Publications of BioToP PhD-Students

(Highlighted are BioToP students and BioToP faculty members)


2018

Eisenhut, P., Klanert, G., Weinguny, M., Baier, L., Jadhav, V., Ivansson, D., Borth, N. (2018) A CRISPR/Cas9 based engineering strategy for overexpression of multiple genes in Chinese hamster ovary cells. Metab. Eng. doi: 10.1016/j.ymben.2018.05.017

Pfanzagl, V., Nys, K., Bellei, M., Michlits, H., Mlynek, G., Battistuzzi, G., Djinovic-Carugo, K., Van Doorslaer, S., Furtmuller, P. G., Hofbauer, S., Obinger, C. (2018) Roles of distal aspartate and arginine of B-class dye-decolorizing peroxidase in heterolytic hydrogen peroxide cleavage. J. Biol. Chem. 293, 14823-14838. doi: 10.1074/jbc.RA118.004773

Blackler, R. J., Lopez-Guzman, A., Hager, F. F., Janesch, B., Martinz, G., Gagnon, S. M. L., Haji-Ghassemi, O., Kosma, P., Messner, P., Schäffer, C., Evans, S. V. (2018) Structural basis of cell wall anchoring by SLH domains in Paenibacillus alvei. Nat. Commun. 9, 3120. doi: 10.1038/s41467-018-05471-3

Turupcu, A., Almohamed, W., Oostenbrink, C., Seifert, G. J. (2018) A speculation on the tandem fasciclin 1 repeat of FLA4 proteins in angiosperms. Plant signaling & behavior  1-5. doi: 10.1080/15592324.2018.1507403

Vogt, S., Stadlmayr, G., Stadlbauer, K., Sádio, F., Andorfer, P., Grillari, J., Rüker, F., Wozniak-Knopp, G. (2018) Stabilization of the CD81 Large Extracellular Loop with De Novo Disulfide Bonds Improves Its Amenability for Peptide Grafting. Pharmaceutics doi: 10.3390/pharmaceutics10030138

Bydlinski, N., Maresch, D., Schmieder, V., Klanert, G., Strasser, R., Borth, N. (2018) The contributions of individual galactosyltransferases to protein specific N-glycan processing in Chinese Hamster Ovary cells. J. Biotechnol. doi: 10.1016/j.jbiotec.2018.07.015

Hager, F., Lopez Guzman, A., Krauter, S., Blaukopf, M., Polter, M., Brockhausen, I., Kosma, P., Schäffer, C. (2018) Functional Characterization of Enzymatic Steps Involved in Pyruvylation of Bacterial Secondary Cell Wall Polymer Fragments. Front. Microbiol. doi:10.3389/fmicb.2018.01356

Montero-Morales, L. and Steinkellner, H. (2018) Advanced Plant-Based Glycan Engineering. Front. Bioeng. Biotechnol. 6, 81. doi: 10.3389/fbioe.2018.00081

Porodko, A., Cirnski, A., Petrov, D., Mayer, T., Paireder, M., Mayer, B., Maresch, D., Nika, L., Biniossek, M.L., Gallois, P., Schilling, O., Oostenbrink, C., Novinec, M., Mach, L. (2018) The two cathepsin B-like proteases of Arabidopsis thaliana are closely related enzymes with discrete endopeptidase and carboxydipeptidase activities. Biol. Chem. doi: 10.1515/hsz-2018-0186

Kallolimath, S., Gruber, C., Steinkellner, H., Castilho, A. (2018) Promoter choice impacts the efficiency of plant glyco-engineering. Biotechnol. J. 13, 1700380. doi: 10.1002/biot.201700380

Medfai, H., Kalil, A., Rousseau, A., Nuyens, V., Paumann-Page, M., Sevcnikar, B., Furtmüller, P.G., Obinger, C., Moguilevsky, N., Peulen, O., Herfs, M., Castronovo, V., Amri, M., Vanhamme, L., Van Antwerpen, P., Zouaoui Boudjeltia, K. (2018) Human peroxidasin 1 promotes angiogenesis through ERK1/2, Akt and FAK pathways. Cardiovasc. Res. 114, doi: 10.1093/cvr/cvy/118                                                

Schwaigerlehner, L., Pechlaner, M., Mayrhofer, P., Oostenbrink, C., Kunert, R. (2018) Lessons learned from merging wet lab experiments with molecular simulation to improve mAb humanization. Protein Eng. Des. Sel., doi: 10.1093/protein/gzy009

Reinhart, D., Damjanovic, L., Kaisermayer, C., Sommeregger, W., Gili, A., Gasselhuber, B., Castan, A., Mayrhofer, P., Grünwald-Gruber, C., Kunert, R. (2018) Bioprocessing of recombinant CHO-K1, CHO-DG44 and CHO-S: CHO expression hosts favor either mAb production or biomass synthesis. Biotechnol. J., doi: 10.1002/biot.201700686.

Terlecki-Zaniewicz, L., Lämmermann, I., Latreille, J., Bobbili, M.R., Pils, V., Schosserer, M., Weinmüllner, R., Dellago, H., Skalicky, S., Pum, D., Higareda Almaraz, J.C., Scheideler, M., Morizot, F., Hackl, M., Gruber, F., Grillari, J., (2018) Extracellular vesicles and their miRNA cargo are anti-apoptotic members of the SASP. Aging10, 1103 – 1132, doi:10.18632/aging.101452

Heistinger, L., Moser, J., Tatto, N.E., Valli, M., Gasser, B., Mattanovich, D. (2018) Identification and characterization of the Komagataella phaffii mating pheromone genes. FEMS Yeast Res. 18, foy051. doi: 10.1093/femsyr/foy051

Gassler, T., Heistinger, L., Mattanovich, D., Gasser, B., Prielhofer R. (2018) CRISPR/Cas9-mediated homology directed genome editing in Pichia pastoris. Methods Mol. Biol., accepted

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. Biotechnol. Biofuels 11, 79. doi:10.1186/s13068-018-1063-6
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

Schmieder, V., Bydlinski, N., Strasser, R., Baumann, M., Kildegaard, H.F., Jadhav, V., Borth, N. (2018) Enhanced Genome Editing Tools For Multi-Gene Deletion Knock-Out Approaches Using Paired CRISPR sgRNAs in CHO Cells. Biotechnol. J. 13, e1700211. doi: 10.1002/biot.201700211

Nagelreiter, F., Coats, M.T., Klanert, G., Gludovacz, E., Borth, N., Grillari, J., Schosserer, M. (2018) OPP Labeling Enables Total Protein Synthesis Quantification in CHO Production Cell Lines at the Single-Cell Level. Biotechnol. J. doi: 10.1002/biot.201700492

Gludovacz, E., Maresch, D., Lopes de Carvalho, L., Puxbaum, V., Baier, L.J., Sutzl, L., Guedez, G., Grunwald-Gruber, C., Ulm, B., Pils, S., Ristl, R., Altmann, F., Jilma, B., Salminen, T.A., Borth, N., Boehm, T. (2018) Oligomannosidic glycans at Asn-110 are essential for secretion of human diamine oxidase. J. Biol. Chem. 293, 1070-1087. doi: 10.1074/jbc.M117.814244

