Publications of BioToP PhD-Students

(Highlighted are BioToP students and BioToP faculty members)

2024

Cassiani A., Furtmüller P. G., Borsari M., Battistuzzi G., Hofbauer S. 2024. Insights into heme degradation and hydrogen peroxide induced dimerization of human neuroglobin. Biosci. Rep. doi: 10.1042/BSR20241265

Rebnegger C., Coltman B.L., Kowarz V., Peña D.A., Mentler A., Troyer C., Hann S., Schöny H., Koellensperger G., Mattanovich D., Gasser B. Microb Cell Fact. 23(1):43. doi: 10.1186/s12934-024-02314-3

Välimets S., Schwaiger L., Bennett A., Maresch D., Ludwig R., Hann S., Linde D., Ruiz-Dueñas F.J., Peterbauer C. (2024) Dye-Decolorizing Peroxidases Maintain High Stability and Turnover on Kraft Lignin and Lignocellulose Substrates. ACS Omega 9, 45025-45034. doi: 10.1021/acsomega.4c05043

Dobersberger M., Sumesgutner D., Zajc C.U., Traxlmayr M.W. (2024) Protocol for engineering binding domains to recognize ligand-bound receptors by using yeast surface display. STAR Protoc. 5(4), 103339. doi: 10.1016/j.xpro.2024.103339

Välimets S., Sun P., Virginia L.J., van Erven G., Sanders M.G., Kabel M.A., Peterbauer C. (2024) Characterization of Amycolatopsis 75iv2 dye-decolorizing peroxidase on O-glycosides. Appl. Environ. Microbiol. 90(5), e00205-24. doi: 10.1128/AEM.00205-24

Dali A., Gabler T., Sebastiani F., Furtmüller P. G., Becucci M., Hofbauer S., Smulevich G. 2024. Entrance channels to coproheme in coproporphyrin ferrochelatase probed by exogenous imidazole binding. J. Inorg. Biochem. 260, 112681, doi: 10.1016/j.jinorgbio.2024.112681

Bobbili M.R., Görgens A., Yan Y., Vogt S., Gupta D., Corso G., Barbaria S., Patrioli C., Weilner S., Pultar M., Jacak J., Hackl M., Schosserer M., Grillari R., Kjems J., Andaloussi S.E., Grillari J. (2024) Snorkel-tag based affinity chromatography for recombinant extracellular vesicle purification. J. Extracell. Vesicles 13(10), e12523. doi: 10.1002/jev2.12523

Zajc C.U., Sylvander E., Lehner M., Traxlmayr M.W. (2024) Small molecule-regulated switches to provide functional control of CAR T cells within the patient. Expert Opin Biol Ther. 24(6), 425-432. doi: 10.1080/14712598.2024.2371034

Baumschabl M., Mitic B.M., Troyer C., Hann S., Ata Ö., Mattanovich D. (2024) A native phosphoglycolate salvage pathway of the synthetic autotrophic yeast Komagataella phaffii. microLife. 5, uqad046. doi: 10.1093/femsml/uqad046

Kuvek T., Marcher C., Berteotti A., Lopez Carrillo V., Schleifer K.-J., Oostenbrink C. (2024) A Computational Pipeline Observes the Flexibility and Dynamics of Plant Cytochrome P450 Binding Sites. Int. J. Mol. Sci. 25, 11381. doi: 10.3390/ijms252111381

Martschini A., Kostelac A., Haltrich D., Peterbauer C.K. (2024) Characterization of a Pyranose Oxidase/C-Glycoside Oxidase from Microbacterium sp. 3H14, Belonging to the Unexplored Clade II of Actinobacterial POx/CGOx. Biomolecules. 14, 1510. doi: 10.3390/biom14121510

Ruocco V., Grünwald-Gruber C., Rad B., Tscheliessnig R., Hammel M., Strasser R. (2024) Effects of N-glycans on the structure of human IgA2. Front. Mol. Biosci. 11, 1390659. doi: 10.3389/fmolb.2024.1390659

Uetz P., Göritzer K., Vergara E., Melnik S., Grünwald-Gruber C., Figl R., Deghmane A.-E., Groppelli E., Reljic R., Ma J.K.-C., Stöger E., Strasser R. (2024) Implications of O-glycan modifications in the hinge region of a plant produced SARS-CoV-2-IgA antibody on functionality. Front. Bioeng. Biotechnol. 12, 1329018. doi: 10.3389/fbioe.2024.1329018

Dutkiewicz Z., Varrot A., Breese K.J., Stubbs K.A., Nuschy L., Adduci I., Paschinger K., Wilson I.B.H. (2024) Bioinformatic, enzymatic, and structural characterization of Trichuris suis hexosaminidase HEX-2. Biochemistry. 63(15), 1941-1954. doi: 10.1021/acs.biochem.4c00187

Guzman Ruiz L., Zollner A.M., Hoxie I., Jungbauer A., Grabherr R. (2024) Increased efficacy of influenza virus vaccine candidate through display of recombinant neuraminidase on virus like particles. Front. Immunol. 15, 1425842. doi: 10.3389/fimmu.2024.1425842

Walcher S., Hager-Mair F.F., Stadlmann J., Kählig H., Schäffer C. (2024) Deciphering fucosylated protein-linked O-glycans in oral Tannerella serpentiformis: Insights from NMR spectroscopy and glycoproteomics. Glycobiology, in press. doi: 10.1093/glycob/cwae072

Stefanović C., Legg M.S.G., Ender J., Oostenbrink C., Schäffer C., Evans S.V., Hager-Mair F.F. (2024) Insights into structure and activity of a UDP-GlcNAc 2-epimerase involved in secondary cell wall polymer biosynthesis in Paenibacillus alvei. Front. Mol. Biosci. 11, 1470989. doi: 10.3389/fmolb.2024.147098

Dali A., Sebastiani F., Gabler T., Frattini G., Moreno D. M., Estrin D. A., Becucci M., Hofbauer S., Smulevich G. 2024. Proximal ligand tunes active site structure and reactivity in bacterial L. monocytogenes coproheme ferrochelatase. Spectrochimica Acta Part A. 313, 124120, doi: 10.1016/j.saa.2024.124120

