Publications of BioToP PhD-Students

(Highlighted are BioToP students and BioToP faculty members)


Mairinger, T., Wegscheider, W., Peña, D.A., Steiger, M.G., Koellensperger, G., Zanghellini, J., Hann, S. (2018) Comprehensive assessment of measurement uncertainty in 13C-based metabolic flux experiments Anal Bioanal Chem. doi: 10.1007/s00216-018-1017-7

Breslmayr, E., Hanžek, M., Hanrahan, A., Leitner, C., Kittl, R., Šantek, B., Oostenbrink, C., Ludwig, R. (2018). A fast and sensitive activity assay for lytic polysaccharide monooxygenase. Biotechnology for Biofuels, 11(1), 79. doi:10.1186/s13068-018-1063-6

Nicolussi, A., Auer, M., Sevcnikar, B., Paumann-Page, M., Pfanzagl, V., Zámocký, M., Hofbauer, S., Furtmüller, P.G., Obinger, C. (2018).Posttranslational modification of heme in peroxidases - Impact on structure and catalysis. Arch. Biochem. Biophys. 643, 14-23. doi: 10.1016/

Castilho, A., Beihammer, G., Christina Pfeiffer, C., Göritzer, K., Montero-Morales, L., Vavra, U., Maresch, D., Grünwald-Gruber, C., Altmann, F., Steinkellner H., Strasser, R. (2018) An oligosaccharyltransferase from Leishmania major increases the N-glycan occupancy on recombinant glycoproteins produced in Nicotiana benthamiana. Plant Biotechnol. J. doi: 10.1111/pbi.12906

Koczka, K., Peters, P., Ernst, W., Himmelbauer, H., Nika, L., Grabherr, R. (2018) Comparative transcriptome analysis of a Trichoplusia ni cell line reveals distinct host responses to intracellular and secreted protein products expressed by recombinant baculoviruses. J. Biotechnol. 270, 61–69. doi: 10.1016/j.jbiotec.2018.02.001

Heistinger, L., Gasser, B., Mattanovich, D. (2018) Creation of stable heterothallic strains of Komagataella phaffii enables dissection of mating gene regulation. Mol. Cell. Biol. 38:e00398-17. doi: 10.1128/MCB.00398-17

Sützl, L., Laurent, C.V.F.P., Abrera, A.T., Schütz, G., Ludwig, R., Haltrich, D. (2018) Multiplicity of enzymatic functions in the CAZy AA3 family. Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-018-8784-0

Bloch, S., Zwicker, S., Bostanci, N., Sjöling, A., Boström, E.A., Belibasakis, G.N., Schäffer, C. (2018) Immune response profiling of primary monocytes and oral keratinocytes to different Tannerella forsythia strains and their cell surface mutants. Mol. Oral. Microbiol. 00:1–13. doi:10.1111/omi.12208

Pfanzagl, V., Holcik, L., Maresch, D., Gorgone, G., Michlits, H., Furtmüller, P.G., Hofbauer, S. (2018) Coproheme decarboxylases - Phylogenetic prediction versus biochemical experiments. Arch. Biochem. Biophys. 640, 27-36. doi: 10.1016/

Nagelreiter, F., Coats, M., Klanert, G., Gludovacz, E., Borth, N., Grillari, J., Schosserer, M. (2018) OPP labelling enables total protein synthesis quantification in CHO production cell lines at the single-cell level. Biotechnol. J. doi: 10.1002/biot.201700492.

Proff, J., Brey, U.C., Ensser, A., Holter, W., Lehner, M (2018) Turning the tables on cytomegalovirus: targeting viral Fc receptors by CARs containing mutated CH2–CH3 IgG spacer domains. J. Transl. Med., 16-26.

Jungreuthmayer, C., Gerstl M.P., Peña Navarro, D.A., Hanscho, M., Ruckerbauer, D.E., Zanghellini, J. (2018) Designing Optimized Production Hosts by Metabolic Modeling. In: Fondi M. (eds) Metabolic Network Reconstruction and Modeling. Methods in Molecular Biology, vol 1716. Humana Press, New York, NY doi: 10.1007/978-1-4939-7528-0_17

Bönisch, E., Oh, Y.J., Anzengruber, J., Hager, F.F., Lopez-Guzman, A., Zayni, S., Hinterdorfer, P., Kosma, P., Messner, P., Duda, K.A., Schäffer C. (2018) Lipoteichoic acid mediates binding of a Lactobacillus S-layer protein. Glycobiology. doi: 10.1093/glycob/cwx102.

Weinmuellner, R., Kryeziu, K., Zbiral, B., Tav, K., Schoenhacker-Alte, B., Groza, D., Wimmer, L., Schosserer, M., Nagelreiter, F., Rösinger, S., Mildner, M., Tschachler, E., Grusch, M., Grillari, J., Heffeter, P. (2018)  Long-term exposure of immortalized keratinocytes to arsenic induces EMT, impairs differentiation in organotypic skin models and mimics aspects of human skin derangements. Arch. Toxicol. 92, 1, 181-194. doi: 10.1007/s00204-017-2034-6


Lobner, E., Humm, A., Mlynek, G., Kubinger, K., Kitzmüller, M., Traxlmayr, M. W., Djinović-Carugo, K., Obinger, C. (2017) Two-faced Fcab prevents polymerization with VEGF and reveals thermodynamics and the 2.15 A crystal structure of the complex. mAbs. 9, 1088-1104. doi: 10.1080/19420862.2017.1364825

Schmieder, V., Bydlinski, N., Strasser, R., Baumann, M., Kildegaard, H.F., Jadhav, V., Borth, N. (2017) Enhanced Genome Editing Tools For Multi-Gene Deletion Knock-Out Approaches Using Paired CRISPR sgRNAs in CHO Cells. Biotechnol. J. doi: 10.1002/biot.201700211

Prielhofer, R., Barrero, J.J., Steuer, S., Gassler, T., Zahrl, R., Baumann, K., Sauer, M., Mattanovich, D., Gasser, B., Marx, H. (2017)  GoldenPiCS: A Golden Gate-Derived Modular Cloning System for Applied Synthetic Biology in the Yeast Pichia Pastoris. BMC Sys Biol: 1–14. doi:10.1186/s12918-017-0492-3.

Schaffner, I., Mlynek, G., Flego, N., Pühringer, D., Libiseller-Egger, J., Coates, L.  Hofbauer, S., Bellei, M., Furtmüller, P. G., Battistuzzi, G.,  Smulevich, G., Djinovic-Carugo, K., Obinger, C. (2017) Molecular Mechanism of Enzymatic Chlorite Detoxification: Insights from Structural and Kinetic Studies. ACS Catal. 7, 7962-7976. doi: 10.1021/acscatal.7b01749

Zahrl, R.J., Peña, D.A., Mattanovich, D., Gasser, B. (2017) Systems biotechnology for protein production in Pichia pastoris. FEMS Yeast Research.17(7). doi:10.1093/femsyr/fox068

Nicolussi, A., Dunn, J. D., Mlynek, G., Bellei, M., Zamocky, M., Battistuzzi, G., Djinović-Carugo, K., Furtmuller, P. G., Soldati, T., Obinger, C. (2017) Secreted Heme Peroxidase from Dictyostelium discoideum: Insights into Catalysis, Structure and Biological Role. J Biol. Chem. 293, 1330-1345. doi: 10.1074/jbc.RA117.000463

Gludovacz, E., Maresch, D.,Carvalho, L.L. de, Puxbaum, V., Baier, L.J., Sützl, L., Guédez, G., Grünwald-Gruber, C., Ulm, B., Pils, S., Ristl, R., Altmann, F., Jilma, B., Salminen, T.A., Borth, N., Boehm, T. (2017) Oligomannosidic glycans at Asn110 are essential for secretion of human diamine oxidase. J. Biol. Chem. doi: 10.1074/jbc.M117.814244

Jandova, Z., Fast, D., Setz, M., Pechlaner, M., Oostenbrink, C. (2017) Saturation mutagenesis by efficient free-energy calculation. J. Chem. Theory Comput. online doi: 10.1021/acs.jctc.7b01099

Jandova, Z., Trosanova, Z., Weisova, V., Oostenbrink, C, Hritz, J. (2017) Free energy calculations on the stability of the 14-3-3ζ protein. BBA - Proteins and Proteomics 1866, 442-450. doi: 10.1016/j.bbapap.2017.11.012

Hennicke, J., Lastin, AM., Reinhart, D., Grünwald-Gruber, C., Altmann, F. and Kunert, R. (2017) Glycan profile of CHO derived IgM purified by highly efficient single step affinity chromatography. Anal Biochem. 539:162–166. doi: 10.1016/j.ab.2017.10.020

Scheiblbrandner, S., Breslmayr, E., Csarman, F., Paukner, R., Führer, J., Herzog, PL., Shleev, SV., Osipov, EM., Tikhonova, TV., Popov, VO., Haltrich, D., Ludwig, R. and Kittl, R. (2017) Evolving stability and pH-dependent activity of the high redox potential Botrytis aclada laccase for enzymatic fuel cells. Sci Rep. 7: 1368. doi: 10.1038/s41598-017-13734-0

Dillinger, B., Ahmadi-Erber, S., Soukup, K., Halfmann, A., Schrom, S., Vanhove, B., Steinberger, P., Geyeregger, R., Ladisch, S. and Dohnal, A. (2017) CD28 blockade ex vivo induces alloantigen-specific immune tolerance but preserves T cell pathogen reactivity. Front Immunol. 8: 1152 doi:10.3389/fimmu.2017.01152

Cong, J., Wang, Y, Zhang, X., Zhang, N., Liu, L., Soukup, K., Michelakos, T., Hong, T., DeLeo, A., Cai, L., Sabbatino, F., Ferrone, S., Lee, H., Levina, V., Fuchs, B., Tanabe, K., Lillemoe, K., Ferrone, C. and Wang, X. (2017) A novel chemoradiation targeting stem and nonstem pancreatic cancer cells by repurposing disulfiram. Cancer Letters. 409: 9-19. doi: 10.1016/j.canlet.2017.08.028