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. doi: 10.1128/MCB.00398-17

Pfanzagl, V., Holcik, L., Maresch, D., Gorgone, G., Michlits, H., Furtmuller, P.G., Hofbauer, S. (2018) Coproheme decarboxylases - Phylogenetic prediction versus biochemical experiments. Arch. Biochem. Biophys. 640, 27-36. doi: 10.1016/j.abb.2018.01.005

Jandova, Z., Fast, D., Setz, M., Pechlaner, M., Oostenbrink, C. (2018) Saturation Mutagenesis by Efficient Free-Energy Calculation. J. Chem. Theory Comput. 14, 894-904. doi: 10.1021/acs.jctc.7b01099

Proff, J., Brey, C.U., 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. doi: 10.1186/s12967-018-1394-x

Rupp, O., MacDonald, M.L., Li, S., Dhiman, H., Polson, S., Griep, S., Heffner, K., Hernandez, I., Brinkrolf, K., Jadhav, V., Samoudi, M., Hao, H., Kingham, B., Goesmann, A., Betenbaugh, M.J., Lewis, N.E., Borth, N., Lee, K.H. (2018) A reference genome of the Chinese hamster based on a hybrid assembly strategy. Biotechnol. Bioeng. doi: 10.1002/bit.26722

Pena, D.A., Gasser, B., Zanghellini, J., Steiger, M.G., Mattanovich, D. (2018) Metabolic engineering of Pichia pastoris. Metab. Eng. doi: 10.1016/j.ymben.2018.04.017

Bloch, S., Zwicker, S., Bostanci, N., Sjöling, Å., 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. 33, 155-167. doi: 10.1111/omi.12208

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/j.abb.2018.02.008

Delporte, C., Zouaoui Boudjeltia, K., Furtmueller, P.G., Maki, R.A., Dieu, M., Noyon, C., Soudi, M., Dufour, D., Coremans, C., Nuyens, V., Reye, F., Rousseau, A., Raes, M., Moguilevsky, N., Vanhaeverbeek, M., Ducobu, J., Neve, J., Robaye, B., Vanhamme, L., Reynolds, W.F., Obinger, C., Van Antwerpen, P. (2018) Myeloperoxidase-catalyzed oxidation of cyanide to cyanate: A potential carbamylation route involved in the formation of atherosclerotic plaques? J. Biol. Chem. doi: 10.1074/jbc.m117.801076

Jandova, Z., Trosanova, Z., Weisova, V., Oostenbrink, C., Hritz, J. (2018) Free energy calculations on the stability of the 14-3-3ζ protein. Biochim. Biophys. Acta 1866, 442-450. doi: 10.1016/j.bbapap.2017.11.012

Bönisch, E., Oh, Y.J., Anzengruber, J., Hager, F.F., López-Guzmán, 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 28, 148-158. doi: 10.1093/glycob/cwx102

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. 102, 2477-2492. doi: 10.1007/s00253-018-8784-0

Kracher, D., Andlar, M., Furtmüller, P.G., Ludwig, R. (2018) Active-site copper reduction promotes substrate binding of fungal lytic polysaccharide monooxygenase and reduces stability. J. Biol. Chem. 293, 1676-1687. doi: 10.1074/jbc.ra117.000109

Castilho, A., Beihammer, G., 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

Nicolussi, A., Dunn, J.D., Mlynek, G., Bellei, M., Zamocky, M., Battistuzzi, G., Djinović-Carugo, K., Furtmüller, P.G., Soldati, T., Obinger, C. (2018) 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

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, 181-194. doi: 10.1007/s00204-017-2034-6

Hottmann, I., Mayer, V.M.T., Tomek, M.B., Friedrich, V., Calvert, M.B., Titz, A., Schäffer, C., Mayer, C. (2018) N-Acetylmuramic Acid (MurNAc) Auxotrophy of the Oral Pathogen Tannerella forsythia: Characterization of a MurNAc Kinase and Analysis of Its Role in Cell Wall Metabolism. Front. Microbiol. 9, 19. doi: 10.3389/fmicb.2018.00019

Jungreuthmayer, C., Gerstl, M.P., Pena Navarro, D.A., Hanscho, M., Ruckerbauer, D.E., Zanghellini, J. (2018) Designing Optimized Production Hosts by Metabolic Modeling. Methods Mol. Biol. 1716, 371-387. doi: 10.1007/978-1-4939-7528-0_17

Eisenhut, P., Klanert, G., Weinguny, M., Baier, L., Jadhav, V., Ivansson, D., Borth, N. (2018) A CRISPR/Cas9 based engineering strategy for overexpression of multiple genes in Chinese hamster ovary cells. Metab. Eng. doi: 10.1016/j.ymben.2018.05.017

Marx, N., Grünwald‐Gruber, C., Bydlinski, N., Dhiman, H., Ngoc Ly, N., Klanert, G., Borth, N. (2018) CRISPR‐based targeted epigenetic editing enables gene expression modulation of the silenced beta‐galactoside alpha‐2,6‐sialyltransferase 1 in CHO cells. Biotechnol. J., 1700217. doi: 10.1002/biot.201700217

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

 

2017

Turupcu, A. and Oostenbrink, C. (2017) Modeling of Oligosaccharides within Glycoproteins from Free-Energy Landscapes. J. Chem. Inf. Model. 57, 2222-2236. doi: 10.1021/acs.jcim.7b00351

Bönisch, M., Sellmann, C., Maresch, D., Halbig, C., Becker, S., Toleikis, L., Hock, B., Rüker, F. (2017) Novel CH1:CL interfaces that enhance correct light chain pairing in heterodimeric bispecific antibodies. Protein Eng. Des. Sel. 30, 685-696. doi: 10.1093/protein/gzx044

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., Wang, X. (2017) A novel chemoradiation targeting stem and nonstem pancreatic cancer cells by repurposing disulfiram. Cancer Lett. 409, 9-19. doi: 10.1016/j.canlet.2017.08.028

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

Paumann-Page, M., Katz, R.S., Bellei, M., Schwartz, I., Edenhofer, E., Sevcnikar, B., Soudi, M., Hofbauer, S., Battistuzzi, G., Furtmuller, P.G., 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, 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. Microb. Cell Fact. 16, 37. doi: 10.1186/s12934-017-0653-5

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 Syst. Biol. 11, 123. doi: 10.1186/s12918-017-0492-3

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

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. Acta 1865, 444-452. doi: 10.1016/j.bbapap.2017.02.007

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

Hennicke, J., Lastin, A.M., Reinhart, D., Grünwald-Gruber, C., Altmann, F., 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

Mayrhofer, P., and Kunert, R. (2017) Cloning of single-chain antibody variants by overlap-extension PCR for evaluation of antibody expression in transient gene expression. Methods Mol. Biol. 1603, 57-69. doi:10.1007/978-1-4939-6972-2

Schaffner, I., Mlynek, G., Flego, N., Pühringer, D., Libiseller-Egger, J., Coates, L., Hofbauer, S., Bellei, M., Furtmüller, P.G., Battistuzzi, G., Smulevich, G., Djinović-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 Res. 17, fox068. doi: 10.1093/femsyr/fox068

Bloch, S., Thurnheer, T., Murakami, Y., Belibasakis, G.N., Schäffer, C. (2017) Behavior of two Tannerella forsythia strains and their cell surface mutants in multispecies oral biofilms. Mol. Oral Microbiol. 32, 404-418. doi: 10.1111/omi.12182