Tsvik L., Zhang S., O'Hare D., Haltrich D., Sützl L. (2024) More Than One Enzyme: Exploring Alternative FMN-Dependent L-Lactate Oxidases for Biosensor Development. ACS Omega. 9, 29442-29452. doi: 10.1021/acsomega.4c01897

Sulaj E., Schwaigerlehner L., Sandell F.L., Dohm J.C., Marzban G., Kunert R. (2024) Quantitative proteomics reveals cellular responses to individual mAb expression and tunicamycin in CHO cells. Applied Microbiology and Biotechnology. 108, 381. doi:10.1007/s00253-024-13223-1

Bloch S., Hager-Mair F.F., Bacher J., Tomek M.B., Janesch B., Andrukhov O., Schäffer C. (2024) Investigating the role of a Tannerella forsythia HtrA protease in host protein degradation and inflammatory response. Front. Oral Health. 5, 1425937. doi: 10.3389/froh.2024.1425937

Gabler T., Dali A., Bellei M., Sebastiani F., Becucci M., Battistuzzi G., Furtmüller P. G., Smulevich G., Hofbauer S. 2024. Revisiting catalytic His and Glu residues in coproporphyrin ferrochelatase – unexpected activities of active site variants. FEBS J. 291, 2260-2272, doi: 10.1111/febs.17101

Furlanetto V., Kalyani D.C., Kostelac A., Puc J., Haltrich D., Hällberg B.M., Divne C. (2024) Structural and Functional Characterization of a Gene Cluster Responsible for Deglycosylation of C-glucosyl Flavonoids and Xanthonoids by Deinococcus aerius. Journal of Molecular Biology. 436, 168547. doi:10.1016/j.jmb.2024.168547

Dobersberger M., Sumesgutner D., Zajc C.U., Salzer B., Laurent E., Emminger D., Sylvander E., Lehner E., Teufl M., Seigner J., Bobbili M.R., Kunert R., Lehner M., Traxlmayr M.W. (2024) An engineering strategy to target activated EGFR with CAR T cells. Cell Reports Methods. 100728. doi: 10.1016/j.crmeth.2024.100728

Hermann E., Rodrigues C.F.,Martins L.O., Peterbauer C.,Oostenbrink C. (2024) Engineering A-type Dye-decolorizing Peroxidases by Modification of a Conserved Glutamate Residue. ChemBioChem. e202300872. doi: 10.1002/cbic.202300872

Eckmair B., Gao C., Mehta A.Y., Dutkiewicz Z., Vanbeselaere J., Cummings R.D., Paschinger K., Wilson I.B.H. (2024) Recognition of highly branched N-glycans of the porcine whipworm by the immune system. Mol. Cell. Proteomics. 23(2), 100711. doi: 10.1016/j.mcpro.2024.100711

2023

Stefanović C., Hager-Mair F.F., Breslmayr E., López Guzmán A., Lim C., Blaukopf M., Kosma P., Oostenbrink C., Ludwig R., Schäffer C. (2023) Molecular modelling and site-directed mutagenesis provide insight into saccharide pyruvylation by the Paenibacillus alvei CsaB enzyme. Sci. Rep. 13, 13394. doi: 10.1038/s41598-023-40072-1

Gracia Carmona O., Lahham M., Poliak P., Goj D., Frießer E., Wallner S., Macheroux P., Oostenbrink C. (2023) Understanding the riddle of amine oxidase flavoenzyme reactivity on the stereoisomers of N-methyl-dopa and N-methyl-tyrosine. J. Mol. Recogn. e3068. doi: 10.1002/jmr.3068

Gracia Carmona O., Oostenbrink C. (2023) Flexible Gaussian accelerated molecular dynamics to enhance biological sampling. J. Chem. Theory Comput. 19, 6521 – 6531. doi: 10.1021/acs.jctc.3c00619

Kostelac A., Taborda A., Martins L.O., Haltrich D. (2023) Evolution and separation of actinobacterial pyranose and C-glycoside-3-oxidases. Appl Environ Microbiol. Jan 5:e0167623. doi: 10.1128/aem.01676-23

Seigner J., Zajc C.U., Dötsch S., Eigner C., Laurent, E. Busch D.H., Lehner M., Traxlmayr M.W. (2023) Solving the mystery of the FMC63-CD19 affinity. Scientific Reports. 13, 23024. doi: 10.1038/s41598-023-48528-0

Mitic B.M., Troyer C., Lutz L., Baumschabl M., Hann S., Mattanovich D. (2023) The oxygen-tolerant reductive glycine pathway assimilates methanol, formate and CO₂ in the yeast Komagataella phaffii. Nature Communications. 14, 7754. doi: 10.1038/s41467-023-43610-7

Pfanzagl V., Grünwald-Gruber C., Leitgeb U., Furtmüller P.G., Obinger C. (2023) Posttranslational modification and heme cavity architecture of human eosinophil peroxidase—insights from first crystal structure and biochemical characterization. Journal of Biological Chemistry. 299, 105402. doi: 10.1016/j.jbc.2023.105402

Motycka M., Csarman F., Rupp M., Nagy G., Karnpakdee K. Scheiblbrandner S., Tscheliessnig R., Oostenbrink C. , Hammel M., Ludwig R. (2023) Amino Acid Residues Controlling Domain Interaction and Interdomain Electron Transfer in Cellobiose Dehydrogenase. ChemBioChem. 24, e20230043. doi: 10.1002/cbic.202300431

Rodak A., Stadlbauer K., Bobbili M.R., Smrzka O., Rüker F., Wozniak-Knopp G. (2023) Development of a Cytotoxic Antibody-Drug Conjugate Targeting Membrane Immunoglobulin E-Positive Cells. Int. J. Mol. Sci. 24, 14997. doi: 10.3390/ijms24191499