Soukup, K., Halfmann, A., Dillinger, B., Poyer, F., Martin, K., Blauensteiner, B., Kauer, M., Kuttke, M., Schabbauer, G. and Dohnal, A.M. (2017) Loss of MAPK-activated protein kinase 2 enables potent dendritic cell-driven anti-tumour T cell response. Sci Rep. 7:11746. doi: 10.1038/s41598-017-12208-7

Turupcu, A. and Oostenbrink, C.(2017) Modeling of oligosaccharides within glycoproteins from free-energy landscapes. J. Chem. Inf. Model. 57 (2017) 2222 – 2236 doi: 10.1021/acs.jcim.7b00351

Sergelen, K., Fossati, S., Turupcu, A., Oostenbrink, C., Liedberg, B., Knoll, W. and Dostálek, J. (2017) Plasmon Field-Enhanced Fluorescence Energy Transfer for Hairpin Aptamer Assay Readout. ACS Sens. 2 (7): 916–923. doi: 10.1021/acssensors.7b00131

Nicolussi, A., Auer, M., Weissensteiner, J., Schütz, G., Katz, S., Maresch, D., Hofbauer, S., Bellei, M., Battistuzzi, G., Furtmüller, P.G. and Obinger, C. (2017) Posttranslational Modification of Heme b in a Bacterial Peroxidase: The Role of Heme to Protein Ester Bonds in Ligand Binding and Catalysis. Biochemistry 56, 4525-4538 doi: 10.1021/acs.biochem.7b00632.

Bönisch, M., Sellmann,C., Maresch, D., Halbig, C., Becker, S.,Toleikis L., Hock, B. and Rüker F. (2017) Novel CH1:CL interfaces that enhance correct light chain pairing in heterodimeric bispecific antibodies. Protein Eng Design Sel 1-12. doi: 10.1093/protein/gzx044.

Bobbili, MR., Mader, RM., Grillari, J. and Dellago H. (2017) OncomiR-17-5p: alarm signal in cancer? Oncotarget,

Lobner, E., Humm, A., Göritzer, K., Mlynek, G., Puchinger, M.G., Hasenhindl, C., Rüker, F., Traxlmayr, M.W., Djinovic-Carugo, K., Obinger, C. (2017) Fcab-HER2 interaction: a ménage à trois. Lessons from X-ray and solution studies. Structure 25(6): 878-889. doi: 10.1016/j.str.2017.04.014.

Nika, L., Wallner, J., Palmberger, D., Koczka, K., Vorauer-Uhl, K., Grabherr, R. (2017) Expression of full-length HER2 protein in Sf9 insect cells and its presentation on the surface of budded virus-like particles. Protein Expr Purif. 136:27-38. doi: 10.1016/j.pep.2017.06.005.

Göritzer K., Maresch D., Altmann F., Obinger C., Strasser R. (2017) Exploring Site-Specific N-Glycosylation of HEK293 and Plant-Produced Human IgA Isotypes. J. Proteome Res. doi: 10.1021/acs.jproteome.7b00121

Montero Morales, L., Maresch, D., Castilho, A., Turupcu, A., Ilieva, K. M., Crescioli, S., Karagiannis, S. N.,  Lupinek, C., Oostenbrink, C., Altmann, F., Steinkellner, H. (2017)  Recombinant plant-derived human IgE glycoproteomics. J Proteomics. 161:81–87. doi: 10.1016/j.jprot.2017.04.002

Shridhar, S., Klanert, G., Auer, N., Hernandez-Lopez, I., Kanduła, MM, Hackl, M., Grillari, J., Stralis-Pavese, N., Kreil, DP, Borth, N. (2017) Transcriptomic changes in CHO cells after adaptation to suspension growth in protein-free medium analysed by a  species-specific microarray. J Biotechnol. doi: 10.1016/j.jbiotec.2017.03.012.

Bloch, S., Thurnheer, T.,  Murakami, Y., Belibasakis, GN., Schäffer, C. (2017) Behavior of two Tannerella forsythia strains and their cell surface mutants in multispecies oral biofilms Mol Oral Microbiol. 00:1–15. doi: 10.1111/omi.12182

Grishkovskaya, I., Paumann-Page, M., Tscheliessnig, R., Stampler, J., Hofbauer, S., Soudi, M., Sevcnikar, B., Oostenbrink, C., Furtmüller, PG, Djinovic-Carugo, K., Nauseef, WM, Obinger, C. (2017) Structure of human promyeloperoxidase(proMPO) and the role of the propeptide in processing and maturation. J Biol Chem.  292(20):8244-8261. doi:10.1074/jbc.M117.775031

Stanton, R.,  Hykollari, A., Eckmair, B., Malzl, D., Dragosits, M., Pamberger, D., Wang, P., Wilson, IB., Paschinger, K. (2017) The underestimated N-glycomes of lepidopteran species. Biochim Biophys Acta. 1861(4):699-714. doi: 10.1016/j.bbagen.2017.01.009.

Hykollari, A., Paschinger, K., Eckmair, B., Wilson, IB. (2017) Analysis of Invertebrate and Protist N-glycans. Methods Mol Biol. 1503:167-184.

Paumann-Page, M., Katz, RS, Bellei, M., Schwartz, I., Edenhofer, E., Sevcnikar, B., Soudi, M., Hofbauer, S., Battistuzzi, G., Furtmüller, PG, Obinger, C. (2017) Pre-steady-state Kinetics Reveal the Substrate Specificity and Mechanism of Halide Oxidation of Truncated
Human Peroxidasin 1. J Biol Chem. 292(11):4583-4592. doi: 10.1074/jbc.M117.775213.

Ma, S., Preims, M., Piumi, F., Kappel, L., Seiboth, B., Record, E., Kracher, D., Ludwig, R. (2017) Molecular and catalytic properties of fungal extracellular cellobiose dehydrogenase produced in prokaryotic and eukaryotic expression systems. Microbial Cell Factories 16, no. 1 (2017): 37, doi:10.1186/s12934-017-0653-5.

Graf, M.M., Weber, S., Kracher, D., Kittl, R., Sygmund, C., Ludwig, R., Peterbauer, C., Haltrich, D. (2017) Characterization of three pyranose dehydrogenase isoforms from the litter-decomposing basidiomycete Leucoagaricus meleagris (syn. Agaricus meleagri) Appl Microbiol Biotechnol. 101(7):2879-2891. doi: 10.1007/s00253-016-8051-1.

Paireder, M., Tholen, S., Porodko, A., Biniossek, M.L., Mayer, B., Novinec, M., Schilling, O., Mach, L. (2017) The papain-like cysteine proteinases NbCysP6 and NbCysP7 are highly processive enzymes with substrate specificities complementary to Nicotiana benthamiana cathepsin B. Biochim Biophys Acta1865(4):444-452. doi: 10.1016/j.bbapap.2017.02.007

Tomek, M., Janesch, B., Maresch, D., Windwarder, M., Altmann, F., Messner, P., Schaeffer, C. (2017) A pseudaminic acid or a legionaminic acid derivative transferase is strain-specifically implicated in the general protein O-glycosylation system of the periodontal pathogen Tannerella forsythia. Glycobiology, doi: 10.1093/glycob/cwx019

Dellago, H., Bobbili, MR,  Grillari, J. (2017) MicroRNA-17-5p: At the Crossroads of Cancer and Aging - A Mini-Review. Gerontology 63(1):20-28. doi:10.1159/000447773

Anzengruber, J., Bublin, M., Bönisch, E., Janesch, B., Tscheppe, A., Braun, M.L., Varga, E.M., Hafner, C., Breiteneder, H., Schäffer, C. (2017) Lactobacillus buchneri S-layer as carrier for an Ara h 2-derived peptide for peanut allergen-specific immunotherapy. Mol Immunol. 85:81-88. doi: 10.1016/j.molimm.2017.02.005


Friedrich, V., Janesch, B., Windwarder, M., Maresch, D., Braun, M.L., Megson, Z.A., Vinogradov, E., Goneau, M.F., Sharma, A., Altmann, F., Messner, P., Schoenhofen, I.C., Schäffer,C. (2016) Tannerella forsythia strains display different cell-surface nonulosonic acids: biosynthetic pathway characterization and first insight into biological implications. Glycobiology. 2016 Dec 16. doi: 10.1093/glycob/cww129.

Kallolimath, S., Castilho, A., Strasser, R., Grünwald-Gruber, C., Altmann, F., Strubl, S., Galuska, C.E., Zlatina, K., Galuska, S., Werner, S., Thiesler, S., Werneburg, S., Hildebrandt, H., Gerardy-Schahn, R and Steinkellner, H (2016) Engineering of complex protein sialylation in plants.Proc Natl Acad Sci U S A. 113(34):9498-503. doi: 10.1073/pnas.1604371113.

Brugger, D., Sützl, L., Zahma, K., Haltrich, D., Peterbauer, C., Stoica, L. (2016) Electrochemical characterization of the pyranose 2-oxidase variant N593C shows a complete loss of the oxidase function with full preservation of substrate (dehydrogenase) activity. Phys. Chem. Chem. Phys., doi: 10.1039/C6CP06009A

Ortmayr, K., Causon, T., Hann, S., Koellensperger, G. (2016) Increasing selectivity and coverage in LC-MS based metabolome analysis. Trends in Analytical Chemistry (TrAC) 82, 358–366. doi:10.1016/j.trac.2016.06.011

Hofbauer, S., Dalla Sega, M. Scheiblbrandner, S., Jandova, Z., Schaffner, I. Mlynek, G., Djinovic-Carugo, K., Battistuzzi, G., Furtmüller, P. G., Oostenbrink, C., Obinger, C. (2016) Chemistry and Molecular Dynamics Simulations of Heme b -HemQ and Coproheme-HemQ. Biochemistry 55, 5398-5412. doi: 10.1021/acs.biochem.6b00701

Rebnegger, C., Vos, T., Graf, A.B., Valli, M., Pronk, J.T., Daran-Lapujade, P., Mattanovich, D. (2016) Pichia pastoris exhibits high viability and low maintenance-energy requirement at near-zero specific growth rates. Appl Environ Microbiol. pii:AEM.00638-16.