Lobner, E., Humm, A.-S., 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 Å crystal structure of the complex. MAbs 9, 1088-1104. doi: 10.1080/19420862.2017.1364825

Scheiblbrandner, S., Breslmayr, E., Csarman, F., Paukner, R., Führer, J., Herzog, P.L., Shleev, S.V., Osipov, E.M., Tikhonova, T.V., Popov, V.O., Haltrich, D., Ludwig, R., Kittl, R. (2017) Evolving stability and pH-dependent activity of the high redox potential Botrytis aclada laccase for enzymatic fuel cells. Sci. Rep. 7, 13688. doi: 10.1038/s41598-017-13734-0

Shridhar, S., Klanert, G., Auer, N., Hernandez-Lopez, I., Kańduła, M.M., Hackl, M., Grillari, J., Stralis-Pavese, N., Kreil, D.P., 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. 257, 13-21. doi: 10.1016/j.jbiotec.2017.03.012

Soukup, K., Halfmann, A., Dillinger, B., Poyer, F., Martin, K., Blauensteiner, B., Kauer, M., Kuttke, M., Schabbauer, G., 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
Bobbili, M.R., Mader, R.M., Grillari, J., Dellago, H. (2017) OncomiR-17-5p: alarm signal in cancer? Oncotarget 8, 71206-71222. doi: 10.18632/oncotarget.19331

Nicolussi, A., Auer, M., Weissensteiner, J., Schütz, G., Katz, S., Maresch, D., Hofbauer, S., Bellei, M., Battistuzzi, G., Furtmüller, P.G., 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

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. 16, 2560-2570. doi: 10.1021/acs.jproteome.7b00121

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

Lobner, E., Humm, A.-S., Göritzer, K., Mlynek, G., Puchinger, M.G., Hasenhindl, C., Rüker, F., Traxlmayr, M.W., Djinović-Carugo, K., Obinger, C. (2017) Fcab-HER2 Interaction: a Ménage à Trois. Lessons from X-Ray and Solution Studies. Structure 25, 878-889.e875. doi: 10.1016/j.str.2017.04.014

Tomek, M.B., Janesch, B., Maresch, D., Windwarder, M., Altmann, F., Messner, P., Schäffer, 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 27, 555-567. doi: 10.1093/glycob/cwx019

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

Grishkovskaya, I., Paumann-Page, M., Tscheliessnig, R., Stampler, J., Hofbauer, S., Soudi, M., Sevcnikar, B., Oostenbrink, C., Furtmüller, P.G., Djinović-Carugo, K., Nauseef, W.M., Obinger, C. (2017) Structure of human promyeloperoxidase (proMPO) and the role of the propeptide in processing and maturation. J. Biol. Chem. 292, 8244-8261. doi: 10.1074/jbc.m117.775031

Gonaus, C., Maresch, D., Schropp, K., Ó Conghaile, P., Leech, D., Gorton, L., Peterbauer, C.K. (2017) Analysis of Agaricus meleagris pyranose dehydrogenase N-glycosylation sites and performance of partially non-glycosylated enzymes. Enzyme Microb. Technol. 99, 57-66. doi: 10.1016/j.enzmictec.2017.01.008

Graf, M.M.H., 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 meleagris). Appl. Microbiol. Biotechnol. 101, 2879-2891. doi: 10.1007/s00253-016-8051-1

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. (2017) Tannerella forsythia strains display different cell-surface nonulosonic acids: biosynthetic pathway characterization and first insight into biological implications. Glycobiology 27, 342-357. doi: 10.1093/glycob/cww129

Prats Mateu, B., Harreither, E., Schosserer, M., Puxbaum, V., Gludovacz, E., Borth, N., Gierlinger, N., Grillari, J. (2017) Label-free live cell imaging by Confocal Raman Microscopy identifies CHO host and producer cell lines. Biotechnol. J. 12, 1600037. doi: 10.1002/biot.201600037
Kapusi, E., Corcuera-Gómez, M., Melnik, S., Stoger, E. (2017) Heritable Genomic Fragment Deletions and Small Indels in the Putative ENGase Gene Induced by CRISPR/Cas9 in Barley. Front. Plant Sci. 8, 540. doi: 10.3389/fpls.2017.00540

Nagy, G., Oostenbrink, C., Hritz, J. (2017) Exploring the binding pathways of the 14-3-3ζ protein: Structural and free-energy profiles revealed by Hamiltonian replica exchange molecular dynamics with distancefield distance restraints. PLoS One 12, e0180633. doi: 10.1371/journal.pone.0180633

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

Dillinger, B., Ahmadi-Erber, S., Soukup, K., Halfmann, A., Schrom, S., Vanhove, B., Steinberger, P., Geyeregger, R., Ladisch, S., Dohnal, A.M. (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

Hykollari, A., Paschinger, K., Eckmair, B., Wilson, I.B.H. (2017) Analysis of Invertebrate and Protist N-Glycans. Methods Mol. Biol. 1503, 167-184. doi: 10.1007/978-1-4939-6493-2_13

 
2016

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. Proc. Natl. Acad. Sci U S A 113, 5922-5927 doi:10.1073/pnas.1602566113

Traxlmayr, M.W., Kiefer, J.D., Srinivas, R.R., Lobner, E., Tisdale, A.W., Mehta, N.K., Yang, N.J., Tidor, B., Wittrup, K.D. (2016) Strong Enrichment of Aromatic Residues in Binding Sites from a Charge-neutralized Hyperthermostable Sso7d Scaffold Library. J. Biol. Chem. 291, 22496-22508. doi: 10.1074/jbc.M116.741314

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., Bluml, 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, e1164918. doi: 10.1080/2162402X.2016.1164918

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, 73-92. doi: 10.1074/mcp.M115.055061

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, 2156-2163. doi: 10.1021/acs.analchem.5b03745

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, 573-597. doi: 10.1074/mcp.M115.051573

Kallolimath, S., Castilho, A., Strasser, R., Grunwald-Gruber, C., Altmann, F., Strubl, S., Galuska, C.E., Zlatina, K., Galuska, S.P., Werner, S., Thiesler, H., Werneburg, S., Hildebrandt, H., Gerardy-Schahn, R., Steinkellner, H. (2016) Engineering of complex protein sialylation in plants. Proc. Natl. Acad. Sci. U. S. A. 113, 9498-9503. doi: 10.1073/pnas.1604371113

Stafford, G.P., Chaudhuri, R.R., Haraszthy, V., Friedrich, V., Schäffer, C., Ruscitto, A., Honma, K., Sharma, A. (2016) Draft Genome Sequences of Three Clinical Isolates of Tannerella forsythia Isolated from Subgingival Plaque from Periodontitis Patients in the United States. Genome Announc. 4. doi: 10.1128/genomea.01286-16

Ortmayr, K., Charwat, V., Kasper, C., Hann, S., Koellensperger, G. (2016) Uncertainty budgeting in fold change determination and implications for non-targeted metabolomics studies in model systems. The Analyst 142, 80-90. doi: 10.1039/c6an01342b

Geiger, B.*, Nguyen, H.-M.*, Wenig, S., Nguyen, H.A., Lorenz, C., Kittl, R., Mathiesen, G., 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 thermophilus. Biochem. Eng. J. 116, 45-53. doi: 10.1016/j.bej.2016.04.003. *equally contributing first authors