Wijayanti S.D., Tsvik, L., Haltrich, D. (2023) Recent Advances in Electrochemical Enzyme-Based Biosensors for Food and Beverage Analysis. Foods. 12, 3355. doi: 10.3390/foods12183355

Gracia Carmona O., Gillhofer M., Tomasiak L., de Ruiter A., Oostenbrink C. (2023) Accelerated enveloping distribution sampling to probe the presence of water molecules. J. Chem. Theory Comput. 19, 3379-3390. doi: 10.1021/acs.jctc.3c00109

Beihammer G. , König-Beihammer J., Kogelmann B., Ruocco V. , Grünwald-Gruber C., D’Aoust M.-A., Lavoie P.-O., Saxena P., Gach J.S., Steinkellner H., Strasser R. (2023) An oligosaccharyltransferase from Leishmania donovani increases the N-glycan occupancy on plant-produced IgG1. Front. Plant Sci. 14, 1233666. doi: 10.3389/fpls.2023.1233666

Falb, N., Patil, G. , Furtmüller, P. G., Gabler, T., Hofbauer, S. (2023) Structural aspects of enzymes involved in prokaryotic heme biosynthesis. Comp. Struct. Biotechnol. J., doi: 10.1016/j.csbj.2023.07.024

Patil, G., Michlits, H. , Furtmüller, P. G., Hofbauer, S. (2023) Reactivity of coproheme decarboxylase with monovinyl, monopropionate deuteroheme. Biomolecules. 13, 946. doi: 10.3390/biom13060946

Hausjell, C.S., Klausberger, M., Ernst, W., Grabherr, R. (2023) Evaluation of an inducible knockout system in insect cells based on co-infection and CRISPR/Cas9. PLOS ONE 18, e0289178. doi: 10.1371/journal.pone.0289178

Nagode A., Vanbeselaere J., Dutkiewicz Z., Kaltenbrunner S., Wilson I.B.H., Duchêne M. (2023) Molecular characterization of Entamoeba histolytica UDP-glucose 4-epimerase, an enzyme able to provide building blocks for cyst wall formation. PLoS Negl. Trop. Dis. 17(8), e0011574. doi: 10.1371/journal.pntd.0011574

Billerhart, M., Hunjadi, M., Hawlin, V., Grünwald-Gruber, C., Maresch, D., Mayrhofer, P., Kunert, P. (2023) Recombinant Human CD19 in CHO-K1 Cells: Glycosylation Patterns as a Quality Attribute of High Yield Processes. Int. J. Mol. Sci. 24, 10891. doi: 10.3390/ijms241310891

Beihammer G. , Romero-Pérez A., Maresch D., Figl R., Mócsai R., Grünwald-Gruber C., Altmann F. , Van Damme E.J.M., Strasser R. (2023) Pseudomonas syringae DC3000 infection increases glucosylated N-glycans in Arabidopsis thaliana. Glycoconj. J. 40, 97-108. doi: 10.1007/s10719-022-10084-6

Sebastiani, F., Dali, A., Alonso de Armiño, J.A., Campagni, L., Patil, G. , Becucci, M., Hofbauer, S. , Estrin, D., Smulevich, G. (2023) The role of the distal cavity in carbon monoxide stabilization in the coproheme decarboxylase from C. diphtheriae. J. Inorg. Biochem., 245, 112243. doi: 10.1016/j.jinorgbio.2023.112243

Schmidt, D., Falb, N. , Serra, I., Bellei, M., Pfanzagl, V., Hofbauer, S. , Van Doorslaer, S., Battistuzzi, G., Furtmüller, P.G., Obinger, C. (2023) Compound I formation and reactivity in dimeric chlorite dismutase – Impact of pH and the dynamics of the catalytic arginine. Biochemistry. 62, 835-850. doi:10.1021/acs.biochem.2c00696

Paschinger K., Wöls F., Yan S., Jin C., Vanbeselaere J., Dutkiewicz Z., Arcalis E., Malzl D., Wilson I.B.H. (2023) N-glycan antennal modifications are altered in Caenorhabditis elegans lacking the HEX-4 N-acetylgalactosamine-specific hexosaminidase. J. Biol. Chem. 299(4), 103053. doi: 10.1016/j.jbc.2023.103053

Wijayanti, S.D., Schachinger, F., Ludwig, R., Haltrich, D. (2023) Electrochemical and biosensing properties of an FAD-dependent glucose dehydrogenase from Trichoderma virens. Bioelectrochemistry 153, 108480. doi: 10.1016/j.bioelechem.2023.108480

Motycka, B., Csarman, F., Tscheliessnig, R., Hammel, M., Ludwig, R. (2023) Resolving domain positions of cellobiose dehydrogenase by small angle X-ray scattering. FEBS. doi: 0.1111/febs.16885

Zhang, S.L., Chen, Y.C., Riezk, A., Ming, D.M., Tsvik, L., Sützl, L., Holmes, A., O'Hare, D. (2022) Rapid Measurement of Lactate in the Exhaled Breath Condensate: Biosensor Optimization and In-Human Proof of Concept. ACS SENSORS 7 (12), 3809-3816. doi: 10.1021/acssensors.2c01739

Valimets, S., Pedetti, P., Virginia, L.J., Hoang, M.N., Sauer, M., Peterbauer, C. (2023) Secretory expression of recombinant small laccase genes in Gram-positive bacteria. MICROB CELL FACT 22, 72. doi: 10.1186/s12934-023-02075-5

Wilson I.B.H., Yan S., Jin C., Dutkiewicz Z., Rendić D., Palmberger D., Schnabel R., Paschinger K. (2023) Increasing complexity of the N-glycome during Caenorhabditis development. Mol. Cell. Proteomics 22(3), 100505. doi: 10.1016/j.mcpro.2023.100505

Virginia, L.J., Peterbauer, C. (2023) Localization of Pyranose 2-Oxidase from Kitasatospora aureofaciens: A Step Closer to Elucidate a Biological Role. INT J MOL SCI 24, 1975. doi: 10.3390/ijms24031975