Feichtinger, J., Hernandez, I., Fischer, C., Hanscho, M., Auer, N., Hackl, M., Jadhav, V., Baumann, M., Krempl, P.M., Schmidl, C., Farlik, M., Schuster, M., Merkel, A., Sommer, A., Heath, S., Rico, D., Bock, C., Thallinger, G.G., Borth, N. (2016) Comprehensive genome and epigenome characterization of CHO cells in response to evolutionary pressures and overtime. Biotechnol Bioeng. doi: 10.1002/bit.25990.

Hofbauer, S., Mlynek, G., Milazzo, L., Pühringer, D., Maresch, D., Schaffner, I., Furtmüller, P. G., Smulevich, G., Djinovic-Carugo, K., Obinger, C. (2016) Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ - Lessons from the first crystal structure and kinetic studies. FEBS J. 283, 4386–4401. doi: 10.1111/febs.13930

Paireder, M., Mehofer, U., Tholen, S., Porodko, A., Schaehs, P., Maresch, D., Biniossek, M.L.,van der Hoorn, R.A., Lenarcic, B., Novinec, M., Schilling, O., Mach, L. (2016) The death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivity. Arch Biochem Biophys 28;603:110-117. doi:10.1016/

Kuttke, M., Sahin, E., Pisoni, J., Percig, S., Vogel, A., Kraemmer, D., Hanzl, L., Brunner, J.S., Paar, H., Soukup, K., Halfmann, A., Dohnal, A.M., Steiner, C.W., Blaeuml, S., Basilio, J., Hochreiter, B., Salzmann, M., Hoesel, B., Lametschwandtner, G., Eferl, R., Schmid, J.A., Schabbauer, G. (2016) Myeloid PTEN deficiency impairs tumor-immune surveillance via immune-checkpoint inhibition. Oncoimmunology 5(7):e1164918. doi:10.1080/2162402X.2016.1164918

Biniossek, M.L., Niemer, M., Maksimchuk, K., Mayer, B., Fuchs, J., Huesgen, P.F., McCafferty, D.G., Turk, B., Fritz, G., Mayer, J., Haecker, G., Mach, L., Schilling, O. (2016) Identification of Protease Specificity by Combining Proteome-Derived Peptide Libraries and Quantitative Proteomics. Mol Cell Proteomics. 15(7):2515-24. doi:10.1074/mcp.O115.056671.

O´Conghaile, P, Falk, M.. MacAodha, D., Yakovleva, M.E., Gonaus, C., Peterbauer, C.K., Gorton, L., Shleev, S., Leech, D. ( 2016) Fully Enzymatic Membraneless Glucose/Oxygen Fuel Cell That Provides 0.275 mA cm(-2) in 5 mM Glucose, Operates in Human Physiological Solutions, and Powers Transmission of Sensing Data, Anal Chem. 88(4): 2156-2163. doi:10.1021/acs.analchem.5b03745

Courtade, G., Wimmer, R., Rohr, A.K., Preims, M., Felice, A.K.G., Dimarogona, M., Vaaje-Kolstad, G., Sorliem M., Sandgren, M., Ludwig, R., Eijsink, V.G.H., Aachmann, L. (2016) Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase. PNAS, doi:10.1073/pnas.1602566113

Kracher, D., Scheiblbrandner, S., Felice, A.K.G., Breslmayr, E., Preims, M., Ludwicka, K., Haltrich, D., Eijsink, V.G.H., Ludwig, R. (2016) Extracellular electron transfer systems fuel cellulose oxidative degradation. Science. doi: 10.1126/science.aaf3165

Klausberger, M., Tscheliessnig, R., Neff, S., Nachbagauer, R., Wohlbold, T.J., Wilde, M.,Palmberger, D., Krammer, F., Jungbauer, A., Grabherr, R. (2016) Globular Head-Displayed Conserved Influenza H1 Hemagglutinin Stalk Epitopes Confer Protection against Heterologous H1N1 Virus. PLoS One. 11(4):e0153579. doi:10.1371/journal.pone.0153579.

Klanert, G., Jadhav, V., Shanmukam, V., Diendorfer, A., Karbiener, M., Scheideler, M., Bort, J.H., Grillari, J., Hackl, M., Borth, N. (2016) A signature of 12 microRNAs is robustly associated with growth rate in a variety of CHO cell lines. J Biotechnol. doi: 10.1016/j.jbiotec.2016.03.022.

Nocon, J., Steiger, M., Mairinger, T., Hohlweg, J., Rußmayer, H., Hann, S., Gasser, B.,Mattanovich, D. (2016) Increasing pentose phosphate pathway flux enhances recombinant protein production in Pichia pastoris. Appl Microbiol Biotechnol. doi: 10.1007/s00253-016-7363-5

Geiger, B., Nguyen, H.M., Wenig, S., Nguyen, H.A., Lorenz, C., Kittl, R., Mathiesen, G., G.H. Eijsink, V.G.H., Haltrich, D., Nguyen, T.H. (2016) From by-product to valuable components: Efficient enzymatic conversion of lactose in whey using β-galactosidase from Streptococcus thermophiles. Biochem Eng J, doi:10.1016/j.bej.2016.04.003

Hassan, N., Geiger, B,, Gandini, R., Patel, B.K., Kittl, R., Haltrich, D., Nguyen, T.H., Divne, C., Tan, T.C. (2016) Engineering a thermostable Halothermothrix orenii β-glucosidase for improved galacto-oligosaccharide synthesis. Appl Microbiol Biotechnol. 100(8):3533-43. doi: 10.1007/s00253-015-7118-8.

Kurz, S., King, J.G., Dinglasan, R.R., Paschinger, K., Wilson, I.B.H. (2016) The fucomic potential of mosquitoes: Fucosylated N-glycan epitopes and their cognate fucosyltransferases. Insect Biochem Mol Biol. 68:52-63. doi: 10.1016/j.ibmb.2015.11.001

Sommeregger, W., Mayrhofer, P., Steinfellner, W., Reinhart, D., Henry, M., Clynes, M., Meleady, P., Kunert, R. (2016), Proteomic differences in recombinant CHO cells producing two similar antibody fragments. Biotechnol. Bioeng. doi:10.1002/bit.25957

Lobner, E., Traxlmayr, M. W., Obinger, C. Hasenhindl, C. (2016)  Engineered IgG1-Fc – one fragment to bind them all. Immunological Reviews  270: 113–131. doi: 10.1111/imr.12385

Tschofen, M., Knopp, D., Hood, E., Stoger, E. (2016) Plant Molecular Farming: Much More than Medicines. Annu. Rev. Anal. Chem. doi: 10.1146/annurev-anchem-071015-041706

Hofbauer, A., Melnik, S., Tschofen, M., Arcalis, E., Phan, H., Gresch, U., Lampel, J., Conrad, U., Stoger, E. (2016) The Encapsulation of Hemagglutinin in Protein Bodies Achieves a Stronger Immune Response in Mice than the Soluble Antigen. Front Plant Sci

Eckmair, B., Jin, C., Abed-Navandi, D., Paschinger, K. (2016) Multistep Fractionation and Mass Spectrometry Reveal Zwitterionic and Anionic Modifications of the N- and O-glycans of a Marine Snail. Mol Cell Proteomics 15(2):573-97. doi: 10.1074/mcp.M115.051573

Hykollari, A., Eckmair, B., Voglmeir, J., Jin, C., Yan, S., Vanbeselaere, J., Razzazi-Fazeli, E., Wilson, I.B.H., Paschinger K. (2016) More Than Just Oligomannose: An N-glycomic Comparison of Penicillium Species. Mol Cell Proteomics 15(1):73-92. doi: 10.1074/mcp.M115.055061

Vamvaka, E., Twyman, R.M., Murad, A.M., Melnik, S., The, A.Y., Arcalis, E., Altmann, F., Stoger, E., Rech, E., Ma, J.K., Christou, P., Capell, T. (2016) Rice endosperm produces an underglycosylated and potent form of the HIV-neutralizing monoclonal antibody 2G12. Plant Biotechnol J. 1, 97-108. doi: 10.1111/pbi.12360.

Hofbauer, S., Howes, B.D., Flego, N., Pirker, K.F., Schaffner, I., Mlynek, G.,Djinovic-Carugo, K., Furtmueller, P.G., Smulevich, G., Obinger, C. (2016) From chlorite dismutase towards HemQ - the role of the proximal H-bonding network in heme binding. BiosciRep. pii: BSR20150330.

