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Biochemisches Institut

Calendar of Events

Publications of Dr. Annemarie Honegger

Jost C., Stüber, JC., Honegger, A., Wu, Y., Batyuk, A. & Plückthun, A.  Rigidity of the ewxtracellular part of HER2: Evidence from engineering subdomain interfaces and shared-helix DARPin-DARPin fusions.  Protein Sci. 26, 1796-1806 (2017). PMID: 28639341.

Wu, Y., Batyuk, A., Honegger, A., Brandl, F., Mittl, PRE. & Plückthun, A. Rigidly connected multispecific artificial binders with adjustable geometries. Sci Rep 7, 11217 (2017). PMID: 28894181.

Batyuk, A., Wu, Y., Honegger, A., Heberling, MM. & Plückthun, A. DARPin-based crystallization chaperones exploit molecular geometry as a screening dimension in protein crystallography. J. Mol. Biol. 428, 1574-88 (2016). PMID: 26975886.

Tamaskovic, R., Schwill, M., Nagy-Davidescu, G., Jost, C., Schaefer, DC., Verdurmen, WP., Schaefer, JV., Honegger, A. & Plückthun, A. Intermolecular biparatopic trapping of ErbB2 prevents compensatory activation of PI3K/AKT via RAS-p110 crosstalk. Nat Commun 7, 11672 (2016). PMID: 27255951.

Ewald, C., Christen, MT., Watson, RP., Mihajlovic, M., Zhou, T., Honegger, A., Plückthun, A., Caflisch, A. & Zerbe, O. A combined NMR and computational approach to investigate peptide binding to a designed Armadillo repeat protein. J. Mol. Biol. 427, 1916-33 (2015). PMID: 25816772.

Friedel, T., Hanisch, LJ., Muth, A., Honegger, A., Abken, H., Plückthun, A., Buchholz, CJ. & Schneider, IC. Receptor-targeted lentiviral vectors are exceptionally sensitive toward the biophysical properties of the displayed single-chain Fv. Protein Eng. Des. Sel. 28, 93-106 (2015). PMID: 25715658.

Verdurmen, WP., Luginbühl, M., Honegger, A. & Plückthun, A. Efficient cell-specific uptake of binding proteins into the cytoplasm through engineered modular transport systems. J Control Release 200, 13-22 (2015). PMID: 25526701.

Dreier, B., Honegger, A., Hess, C., Nagy-Davidescu, G., Mittl, PR., Grütter, MG., Belousova, N., Mekheeva, G., Krasnykh, V. & Plückthun, A. Development of a generic adenovirus delivery system based on structure-guided design of bispecific trimeric DARPin adapters. PNAS USA 110, E869-877 (2013).

Jost, C., Schilling, J., Tamaskovic, R., Schwill, M., Honegger, A. & Plückthun, A. Structural basis for eliciting a cytotoxic effect in HER2-overexpressing cancer cells via binding to the extracellular domain of HER2. Structure 21, 1979-91 (2013).

Schlinkmann, KM., Honegger, A., Türeci, E., Robison, KE., Lipovsek, D. & Plückthun, A. Critical features for biosynthesis, stability, and functionality of a G protein-coupled receptor. PNAS USA 109, 9810-9815 (2012). 

Zhou, Q., Schneider, IC., Edes, I., Honegger, A., Bach, P., Schönfeld, K., Schambach, A., Wels, WS., Kneissl, S., Uckert, W. & Buchholz, CJ. T cell receptor gene transfer exclusively to human CD8+ cells enhances tumor cell killing. Blood 120, 4334-4442 (2012).

Stefan, N., Martin-Killias, P., Wyss-Stoeckle, S., Honegger, A., Zangemeister-Wittke, U. & Plückthun, A. DARPins recognizing the tumor-associated antigen EpCAM selected by phage and ribosome display and engineered for multivalency. J Mol Biol. 413, 826-843 (2011).

