bioelectron 17, 305-313.

• Mercader, J. V. & Skerra, A. (2002) Generation of anticalins with specificity for a nonsymmetric phthalic acid ester. Anal Biochem 308, 269-277.

• Schlehuber, S. & Skerra, A. (2002) Tuning ligand affinity, specificity, and folding stability of an engineered lipocalin variant -- a so-called 'anticalin' -- using a molecular random approach. Biophys Chem 96, 213-228.

• Tatagiba, M., Rosahl, S., Gharabaghi, A., Blomer, U., Brandis, A., Skerra, A., Samii, M. & Schwab, M. E. (2002) Regeneration of auditory nerve following complete sectioning and intrathecal application of the IN-1 antibody. Acta Neurochir (Wien) 144, 181-187.

• Fiedler, M. & Skerra, A. (2001) proBA complementation of an auxotrophic E. coli strain improves plasmid stability and expression yield during fermenter production of a recombinant antibody fragment. Gene 274, 111-118.

• Schlehuber, S. & Skerra, A. (2001) Duocalins: engineered ligand-binding proteins with dual specificity derived from the lipocalin fold. Biol Chem 382, 1335-1342.

• Skerra, A. (2001) 'Anticalins': a new class of engineered ligand-binding proteins with antibody-like properties. J Biotechnol 74, 257-275.

• Vogt, M. & Skerra, A. (2001) Bacterially produced apolipoprotein D binds progesterone and arachidonic acid, but not bilirubin or E-3M2H. J Mol Recognit 14, 79-86.

• Brösamle, C., Huber, A. B., Fiedler, M., Skerra, A. & Schwab, M. E. (2000) Regeneration of lesioned corticospinal tract fibers in the adult rat induced by a recombinant, humanized IN-1 antibody fragment.  J Neurosci 20, 8061-8068.

• Buffo, A., Zagrebelsky, M., Huber, A. B., Skerra, A., Schwab, M. E., Strata, P. & Rossi, F. (2000) Application of neutralizing antibodies against NI-35/250 myelin-associated neurite growth inhibitory proteins to the adult rat cerebellum induces sprouting of uninjured purkinje cell axons. J Neurosci 20, 2275-2286.

• Schlehuber, S., Beste, G. & Skerra, A. (2000) A novel type of receptor protein, based on the lipocalin scaffold, with specificity for digoxigenin. J Mol Biol 297, 1105-1120.

• Skerra, A. (2000) Lipocalins as a scaffold. Biochim Biophys Acta 1482, 337-350.

• Skerra, A. & Schmidt, T. G. (2000) Use of the Strep-tag and streptavidin for detection and purification of recombinant proteins. Methods Enzymol 326, 271-304.

• Skerra, A. (2000) Engineered protein scaffolds for molecular recognition. J Mol Recognit 13, 167-187.

• Skerra, A. & Schmidt T.G.M. (2000) Use of the Strep- tag and streptavidin for detection and purification of recombinant proteins. Methods in Enzymology 326, 271-304

• Beste, G., Schmidt, F. S., Stibora, T. & Skerra, A. (1999) Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold. Proc Natl Acad Sci U S A 96, 1898-1903.

• Fiedler, M. & Skerra, A. (1999) Use of thiophilic adsorption chromatography for the one-step purification of a bacterially produced antibody F(ab) fragment without the need for an affinity tag. Protein Expr Purif 17, 421-427.

• Kröger, D., Liley, M., Schiweck, W., Skerra, A. & Vogel, H. (1999) Immobilization of histidine-tagged proteins on gold surfaces using chelator thioalkanes. Biosens Bioelectron 14, 155-161.

• Osterroth, F., Alkan, O., Mackensen, A., Lindemann, A., Fisch, P., Skerra, A. & Veelken, H. (1999) Rapid expression cloning of human immunoglobulin Fab fragments for the analysis of antigen specificity of B cell lymphomas and anti-idiotype lymphoma vaccination. J Immunol Methods 229, 141-153.

• Skerra, A. & Schmidt, T. G. (1999) Applications of a peptide ligand for streptavidin: the Strep-tag. Biomol Eng 16, 79-86.