Margreitter, C.*, Mayrhofer, P.*, Kunert, R., Oostenbrink, C. (2016) Antibody humanization by molecular dynamics simulations – in-silico guided selection of critical backmutations. J. Mol. Recogn., doi: 10.1002/jmr.2527. *equally contributing first authors

Halada, P., Brugger, D., Volc, J., Peterbauer, C.K., Leitner, C., Haltrich, D. (2016) Oxidation of Phe454 in the Gating Segment Inactivates Trametes multicolor Pyranose Oxidase during Substrate Turnover. PLoS ONE 11(2): e0148108. doi:10.1371/journal.pone.0148108


Yakovleva, M.E.*, Gonaus, C.*, Schropp, K., O´Conghaile, P.; Leech, D., Peterbauer, C.K., Gorton, L. (2015) Engineering of pyranose dehydrogenase for application to enzymatic anodes in biofuel cells Phys Chem Chem Phys. 17(14): 9074-9081. doi:10.1039/C5CP00430F *equally contributing first authors

Kallolimath, S and Steinkellner, H (2015) Glycosylation of plant produced human antibodies. Hum antibodies, 23(3-4):45-48. doi: 10.3233/HAB-150283

Kurz, S., Aoki, K., Jin, C., Karlsson, N.G., Tiemeyer, M., Wilson, I.B.H., Paschinger, K. (2015) Targeted release and fractionation reveal glucuronylated and sulphated N- and O-glycans in larvae of dipteran insects. J Proteomics 126:172-188

Ortmayr, K., Schwaiger M., Hann, S., Koellensperger, G. (2015) An integrated metabolomics workflow for the quantification of sulfur pathway intermediates employing thiol protection with N-ethyl maleimide and hydrophilic interaction liquid chromatography tandem mass spectrometry. Analyst. DOI: 10.1039/C5AN01629K

Hensel, G., Floss, D.M., Arcalis, E., Sack, M., Melnik, S., Altmann, F., Rutten, T., Kumlehn, J., Stoger, E., Conrad, U. (2015) Transgenic Production of an Anti HIV Antibody in the Barley Endosperm. PLoS One. doi: 10.1371/journal.pone.0140476.

Gasselhuber, B., Carpena, X., Graf, M.M., Pirker, K.F., Nicolussi, A., Sündermann, A.,Hofbauer, S., Zamocky, M., Furtmueller, P.G., Jakopitsch, C., Oostenbrink, C., Fita, I., Obinger, C.(2015) Eukaryotic Catalase-Peroxidase: The Role of the Trp-Tyr-Met Adduct in Protein Stability, Substrate Accessibility, and Catalysis of Hydrogen Peroxide Dismutation. Biochemistry. PubMed PMID:26290940.

Gonaus, C., Kittl, R., Sygmund, C., Haltrich, D., Peterbauer, C. (2015) Transcription analysis of pyranose dehydrogenase from the basidiomycete Agaricus bisporus and characterization of the recombinantly expressed enzyme. Protein Expr Purif. doi: 10.1016/j.pep.2015.11.003.

Satzer, P., Svec, F., Sekot, G., Jungbauer, A. (2015) Protein adsorption onto nanoparticles induces conformational changes: Particle size dependency, kinetics and mechanisms. Engineering in Life Sciences, doi:10.1002/elsc.201500059

Loos, A., Gach, J.S., Hackl, T., Maresch, D., Henkel, T., Porodko, A., Bui-Minh, D., Sommeregger, W., Wozniak-Knopp, G., Forthal, D., Altmann, F., Steinkellner, H., Mach, L. (2015). Glycan modulation and sulfoengineering of anti–HIV-1 monoclonal antibody PG9 in plants. Proceedings of the National Academy of Sciences, pii: 201509090

Zboray, K.*, Sommeregger, W.*, Bogner, E., Gili, A., Sterovsky, T., Fauland, K., Grabner, B., Stiedl, P., Moll, H. P., Bauer, A., Kunert, R., Casanova, E.. (2015). Heterologous protein production using euchromatin-containing expression vectors in mammalian cells. Nucleic acids research, doi: 10.1093/nar/gkv475. *equally contributing first authors

Friedrich, V., Pabinger, S., Chen, T., Messner, P., Dewhirst, F.E., Schaeffer, C. (2015) Draft Genome Sequence of Tannerella forsythia Type Strain ATCC 43037. Genome Announc. 3(3). doi: 10.1128/genomeA.00660-15.

Niemer, M., Mehofer, U., Verdianz, M., Porodko, A., Schaehs, P., Kracher, D., Lenarcic, B., Novinec, M., Mach, L. (2015) Nicotiana benthamiana cathepsin B displays distinct enzymatic features which differ from its human relative and aleurain-like protease. Biochimie, doi: 10.1016/j.biochi.2015.06.017.

Megson, Z.A., Pittenauer, E., Duda, K.A., Engel, R., Ortmayr, K., Koellensperger, G., Mach, L., Allmaier, G., Holst, O., Messner, P., Schaeffer, C. (2015) Inositol phosphodihydroceramides in the periodontal pathogen Tannerella forsythia: Structural analysis and incorporation of exogenous myo-inositol. Biochim Biophys Acta. doi: 10.1016/j.bbalip.2015.08.004.

Graf, M.M., Sucharitakul, J., Bren, U., Chu, D.B., Koellensperger, G., Hann, S., Furtmueller, P.G., Obinger, C., Peterbauer, C.K., Oostenbrink, C., Chaiyen, P., Haltrich, D. (2015) Reaction of pyranose dehydrogenase from Agaricus meleagris with its carbohydrate substrates. FEBS, doi: 10.1111/febs.13417.

Harreither, E., Hackl, M., Pichler, J., Shridhar, S., Auer, N., Labaj, P.P., Scheideler, M., Karbiener, M., Grillari, J., Kreil, D.P., Borth, N. (2015) Microarray profiling of preselected CHO host cell subclones identifies gene expression patterns associated with increased production capacity. Biotechnology J., doi:10.1002/biot.201400857

Soukup, K., Halfmann, A., Le Bras, M., Sahin, E., Vittori, S., Poyer, F., Schuh, C., Luger, R., Niederreiter, B., Haider, T., Stoiber, D., Bleuml, S., Schabbauer, G., Kotlyarov, A., Gaestel, M., Felzmann, T., Dohnal, A. M. (2015) The MAPK-Activated Kinase MK2 Attenuates Dendritic Cell-Mediated Th1 Differentiation and Autoimmune Encephalomyelitis. J Immunol 195(2):541-52

Sahin, E., Brunner, J. S., Kral, J. B., Kuttke, M., Hanzl, L., Datler, H., Paar, H., Neuwinger, N., Saferding, V., Zinser, E., Halfmann, A., Soukup, K., Hainzl, E., Lohmeyer, T., Niederreiter, B., Haider, T., Dohnal, A. M., Kroenke, G., Bleuml, S., Schabbauer, G. (2015) Loss of Phosphatase and Tensin Homolog in APCs Impedes Th17-Mediated Autoimmune Encephalomyelitis. J Immunol pii: 1402511.

Tan, T-C.*, Kracher, D.*, Gandini, R., Sygmund, C., Kittl, R., Haltrich, D., Hallberg, M.B., Ludwig, R.+ & Divne, C.+ (2015) Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation. Nat Commun. doi:10.1038/ncomms8542; *equally contributing first authors; + equally contributing corresponding authors

Pham, N.H., Hollmann, F., Kracher, D., Preims, M., Haltrich, D., Ludwig, R. (2015) Engineering an Enzymatic Regeneration System for NAD(P)H Oxidation. J. Mol. Catal. B Enzym.doi:10.1016/j.molcatb.2015.06.011

Friedrich. V., Gruber, C., Nimeth, I., Pabinger, S., Sekot, G., Posch, G., Altmann, F., Messner, P., Andrukhov, O., Schaeffer, C. (2015) Outer membrane vesicles of Tannerella forsythia: Biogenesis, composition, and virulence. Mol Oral Microbiol. doi: 10.1111/omi.12104.

Kracher, D., Zahma, K., Schulz, C., Sygmund, C., Gorton, L., Ludwig, R. (2015) Interdomain Electron Transfer in Cellobiose Dehydrogenase: Modulation by pH and Divalent Cations. FEBS J. doi: 10.1111/febs.13310

Nguyen, T.T., Nguyen, H.M., Geiger, B., Mathiesen, G., Eijsink, V.G., Peterbauer, C.K., Haltrich, D., Nguyen, T.H. (2015) Heterologous expression of a recombinant lactobacillal β-galactosidase in Lactobacillus plantarum: effect of different parameters on the sakacin P-based expression system. Microb Cell Fact. 14(1):30. doi: 10.1186/s12934-015-0214-8.

Soukup, K., Wang, X. (2015) Radiation Meets Immunotherapy - A Perfect Match in the Era of Combination Therapy? Int. J. Radiat. Biol. doi:10.3109/09553002.2014.995383

Schaffner, I., Hofbauer, S., Krutzler, M., Pirker, K.F., Furtmueller, P.G., Obinger, C. (2015) Mechanism of chlorite degradation to chloride and dioxygen by the enzyme chlorite dismutase. Arch Biochem Biophys. doi: 10.1016/

Chromikova, V., Mader, A., Hofbauer, S., Göbl, C., Madl, T., Gach, J.S., Bauernfried, S., Furtmueller, P.G., Forthal, D.N., Mach, L, Obinger, C., Kunert, R. (2015) Introduction of germline residues improves the stability of anti-HIV mAb 2G12-IgM. Biochim Biophys Acta. doi:10.1016/j.bbapap.2015.02.018.

Ortmayr, K., Hann, S., Koellensperger, G. (2015) Complementing reversed-phase selectivity with porous graphitized carbon to increase the metabolome coverage in an on-line two-dimensional LC-MS setup for metabolomics. Analyst doi:10.1039/C5AN00206K

Schaffner, I., Hofbauer, S., Krutzler, M., Pirker, K.F., Bellei, M., Stadlmayr, G., Mlynek, G., Djinovic-Carugo, K., Battistuzzi, G., Furtmüller, P.G., Daims, H., Obinger, C. (2015) Dimeric chlorite dismutase from the nitrogen-fixing cyanobacterium Cyanothece sp. PCC7425. Mol Microbiol. doi: 10.1111/mmi.12989.