Hofbauer, S., Mlynek, G., Milazzo, L., Pühringer, D., Maresch, D., Schaffner, I., Furtmüller, P.G., Smulevich, G., Djinović-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

Graf, M.M.H., Maurer, M., Oostenbrink, C. (2016) Free-energy calculations of residue mutations in a tripeptide using various methods to overcome inefficient sampling. J. Comput. Chem. 37, 2597-2605. doi: 10.1002/jcc.24488

Brugger, D., Sützl, L., Zahma, K., Haltrich, D., Peterbauer, C.K., 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. 18, 32072-32077. doi: 10.1039/c6cp06009a

Feichtinger, J., Hernández, 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 over time. Biotechnol. Bioeng. 113, 2241-2253. doi: 10.1002/bit.25990

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. 235, 150-161. doi: 10.1016/j.jbiotec.2016.03.022

Nguyen, H.-M., Mathiesen, G., Stelzer, E.M., Pham, M.L., Kuczkowska, K., Mackenzie, A., Agger, J.W., Eijsink, V.G.H., Yamabhai, M., Peterbauer, C.K., Haltrich, D., Nguyen, T.-H. (2016) Display of a β-mannanase and a chitosanase on the cell surface of Lactobacillus plantarum towards the development of whole-cell biocatalysts. Microb. Cell Fact. 15, 169. doi: 10.1186/s12934-016-0570-z

Hofbauer, S., Dalla Sega, M., Scheiblbrandner, S., Jandova, Z., Schaffner, I., Mlynek, G., Djinović-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

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. 113, 1902-1912. doi: 10.1002/bit.25957

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

Rebnegger, C., Vos, T., Graf, A.B., Valli, M., Pronk, J.T., Daran-Lapujade, P., Mattanovich, D. (2016) Pichia pastoris Exhibits High Viability and a Low Maintenance Energy Requirement at Near-Zero Specific Growth Rates. Appl. Environ. Microbiol. 82, 4570-4583. doi: 10.1128/aem.00638-16

Paireder, M., Mehofer, U., Tholen, S., Porodko, A., Schähs, P., Maresch, D., Biniossek, M.L., van der Hoorn, R.A.L., 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. 603, 110-117. doi: 10.1016/j.abb.2016.05.017

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. 100, 5955-5963. doi: 10.1007/s00253-016-7363-5

Steppert, P., Burgstaller, D., Klausberger, M., Berger, E., Aguilar, P.P., Schneider, T.A., Kramberger, P., Tover, A., Nöbauer, K., Razzazi-Fazeli, E., Jungbauer, A. (2016) Purification of HIV-1 gag virus-like particles and separation of other extracellular particles. J. Chromatogr. A 1455, 93-101. doi: 10.1016/j.chroma.2016.05.053

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, 2515-2524. doi: 10.1074/mcp.o115.056671

Margreitter, C.*, Mayrhofer, P.*, Kunert, R., Oostenbrink, C. (2016) Antibody humanization by molecular dynamics simulations-in-silico guided selection of critical backmutations. J. Mol. Recognit. 29, 266-275. doi: 10.1002/jmr.2527. *equally contributing first authors

Gasselhuber, B., Graf, M.M.H., Jakopitsch, C., Zamocky, M., Nicolussi, A., Furtmüller, P.G., Oostenbrink, C., Carpena, X., Obinger, C. (2016) Interaction with the Redox Cofactor MYW and Functional Role of a Mobile Arginine in Eukaryotic Catalase-Peroxidase. Biochemistry 55, 3528-3541. doi: 10.1021/ acs.biochem.6b00436

Tschofen, M., Knopp, D., Hood, E., Stöger, E. (2016) Plant Molecular Farming: Much More than Medicines. Annu. Rev. Anal. Chem. 9, 271-294. doi: 10.1146/annurev-anchem-071015-041706

Schosserer, M., Minois, N., Angerer, T.B., Amring, M., Dellago, H., Harreither, E., Calle-Perez, A., Pircher, A., Peter Gerstl, M., Pfeifenberger, S., Brandl, C., Sonntagbauer, M., Kriegner, A., Linder, A., Weinhäusel, A., Mohr, T., Steiger, M., Mattanovich, D., Rinnerthaler, M., Karl, T., Sharma, S., Entian, K.-D., Kos, M.,

Breitenbach, M., Wilson, I.B.H., Polacek, N., Grillari-Voglauer, R., Breitenbach-Koller, L., Grillari, J. (2016) Corrigendum: Methylation of ribosomal RNA by NSUN5 is a conserved mechanism modulating organismal lifespan. Nat. Commun. 7, 11530. doi: 10.1038/ncomms11530

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 352, 1098-1101. doi: 10.1126/science.aaf3165

Hassan, N., Geiger, B., Gandini, R., Patel, B.K.C., 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, 3533-3543. doi: 10.1007/s00253-015-7118-8

Satzer, P., Svec, F., Sekot, G., Jungbauer, A. (2016) Protein adsorption onto nanoparticles induces conformational changes: Particle size dependency, kinetics, and mechanisms. Eng. Life. Sci. 16, 238-246. doi: 10.1002/elsc.201500059

Maurer, M., de Beer, S.B.A., Oostenbrink, C. (2016) Calculation of Relative Binding Free Energy in the Water-Filled Active Site of Oligopeptide-Binding Protein A. Molecules 21, 499. doi: 10.3390/molecules21040499

Gonaus, C., Kittl, R., Sygmund, C., Haltrich, D., Peterbauer, C. (2016) Transcription analysis of pyranose dehydrogenase from the basidiomycete Agaricus bisporus and characterization of the recombinantly expressed enzyme. Protein Expr. Purif. 119, 36-44. doi: 10.1016/j.pep.2015.11.003

Niemer, M., Mehofer, U., Verdianz, M., Porodko, A., Schähs, P., Kracher, D., Lenarcic, B., Novinec, M., Mach, L. (2016) Nicotiana benthamiana cathepsin B displays distinct enzymatic features which differ from its human relative and aleurain-like protease. Biochimie 122, 119-125. doi: 10.1016/j.biochi.2015.06.017

Hofbauer, S., Howes, B.D., Flego, N., Pirker, K.F., Schaffner, I., Mlynek, G., Djinović-Carugo, K., Furtmüller, P.G., Smulevich, G., Obinger, C. (2016) From chlorite dismutase towards HemQ - the role of the proximal H-bonding network in haeme binding. Biosci. Rep. 36. doi: 10.1042/bsr20150330

Kurz, S., King, J.G., Dinglasan, R.R., 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

Weilner, S., Keider, V., Winter, M., Harreither, E., Salzer, B., Weiss, F., Schraml, E., Messner, P., Pietschmann, P., Hildner, F., Gabriel, C., Redl, H., Grillari-Voglauer, R., Grillari, J. (2016) Vesicular Galectin-3 levels decrease with donor age and contribute to the reduced osteo-inductive potential of human plasma derived extracellular vesicles. Aging 8, 16-33. doi: 10.18632/aging.100865

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, e0153579. doi: 10.1371/journal.pone.0153579

van Teeseling, M.C.F., Maresch, D., Rath, C.B., Figl, R., Altmann, F., Jetten, M.S.M., Messner, P., Schäffer, C., van Niftrik, L. (2016) The S-Layer Protein of the Anammox Bacterium Kuenenia stuttgartiens is Is Heavily O-Glycosylated. Front. Microbiol. 7, 1721. doi: 10.3389/fmicb.2016.01721

Hofbauer, A., Melnik, S., Tschofen, M., Arcalis, E., Phan, H.T., 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. 7, 142. doi: 10.3389/fpls.2016.00142

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, e0148108. doi: 10.1371/journal.pone.0148108

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

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, 2156-2163. doi:10.1021/acs.analchem.5b03745

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.