Antunovics Z., Szabo A., Heistinger L., Mattanovich D. , Sipiczki M. (2023) Synthetic two-species allodiploid and three-species allotetraploid Saccharomyces hybrids with euploid (complete) parental subgenomes. Sci Rep. 13 (1), 1112. doi: 10.1038/s41598-023-27693-2

Sebastiani, F., Baroni, C., Patil, G. , Dali, A., Becucci, M., Hofbauer, S. , Smulevich, G. (2023) The role of the hydrogen bond network in maintaining heme pocket stability and protein function specificity of C. diphtheriae coproheme decarboxylase. Biomolecules. 13, 235. doi: 10.3390/biom13020235

Dali, A., Gabler, T. , Sebastiani, F., Destinger, A., Furtmüller, P. G., Pfanzagl, V., Becucci, M., Smulevich, G., Hofbauer, S. (2023) Active site architecture of coproporphyrin ferrochelatase with its physiological substrate coproporphyrin III: propionate interactions and porphyrin core deformation. Protein Sci. 32, e4534. doi: 10.1002/pro.4534

Mitic B.M., Mattanovich D., Hann S. , Causon T. (2023) Tailored extraction and ion mobility-mass spectrometry enables isotopologue analysis of tetrahydrofolate vitamers. Anal Bioanal Chem. 415 (21), 5151-5163. doi: 10.1007/s00216-023-04786-5

Psotta, C., Cirovic, S., Gudmundsson, P., Falk, M., Mandal, T., Reichhart, T., Leech, D., Ludwig, R., Kittel, R., Schuhmann, W., Shleev, S. (2023) Continuous ex vivo glucose sensing in human physiological fluids using an enzymatic sensor in a vein replica. BIOELECTROCHEMISTRY 152, 108441. doi: 10.1016/j.bioelechem.2023.108441

Sun, P.C., Huang, Z.Y., Banerjee, S., Kadowaki, M.A.S., Veersma, R.J., Magri, S., Hilgers, R., Muderspach, S.J., Laurent, C.V.F.P., Ludwig, R., Cannella, D., Lo Leggio, L., van Berkel, W.J.H., Kabel, MA. (2023) AA16 Oxidoreductases Boost Cellulose-Active AA9 Lytic Polysaccharide Monooxygenases from Myceliophthora thermophila. ACS CATAL 13, 4454-4467, doi: 10.1021/acscatal.3c00874

Schwaiger, L., Zenone, A., Csarman, F., Ludwig, R. (2023) Continuous photometric activity assays for lytic polysaccharide monooxygenase-Critical assessment and practical considerations. Methods Enzymol 679, 381-404. doi: 0.1016/bs.mie.2022.08.054

Schachinger, F., Scheiblbrandner, S., Karnpakdee, K., Breslmayr, E., Ma, S., Roland, L. (2023) Cytochromes as electron shuttles from FAD-dependent glucose dehydrogenase to electrodes. Electrochimica Acta 458, 142485. doi: 10.1016/j.electacta.2023.142485

Hausjell, C.S., Ernst, W., Grünwald-Gruber, C., Arcalis, E. Grabherr, R. (2023) Quantitative proteomic analysis of extracellular vesicles in response to baculovirus infection of a Trichoplusia ni cell line. PLOS ONE 18, e0281060. doi: 10.1371/journal.pone.0281060

2022

Klausberger M., Kienzl N.F., Stadlmayr G., Grünwald-Gruber C., Laurent E., Stadlbauer K., Stracke F., Vierlinger K., Hofner M., Manhart G., Gerner W., Grebien F., Weinhäusel A., Mach L., Wozniak-Knopp G. (2022) Designed SARS-CoV-2 receptor binding domain variants form stable monomers. Biotechnology Journal 17, 2100422. doi: 10.1002/biot.202100422

Breslmayr, E., Poliak, P., Pozgajcic, A., Schindler, R., Kracher, D., Oostenbrink, C., Ludwig, R. (2022) Inhibition of the Peroxygenase Lytic Polysaccharide Monooxygenase by Carboxylic Acids and Amino Acids. ANTIOXIDANTS-BASEL 11, 1096. doi: 10.3390/antiox11061096

Zhu R., Canena D., Sikora M., Klausberger M., Seferovic H., Mehdipour A.R., Hain L., Laurent E., Monteil V., Wirnsberger G., Wieneke R., Tampé R., Kienzl N.F., Mach L., Mirazimi A., Oh Y.J., Penninger J.M., Hummer G., Hinterdorfer P (2022)Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level. Nat Commun 13, 7926. doi: 10.1038/s41467-022-35641-3

Chang, H.C., Amengual, N.G., Botz, A., Schwaiger, L., Kracher, D., Scheiblbrandner, S., Csarman, F., Ludwig, R. (2022) Investigating lytic polysaccharide monooxygenase-assisted wood cell wall degradation with microsensors. NAT COMMUN 13, 6258. doi: 10.1038/s41467-022-33963-w

Jayakumar, K., Reichhart, T.M.B., Schulz, C., Ludwig, R., Felice, AKG., Leech, D. (2022) An Oxygen Insensitive Amperometric Glucose Biosensor Based on An Engineered Cellobiose Dehydrogenase: Direct versus Mediated Electron Transfer Responses. CHEMELECTROCHEM 9, e202200418. doi: 10.1002/celc.202200418

Mansouri, H.R., Gracia Carmona, O., Jodlbauer, J., Schweiger, L., Fink, M.J., Breslmayr, E., Laurent, C., Feroz, S., P Goncalves, L.C., Rial, D.V., Mihovilovic, M.D., Bommarius, A.S., Ludwig, R., Oostenbrink, C., Rudroff, F. (2022) Mutations Increasing Cofactor Affinity, Improve Stability and Activity of a Baeyer-Villiger Monooxygenase. ACS Catal 12, 11761-11766. doi: 10.1021/acscatal.2c03225