Hofbauer, S., Hagmüller, A., Schaffner, I., Mlynek, G., Krutzler, M., Stadlmayr, G., Pirker, K.F., Obinger, C., Daims, H., Djinovic-Carugo, K., Furtmueller, P.G. (2015) Structure and heme-binding properties of HemQ (chlorite dismutase-like protein) from Listeria monocytogenes. Arch Biochem Biophys. doi: 10.1016/

Chu, D. B., Troyer, C., Mairinger, T., Ortmayr, K., Neubauer, S., Koellensperger, G., Hann, S. (2015) Isotopologue analysis of sugar phosphates in yeast cell extracts by gas chromatography chemical ionization time-of-flight mass spectrometry. Anal. Bioanal. Chem. doi:10.1007/s00216-015-8521-9

Schosserer, M., Minois, N., Angerer, T.B., Amring, M., Dellago, H., Harreither, E., Calle-Perez, A., Pircher, A., Gerstl, M.P., Pfeifenberger, S., Brandl, C., Sonntagbauer, M., Kriegner A., Linder, A., Weinhaeusel, A., Mohr, T., Steiger, M., Mattanovich, D., Rinnerthaler, M., Karl, T., Sharma, S., Entian, K.D., Kos, M., Breitenbach, M., Wilson, I.B., Polacek, N., Grillari-Voglauer, R., Breitenbach-Koller, L., Grillari, J. (2015) Methylation of ribosomal RNA by NSUN5 is a conserved mechanism modulating organismal lifespan. Nat Commun.30;6:6158. doi: 10.1038/ncomms7158.

Zolghadr, B., Gasselhuber, B., Windwarder, M., Pabst, M., Kracher, D., Kerndl, M., Zayni, S., Hofinger-Horvath, A., Ludwig, R., Haltrich, D., Oostenbrink, C., Obinger, C., Kosma, P.,Messner, P., Schaeffer, C. (2015) UDP-sulfoquinovose formation by Sulfolobus acidocaldarius. Extremophiles, doi10.1007/s00792-015-0730-9

Diendorfer, A.B., Hackl, M., Klanert, G., Jadhav, V., Reithofer, M., Stiefel, F., Hesse, F., Grillari. J., Borth, N. (2015) Annotation of additional evolutionary conserved microRNAs in CHO cells from updated genomic data. Biotechnol Bioeng. doi:10.1002/bit.25539



Hofbauer, A., Peters, J., Arcalis, E., Rademacher, T., Lampel, J., Eudes, F., Vitale, A., Stoger, E. (2014) The Induction of Recombinant Protein Bodies in Different Subcellular Compartments Reveals a Cryptic Plastid-Targeting Signal in the 27-kDa γ-Zein Sequence. Front Bioeng Biotechnol. doi:10.3389/fbioe.2014.00067

Graf, M.M.H., Zhixiong, L., Bren, U., Haltrich, D., van Gunsteren, W.F., Oostenbrink, C. (2014) Pyranose Dehydrogenase Ligand Promiscuity: A Generalized Approach to Simulate Monosaccharide Solvation, Binding, and Product Formation. PLoS Comput Biol 10(12): e1003995

Eibinger, M., Ganner, T., Bubner, P., Rosker, S., Kracher, D., Haltrich D., Ludwig, R., Plank, H., Nidetzky, B. (2014) Cellulose surface degradation by a lytic polysaccharide monooxygenase and its effect on cellulase hydrolytic efficiency. J. Biol. Chem. pii: jbc.M114.602227

Tanne, J., Kracher, D., Dietzel, D., Schulz, B., Ludwig, R., Lisdat, F., Scheller, F.W., Bier, F.F. (2014) Carboxylated or Aminated Polyaniline-Multiwalled Carbon Nanotubes Nanohybrids for Immobilization of Cellobiose Dehydrogenase on Gold Electrodes. Biosensors 4, 370-386

Brugger, D., Krondorfer, I., Shelswell C., Huber-Dittes, B., Haltrich, D., Peterbauer, C.K. (2014) Engineering Pyranose 2-Oxidase for Modified Oxygen Reactivity. PLoS One 9

Mayrhofer, P., Kratzer, B., Sommeregger, W., Steinfellner, W., Reinhart, D., Mader, A., Turan, S., Qiao, J., Bode, J., Kunert, R. (2014) Accurate comparison of antibody expression levels by reproducible transgene targeting in engineered recombination-competent CHO cells. Appl. Microbiol. Biotechnol., doi 10.1007/s00253-014-6011-1

Maccani, A., Hackl, M., Leitner, C., Steinfellner, W., Graf, A.B., Tatto, N.E., Karbiener, M., Scheideler, M., Grillari, J., Mattanovich, D., Kunert, R., Borth, N., Grabherr, R., Ernst, W. (2014) Identification of microRNAs specific for high producer CHO cell lines using steady-state cultivation. Appl. Microbiol. Biotechnol., in press, DOI: 10.1007/s00253-014-5911-4

Hofbauer, S., Gysel, K., Bellei, M., Hagmueller, A., Schaffner, I., Mlynek, G., Kostan, J., Pirker, K.F., Daims, H., Furtmueller, P.G., Battistuzzi, G., Djinovic-Carugo, K., Obinger, C. (2014) Manipulating conserved heme cavity residues of chlorite dismutase: effect on structure, redox chemistry and reactivity. Biochemistry 53, 77-89

Lai, B.*, Nagy, G.*, Garate, J. A., Oostenbrink, C. (2014) Entropic and enthalpic contributions to stereospecific ligand binding from enhanced sampling methods. J. Chem. Inf. Model. 54, 151-158. *: both authors contributed equally

Hofbauer, S., Gruber, C., Pirker, K., Suendermann, A., Schaffner, I., Jakopitsch, C., Oostenbrink, C., Furtmüller, P., Obinger, C. (2014) Transiently produced hypochlorite is responsible for the irreversible inhibition of chlorite dismutase. Biochemistry 53, 3145–3157

Krondorfer, I., Brugger, D., Paukner, R., Pirker, K. F., Hofbauer, S., Furtmueller, P.G., Obinger, C., Haltrich, D., Peterbauer, C.K. (2014) Agaricus meleagris dehydrogenase: Influence of covalent FAD linkage on catalysis and stability. Arch. Biochem. Biophys.558, 111-119

Kurz, S., Jin, C., Hykollari, A., Gregorich, D., Giomarelli, B., Vasta, G.R., Wilson, I.B.H., Paschinger, K. (2013) Haemocytes and plasma of the eastern oyster (Crassostrea virginica) display a diverse repertoire of sulphated and blood group A-modified N-glycans. J. Biol. Chem. 288, 24410–24428

Hofbauer, S., Schaffner, I., Furtmueller, P.G., Obinger, C. (2014) Chlorite dismutases – a heme enzyme family for use in bioremediation and generation of molecular oxygen. Biotechnol. J. 9, 461-473

Anzengruber, J., Courtin, P., Claes, I.J.J., Debreczeny, M., Hofbauer, S., Obinger, C., Chapot-Chartier, M.-P., Vanderleyden, J., Messner, P., Schaeffer, C. (2014) Biochemical characterization of the major N-acetylmuramidase from Lactobacillus buchneri. Microbiology 160, 1807-1819

Tomek, M., Neumann, L., Nimeth, I., Koerdt, A, Andesner, P., Mach, L., Messner, P., Potempa, J., Schaeffer, C. (2014) S-layer glycoproteins of Tannerella forsythia are secreted via a type IX secretion system that is decoupled from protein glycosylation. Mol. Oral Microbiol., doi: 10.1111/omi.12062

Brugger, D., Krondorfer, I., Zahma, K., Stoisser, T., Bolivar, J. M., Nidetzky, B., Peterbauer, C. K., Haltrich, D. (2014) Convenient microtiter plate-based, oxygen-independent activity assays for flavin-dependent oxidoreductases based on different redox dyes. Biotechnol. J. 9, 474-482

Krondorfer, I., Lipp, K., Brugger, D., Staudigl, P., Sygmund, C., Haltrich, D., Peterbauer, C. K. (2014) Engineering of pyranose dehydrogenase for increased oxygen reactivity. PLoS One 9, e91145

Kracher, D., Oros, D., Yao, W., Preims, M., Rezic, I., Haltrich, D., Rezic, T., Ludwig, R. (2014) Fungal secretomes enhance sugar beet pulp hydrolysis. Biotechnol. J. 9, 483–492

Mlynek, G., Lehner, A., Neuhold, J., Leeb, S., Kostan, J., Charnagalov, A., Stolt-Bergner, P., Djinovic-Carugo, K., Pinotsis, N. (2014) The Center for Optimized Structural Studies (COSS) platform for automation in cloning, expression, and purification of single proteins and protein-protein complexes. Amino Acids, in press

Anzengruber, J., Pabst, M., Neumann, L., Sekot, G., Heinl, S., Grabherr, R., Altmann, F.,Messner, P., Schaeffer, C. (2014) Protein O-glucosylation in Lactobacillus buchneri. Glycoconj. J. 31, 117-131

Hasenhindl, C., Lai, B., Delgado, J., Traxlmayr, M. W., Stadlmayr, G., Rueker, F., Serrano, L., Oostenbrink, C., Obinger, C. (2014) Creating stable stem regions for loop elongation in Fcabs – Insights from combining yeast surface display, in silico loop reconstruction and molecular dynamics simulations. Biochim. Biophys. Acta – Proteins and Proteomics 1844, 1530-1540

Lai, B., Hasenhindl, C., Obinger, C., Oostenbrink, C. (2014) Molecular dynamics simulation of the crystallizable fragment of IgG1 – Insights for the design of Fcabs. Int. J. Mol. Sci. 15, 438-455

Wilde, M., Klausberger, M., Palmberger, D., Ernst, W., Grabherr, R. (2014) Tnao38, high five and Sf9—evaluation of host–virus interactions in three different insect cell lines: baculovirus production and recombinant protein expression. Biotechnol. Lett. 36, 743-749

Maccani, A., Landes, N., Stadlmayr, G., Maresch, D., Leitner, C., Maurer, M., Gasser, B., Ernst, W., Kunert, R., Mattanovich, D. (2014) Pichia pastoris secretes recombinant proteins less efficiently than Chinese hamster ovary cells but allows higher space-time yields for less complex proteins. Biotechnol. J. 9, 526-537

Klausberger, M., Wilde, M., Palmberger, D., Hai, R., Albrecht, R.A., Margine, I., Hirsh, A., Garcia-Sastre, A., Grabherr, R., Krammer, F. (2014) One-shot vaccination with an insect-cell derived low-dose influenza A H7 virus-like particle preparation protects mice against H7N9 challenge. Vaccine 32, 355-362

Klanert, G., Jadhav, V., Chanoumidou, K., Grillari, J., Borth, N., Hackl, M. (2014) Endogenous microRNA clusters outperform chimeric sequence clusters in Chinese hamster ovary cells. Biotechnol. J. 9, 538-544

Niemer, M., Mehofer, U., Torres Acosta, J.A., Verdianz, M., Henkel, T., Loos, A., Strasser, R., Maresch, D., Rademacher, T., Steinkellner, H., Mach, L. (2014) The human anti-HIV antibodies 2F5, 2G12 and PG9 differ in their susceptibility to proteolytic degradation: Down-regulation of endogenous serine and cysteine proteinase activities could improve antibody production in plant-based expression platforms. Biotechnol. J. 9, 493-500.