 

2015

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., Kronke, G., Bluml, S., Schabbauer, G. (2015) Loss of Phosphatase and Tensin Homolog in APCs Impedes Th17-Mediated Autoimmune Encephalomyelitis. J. Immunol. 195, 2560-2570. doi: 10.4049/jimmunol.1402511

Loos, A., Gach, J.S., Hackl, T., Maresch, D., Henkel, T., Porodko, A., Bui-Minh, D., Sommeregger, W., Wozniak-Knopp, G., Forthal, D.N., Altmann, F., Steinkellner, H., Mach, L. (2015) Glycan modulation and sulfoengineering of anti-HIV-1 monoclonal antibody PG9 in plants. Proc. Natl. Acad. Sci. U. S. A. 112, 12675-12680. doi: 10.1073/pnas.1509090112

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. 407, 2865-2875. doi: 10.1007/s00216-015-8521-9

Friedrich, V., Gruber, C., Nimeth, I., Pabinger, S., Sekot, G., Posch, G., Altmann, F., Messner, P., Andrukhov, O., Schäffer, C. (2015) Outer membrane vesicles of Tannerella forsythia: biogenesis, composition, and virulence. Mol. Oral Microbiol. 30, 451-473. doi: 10.1111/omi.12104

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. The Analyst 140, 7687-7695. doi: 10.1039/c5an01629k

Graf, M.M.H., Sucharitakul, J., Bren, U., Chu, D.B., Koellensperger, G., Hann, S., Furtmüller, 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 J. 282, 4218-4241. doi: 10.1111/febs.13417

Megson, Z.A., Pittenauer, E., Duda, K.A., Engel, R., Ortmayr, K., Koellensperger, G., Mach, L., Allmaier, G., Holst, O., Messner, P., Schäffer, C. (2015) Inositol-phosphodihydroceramides in the periodontal pathogen Tannerella forsythia: Structural analysis and incorporation of exogenous myo-inositol. Biochim. Biophys. Acta 1851, 1417-1427. doi: 10.1016/j.bbalip.2015.08.004

Chromikova, V., Mader, A., Hofbauer, S., Göbl, C., Madl, T., Gach, J.S., Bauernfried, S., Furtmüller, 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 1854, 1536-1544. doi: 10.1016/ j.bbapap.2015.02.018

Harreither, E., Hackl, M., Pichler, J., Shridhar, S., Auer, N., Łabaj, 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. Biotechnol. J. 10, 1625-1638. doi: 10.1002/biot.201400857

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. 120, 38-46. doi: 10.1016/j.molcatb.2015.06.011

Gasselhuber, B., Carpena, X., Graf, M.M.H., Pirker, K.F., Nicolussi, A., Sündermann, A., Hofbauer, S., Zamocky, M., Furtmüller, 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 54, 5425-5438. doi: 10.1021/acs.biochem.5b00831

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 Res. 43, e102. doi: 10.1093/nar/gkv475. *equally contributing first authors

Kracher, D., Zahma, K., Schulz, C., Sygmund, C., Gorton, L., Ludwig, R. (2015) Inter-domain electron transfer in cellobiose dehydrogenase: modulation by pH and divalent cations. FEBS J. 282, 3136-3148. doi: 10.1111/febs.13310

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. doi: 10.1016/j.jprot.2015.05.030

Soukup, K., Halfmann, A., Le Bras, M., Sahin, E., Vittori, S., Poyer, F., Schuh, C., Luger, R., Niederreiter, B., Haider, T., Stoiber, D., Blüml, 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, 541-552. doi: 10.4049/jimmunol.1401663

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. 112, 1488-1493. doi: 10.1002/bit.25539

Tan, T.-C.*, Kracher, D.*, Gandini, R., Sygmund, C., Kittl, R., Haltrich, D., Hällberg, B.M., Ludwig, R., Divne, C. (2015) Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation. Nat. Commun. 6, 7542. doi: 10.1038/ncomms8542. *equally contributing first authors

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

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. 96, 1053-1068. doi: 10.1111/mmi.12989

Schaffner, I., Hofbauer, S., Krutzler, M., Pirker, K.F., Furtmüller, P.G., Obinger, C. (2015) Mechanism of chlorite degradation to chloride and dioxygen by the enzyme chlorite dismutase. Arch. Biochem. Biophys. 574, 18-26. doi: 10.1016/j.abb.2015.02.031

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. The Analyst 140, 3465-3473. doi: 10.1039/c5an00206k

Zámocký, M., Hofbauer, S., Schaffner, I., Gasselhuber, B., Nicolussi, A., Soudi, M., Pirker, K.F., Furtmüller, P.G., Obinger, C. (2015) Independent evolution of four heme peroxidase superfamilies. Arch. Biochem. Biophys. 574, 108-119. doi: 10.1016/j.abb.2014.12.025

Hofbauer, S., Hagmüller, A., Schaffner, I., Mlynek, G., Krutzler, M., Stadlmayr, G., Pirker, K.F., Obinger, C., Daims, H., Djinović-Carugo, K., Furtmüller, P.G. (2015) Structure and heme-binding properties of HemQ (chlorite dismutase-like protein) from Listeria monocytogenes. Arch. Biochem. Biophys. 574, 36-48. doi: 10.1016/j.abb.2015.01.010

Yakovleva, M.E., Gonaus, C., Schropp, K., Ó 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, 9074-9081. doi: 10.1039/c5cp00430f

Soukup, K. and Wang, X. (2015) Radiation meets immunotherapy - a perfect match in the era of combination therapy? Int. J. Radiat. Biol. 91, 299-305. doi: 10.3109/09553002.2014.995383

Soudi, M., Paumann-Page, M., Delporte, C., Pirker, K.F., Bellei, M., Edenhofer, E., Stadlmayr, G., Battistuzzi, G., Boudjeltia, K.Z., Furtmüller, P.G., Van Antwerpen, P., Obinger, C. (2015) Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase. J. Biol. Chem. 290, 10876-10890. doi: 10.1074/jbc.m114.632273

Nguyen, T.-T., Nguyen, H.-M., Geiger, B., Mathiesen, G., Eijsink, V.G.H., 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, 30. doi: 10.1186/s12934-015-0214-8

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., Schäffer, C. (2015) UDP-sulfoquinovose formation by Sulfolobus acidocaldarius. Extremophiles 19, 451-467. doi: 10.1007/s00792-015-0730-9

Chromikova, V., Mader, A., Steinfellner, W., Kunert, R. (2015) Evaluating the bottlenecks of recombinant IgM production in mammalian cells. Cytotechnology 67, 343-356. doi: 10.1007/s10616-014-9693-4