Sun, P.C., Laurent, C.V.F.P., Boerkamp, V.J.P., van Erven, G., Ludwig, R., van Berkel, W.J.H., Kabel, M.A. (2022) Regioselective C4 and C6 Double Oxidation of Cellulose by Lytic Polysaccharide Monooxygenases. CHEMSUSCHEM 15, e202102203. doi: 10.1002/cssc.202102203

Viehauser, M.C., Breslmayr, E., Scheiblbrandner, S., Schachinger, F., Ma, S., Ludwig, R. (2022) A cytochrome b-glucose dehydrogenase chimeric enzyme capable of direct electron transfer. BIOSENS BIOELECTRON 196, 113704. doi: 0.1016/j.bios.2021.113704

Eidenberger, L., Eminger, F., Castilho A., Steinkellner, H. (2022) Comparative analysis of plant transient expression vectors for targeted N-glycosylation. Frontiers in Bioengineering and Biotechnology 10, 1073455. doi: 10.3389/fbioe.2022.1073455

Tsvik, L., Steiner, B., Herzog, P., Haltrich, D., Sützl, L. (2022) Flavin Mononucleotide-Dependent l-Lactate Dehydrogenases: Expanding the Toolbox of Enzymes for l-Lactate Biosensors. ACS Omega 7, pp. 41480-41492. doi: 10.1021/acsomega.2c05257

Kostelac, A., Sützl, L., Puc, J., Furlanetto, V., Divne, C., Haltrich, D. (2022) Biochemical Characterization of Pyranose Oxidase from Streptomyces canus—Towards a Better Understanding of Pyranose Oxidase Homologues in Bacteria. International Journal of Molecular Sciences 23, 13595. doi: 10.3390/ijms232113595

Foley, G., Mora, A., Ross, C.M., Bottoms, D., Sützl, L., Lamprecht, M.L., Zaugg, J., Essebier, A., Balderson, B., Newell, R., Thomson, R.E.S., Kobe, B., Barnard, R.T., Guddat, L., Schenk, G., Carsten, J., Gumulya, Y., Rost, B., Haltrich, D., Sieber, V., Gillam, E.M.L., Bodén, M. (2022) Engineering indel and substitution variants of diverse and ancient enzymes using Graphical Representation of Ancestral Sequence Predictions (GRASP). PLoS Computational Biology 18, e1010633. doi: 10.1371/journal.pcbi.1010633

Schachinger, F., Ma, S., Ludwig, R. (2022) Redox potential of FAD-dependent glucose dehydrogenase. Electrochem. Commun. 146, 107405. doi: 10.1016/j.elecom.2022.107405

Baumschabl, M., Ata, Ö., Mitic, B., Mattanovich, D. (2022) Conversion of CO₂ into organic acids by engineered autotrophic yeast. PNAS 119, e2211827119. doi: 10.1073/pnas.2211827119

Teufl, M., Zajc, C. U., Traxlmayr, M. W. (2022) Engineering Strategies to Overcome the Stability-Function Trade-Off in Proteins. Acs Synth Biol 11, 1030-1039. doi: 10.1021/acssynbio.1c00512

Sebastiani, F., Niccoli, C., Michlits, H., Risorti, R., Becucci, M., Hofbauer, S., Smulevich, G. (2022) Spectroscopic evidence of the effect of hydrogen peroxide excess on the coproheme decarboxylase from actinobacterial Corynebacterium diphtheriae. J. Raman Spectrosc. doi: 10.1002/jrs.6326

Klausberger, M., Kienzl, N. F. , Stadlmayr, G., Grunwald-Gruber, C., Laurent, E., Stadlbauer, K., Stracke, F., Vierlinger, K., Hofner, M., Manhart, G., Gerner, W., Grebien, F., Weinhausel, A., Mach, L., Wozniak-Knopp, G. (2022) Designed SARS-CoV-2 receptor binding domain variants form stable monomers. Biotechnol. J. doi: 10.1002/biot.202100422

Sebastiani, F., Risorti, R., Niccoli, C., Michlits, H., Becucci, M., Hofbauer, S., Smulevich, G. (2022) An active site at work – the role of key residues in C. diphteriae, coproheme decarobxlyase. J. Inorg. Biochem., 229, 111718, doi: 10.1016/j.jinorgbio.2022.111718

Michlits, H., Valente, N., Mlynek, G., Hofbauer, S. (2022) Initial Steps to Engineer Coproheme Decarboxylase to Obtain Stereospecific Monovinyl, Monopropionyl Deuterohemes. Front. Bioeng. Biotechnol. 9. doi: 10.3389/fbioe.2021.807678

Wagner A. , Galicia-Andrés E., Teufl M. , Gold L., Obinger C. , Sykacek P., Oostenbrink C., Traxlmayr M.W. (2022) Identification of activating mutations in the transmembrane and extracellular domains of EGFR. Biochemistry. 61, 2049-2062. doi: 10.1021/acs.biochem.2c00384

Gracia Carmona O., Oostenbrink C. (2022) Accelerated Enveloping Distribution Sampling (AEDS) allows for efficient sampling of orthogonal degrees of freedom. J. Chem. Inf. Model. 63, 197-207. doi: 10.1021/acs.jcim.2c01272

Marx N., Eisenhut P., Weinguny M., Klanert G., Borth N. (2022) How to train your cell – towards controlling phenotypes by harnessing the epigenome of Chinese Hamster ovary production cell lines. Biotechnol. Adv. 56, 107924. doi: 10.1016/j.biotechadv.2022.107924

Zajc C.U., Teufl M., Traxlmayr M.W. (2022) Affinity and Stability Analysis of Yeast Displayed Proteins. Methods Mol Biol. 2491, 155-173. doi: 10.1007/978-1-0716-2285-8_9

Ruocco V., Strasser R. (2022) Transient expression of glycosylated SARS-CoV-2 antigens in Nicotiana benthamiana. Plants, 11, 1093. doi: 10.3390/plants11081093

Uetz P. , Melnik S., Grünwald-Gruber C., Strasser R., Stoger E. (2022) CRISPR/Cas9-mediated knockout of a prolyl-4-hydroxylase subfamily in N. benthamiana using DsRed2 for plant selection. Biotechnol. J. 7, e2100698. doi: 10.1002/biot.202100698