Jadhav, V., Hackl, M., Klanert, G., Hernandez Bort, J.A., Kunert, R., Grillari, J., Borth, N. (2014) Stable overexpression of miR-17 enhances recombinant protein production of CHO cells. J. Biotechnol. 10, 38-44

Rebnegger, C., Graf, A.B., Valli, M., Steiger, M.G., Gasser, B., Maurer, M., Mattanovich, D. (2014) In Pichia pastoris, growth rate regulates protein synthesis and secretion, mating and stress response. Biotechnol. J. 9, 511-525

Harreither, E., Rydberg, H.A., Amand, H.L., Jadhav, V., Fliedl, L., Benda, C., Esteban, M.A., Pei, D., Borth, N., Grillari-Voglauer, R, Hommerding, O., Edenhofer, F., Norden, B., Grillari, J. (2014) Characterization of a novel cell penetrating peptide derived from human Oct4. Cell Regeneration 3, 1-14

Satzer, P., Wellhoefer, M., Jungbauer, A. (2014) Continuous separation of protein loaded nanoparticles by simulated moving bed chromatography. J. Chromatogr. A. doi: 10.1016/j.chroma.2014.04.093

Chromikova, V., Mader, A., Steinfellner, W., Kunert, R. (2014) Evaluating the bottlenecks of recombinant IgM production in mammalian cells. Cytotechnology doi: 10.1007/s10616-014-9693-4

Nocon, J., Steiger, M.G., Pfeffer, M., Sohn, S.B., Tae Yong Kim, T.Y., Maurer, M., Rußmayer, H., Pfluegl, S., Ask, M., Haberhauer-Troyer, C., Ortmayr, K., Hann, S., Koellensperger, G., Gasser, B., Lee, S.Y., Mattanovich, D. (2014) Model based engineering of Pichia pastoris central metabolism enhances recombinant protein production. Metab. Eng., doi: 10.1016/j.ymben.2014.05.011

Nagy, G., Oostenbrink, C. (2014) Dihedral-Based Segment Identification and Classification of Biopolymers I: Proteins. J. Chem. Inf. Model. 54, 266-277

Nagy, G., Oostenbrink, C. (2014) Dihedral-Based Segment Identification and Classification of Biopolymers II: Polynucleotides. J. Chem. Inf. Model.  54, 278-288

Auer, M., Nicolussi, A., Schuetz, G., Furtmueller, P. G., Obinger, C. (2014) How covalent heme to protein bonds influence the formation and reactivity of redox intermediates of a bacterial peroxidase. J. Biol. Chem.,doi:10.1074/jbc.M114.595157

Zamocky, M., Gasselhuber, B., Furtmueller, P. G., Obinger, C. (2014) Turning points in the evolution of peroxidase-catalase superfamily – Molecular phylogeny of hybrid heme peroxidases. Cell. Mol. Life Sci., DOI: 10.1007/s00018-014-1643-y

Traxlmayr, M. W., Lobner, E., Hasenhindl, C., Stadlmayr, G., Oostenbrink, C., Antes, B., Rüker, F., Obinger, C. (2014) Construction of a pH-sensitive Her2-binding IgG1-Fc by directed evolution. Biotechnol. J. 9, 1013-1022

Pabst, M., Neumann, L., Sekot, G., Heinl, S., Grabherr, R., Altmann, F., Messner, P., Schaeffer, C. (2014) Protein O-glucosylation in Lactobacillus buchneri. Glycoconj. J. 31, 117-131

Hackl, M., Jadhav, V., Klanert, G., Karbiener, M., Scheideler, M., Grillari, J., Borth, N. (2014) Analysis of microRNA transcription and post-transcriptional processing by Dicer in the context of CHO cell proliferation. J. Biotechnol., doi: 10.1016/j.jbiotec.2013

Reinhart, D., Sommeregger, W., Debreczeny, M., Gludovacz, E., Kunert, R. (2014) In search of expression bottlenecks in recombinant CHO cell lines - a case study. Appl. Microbiol. Biotechnol., doi:10.1007/s00253-014-5584-z

Ortmayr, K., Nocon, J., Gasser B., Mattanovich, D., Hann, S., Koellensperger, G. (2014) Sample preparation workflow for LC-MS/MS based analysis of nicotinamide adenine dinucleotide phosphate cofactors in yeast. J. Sep. Sci., in press

Jakopitsch, C., Pirker, K.F., Flemmig, J., Hofbauer, S., Furtmueller, P.G., Schlorke, D., Arnhold, J., Obinger, C. (2014) Mechanism of reaction of chlorite with mammalian heme peroxidases. J. Inorg. Biochem. 135, 10-19

Suendermann, A., Reif, M., Hofbauer, S., Obinger, C., Oostenbrink, C. (2014) Structural implications of an ion binding to chlorite dismutase in ferrous, ferric and Compound I state – a molecular dynamics simulation study. Biochemistry 53, accepted for publication

Dragosits, M., Pfluegl, S., Kurz, S., Razzazi-Fazeli, E., Wilson, I.B.H., Rendic, D. (2014) Recombinant Aspergillus β-galactosidases as a robust glycomic and biotechnological tool. Appl. Microbiol. Biotechnol. 98, 3553–3567

Killyeni, A., Yakovleva, M.F., MacAodha, D., Conghaile, P.O., Gonaus, C., Ortiz, R., Leech, D., Popescu, I.C., Peterbauer, C.K., Gorton, L (2014) Effect of deglycosylation on the mediated electrocatalytic activity of recombinantly expressed Agaricus meleagris pyranose dehydrogenase wired by osmium redox polymer. Electrochim. Acta 126, 61-67

Isaksen, T., Westereng, B., Aachmann, F.L., Agger, J.W., Kracher, D., Kittl, R., Ludwig, R., Haltrich, D., Eijsink, V.G., Horn, S.J. (2014) A C4-oxidizing lytic polysaccharide monooxygenase cleaving both cellulose and cello-oligosaccharides. J. Biol. Chem. 289, 2632–2642

Nemeth, E., Schilli, G. K., Nagy, G., Hasenhindl, C., Gyurcsik, B., Oostenbrink, C. (2014) Design of a colicin E7 based chimeric zinc-finger nuclease. J. Comp.-Aided Mol. Des., accepted for publication

Hernandez Bort, J. A., Shanmukam, V., Pabst, M., Windwarder, M., Neumann, L., Alchalabi, A., Krebiehl, G, Koellensperger, G., Hann, S., Sonntag, D., Altmann, F., Heel, C., Borth, N. (2014) Reduced quenching and extraction time for mammalian cells using filtration and syringe extraction. J. Biotechnol., doi: 10.1016/j.jbiotec.2014.04.014.

Schneider, J. D., Castilho, A., Neumann, L., Altmann, F., Loos, A., Kannan, L., Mor, T. S., Steinkellner, H. (2014) Expression of human butyrylcholinesterase with a glycosylation profile resembling the plasma derived orthologue. Biotechnol. J. 9, 501-510

Gach, J. S., Achenbach, C. J., Chromikova, V., Berzins, B., Lambert, N., Landucci, G., Forthal, D. N., Katlama, C., Jung, B. H., Murphy, R. L. (2014) HIV-1 specific antibody titers and neutralization among chronically infected patients on long-term suppressive antiretroviral therapy (ART): a cross-sectional study. PLoS One 9:e85371


Sommeregger, W., Prewein, B., Reinhart, D., Mader, A., Kunert, R. (2013) Transgene copy number comparison in recombinant mammalian cell lines: critical reflection of quantitative real-time PCR evaluation. Cytotechnology 65, 811-818

Graf M.M.H., Bren U., Haltrich D., Oostenbrink C. (2013) Molecular dynamics simulations give insight into d-glucose dioxidation at C2 and C3 by Agaricus meleagris pyranose dehydrogenase. J. Comput. Aided Mol. Des. 27, 295-304

Maccani, A., Ernst, W., Grabherr, R. (2013) Whole genome sequencing improves estimation of nuclear DNA content of Chinese hamster ovary cells. Cytometry A 83, 893-895

Hofbauer, A., Stoeger, E. (2013) Subcellular accumulation and modification of pharmaceutical proteins in different plant tissues. Curr. Pharm. Design 19, 5495-5502

Melnik, S., Stoeger, E. (2013) Green factories for biopharmaceuticals. Curr. Med. Chem. 20, 1038-1046

Lai, B., Nagy, G., Garate J.A., Oostenbrink, C. (2013) Entropic and enthalpic contributions to stereospecific ligand binding from enhanced sampling methods. J. Chem. Inf. Model. 54, 151-158