Honegger, A., Malebranche, AD., Röthlisberger, D. & Plückthun, A. The influence of the framework core residues on the biophysical properties of immunoglobulin heavy chain variable domains. Protein Eng. Des. Sel. 22, 121-134 (2009).

Kügler, M., Stein C., Schwenkert M., Saul D., Vockentanz L., Huber T., Wetzel SK., Scholz O., Plückthun A., Honegger A. & Fey GH. Stabilization and humanization of a single-chain Fv antibody fragment specific for human lymphocyte antigen CD19 by designed point mutations and CDR-grafting onto a human framework. Protein Eng. Des. Sel. 22, 135-147 (2009).

Honegger, A. Engineering antibodies for stability and efficient folding. in: Handb. Exp. Pharmacol. 181, 47-68 (2008).

Rothe, C., Urlinger, S., Löhning, C., Prassler, J., Stark, Y., Jäger, U., Hubner, B., Bardroff, M., Pradel, I., Boss, M., Bittlingmaier, R., Bataa, T., Frisch, C., Brocks, B., Honegger, A. & Urban, M. The human combinatorial antibody library HuCAL GOLD combines diversification of all six CDRs according to the natural immune system with a novel display method for efficient selection of high-affinity antibodies. J Mol Biol 376, 1182-1200 (2008).

Honegger, A., Spinelli, S., Cambillau, C. & Plückthun, A. A mutation designed to alter crystal packing permits structural analysis of a tight-binding fluorescein-scFv complex. Protein Sci. 14, 2537-2549 (2005).

Röthlisberger, D., Honegger, A. & Plückthun, A. Domain interactions in the Fab fragment: a comparative evaluation of the single-chain Fv and Fab format engineered with variable domains of different stability. J. Mol. Biol. 347, 773-789 (2005).

Ewert, S., Honegger, A. & Plückthun, A. Stability improvement of antibodies for extracellular and intracellular applications: CDR grafting to stable frameworks and structure-based framework engineering. Methods 34, 184-199 (2004).

Cesaro-Tadic, S., Lagos, D., Honegger, A., Rickard, J. H., Partridge, L. J., Blackburn, G. M. & Plückthun, A. Turnover-based in vitro selection and evolution of biocatalysts from a fully synthetic antibody library. Nat. Biotechnol. 21, 679-685 (2003).

Ewert, S., Honegger, A. & Plückthun, A. Structure-based improvement of the biophysical properties of immunoglobulin Vh domains with a generalizable approach. Biochemistry 42, 1517-1528 (2003).

Ewert, S., Huber, T., Honegger, A. & Plückthun, A. Biophysical properties of human antibody variable domains. J. Mol. Biol 325, 531-553 (2003).

Auf Der Maur, A., Zahnd, C., Fischer, F., Spinelli, S., Honegger, A., Cambillau, C., Escher, D., Plückthun, A. & Barberis, A. Direct in vivo screening of intrabody libraries constructed on a highly stable single-chain framework. J. Biol. Chem. 277, 45075-45086 (2002).

Kaufmann, M., Lindner, P., Honegger, A., Blank, K., Tschopp, M., Capitani, G., Plückthun, A.& Grütter, M. Crystal structure of the anti-His tag antibody 3D5 single-chain fragment complexed to its antigen. J. Mol. Biol. 318, 135-147 (2002)

Honegger, A. & Plückthun, A. Yet another numbering scheme for immunoglobulin variable domains: An automatic modeling and analysis tool. J. Mol. Biol. 309, 657-670 (2001).

Honegger, A. & Plückthun, A. The influence of the buried glutamine or glutamate residue in position 6 on the structure of Immunoglobulin variable domains. J. Mol. Biol. 309, 687-699 (2001).

Jermutus, L., Honegger, A., Schwesinger, F., Hanes, J. & Plückthun, A. Tailoring in vitro evolution for protein affinity or stability. Proc. Natl. Acad. Sci. USA 98, 75-80 (2001).