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., Weinhäusel, A., Mohr, T., Steiger, M., Mattanovich, D., Rinnerthaler, M., Karl, T., Sharma, S., Entian, K.-D., Kos, M., Breitenbach, M., Wilson, I.B.H., 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. 6, 6158. doi: 10.1038/ncomms7158

Megson, Z.A., Koerdt, A., Schuster, H., Ludwig, R., Janesch, B., Frey, A., Naylor, K., Wilson, I.B.H., Stafford, G.P., Messner, P., Schäffer, C. (2015) Characterization of an α-l-fucosidase from the periodontal pathogen Tannerella forsythia. Virulence 6, 282-292. doi: 10.1080/21505594.2015.1010982

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 10, e0140476. doi: 10.1371/journal.pone.0140476

 

2014

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,  e1003995. doi: 10.1371/journal.pcbi.1003995

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. doi: 10.1007/s10719-013-9505-7

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. doi: 10.1007/s00253-013-5192-3

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. doi: 10.1074/jbc.M113.530196

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. doi: 10.1007/s00253-014-5584-z

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. doi: 10.1007/s10529-013-1429-6

Nagy, G. and Oostenbrink, C. (2014) Dihedral-based segment identification and classification of biopolymers II: polynucleotides. J. Chem. Inf. Model. 54, 278-288. doi: 10.1021/ci400542n

Nagy, G. and Oostenbrink, C. (2014) Dihedral-based segment identification and classification of biopolymers I: proteins. J. Chem. Inf. Model. 54, 266-277. doi: 10.1021/ci400541d

Tomek, M.B., Neumann, L., Nimeth, I., Koerdt, A., Andesner, P., Messner, P., Mach, L., Potempa, J.S., Schäffer, C. (2014) The S-layer proteins of Tannerella forsythia are secreted via a type IX secretion system that is decoupled from protein O-glycosylation. Mol. Oral Microbiol. 29, 307-320. doi: 10.1111/omi.12062

Tanne, J., Kracher, D., Dietzel, B., 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. doi: 10.3390/bios4040370

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. 98, 9723-9733. doi: 10.1007/s00253-014-6011-1

Eibinger, M., Ganner, T., Bubner, P., Rošker, 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. 289, 35929-35938. doi: 10.1074/jbc.m114.602227

Zámocký, M., Gasselhuber, B., Furtmüller, P.G., Obinger, C. (2014) Turning points in the evolution of peroxidase-catalase superfamily: molecular phylogeny of hybrid heme peroxidases. Cell. Mol. Life Sci. 71, 4681-4696. doi: 10.1007/s00018-014-1643-y

Auer, M., Nicolussi, A., Schütz, G., Furtmüller, 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. 289, 31480-31491. doi: 10.1074/jbc.m114.595157

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. 190, 76-84. doi: 10.1016/j.jbiotec.2013.12.018

Hasenhindl, C., Lai, B., Delgado, J., Traxlmayr, M.W., Stadlmayr, G., Rüker, 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 1844, 1530-1540. doi: 10.1016/j.bbapap.2014.04.020

Krondorfer, I., Brugger, D., Paukner, R., Scheiblbrandner, S., Pirker, K.F., Hofbauer, S., Furtmüller, P.G., Obinger, C., Haltrich, D., Peterbauer, C.K. (2014) Agaricus meleagris pyranose dehydrogenase: influence of covalent FAD linkage on catalysis and stability. Arch. Biochem. Biophys. 558, 111-119. doi: 10.1016/j.abb.2014.07.008

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. 98, 7535-7548. doi: 10.1007/s00253-014-5911-4

Németh, E., Schilli, G.K., Nagy, G., Hasenhindl, C., Gyurcsik, B., Oostenbrink, C. (2014) Design of a colicin E7 based chimeric zinc-finger nuclease. J. Comput. Aided Mol. Des. 28, 841-850. doi: 10.1007/s10822-014-9765-8

Traxlmayr, M.W., Lobner, E., Hasenhindl, C., Stadlmayr, G., Oostenbrink, C., Rüker, F., Obinger, C. (2014) Construction of pH-sensitive Her2-binding IgG1-Fc by directed evolution. Biotechnol. J. 9, 1013-1022. doi: 10.1002/biot.201300483

Anzengruber, J., Courtin, P., Claes, I.J.J., Debreczeny, M., Hofbauer, S., Obinger, C., Chapot-Chartier, M.-P., Vanderleyden, J., Messner, P., Schäffer, C. (2014) Biochemical characterization of the major N-acetylmuramidase from Lactobacillus buchneri. Microbiology 160, 1807-1819. doi: 10.1099/mic.0.078162-0

Ortmayr, K., Nocon, J., Gasser, B., Mattanovich, D., Hann, S., Koellensperger, G. (2014) Sample preparation workflow for the liquid chromatography tandem mass spectrometry based analysis of nicotinamide adenine dinucleotide phosphate cofactors in yeast. J. Sep. Sci. 37, 2185-2191. doi: 10.1002/jssc.201400290

Nocon, J., Steiger, M.G., Pfeffer, M., Sohn, S.B., Kim, T.Y., Maurer, M., Rußmayer, H., Pflügl, 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. 24, 129-138. doi: 10.1016/j.ymben.2014.05.011

Satzer, P., Wellhoefer, M., Jungbauer, A. (2014) Continuous separation of protein loaded nanoparticles by simulated moving bed chromatography. J. Chromatogr. A 1349, 44-49. doi: 10.1016/j.chroma.2014.04.093

Sündermann, A., Reif, M.M., Hofbauer, S., Obinger, C., Oostenbrink, C. (2014) Investigation of ion binding in chlorite dismutases by means of molecular dynamics simulations. Biochemistry 53, 4869-4879. doi: 10.1021/bi500467h

Hernández 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. 182-183, 97-103. doi: 10.1016/j.jbiotec.2014.04.014

Jakopitsch, C., Pirker, K.F., Flemmig, J., Hofbauer, S., Schlorke, D., Furtmüller, P.G., Arnhold, J., Obinger, C. (2014) Mechanism of reaction of chlorite with mammalian heme peroxidases. J. Inorg. Biochem. 135, 10-19. doi: 10.1016/j.jinorgbio.2014.02.010

Mlynek, G., Lehner, A., Neuhold, J., Leeb, S., Kostan, J., Charnagalov, A., Stolt-Bergner, P., Djinović-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 46, 1565-1582. doi: 10.1007/s00726-014-1699-x

Hofbauer, S., Gruber, C., Pirker, K.F., Sündermann, A., Schaffner, I., Jakopitsch, C., Oostenbrink, C., Furtmüller, P.G., Obinger, C. (2014) Transiently produced hypochlorite is responsible for the irreversible inhibition of chlorite dismutase. Biochemistry 53, 3145-3157. doi: 10.1021/bi500401k

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. 175, 38-44. doi: 10.1016/j.jbiotec.2014.01.032

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. doi: 10.1002/biot.201300334

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. doi: 10.1002/biot.201300214

Schneider, J.D., Castilho, A., Neumann, L., Altmann, F., Loos, A., Kannan, L., Mor, T.S., Steinkellner, H. (2014) Expression of human butyrylcholinesterase with an engineered glycosylation profile resembling the plasma-derived orthologue. Biotechnol. J. 9, 501-510. doi: 10.1002/biot.201300229

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. doi: 10.1002/biot.201300305

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. doi: 10.1002/biot.201300207