Hasenhindl, C., Traxlmayr, M. W., Wozniak-Knopp, G., Jones, P. C., Stadlmayr, G., Rueker, F., Obinger, C. (2013) Stability assessment on a library scale: a rapid method for the evaluation of the commutability and insertion of residues in C-terminal loops of the CH3 domains of IgG1-Fc. Prot. Eng. Des. Sel. 26, 675-682

Jadhav, V., Hackl, M., Druz, A., Shridhar, S., Chung, C.Y., Heffner, K.M., Kreil, D.P., Betenbaugh, M., Shiloach, J., Barron, N., Grillari, J., Borth, N. (2013) CHO microRNA engineering is growing up: recent successes and future challenges. Biotechnol. Adv. 31, 1501-1513

Sommeregger, W., Gili, A., Sterovsky, T., Casanova, E., Kunert, R. (2013) Powerful expression in Chinese Hamster Ovary cells using bacterial artificial chromosomes: Parameters influencing productivity. In: BMC Proceedings, doi:10.1186/1753-6561-7-S6-P25

Castilho, A., Neumann, L., Gattinger, P., Strasser, R., Vorauer-Uhl, K., Sterovsky, T., Altmann, F., Steinkellner, H. (2013) Generation of biologically active multi-sialylated recombinant human EPOFc in plants. PLoS One 8, e54836

Mulla, D., Kracher, D., Ludwig, R., Nagy, G., Grandits, M., Holzer, W., Saber, Y., Gabra, N., Viernstein, H., Unger, F.M. (2013) Azido derivatives of cellobiose: oxidation at C1 with cellobiose dehydrogenase from Sclerotium rolfsii. Carbohydr. Res. 382, 86-94

Traxlmayr, M. W., Lobner, E., Antes, B., Kainer, M., Wiederkum, S., Hasenhindl, C., Stadlmayr, G., Rueker, F., Woisetschlaeger, M., Moulder, K., Obinger, C. (2013) Directed evolution of yeast surface displayed Her2/neu-binding IgG-Fc for improvement of stability and resistance to aggregation. Prot. Eng. Des. Sel. 26, 255-265

Shigeta, K., Koellensperger, G., Rampler, E., Traub, H., Rottmann, L., Panne, U., Okino, A., Jakubowski, N. (2013) Sample introduction of single selenized yeast cells (Saccharomyces cerevisiae) by micro droplet generation into an ICP-sector field mass spectrometer for label-free detection of trace elements in the production process of selenized yeast by elemental speciation analysis. J. Anal. Atom. Spectrom. 28, 637-645

Gasser. B., Prielhofer, R., Marx, H., Maurer, M., Nocon, J., Steiger, M., Puxbaum, V., Sauer, M., Mattanovich, D. (2013) Pichia pastoris: protein production host and model organism for biomedical research. Future Microbiol. 8,191-208

Mulla, D., Kracher, D., Ludwig, R., Nagy, G., Grandits, M., Holzer, W., Saber, Y., Gabra, N., Viernstein, H., Unger, F. M. (2013) Azido derivatives of cellobiose: oxidation at C1 with cellobiose dehydrogenase from Sclerotium rolfsii. Carbohydr. Res. 382, 86–94

Reinhart, D., Sommeregger, W., Debreczeny, M., Gludovacz, E., Kunert, R. (2013) Characterization of recombinant IgA producing CHO cell lines by qPCR. In: BMC Proceedings, doi:10.1186/1753-6561-7-S6-P114

Posch, G., Pabst, M., Neumann, L., Coyne, M. J., Altmann, F., Messner, P., Comstock, L. E., Schaeffer, C. (2013) Cross-glycosylation of proteins in Bacteriodales species. Glycobiology 23, 568-577

Staudigl, P.*, Krondorfer, I.*, Haltrich, D., Peterbauer C.K. (2013) Pyranose dehydrogenase from Agaricus campestris and Agaricus xanthoderma: Characterization and applications in carbohydrate conversions. Biomolecules 3, 535-552 (*equally contributing)

Yakovleva, M.E., Killyeni, A., Seubert, O., Conghaile, P.Ó., MacAodha, D., Leech, D., Gonaus, C., Popescu, I.C., Peterbauer, C.K., Kjellstrom, S., Gorton, L. (2013) Further insights into the catalytical properties of deglycosylated pyranose dehydrogenase from Agaricus meleagris recombinantly expressed in Pichia pastoris. Anal. Chem. 85, 9852-9858

Rezic, T., Oros, D., Marković, I., Parat, Z., Kracher, D., Ludwig, R., Santek B. (2013) Integrated hydrolysation and fermentation of sugar beet pulp to bioethanol. J. Microbiol. Biotechnol. 23, 1244-1252

Sygmund, C., Santner, P., Krondorfer, I., Peterbauer, C.K., Alcalde, M., Nyangho, G.S., Guebitz, G.M., Ludwig R. (2013) Semi-rational engineering of cellobiose dehydrogenase for improved hydrogen peroxide production. Microb. Cell Fact. 12:38

Tan, T. C., Spadiut, O., Wongnate, T., Sucharitakul, J., Krondorfer, I., Sygmund, C., Haltrich, D., Chaiyen, P., Peterbauer, C., Divne, C. (2013) The 1.6-Å crystal structure of pyranose dehydrogenase from Agaricus meleagris rationalizes substrate specificity and reveals a flavin intermediate. PLoS ONE 8, e53567

Petricevic, L., Domig, K.J., Nierscher, F.J., Sandhofer, M.J., Krondorfer, I., Kneifel, W., Kiss, H. (2013) Differences in the vaginal lactobacilli of postmenopausal women and influence of rectal lactobacilli. Climacteric 16, 356-361

Ojea-Jimenez, I., Comenge, J., Garcia-Fernandez, L., Megson, Z. A., Casals, E., Puntes, V. F. (2013) Engineered inorganic nanoparticles for drug delivery applications. Curr. Drug Metab. 14, 518-530

Auer, M., Gruber, C., Bellei, M., Pirker, K.F., Zamocky, M., Kroiss, D., Teufer, S.A., Hofbauer, S., Soudi, M., Battistuzzi, G., Furtmueller, P.G., Obinger, C. (2013) A stable bacterial peroxidase with novel halogenating activity and an autocatalytically linked heme prosthetic group. J. Biol. Chem. 288, 181-199

Paumann-Page, M., Furtmueller, P.G., Hofbauer, S., Paton, L.N., Obinger, C., Kettle, A. J. (2013) Inactivation of human myeloperoxidase by hydrogen peroxide. Arch. Biochem. Biophys. 539, 51-62

Gerster, P., Kopecky, E.M., Hammerschmidt, N., Klausberger, M., Krammer, F., Grabherr, R., Mersich, C., Urbas, L., Kramberger, P., Paril, T., Schreiner, M., Noebauer, K., Razzazi-Fazeli, E., Jungbauer, A. (2013) Purification of infective baculoviruses by monoliths. J. Chromatogr. A 1290, 36-45

Zou, C., Lariska, M., Nagy, G., Srajer, J., Oostenbrink, C., Chen, X., Knoll, W., Liedberg, B., Nowak, C. (2013) Two-dimensional heterospectral correlation analysis of the redox-induced conformational transition in cytochrome c using surface-enhanced Raman and infrared absorption spectroscopies on a two-layer gold surface. J. Phys. Chem. B 33, 9606-9614


Jadhav, V., Hackl, M., Hernandez Bort, J.A., Wieser, M., Harreither, E., Kunert, R., Borth, N., Grillari, J. (2012) A screening method to assess biological effects of microRNA overexpression in Chinese hamster ovary cells. Biotechnol. Bioeng. 109, 1376-1385

Rampler, E., Rose, S., Wieder, D., Ganner, A., Dohnal, I., Dalik, T., Hann, S., Koellensperger, G. (2012) Monitoring the production process of selenized yeast by elemental speciation analysis. Metallomics 4, 1176–1184

Rampler, E., Dalik, T., Stingeder, G., Hann, S., Koellensperger, G. (2012) Sulfur containing amino acids - challenge of accurate quantification. J. Anal. Atom. Spectrom. 27, 1018-1023

Lai, B., Oostenbrink, C. (2012) Binding free energy, energy and entropy calculations using simple model systems. Theor. Chem. Acc., 131, 1272

Hofbauer, S., Bellei, M., Sündermann, A., Pirker, K.F., Hagmueller, A., Mlynek, G., Kostan, J., Daims, H., Furtmueller, P.G., Djinovic-Carugo, K., Oostenbrink, C., Battistuzzi, G., Obinger, C. (2012) Redox thermodynamics of high-spin and low-spin forms of chlorite dismutases with diverse subunit and oligomeric structures. Biochemistry 51, 9501-9512

Hofbauer, S., Gysel, K., Mlynek, G., Kostan, J., Hagmueller, A., Daims, H., Furtmueller, P.G., Djinovic-Carugo, K., Obinger, C. (2012) Impact of subunit and oligomeric structure on the thermal and conformational stability of chlorite dismutases. Biochim. Biophys. Acta 1824,1031-1038

Soudi, M., Zamocky, M., Jakopitsch, C., Furtmueller, P.G., Obinger, C. (2012) Molecular evolution, structure and function of peroxidasins. Chem. Biodivers. 9, 1776-1793

Nagy, G., Oostenbrink, C. (2012) Rationalization of stereospecific binding of propranolol to cytochrome P450 2D6 by free energy calculations. Eur. Biophys. J. 41, 1065–1076

Kittl, R., Gonaus, C., Pillei, C., Haltrich, D., Ludwig, R. (2012) Constitutive expression of Botrytis aclada laccase in Pichia pastoris. Bioengineered 3, 230-233

Traxlmayr, M. W., Hasenhindl, C., Hackl, M., Stadlmayr, G., Rybka, J. D., Borth, N., Grillari, J., Rueker, F., Obinger, C. (2012) Construction of a stability landscape of the CH3 domain of human IgG1 by combining directed evolution with high throughput sequencing. J. Mol. Biol. 423, 397-412