Leitgeb, U. , Furtmüller, P. G., Hofbauer, S. , Brito, J. A., Obinger, C. , Pfanzagl, V. (2022) Slow refolding of the myeloperoxidase inhibitor SPIN after binding results in a picomolar affinity but can only dampen halide oxidation. J. Biol. Chem. 298, 102514. doi: 10.1016/j.jbc.2022.102514

Lier B. , Poliak P., Marquetand P., Westermayr J., Oostenbrink C. (2022) BuRNN: Buffer Region Neural Network Approach for Polarizable-Embedding Neural Network/Molecular Mechanics Simulations. J. Phys. Chem. Lett 13, 3812−3818. doi: 10.1021/acs.jpclett.2c00654

Serra, I., Schmidt, D. , Pfanzagl, V., Mlynek, G., Hofbauer, S. , Djinović-Carugo, K., Furtmüller, P. G., Garcia Rubio, I., Van Doorslaer, S., Obinger, C. (2022) Impact of the dynamics of the catalytic arginine on nitrite and chlorite binding by dimeric chlorite dismutase. J. Inorg. Biochem. 227, 111689. doi: 10.1016/j.jinorgbio.2021.111689

Tir N., Heistinger L. , Grünwald-Gruber C., Jakob L.A., Dickgiesser S., Rasche N., Mattanovich D. (2022) From strain engineering to process development: monoclonal antibody production with an unnatural amino acid in Pichia pastoris. Microb Cell Fact. 21 (1), 157. doi: 10.1186/s12934-022-01882-6

Gabler, T. , Sebastiani, F., Helm, J., Dali, A., Obinger, C. , Furtmüller, P. G., Smulevich, G., Hofbauer, S. (2022) Substrate specificity and complex stability of coproporphyrin ferrochelatase is governed by hydrogen-bonding interactions of the four propionate groups. FEBS J. 289, 1680-1699. doi: 10.1111/febs.16257

Baumschabl M. , Ata Ö., Mitic B.M. , Lutz L., Gassler T. , Troyer C., Hann S., Mattanovich D. (2022) Conversion of CO2 into organic acids by engineered autotrophic yeast. Proc Natl Acad Sci USA. 119, e2211827119. doi: 10.1073/pnas.2211827119

Mitic B.M. , Troyer C., Hann S., Mattanovich D. (2022) The oxygen tolerant reductive glycine pathway in eukaryotes – a native methanol, formate and CO2 assimilation pathway in the yeast Komagataella phaffii. BioRxiv. doi: 10.1101/2022.09.01.506198

Heistinger L. , Dohm J.C., Paes B.G., Koizar D., Troyer C., Ata Ö., Steininger-Mairinger T., Mattanovich D. (2022) Genotypic and phenotypic diversity among Komagataella species reveals a hidden pathway for xylose utilization. Microb Cell Fact. 21 (1), 70. doi: 10.1186/s12934-022-01796-3

Staudacher J., Rebnegger C. , Dohnal T., Landes N., Mattanovich D., Gasser B. (2022) Going beyond the limit: Increasing global translation activity leads to increased productivity of recombinant secreted proteins in Pichia pastoris. Metab Eng. 70, 181-195. doi: 10.1016/j.ymben.2022.01.010

2021

Hofbauer, S., Pfanzagl, V., Michlits, H., Schmidt, D., Obinger, C., Furtmuller, P. G. (2021) Understanding molecular enzymology of porphyrin-binding alpha plus beta barrel proteins - One fold, multiple functions. Bba-Proteins Proteom 1869. doi: 10.1016/j.bbapap.2020.140536

Capraz, T., Kienzl, N. F., Laurent, E., Perthold, J. W., Foderl-Hobenreich, E., Grunwald-Gruber, C., Maresch, D., Monteil, V., Niederhofer, J., Wirnsberger, G., Mirazimi, A., Zatloukal, K., Mach, L., Penninger, J. M., Oostenbrink, C., Stadlmann, J. (2021) Structure-guided glyco-engineering of ACE2 for improved potency as soluble SARS-CoV-2 decoy receptor. Elife 10. doi: 10.7554/eLife.73641

Serra, I., Schmidt, D., Pfanzagl, V., Mlynek, G., Hofbauer, S., Djinovic-Carugo, K., Furtmuller, P. G., Garcia-Rubio, I., Van Doorslaer, S., Obinger, C. (2021) Impact of the dynamics of the catalytic arginine on nitrite and chlorite binding by dimeric chlorite dismutase. J. Inorg. Biochem. 227, 111689. doi: 10.1016/j.jinorgbio.2021.111689

Laurent, E., Sieber, A., Salzer, B., Wachernig, A., Seigner, J., Lehner, M., Geyeregger, R., Kratzer, B., Jager, U., Kunert, R., Pickl, W. F., Traxlmayr, M. W. (2021) Directed Evolution of Stabilized Monomeric CD19 for Monovalent CAR Interaction Studies and Monitoring of CAR-T Cell Patients. Acs Synth Biol 10, 1184-1198. doi: 10.1021/acssynbio.1c00010

Gassler, T., Baumschabl, M., Sallaberger, J., Egermeier, M., Mattanovich, D. (2021) Adaptive laboratory evolution and reverse engineering enhances autotrophic growth in Pichia pastoris. Metab. Eng. 69, 112-121. doi: 10.1016/j.ymben.2021.11.007

Benedetti, F., Stadlbauer, K., Stadlmayr, G., Ruker, F., Wozniak-Knopp, G. (2021) A Tetravalent Biparatopic Antibody Causes life11111157Strong HER2 Internalization and Inhibits Cellular Proliferation. Life (Basel) 11. doi: 10.3390/ life11111157

Hager-Mair, F.F., Stefanović, C., Lim, C.,Webhofer, K., Krauter, S.,  Blaukopf, M., Ludwig, R., Kosma, P., Schäffer, C. (2021) Assaying Paenibacillus alvei CsaB-Catalysed Ketalpyruvyltransfer to Saccharides by Measurement of Phosphate Release. Biomolecules, 11(11), 1732. doi:10.3390/biom11111732