Hofbauer, S., Schaffner, I., Furtmüller, 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. doi: 10.1002/biot.201300210

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. doi: 10.1002/biot.201300216

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. doi: 10.1002/biot.201300336

Killyéni, A., Yakovleva, M.E., MacAodha, D., Conghaile, P.Ó., 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. doi: 10.1016/j.electacta.2013.08.069

Anzengruber, J., Pabst, M., Neumann, L., Sekot, G., Heinl, S., Grabherr, R., Altmann, F., Messner, P., Schäffer, C. (2014) Protein O-glucosylation in Lactobacillus buchneri. Glycoconj. J. 31, 117-131. doi: 10.1007/s10719-013-9505-7

Hofbauer, S., Gysel, K., Bellei, M., Hagmüller, A., Schaffner, I., Mlynek, G., Kostan, J., Pirker, K.F., Daims, H., Furtmüller, P.G., Battistuzzi, G., Djinović-Carugo, K., Obinger, C. (2014) Manipulating conserved heme cavity residues of chlorite dismutase: effect on structure, redox chemistry, and reactivity. Biochemistry 53, 77-89. doi: 10.1021/bi401042z

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. doi: 10.1021/ci4006657

Klausberger, M., Wilde, M., Palmberger, D., Hai, R., Albrecht, R.A., Margine, I., Hirsh, A., García-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. doi: 10.1016/j.vaccine.2013.11.036

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. doi: 10.3390/ijms15010438

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. 2, 67. doi: 10.3389/fbioe.2014.00067

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, e109242. doi: 10.1371/journal.pone.0109242

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. doi: 10.1371/journal.pone.0091145

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., Nordén, B., Grillari, J., Grillari, J. (2014) Characterization of a novel cell penetrating peptide derived from human Oct4. Cell. Regen. (Lond.) 3, 2. doi: 10.1186/2045-9769-3-2

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. doi: 10.1371/journal.pone.0085371

 

2013

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. doi: 10.1002/cyto.a.22331

Jung, G., Pabst, M., Neumann, L., Berger, A., Lubec, G. (2013) Characterization of alpha-l-Iduronidase (Aldurazyme(R)) and its complexes. J. Proteomics 80, 26-33. doi: 10.1016/j.jprot.2012.09.022

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. doi:

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. doi: 10.3109/13697137.2012.725788

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. doi: 10.2217/fmb.12.133

Kurz, S., Jin, C., Hykollari, A., Gregorich, D., Giomarelli, B., Vasta, G.R., Wilson, I.B., Paschinger, K. (2013) Hemocytes and plasma of the eastern oyster (Crassostrea virginica) display a diverse repertoire of sulfated and blood group A-modified N-glycans. J. Biol. Chem. 288, 24410-24428. doi: 10.1074/jbc.M113.478933

Sygmund, C., Santner, P., Krondorfer, I., Peterbauer, C.K., Alcalde, M., Nyanhongo, G.S., Guebitz, G.M., Ludwig, R. (2013) Semi-rational engineering of cellobiose dehydrogenase for improved hydrogen peroxide production. Microb. Cell Fact. 12, 38. doi: 10.1186/1475-2859-12-38

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. doi: 10.1016/j.carres.2013.09.004

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. doi: 10.1016/j.biotechadv.2013.07.007

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

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. BMC Proc. 7, P25. doi: 10.1186/1753-6561-7-S6-P25

Paumann-Page, M., Furtmüller, 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. doi: 10.1016/j.abb.2013.09.004

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. doi: 10.1007/s10616-013-9606-y

Yakovleva, M.E., Killyéni, A., Seubert, O., O Conghaile, P., Macaodha, D., Leech, D., Gonaus, C., Popescu, I.C., Peterbauer, C.K., Kjellström, 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. doi: 10.1021/ac4023988

Hasenhindl, C., Traxlmayr, M.W., Wozniak-Knopp, G., Jones, P.C., Stadlmayr, G., Rüker, 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. Protein Eng. Des. Sel. 26, 675-682. doi: 10.1093/protein/gzt041

Auer, M., Gruber, C., Bellei, M., Pirker, K.F., Zamocky, M., Kroiss, D., Teufer, S.A., Hofbauer, S., Soudi, M., Battistuzzi, G., Furtmüller, P.G., Obinger, C. (2013) A stable bacterial peroxidase with novel halogenating activity and an autocatalytically linked heme prosthetic group. J. Biol. Chem. 288, 27181-27199. doi: 10.1074/jbc.m113.477067

Zou, C., Larisika, 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 117, 9606-9614. doi: 10.1021/jp404573q

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. doi: 10.3390/biom3030535

Gerster, P., Kopecky, E.-M., Hammerschmidt, N., Klausberger, M., Krammer, F., Grabherr, R., Mersich, C., Urbas, L., Kramberger, P., Paril, T., Schreiner, M., Nöbauer, K., Razzazi-Fazeli, E., Jungbauer, A. (2013) Purification of infective baculoviruses by monoliths. J. Chromatogr. A 1290, 36-45. doi: 10.1016/j.chroma.2013.03.047

Posch, G., Pabst, M., Neumann, L., Coyne, M.J., Altmann, F., Messner, P., Comstock, L.E., Schäffer, C. (2013) "Cross-glycosylation" of proteins in Bacteroidales species. Glycobiology 23, 568-577. doi: 10.1093/glycob/cws172

Traxlmayr, M.W., Lobner, E., Antes, B., Kainer, M., Wiederkum, S., Hasenhindl, C., Stadlmayr, G., Rüker, F., Woisetschläger, M., Moulder, K., Obinger, C. (2013) Directed evolution of Her2/neu-binding IgG1-Fc for improved stability and resistance to aggregation by using yeast surface display. Protein Eng. Des. Sel. 26, 255-265. doi: 10.1093/protein/gzs102

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. doi: 10.1007/s10822-013-9645-7

Palmberger, D., Klausberger, M., Berger, I., Grabherr, R. (2013) MultiBac turns sweet. Bioengineered 4, 78-83. doi: 10.4161/bioe.22327

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. doi: 10.1371/journal.pone.0054836

Tan, T.C., Spadiut, O., Wongnate, T., Sucharitakul, J., Krondorfer, I., Sygmund, C., Haltrich, D., Chaiyen, P., Peterbauer, C.K., 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. doi: 10.1371/journal.pone.0053567

Hofbauer, A. and Stoger, E. (2013) Subcellular accumulation and modification of pharmaceutical proteins in different plant tissues. Curr. Pharm. Des. 19, 5495-5502. doi: 10.2174/1381612811319310005

Melnik, S. and Stoger, E. (2013) Green factories for biopharmaceuticals. Curr. Med. Chem. 20, 1038-1046. doi: 10.2174/0929867311320080007

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. J. Anal. At. Spectrom. 28, 637-645. doi: 10.1039/C3JA30370E

 

2012

Posch, G., Sekot, G., Friedrich, V., Megson, Z.A., Koerdt, A., Messner, P., Schaffer, C. (2012) Glycobiology Aspects of the Periodontal Pathogen Tannerella forsythia. Biomolecules 2, 467-482. doi: 10.3390/biom2040467

Kittl, R., Gonaus, C., Pillei, C., Haltrich, D., Ludwig, R. (2012) Constitutive expression of Botrytis aclada laccase in Pichia pastoris. Bioengineered 3, 232-235. doi: 10.4161/bioe.20037