• Zahn, G., Skerra, A. & Höhne, W. (1999) Investigation of a tetracycline-regulated phage display system. Protein Eng 12, 1031-1034.

• zu Putlitz, J., Skerra, A. & Wands, J. R. (1999) Intracellular expression of a cloned antibody fragment interferes with hepatitis B virus surface antigen secretion. Biochem Biophys Res Commun 255, 785-791.

• König, T. & Skerra, A. (1998) Use of an albumin-binding domain for the selective immobilisation of recombinant capture antibody fragments on ELISA plates. J Immunol Methods 218, 73-83.

• Schmidt, A. M., Bloss, I. & Skerra, A. (1998) Improved folding of apo-retinol-binding protein in the periplasm of Escherichia coli: positive influences of dsbC coexpression and of an amino acid exchange in the vitamin A binding site. Protein Eng. 11, 601-607.

• Zagrebelsky, M., Buffo, A., Skerra, A., Schwab, M. E., Strata, P. & Rossi, F. (1998) Retrograde regulation of growth-associated gene expression in adult rat Purkinje cells by myelin-associated neurite growth inhibitory proteins. J Neurosci. 18, 7912-7929.

• zu Putlitz, J., Skerra, A., Schröder, C. H., Zentgraf, H. & Wands, J. R. (1998) Cloning, bacterial synthesis, and characterization of immunoglobulin variable regions of a monoclonal antibody specific for the hepatitis B virus X protein. Gene 221, 143-149.

• Schiweck, W., Buxbaum, B., Schätzlein, C., Neiss, H. G. & Skerra, A. (1997) Sequence analysis and bacterial production of the anti-c-myc antibody 9E10: the V(H) domain has an extended CDR-H3 and exhibits unusual solubility. FEBS Lett 414, 33-38.

• Schiweck, W. & Skerra, A. (1997) The rational construction of an antibody against cystatin: lessons from the crystal structure of an artificial Fab fragment. J Mol Biol 268, 934-951.

• Tudyka, T. & Skerra, A. (1997) Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli. Protein Sci 6, 2180-2187.

• Voss, S. & Skerra, A. (1997) Mutagenesis of a flexible loop in streptavidin leads to higher affinity for the Strep-tag II peptide and improved performance in recombinant protein purification. Protein Eng 10, 975-982.

• Bandtlow, C., Schiweck, W., Tai, H. H., Schwab, M. E. & Skerra, A. (1996) The Escherichia coli-derived Fab fragment of the IgM/kappa antibody IN-1 recognizes and neutralizes myelin-associated inhibitors of neurite growth. Eur J Biochem 241, 468-475.

• Schmidt, A. M., Müller, H. N. & Skerra, A. (1996) A Zn(II)-binding site engineered into retinol-binding protein exhibits metal-ion specificity and allows highly efficient affinity purification with a newly designed metal ligand. Chem Biol 3, 645-653.

• Skerra A. (1996) Design künstlicher Proteine mit neuen Eigenschaften. Spektrum der Wissenschaft, Dossier Pharmaforschung 110-113.

• Schmidt, T. G., Köpke, J., Frank, R. & Skerra, A. (1996) Molecular interaction between the Strep-tag affinity peptide and its cognate target, streptavidin. J Mol Biol 255, 753-766.

• Dübel, S., Breitling, F., Kontermann, R., Schmidt, T., Skerra, A. & Little, M. (1995) Bifunctional and multimeric complexes of streptavidin fused to single chain antibodies (scFv). J Immunol Methods 178, 201-209.

• Kleymann, G., Ostermeier, C., Ludwig, B., Skerra, A. & Michel, H. (1995) Engineered Fv fragments as a tool for the one-step purification of integral multisubunit membrane protein complexes. Biotechnology (N Y) 13, 155-160.

• Schiweck, W. & Skerra, A. (1995) Fermenter production of an artificial fab fragment, rationally designed for the antigen cystatin, and its optimized crystallization through constant domain shuffling. Proteins. 23, 561-565.