Rodak, A., Stadlmayr, G., Stadlbauer, K., Lichtscheidl, D., Bobbili, M.R,. Ruker, F., Wozniak-Knopp, G. (2021) Bispecific T-Cell Engagers Targeting Membrane-Bound IgE. Biomedicines. doi:10.3390/biomedicines9111568

Gabler, T., Sebastiani, F., Helm, J., Dali, A., Obinger, C., Furtmuller, P. G., Smulevich, G., Hofbauer, S. (2021) Substrate specificity and complex stability of coproporphyrin ferrochelatase is governed by hydrogen-bonding interactions of the four propionate groups. FEBS J. doi: 10.1111/febs.16257

Viehauser, M.C., Breslmayr, E., Scheiblbrandner, S., Schachinger, F., Ma, S., Ludwig, R. (2021) A cytochrome b-glucose dehydrogenase chimeric enzyme capable of direct electron transfer. Biosensors and Bioelectronics. doi:10.1016/j.bios.2021.113704

Wijayanti, S.D.; Sützl, L.; Duval, A.; Haltrich, D. (2021) Characterization of Fungal FAD-Dependent AA3_2 Glucose Oxidoreductases from Hitherto Unexplored Phylogenetic Clades. J. Fungi. 7, 873. doi: 10.3390/jof7100873

Schwestka, J., König-Beihammer, J., Shin, Y.J., Vavra, U., Kienzl, N.F., Grünwald-Gruber, C., Maresch, D., Klausberger, M., Laurent, E., Stadler, M., Manhart, G., Huber, J., Hofner, M., Vierlinger, K., Weinhäusel, A., Swoboda, I., Binder C.J., Gerner, W., Grebien, F., Altmann, F., Mach, L., Stöger, E. and Strasser, R. (2021) Impact of Specific N-Glycan Modifications on the Use of Plant-Produced SARS-CoV-2 Antigens in Serological Assays. Front. Plant Sci. 12,747500. doi: 10.3389/fpls.2021.747500

Schachinger, F., Chang, H., Scheiblbrandner, S., Ludwig, R. (2021) Amperometric Biosensors Based on Direct Electron Transfer Enzymes. Molecules. 2021 26(15), 4525. doi: 10.3390/molecules26154525

Sebastiani, F., Michlits, H., Lier, B., Becucci,M., Oostenbrink, C., Obinger, C., Hofbauer, S., Smulevich, G. (2021) Reaction intermediate rotation during the decarboxylation of coproheme to heme b in C. diphtheriae. Biophys J. S0006-3495(21) 00635-4. doi: 10.1016/j.bpj.2021.06.042

Watthanasakphuban, N., Virginia, L.J., Haltrich, D., Peterbauer, C. (2021) Analysis and Reconstitution of the Menaquinone Biosynthesis Pathway in Lactiplantibacillus plantarum and Lentilactibacillus buchneri. Microorganisms 9, 1476. doi:10.3390/microorganisms9071476

Shin, Y. J., Konig-Beihammer, J., Vavra, U., Schwestka, J., Kienzl, N. F., Klausberger, M., Laurent, E., Grunwald-Gruber, C., Vierlinger, K., Hofner, M., Margolin, E., Weinhausel, A., Stoger, E., Mach, L., Strasser, R. (2021) N-Glycosylation of the SARS-CoV-2 Receptor Binding Domain Is Important for Functional Expression in Plants. Front. Plant Sci. 12. doi: 10.3389/fpls.2021.689104

Szeliova, D., Stor, J., Thiel, I., Weinguny, M., Hanscho, M., Lhota, G., Borth, N., Zanghellini, J., Ruckerbauer, D. E., Rocha, I. (2021) Inclusion of maintenance energy improves the intracellular flux predictions of CHO. PLoS Comput. Biol. 17, e1009022. doi: 10.1371/journal.pcbi.1009022

Jakob, L. A., Beyer, B., Ferreira, C. J., Lingg, N., Jungbauer, A., Tscheliessnig, R. (2021) Protein-protein interactions and reduced excluded volume increase dynamic binding capacity of dual salt systems in hydrophobic interaction chromatography. J. Chromatogr. A 1649. doi: ARTN 462231 10.1016/j.chroma.2021.462231

Andreas F. Geiss, A.F., Reichhart, T.M.B., Pejker, B.,  Plattner, E., Herzog, P.L., Schulz, C., Ludwig, R., Felice, A.K.G., Haltrich, D. (2021) Engineering the Turnover Stability of Cellobiose Dehydrogenase toward Long-Term Bioelectronic Applications. ACS Sustainable Chem & Eng  9(20), 7086-7100. doi: 10.1021/acssuschemeng.1c01165

Beihammer, G., Maresch, D., Altmann, F., Van Damme, E. J. M., Strasser, R. (2021) Lewis A Glycans Are Present on Proteins Involved in Cell Wall Biosynthesis and Appear Evolutionarily Conserved Among Natural Arabidopsis thaliana Accessions. Front Plant Sci 12, 630891. doi: 10.3389/fpls.2021.630891

Zavec, D., Troyer, C., Maresch, D., Altmann, F., Hann, S., Gasser, B., Mattanovich, D. (2021) Beyond alcohol oxidase: the methylotrophic yeast Komagataella phaffii utilizes methanol also with its native alcohol dehydrogenase Adh2. FEMS Yeast Res. 21. doi: 10.1093/femsyr/foab009

Schwestka, J. and Stoger, E. (2021) Microparticles and Nanoparticles from Plants-The Benefits of Bioencapsulation. Vaccines (Basel) 9. doi: 10.3390/vaccines9040369

Benedetti, F., Stracke, F., Stadlmayr, G., Stadlbauer, K., Ruker, F., Wozniak-Knopp, G. (2021) Bispecific antibodies with Fab-arms featuring exchanged antigen-binding constant domains. Biochem Biophys Rep 26, 100959. doi: 10.1016/j.bbrep.2021.100959