Jung, S., Spinelli, S., Schimmele, B., Honegger, A., Pugliese, L., Cambillau, C. & Plückthun, A. The importance of framework residue H6, H7 and H10 in antibody heavy chains: Experimental evidence for a new structural subclassification of antibody VH domains. J. Mol. Biol. 309, 701-716 (2001).

Knappik, A., Ge, L., Honegger, A., Pack, P., Fischer, M., Wellnhofer, G., Hoess, A., Wölle, J., Plückthun, A. & Virnekäs, B. Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides. J. Mol. Biol. 296, 57-86 (2000).

Schwesinger, F., Ros, R., Strunz, T., Anselmetti, D., Güntherodt, H.-J., Honegger, A., Jermutus, L., Tiefenauer, L. & Plückthun, A. Unbinding forces of single antibody-antigen complexes correlate with their thermal dissociation rates. Proc. Natl. Acad. Sci. USA 97, 9972-9977 (2000).

Wörn, A., Auf der Maur, A., Escher, D., Honegger, A., Barberis, A. & Plückthun, A. Correlation between in vitro stability and in vivo performance of anti-GCN4 intrabodies as cytoplasmic inhibitors. J. Biol. Chem. 275, 2795-2803 (2000).

Jung, S., Honegger, A. & Plückthun, A. Selection for improved protein stability by phage display. J. Mol. Biol. 294, 163-80 (1999).

Langedijk, A. C., Spinelli, S., Anguille, C., Hermans, P., Nederlof, J., Butenandt, J., Honegger, A., Cambillau, C. & Plückthun, A. Insight into odorant perception: The crystal structure and binding characteristics of antibody fragments directed against the musk odorant traseolide. J. Mol. Biol. 292, 855-869 (1999).

Willuda, J., Honegger, A., Waibel, R., Schubiger, P. A., Stahel, R., Zangemeister-Wittke, U. & Plückthun, A. High thermal stability is essential for tumor targeting of antibody fragments: Engineering of a humanized anti-epithelial glycoprotein-2 (epithelial cell adhesion molecule) single-chain Fv fragment. Cancer Res. 59, 5758-5767 (1999).

Langedijk, A. C., Honegger, A., Maat, J., Planta, R. J., van Schaik, R. C. & Plückthun, A. The nature of antibody heavy chain residue H6 strongly influences the stability of a VH domain lacking the disulfide bridge. J. Mol. Biol. 283, 95-110 (1998).

Proba, K., Wörn, A., Honegger, A. & Plückthun, A. Antibody scFv fragments without disulfide bonds made by molecular evolution. J. Mol. Biol. 275, 245-253 (1998).

Spada, S., Honegger, A. & Plückthun, A. Reproducing the natural evolution of protein structural features with the selectively infective phage (SIP) technology. The kink in the first strand of antibody kappa domains. J. Mol. Biol. 283, 395-407 (1998).

Brüggeman, Y. E., Honegger, A., Kreuwel, H., Visser, A. J., Laane, C., Schots, A. & Hilhorst, R. Regulation of the flavin redox potential by flavin-binding antibodies. Eur J Biochem 249, 393-400 (1997).

Krebber, A., Bornhauser, S., Burmester, J., Honegger, A., Willuda, J., Bosshard, H.R. & Plückthun, A. Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system. J Immunol Meth 201, 35-55 (1997).

Lindner, P., Bauer, K., Krebber, A., Nieba, L., Kremmer, E., Krebber, C., Honegger, A., Klinger, B., Mocikat, R. & Plückthun, A. Specific detection of His-tagged proteins with recombinant anti-His tag scFv-phosphatase or scFv-phage fusions. BioTechniques 22, 140-149 (1997).

Nieba, L., Honegger, A., Krebber, C. & Plückthun, A. Disrupting the hydrophobic patches at the antibody variable/constant domain interface: Improved in vivo folding and physical characterization of an engineered scFv fragment. Protein Eng. 10, 435-444 (1997).