• Essen, L. O. & Skerra, A. (1994) The de novo design of an antibody combining site. Crystallographic analysis of the VL domain confirms the structural model. J Mol Biol 238, 226-244.

• Müller, H. N. & Skerra, A. (1994) Grafting of a high-affinity Zn(II)-binding site on the beta-barrel of retinol-binding protein results in enhanced folding stability and enables simplified purification. Biochemistry 33, 14126-14135.

• Schmidt, F. S. & Skerra, A. (1994) The bilin-binding protein of Pieris brassicae. cDNA sequence and regulation of expression reveal distinct features of this insect pigment protein. Eur J Biochem 219, 855-863.

• Schmidt, T. G. & Skerra, A. (1994) One-step affinity purification of bacterially produced proteins by means of the "Strep tag" and immobilized recombinant core streptavidin. J Chromatogr A 676, 337-345.

• Skerra, A. (1994) Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli. Gene 151, 131-135.

• Skerra, A. (1994) A general vector, pASK84, for cloning, bacterial production, and single-step purification of antibody Fab fragments. Gene 141, 79-84.

• Essen, L. O. & Skerra, A. (1993) Single-step purification of a bacterially expressed antibody Fv fragment by immobilized metal affinity chromatography in the presence of betaine. J Chromatogr A 657, 55-61.

• Müller, H. N. & Skerra, A. (1993) Functional expression of the uncomplexed serum retinol-binding protein in Escherichia coli. Ligand binding and reversible unfolding characteristics. J Mol Biol 230, 725-732.

• Schmidt, T. G. & Skerra, A. (1993) The random peptide library-assisted engineering of a C-terminal affinity peptide, useful for the detection and purification of a functional Ig Fv fragment. Protein Eng 6, 109-122.

• Skerra, A. (1993) Bacterial expression of immunoglobulin fragments. Curr Opin Immunol 5, 256-562.

• Skerra, A. (1992) Phosphorothioate primers improve the amplification of DNA sequences by DNA polymerases with proofreading activity. Nucleic Acids Res 20, 3551-3554.

• Dreher, M. L., Gherardi, E., Skerra, A. & Milstein, C. (1991) Colony assays for antibody fragments expressed in bacteria. J Immunol Methods 139, 197-205.

• Skerra, A. & Plückthun, A. (1991) Secretion and in vivo folding of the Fab fragment of the antibody McPC603 in Escherichia coli: influence of disulphides and cis-prolines. Protein Eng 4, 971-979.

• Skerra, A., Dreher, M. L. & Winter, G. (1991) Filter screening of antibody Fab fragments secreted from individual bacterial colonies: specific detection of antigen binding with a two-membrane system. Anal Biochem 196, 151-155.

• Skerra, A., Pfitzinger, I. & Plückthun, A. (1991) The functional expression of antibody Fv fragments in Escherichia coli: improved vectors and a generally applicable purification technique. Biotechnology (N Y) 9, 273-278.

• Plückthun, A., Glockshuber, R., Skerra, A. & Stadmuller, J. (1990) Properties of FV and Fab fragments of the antibody McPC603 expressed in E. coli. Behring Inst Mitt, 48-55.

• Skerra, A., Glockshuber, R. & Plückthun, A. (1990) Structural features of the McPC603 Fab fragment not defined in the X-ray structure. FEBS Lett 272, 203-206.

• Plückthun, A. & Skerra, A. (1989) Expression of functional antibody Fv and Fab fragments in Escherichia coli. Methods Enzymol 178, 497-515.

• Skerra, A. & Plückthun, A. (1988) Assembly of a functional immunoglobulin Fv fragment in Escherichia coli. Science 240, 1038-1041.

• Plückthun, A., Glockshuber, R., Pfitzinger, I., Skerra, A. & Stadlmüller, J. (1987) Engineering of antibodies with a known three-dimensional structure. Cold Spring Harb Symp Quant Biol 52, 105-112.

• Skerra, A. & Brickmann, J. (1987) Simulation of voltage-driven hydrated cation transport through narrow transmembrane channels. Biophys J. 51, 977-983.

Letzte Änderung: 5. März 2010

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