Publikationen

• Kuhn, S.M., Rubini, M., Müller, M.A. & Skerra, A. (2011) Biosynthesis of a fluorescent protein with extreme pseudo-stokes shift by introducing a genetically encoded non-natural amino acid outside the fluorophore. J Am Chem Soc. 133, 3708-3711

• Eichinger, A., Haneburger, I., Koller, C., Jung, K. & Skerra, A. (2011) Crystal structure of the sensory domain of Escherichia coli CadC, a member of the ToxR-like protein family. Protein Sci. 20, 656-669

• Haneburger, I., Eichinger, A., Skerra, A. & Jung, K. (2011) New insights into the signaling mechanism of the pH-responsive, membrane-integrated transcriptional activator CadC of Escherichia coli. J Biol Chem. 286, 10681-10689

• Stangl, S., Gehrmann, M., Riegger, J., Kuhs, K., Riederer, I., Sievert, W., Hube, K., Mocikat, R., Dressel, R., Kremmer, E., Pockley, A.G., Friedrich, L., Vigh, L., Skerra, A. & Multhoff, G. (2011) Targeting membrane heat-shock protein 70 (Hsp70) on tumors by cmHsp70.1 antibody. Proc Natl Acad Sci USA. 108, 733-738

• Schlapschy, M. & Skerra, A. (2011) Periplasmic chaperones used to enhance functional secretion of proteins in E. coli. Methods Mol Biol. 705, 211-224

• Schiefner, A., Chatwell, L., Breustedt, D.A. & Skerra, A. (2010) Structural and biochemical analyses reveal a monomeric state of the bacterial lipocalin Blc. Acta Crystallogr D Biol Crystallogr. 66, 1308-1315

• Chiu, H.J., Bakolitsa, C., Skerra, A., Lomize, A., Carlton, D., Miller, M.D., Krishna, S.S., Abdubek, P., Astakhova, T., Axelrod, H.L., Clayton, T., Deller, M.C., Duan, L., Feuerhelm, J., Grant, J.C., Grzechnik, S.K., Han, G.W., Jaroszewski, L., Jin, K.K., Klock, H.E., Knuth, M.W., Kozbial, P., Kumar, A., Marciano, D., McMullan, D., Morse, A.T., Nigoghossian, E., Okach, L., Paulsen, J., Reyes, R., Rife, C.L., van den Bedem, H., Weekes, D., Xu, Q., Hodgson, K.O., Wooley, J., Elsliger, M.A., Deacon, A.M., Godzik, A., Lesley, S.A. & Wilson I.A. (2010) Structure of the first representative of Pfam family PF09410 (DUF2006) reveals a structural signature of the calycin superfamily that suggests a role in lipid metabolism. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66, 1153-1159

• Kuhn, S. M., Rubini, M., Fuhrmann, M., Theobald, I. & Skerra, A. (2010) Engineering of an orthogonal aminoacyl-tRNA synthetase for efficient incorporation of the non-natural amino acid O-methyl-L-tyrosine using fluorescence-based bacterial cell sorting. J Mol Biol. 404, 70-87

• Schmidt, M., Raghavan, B., Müller, V., Vogl, T., Fejer, G., Tchaptchet, S., Keck, S., Kalis, C., Nielsen, P. J., Galanos, C., Roth, J., Skerra, A., Martin, S. F., Freudenberg, M. A. & Goebeler, M. (2010) Crucial role for human Toll-like receptor 4 in the development of contact allergy to nickel. Nat Immunol. 11, 814-819.

• Binder, U., Matschiner, G., Theobald, I. & Skerra, A. (2010) High-throughput sorting of an anticalin library via EspP-mediated functional display on the Escherichia coli cell surface. J Mol Biol. 400, 783-802.

• Wiebe, J. C., Schüller, C., Reiche, J. A., Kramer, K., Skerra, A. & Hock, B. (2010) An expression system for the E. coli fermentation of recombinant antibody Fab fragments from mice and rabbits. J AOAC Int. 93, 80-88.

• Schüller, C., Wiebe, J. C., Pegel, A., Kramer, K., Skerra, A. & Hock, B. (2010) A system for repertoire cloning and phage display of murine and leporid antibody fragments. J AOAC Int. 93, 66-79.

• Nava, P., Koch, S., Laukoetter, M. G., Lee, W. Y., Kolegraff, K., Capaldo, C. T., Beeman, N., Addis, C., Gerner-Smidt, K., Neumaier, I., Skerra, A., Li, L., Parkos, C. A., & Nusrat, A. (2010) Interferon-gamma regulates intestinal epithelial homeostasis through converging beta-catenin signaling pathways. Immunity 32, 392-402.

• 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. 23, 161-168.

• Miethke, M. & Skerra, A. (2010) Neutrophil gelatinase-associated lipocalin possesses antimicrobial activity by interfering with L-norepinephrine-mediated bacterial iron acquisition. Antimicrob Agents Chemother. 54, 1580-1589.

• 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, 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, 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, 7411-7419.

• Gebauer M. & Skerra A. (2009) Engineered protein scaffolds as next-generation antibody therapeutics. Curr Opin Chem Biol. 13, 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. (2008) 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: 31. März 2011

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