Pedrazzi, G., Schwesinger, F., Honegger, A., Krebber, C. & Plückthun, A. Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodology. FEBS Lett. 415, 289-293 (1997).

Proba, K., Honegger, A. & Plückthun, A. A natural antibody missing a cysteine in VH: Consequences for thermodynamic stability and folding. J. Mol. Biol. 265, 161-172 (1997).

Freund, C., Honegger, A., Hunziker, P., Holak, TA. & Plückthun, A. Folding nuclei of the scFv fragment of an antibody. Biochemistry 35, 8457-8464 (1996).

Mohammadi, M., Honegger, A., Sorokin, A., Ullrich, A., Schlessinger, J. & Hurwitz, DR. Aggregation-induced activation of the epidermal growth factor receptor protein tyrosine kinase. Biochemistry 32, 8742-8748 (1993).

Mohammadi, M., Dionne, C. A., Li, W., Li, N., Spivak, T., Honegger, AM, Jaye, M. & Schlessinger, J. Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis. Nature 358, 681-684 (1992).

Rotin, D., Honegger, A. M., Margolis, B. L., Ullrich, A. & Schlessinger, J. Presence of SH2 domains of phospholipase C gamma 1 enhances substrate phosphorylation by increasing the affinity toward the epidermal growth factor receptor. J Biol Chem 267, 9678-9683 (1992).

Mohammadi, M., Honegger, A. M., Rotin, D., Fischer, R., Bellot, F., Li, W., Dionne, C. A., Jaye, M., Rubinstein, M. & Schlessinger, J. A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1. Mol Cell Biol 11, 5068-5078 (1991).

Buergisser, DM., Roth, B. V., Luethi, C., Gerber, H. P., Honegger, A. & Humbel, RE. Expression of a human insulin-like growth factor II cDNA in NIH-3T3 cells. BiochemBiophysResComm 169, 832-839 (1990).

Honegger, AM., Schmidt, A., Ullrich, A. & Schlessinger, J. Evidence for epidermal growth factor (EGF)-induced intermolecular autophosphorylation of the EGF receptors in living cells. Mol Cell Biol 10, 4035-4044 (1990).

Honegger, AM., Schmidt, A., Ullrich, A. & Schlessinger, J. Separate endocytic pathways of kinase-defective and -active EGF receptor mutants expressed in same cells. J Cell Biol 110, 1541-1548 (1990).

Hsu, C. Y., Mohammadi, M., Nathan, M., Honegger, A., Ullrich, A., Schlessinger, J. & Hurwitz, DR. Generation of recombinant cytoplasmic domain of epidermal growth factor receptor with intrinsic protein tyrosine kinase activity. Cell Growth & Diff 1, 191-200 (1990).

Lax, I., Bellot, F., Honegger, AM., Schmidt, A., Ullrich, A., Givol, D. & Schlessinger, J. Domain deletion in the extracellular portion of the EGF-receptor reduces ligand binding and impairs cell surface expression. Cell Regul 1, 173-188 (1990).

Margolis, B., Bellot, F., Honegger, AM., Ullrich, A., Schlessinger, J. & Zilberstein, A. Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor. Mol Cell Biol 10, 435-441 (1990).

Honegger, A.M., Kris, R. M., Ullrich, A. & Schlessinger, J. Evidence that autophosphorylation of solubilized receptors for epidermal growth factor is mediated by intermolecular cross-phosphorylation. Proc Natl Acad Sci U S A 86, 925-929 (1989).

Margolis, B. L., Lax, I., Kris, R., Dombalagian, M., Honegger, AM., Howk, R., Givol, D., Ullrich, A. & Schlessinger, J. All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor. Journal of Biological Chemistry 264, 10667-10671 (1989).