Delic, M., Rebnegger, C., Wanka, F., Puxbaum, V., Haberhauer-Troyer, C., Hann, S., Koellensperger, G., Mattanovich, D., Gasser, B. (2012) Oxidative protein folding and unfolded protein response elicit differing redox regulation in endoplasmic reticulum and cytosol of yeast. Free Radic. Biol. Med. 52, 2000–2012

Castilho, A., Neumann, L., Daskalova, S., Mason, H. S., Steinkellner, H., Altmann, F., Strasser, R. (2012) Engineering of sialylated mucin-type O-glycosylation in plants. J. Biol. Chem. 287, 36518-36526

Hackl, M., Jadhav, V., Jakobi, T., Rupp, O., Brinkrolf, K., Goesmann, A., Puehler, A., Noll, T., Borth, N., Grillari, J. (2012) Computational identification of microRNA gene loci and precursor microRNA sequences in CHO cell lines. J. Biotechnol. 158, 151-155

Kittl, R., Kracher, D., Burgstaller, D., Haltrich, D., Ludwig, R. (2012) Production of four Neurospora crassa lytic polysaccharide monooxygenases in Pichia pastoris monitored by a fluorimetric assay. Biotechnol. Biofuels  5:79

Sygmund, C., Kracher, D., Scheiblbrandner, S., Zahma, K., Felice, A.K., Harreither, W., Kittl, R., Ludwig, R. (2012) Characterization of the two Neurospora crassa cellobiose dehydrogenases and their connection to oxidative cellulose degradation. Appl. Environ. Microbiol. 78, 6161-6171

Bort, J.A., Hackl, M., Höflmayer, H., Jadhav, V., Harreither, E., Kumar, N., Ernst, W., Grillari, J., Borth, N. (2012) Dynamic mRNA and miRNA profiling of CHO-K1 suspension cell cultures. Biotechnol. J. 7, 500-515

Posch, G., Sekot, G., Friedrich, V., Megson, Z. A., Koerdt, A., Messner, P., Schaeffer, C. (2012) Glycobiology aspects of the periodontal pathogen Tannerella forsythia. Biomolecules 2, 467-482

Zamocky, M., Gasselhuber, B., Furtmueller, P. G., Obinger, C. (2012) Molecular evolution of hydrogen peroxide degrading enzymes. Arch. Biochem. Biophys. 525, 131-144

Gu, C., Shabab, M., Strasser, R., Wolters, P.J., Shindo, T., Niemer, M., Kaschani, F., Mach, L., van der Hoorn, R.A. (2012) Post-translational regulation and trafficking of the granulin-containing protease RD21 of Arabidopsis thaliana. PLoS One 7:e32422.

Jung, G., Pabst, M., Neumann, L., Berger, A., Lubec, G. (2012) Characterization of α-l-Iduronidase (Aldurazyme®) and its complexes. J. Proteomics 80, 26-33

Liebminger, E., Grass, J., Jez, J., Neumann, L., Altmann, F., Strasser, R. (2012) Myrosinases TGG1 and TGG2 from Arabidopsis thaliana contain exclusively oligomannosidic N-glycans. Phytochemistry 84, 24-30

Traxlmayr, M. W., Faissner, M., Stadlmayr, M., Hasenhindl, C., Rueker, F., Obinger, C. (2012) Directed evolution of stabilized scaffolds by application of strong heat shock to IgG1-Fc libraries displayed on yeast. Biochim. Biophys. Acta 1824, 542-549

Zamocky, M., Droghetti, E., Bellei, M., Furtmueller, P. G., Gasselhuber, B., Pabst, M., Battistuzzi, G., Smulevich, G., Obinger, C. (2012) Eukaryotic extracellular catalase-peroxidase from Magnaporthe grisea – biophysical/chemical characterization of the first representative from a novel phytopathogenic KatG group. Biochimie 94, 673-683

Zamocky, M., Garcia-Fernandez, M. Q., Gasselhuber, B., Furtmueller, P. G., Loewen, P. C., Fita, I., Obinger, C., Carpena, X. (2012) High thermal and conformational stability of secretory eukaryotic catalase-peroxidases - Answers from first crystal structure and unfolding studies. J. Biol. Chem. 287, 32254-32262

Swoboda, M., Henig, J., Cheng, H. M., Brugger, D., Haltrich, D., Plumere, N., Schlierf, M. (2012) Enzymatic oxygen scavenging for photostability without pH drop in single-molecule experiments. ASC Nano 6, 6364–6369

Yakovleva, M.E., Killyeni, A., Ortiz, R., Schulz, C., MacAodha, D., Conghaile, P.O., Leech, D., Popescu, I.C., Gonaus, C., Peterbauer, C.K., Gorton, L. (2012) Recombinant pyranose dehydrogenase - A versatile enzyme possessing both mediated and direct electron transfer. Electrochem. Commun. 24, 120-122

Kittl, R., Mueangtoom, K., Gonaus, C., Khazaneh, S.T., Sygmund, C., Haltrich, D., Ludwig, R. (2012) A chloride tolerant laccase from the plant pathogen ascomycete Botrytis aclada expressed at high levels in Pichia pastoris. J. Biotechnol. 157, 304-314

Petricevic, L., Domig, K.J., Nierscher, F.J., Krondorfer, I., Janitschek, C., Kneifel, W., Kiss, H. (2012) Characterisation of the oral, vaginal and rectal Lactobacillus flora in healthy pregnant and postmenopausal women. EJOG 160, 93-99

Nguyen, T.T., Nguyen, H.A., Arreola, S.L, Mlynek, G., Djinovic-Carugo, K., Mathiesen, G., Nguyen, T.H., Haltrich, D. (2012) Homodimeric β-galactosidase from Lactobacillus delbrueckii subsp. bulgaricus DSM 20081: expression in Lactobacillus plantarum and biochemical characterization. J. Agric. Food Chem. 60,1713-1721

Ristl, R., Janesch, B., Anzengruber, J., Forsthuber, A., Blaha, J., Messner, P., Schaeffer, C. (2012) Description of a putative S-layer protein:oligosaccharyltransferase from the tyrosine O‑glycosylation system of Paenibacillus alvei CCM 2051. Adv. Microbiol. 2, 537-546



Mlynek, G., Sjoeblom, B., Kostan, J., Füreder, S., Maixner, F., Gysel, K., Furtmueller, P.G., Obinger, C., Wagner, M., Daims, H., Djinovic-Carugo, K. (2011) Unexpected diversity of chlorite dismutases: a catalytically efficient dimeric enzyme from Nitrobacter winogradskyi. J. Bacteriol. 193, 2408-2417

Nagy, G., Gyurcsik, B., Hoffmann, E. A., Körtvelyesi, T. (2011) Theoretical design of a specific DNA–Zinc-finger protein interaction with semi-empirical quantum chemical methods. J. Mol. Graph. Model. 29, 928–934

Sygmund, C., Klausberger, M., Felice, A.K., Ludwig, R. (2011) Reduction of quinones and phenoxy radicals by extracellular glucose dehydrogenase from Glomerella cingulata suggests a role in plant pathogenicity. Microbiology 157, 3203-3212

Buchetics, M., Dragosits, M., Maurer, M., Rebnegger, C., Porro, D., Sauer, M., Gasser, B., Mattanovich, D. (2011) Reverse engineering of protein secretion by uncoupling of cell cycle phases from growth. Biotechnol. Bioeng. 108, 2403–2412

Sygmund, C., Gutmann, A., Krondorfer, I., Kujawa, M., Glieder, A., Pscheidt, B., Haltrich, D., Peterbauer, C., Kittl, R. (2011) Simple and efficient expression of Agaricus meleagris pyranose dehydrogenase in Pichia pastoris. Appl. Microbiol. Biotechnol. 94, 695-704

Sygmund, C., Staudigl, P., Klausberger, M., Pinotsis, N., Djinovic-Carugo, K., Gorton, L., Haltrich, D., Ludwig, R. (2011) Heterologous overexpression of Glomerella cingulata FAD-dependent glucose dehydrogenase in Escherichia coli and Pichia pastoris. Microb. Cell Fact. 12: 106

Stampler, J., Bellei, M., Soudi, M., Gruber, C., Battistuzzi, G., Furtmueller, P.G., Obinger, C. (2011) Manipulating the proximal triad His-Asn-Arg in human myeloperoxidase. Arch. Biochem. Biophys. 516, 21-28

Battistuzzi, G., Stampler, J., Bellei, M., Vlasits, J., Soudi, M., Sola, M., Furtmueller, P.G., Obinger, C. (2011) Influence of the covalent heme to protein bonds on the redox thermodynamics of human myeloperoxidase. Biochemistry 50, 7987-7994


Spadiut, O., Brugger, D., Coman, V., Haltrich, D., Gorton, L. (2010) Engineered pyranose 2-oxidase: efficiently turning sugars into electrical energy. Electroanalysis 22, 831-820

Kostan, J., Sjoeblom, B., Maixner, F., Mlynek, G., Furtmueller, P.G., Obinger, C., Wagner, M., Daims, H., Djinovic-Carugo, K. (2010) Structural and functional characterisation of the chlorite dismutase from the nitrite-oxidizing bacterium "Candidatus Nitrospira defluvii": identification of a catalytically important amino acid residue. J. Struct. Biol. 172, 331-342

Krammer, F., Pontiller, J., Tauer, C., Palmberger, D., Maccani, A., Baumann, M., Grabherr, R. (2010) Evaluation of the influenza A replicon for transient expression of recombinant proteins in mammalian cells. PLoS One 5: e13265

Pontiller, J., Maccani, A., Baumann, M., Klancnik, I., Ernst, W. (2010) Identification of CHO endogenous gene regulatory elements. Mol. Biotechnol. 45, 235-240