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. doi: 10.1016/j.jbiotec.2011.11.021

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. Eur. J. Obstet. Gynecol. Reprod. Biol. 160, 93-99. doi: 10.1016/j.ejogrb.2011.10.002

Ristl, R., Janesch, B., Anzengruber, J., Forsthuber, A., Blaha, J., Messner, P., Schaffer, C. (2012) Description of a Putative Oligosaccharyl:S-Layer Protein Transferase from the Tyrosine O-Glycosylation System of Paenibacillus alvei CCM 2051(T). Adv. Microbiol. 2, 537-546. doi: 10.4236/aim.2012.24069

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. doi: 10.1016/j.phytochem.2012.08.023

Nagy, G. and Oostenbrink, C. (2012) Rationalization of stereospecific binding of propranolol to cytochrome P450 2D6 by free energy calculations. Eur. Biophys. J. 41, 1065-1076. doi: 10.1007/s00249-012-0865-x

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

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. doi: 10.1039/c2mt20138k

Hofbauer, S., Bellei, M., Sündermann, A., Pirker, K.F., Hagmüller, A., Mlynek, G., Kostan, J., Daims, H., Furtmüller, P.G., Djinović-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. doi: 10.1021/bi3013033

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. doi: 10.1074/jbc.m112.402685

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. doi: 10.1186/1754-6834-5-79

Traxlmayr, M.W., Hasenhindl, C., Hackl, M., Stadlmayr, G., Rybka, J.D., Borth, N., Grillari, J., Rüker, 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. doi: 10.1016/j.jmb.2012.07.017

Yakovleva, M.E., Killyéni, A., Ortiz, R., Schulz, C., MacAodha, D., Conghaile, P.Ó., 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. doi: 10.1016/j.elecom.2012.08.029

Sygmund, C.*, Kracher, D.*, Scheiblbrandner, S., Zahma, K., Felice, A.K.G., 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. doi: 10.1128/aem.01503-12. *equally contributing first authors

Ristl, R., Kainz, B., Stadlmayr, G., Schuster, H., Pum, D., Messner, P., Obinger, C., Schaffer, C. (2012) A fusion tag to fold on: the S-layer protein SgsE confers improved folding kinetics to translationally fused enhanced green fluorescent protein. J. Microbiol. Biotechnol. 22, 1271-1278. doi:

Hofbauer, S., Gysel, K., Mlynek, G., Kostan, J., Hagmüller, A., Daims, H., Furtmüller, P.G., Djinović-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. doi: 10.1016/j.bbapap.2012.05.012

Soudi, M., Zamocky, M., Jakopitsch, C., Furtmüller, P.G., Obinger, C. (2012) Molecular evolution, structure, and function of peroxidasins. Chem. Biodivers. 9, 1776-1793. doi: 10.1002/cbdv.201100438

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

Zámocký, M., Gasselhuber, B., Furtmüller, P.G., Obinger, C. (2012) Molecular evolution of hydrogen peroxide degrading enzymes. Arch. Biochem. Biophys. 525, 131-144. doi: 10.1016/j.abb.2012.01.017

Zámocký, M., García-Fernández, Q., Gasselhuber, B., Jakopitsch, C., Furtmüller, P.G., Loewen, P.C., Fita, I., Obinger, C., Carpena, X. (2012) High conformational stability of secreted eukaryotic catalase-peroxidases: answers from first crystal structure and unfolding studies. J. Biol. Chem. 287, 32254-32262. doi: 10.1074/jbc.m112.384271

Lai, B. and Oostenbrink, C. (2012) Binding free energy, energy and entropy calculations using simple model systems. Theor. Chem. Acc. 131, 1272. doi: 10.1007/s00214-012-1272-1

Swoboda, M., Henig, J., Cheng, H.-M., Brugger, D., Haltrich, D., Plumeré, N., Schlierf, M. (2012) Enzymatic oxygen scavenging for photostability without pH drop in single-molecule experiments. ACS Nano 6, 6364-6369. doi: 10.1021/nn301895c

Jadhav, V., Hackl, M., Bort, J.A.H., 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. doi: 10.1002/bit.24490

Delic, M., Rebnegger, C., Wanka, F., Puxbaum, V., Haberhauer-Troyer, C., Hann, S., Köllensperger, 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. doi: 10.1016/j.freeradbiomed.2012.02.048

Sygmund, C., Gutmann, A., Krondorfer, I., Kujawa, M., Glieder, A., Pscheidt, B., Haltrich, D., Peterbauer, C., Kittl, R. (2012) Simple and efficient expression of Agaricus meleagris pyranose dehydrogenase in Pichia pastoris. Appl. Microbiol. Biotechnol. 94, 695-704. doi: 10.1007/s00253-011-3667-7

Traxlmayr, M.W., Faissner, M., Stadlmayr, G., Hasenhindl, C., Antes, B., Rüker, F., Obinger, C. (2012) Directed evolution of stabilized IgG1-Fc scaffolds by application of strong heat shock to libraries displayed on yeast. Biochim. Biophys. Acta 1824, 542-549. doi: 10.1016/j.bbapap.2012.01.006

Hackl, M., Jadhav, V., Jakobi, T., Rupp, O., Brinkrolf, K., Goesmann, A., Pühler, 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. doi: 10.1016/j.jbiotec.2012.01.019

Hernández 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. doi: 10.1002/biot.201100143

Nguyen, T.-T., Nguyen, H.A., Arreola, S.L., Mlynek, G., Djinović-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. doi: 10.1021/jf203909e

Gu, C., Shabab, M., Strasser, R., Wolters, P.J., Shindo, T., Niemer, M., Kaschani, F., Mach, L., van der Hoorn, R.A.L. (2012) Post-translational regulation and trafficking of the granulin-containing protease RD21 of Arabidopsis thaliana. PLoS One 7, e32422. doi: 10.1371/journal.pone.0032422

Rampler, E., Dalik, T., Stingeder, G., Hann, S., Koellensperger, G. (2012) Sulfur containing amino acids - challenge of accurate quantification. J. Anal. At. Spectrom. 27, 1018-1023. doi: 10.1039/C2JA10377J

 

2011

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. doi: 10.1099/mic.0.051904-0

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

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. 10, 106. doi: 10.1186/1475-2859-10-106

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. doi: 10.1002/bit.23198

Battistuzzi, G., Stampler, J., Bellei, M., Vlasits, J., Soudi, M., Furtmüller, P.G., Obinger, C. (2011) Influence of the covalent heme-protein bonds on the redox thermodynamics of human myeloperoxidase. Biochemistry 50, 7987-7994. doi: 10.1021/bi2008432

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

 

2010

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. doi: 10.1371/journal.pone.0013265

Pontiller, J., Maccani, A., Baumann, M., Klancnik, I., Ernst, W. (2010) Identification of CHO endogenous gene regulatory elements. Mol. Biotechnol. 45, 235-240. doi: 10.1007/s12033-010-9278-1

Spadiut, O., Brugger, D., Coman, V., Haltrich, D., Gorton, L. (2010) Engineered Pyranose 2‐Oxidase: Efficiently Turning Sugars into Electrical Energy. Electroanal. 22, 813-820. doi: 10.1002/elan.200980015