Riedel, H., Dull, T. J., Honegger, AM., Schlessinger, J. & Ullrich, A. Cytoplasmic domains determine signal specificity, cellular routing characteristics and influence ligand binding of epidermal growth factor and insulin receptors. EMBO J 8, 2943-2954 (1989).

Scimeca, J. C., Ballotti, R., Alengrin, F., Honegger, AM., Ullrich, A., Schlessinger, J. & Obberghen, EV. Metabolic effects induced by epidermal growth factor (EGF) in cells expressing EGF receptor mutants. J Biol Chem 264, 6831-6835 (1989).

Honegger, A., Dull, T. J., Bellot, F., Van Obberghen, E., Szapary, D., Schmidt, A., Ullrich, A. & Schlessinger, J. Biological activities of EGF-receptor mutants with individually altered autophosphorylation sites. EMBO J 7, 3045-3052 (1988).

Honegger, A., Dull, T. J., Szapary, D., Komoriya, A., Kris, R., Ullrich, A. & Schlessinger, J. Kinetic parameters of the protein tyrosine kinase activity of EGF-receptor mutants with individually altered autophosphorylation sites. EMBO J 7, 3053-3060 (1988).

Malek, AA., Hy, M., Honegger, A., Rose, K. & Brenner-Holzach, O. Fructose-1,6-bisphosphate aldolase from Drosophila melanogaster: primary structure analysis, secondary structure prediction, and comparison with vertebrate aldolases. Arch Biochem Biophys 266, 10-31 (1988).

Moolenaar, W. H., Bierman, A. J., Tilly, B. C., Verlaan, I., Defize, L. H., Honegger, A.M., Ullrich, A., & Schlessinger, J. A point mutation at the ATP-binding site of the EGF-receptor abolishes signal transduction. EMBO J 7, 707-710 (1988).

Schlessinger, J., Ullrich, A., Honegger, AM. & Moolenaar, WH. Signal transduction by epidermal growth factor receptor. Cold Spring Harbor Symp Quant Biol 53, 515-519 (1988).

Honegger, AM., Dull, TJ., Felder, S., Van Obberghen, E., Bellot, F., Szapary, D., Schmidt, A., Ullrich, A. & Schlessinger, J. Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing. Cell 51, 199-209 (1987).

Honegger, AM., Szapary, D., Schmidt, A., Lyall, R., Van Obberghen, E., Dull, T. J., Ullrich, A. & Schlessinger, J.. A mutant epidermal growth factor receptor with defective protein tyrosine kinase is unable to stimulate proto-oncogene expression and DNA synthesis. Mol Cell Biol 7, 4568-4571 (1987).

Honegger, A. & Humbel, RE. Insulin-like growth factors I and II in fetal and adult bovine serum. Purification, primary structures, and immunological cross-reactivities. J Biol Chem 261, 569-575 (1986).

Dafgard, E., Bajaj, M., Honegger, AM., Pitts, J., Wood, S. & Blundell, T. The conformation of insulin-like growth factors: relationships with insulins. Journal of Cell Science (Supplement) 3, 53-64 (1985).

Pearl, L. & Honegger, A. Generation of molecular surfaces for graphic display. J Mol Graph 1, 9-12 (1983).

Honegger, A., Hughes, G. J. & Wilson, K. J. Chemical modification of peptides by hydrazine. Biochem J 199, 53-59 (1981).

Wilson, K.J., Berchtold, M. & Honegger, A. The use of HPLC in peptide/protein chemistry. In: High performance liquid chromatography in protein and peptide chemistry, F. Lottspeich, ed. (Walter de Gruyter & Co.), pp. 159-174 (1981).

Wilson, KJ., Honegger, A. & Hughes, G. J.. Comparison of buffers and detection systems for high-pressure liquid chromatography of peptide mixtures. Biochem J 199, 43-51 (1981).

Wilson, K J., Honegger, A., Stötzel, RP. & Hughes, G.J. The behaviour of peptides on reverse-phase supports during high-pressure liquid chromatography. Biochem J 199, 31-41 (1981).