Schmidt, D., Serra, I., Mlynek, G., Pfanzagl, V., Hofbauer, S., Furtmuller, P. G., Djinovic-Carugo, K., Van Doorslaer, S., Obinger, C. (2021) Arresting the Catalytic Arginine in Chlorite Dismutases: Impact on Heme Coordination, Thermal Stability, and Catalysis. Biochemistry 60, 621-634. doi: 10.1021/acs.biochem.0c00910

Felice, A. K. G., Schuster, C., Kadek, A., Filandr, F., Laurent, C., Scheiblbrandner, S., Schwaiger, L., Schachinger, F., Kracher, D., Sygmund, C., Man, P., Halada, P., Oostenbrink, C., Ludwig, R. (2021) Chimeric Cellobiose Dehydrogenases Reveal the Function of Cytochrome Domain Mobility for the Electron Transfer to Lytic Polysaccharide Monooxygenase. ACS Catal 11, 517-532. doi: 10.1021/acscatal.0c05294

Castilho, A., Schwestka, J., Kienzl, N. F., Vavra, U., Grunwald-Gruber, C., Izadi, S., Hiremath, C., Niederhofer, J., Laurent, E., Monteil, V., Mirazimi, A., Wirnsberger, G., Stadlmann, J., Stoger, E., Mach, L., Strasser, R. (2021) Generation of enzymatically competent SARS-CoV-2 decoy receptor ACE2-Fc in glycoengineered Nicotiana benthamiana. Biotechnol. J.  e2000566. doi: 10.1002/biot.202000566

Stefanovic, C., Hager, F. F., Schaffer, C. (2021) LytR-CpsA-Psr Glycopolymer Transferases: Essential Bricks in Gram-Positive Bacterial Cell Wall Assembly. Int. J. Mol. Sci. 22. doi: 10.3390/ijms22020908

Széliová D. , Iurashev D., Ruckerbauer D.E., Koellensperger G., Borth N, Melcher M., Zanghellini J. (2021) Error propagation in constraint-based modeling of Chinese Hamster ovary cells. Biotechnol J. 16, 2000320. doi: 10.1002/biot.202000320

Weinguny M., Klanert G., Eisenhut P. , Lee I., Timp W., Borth N. (2021) Subcloning induces changes in the DNA-methylation pattern of outgrowing colonies. Biotechn J. 16, 2000350. doi: 10.1002/biot.20200350

Wagner A., Teufl M. , Gold L., Lehner M., Obinger C. , Sykacek P., Traxlmayr M.W. (2021) PhosphoFlowSeq - A High-throughput Kinase Activity Assay for Screening Drug Resistance Mutations in EGFR. J Mol Biol. 433 (22), 167210. doi: 10.1016/j.jmb.2021.167210

Stor J., Ruckerbauer D.E., Szeliova D., Zanghellini J., Borth N. (2021) Towards rational glycoengineering in CHO: from data to predictive models. Curr. Op. Biotechn. 71, 9-17. doi: 10.1016/j.copbio.2021.05.003

Barbay D., Mačáková M., Sützl L., De S., Mattanovich D., Gasser B. (2021) Two homologs of the Cat8 transcription factor are involved in the regulation of ethanol utilization in Komagataella phaffii. Curr Genet. 67, pages 641–661. doi: 10.1007/s00294-021-01165-4

Marx N., Dhiman H., Schmieder V., Freire C.M., Nguyen L.N., Klanert G., Borth N. (2021) Enhanced targeted DNA methylation of the CMV and endogenous promoters with dCas9-DNMT3A3L entails distinct subsequent histone modification changes in CHO cells. Metab. Eng. 66, 268-282. doi: 10.1016/j.ymben.2021.04.014

Ata Ö., Ergün B.G., Fickers P., Heistinger L., Mattanovich D., Rebnegger C., Gasser B. (2021) What makes Komagataella phaffii non-conventional? FEMS Yeast Res. 21, foab059. doi: 10.1093/femsyr/foab059

Schmieder V., Novak N., Dhiman H., Nguyen L.N., Serafimova E., Klanert G. , Baumann M., Kildegaard H.F., Borth N. (2021) A pooled CRISPR/AsCpf1 screen using paired gRNAs to induce genomic deletions in Chinese Hamster Ovary cells. Biotechn. Reports 31, e00649. doi: 10.1016/j.btre.2021.e00649

Gludovacz E., Schuetzenberger K., Resch M., Tillmann K., Petroczi K., Schosserer M., Vondra S., Vakal S., Klanert G. , Pollheimer J., Salminen T.A., Jilma B., Borth N. , Boehm T. (2021) Heparin-binding motif mutations of human diamine oxidase allow the development of a first-in-class histamine degrading biopharmaceutical. Elife 3, e68542. doi: 10.7554/eLife.68542

De S., Mattanovich D. , Ferrer P., Gasser B. (2021) Established tools and emerging trends for the production of recombinant proteins and metabolites in Pichia pastoris. Essays Biochem. 65, 293-307. doi: 10.1042/EBC20200138

Paumann-Page M., Kienzl N.F. , Motwani J., Bathish B., Paton L.N., Magon N.J., Sevcnikar B., Furtmüller P.G., Traxlmayr M.W., Obinger C. , Eccles M.R., Winterbourn C.C. (2021) Peroxidasin protein expression and enzymatic activity in metastatic melanoma cell lines are associated with invasive potential. Redox Biol. 46, 102090. doi: 10.1016/j.redox.2021.102090

Radoman B., Grünwald-Gruber C., Schmelzer B., Zavec D., Gasser B., Altmann F., Mattanovich D. (2021) The degree and length of O-glycosylation of recombinant proteins produced in Pichia pastoris depends on the nature of the protein and the process type. Biotechnol J. 16, e2000266. doi: 10.1002/biot.202000266

2020

Labrada K.P., Strobl S., Eckmair B., Blaukopf M., Dutkiewicz Z., Hykollari A., Malzl D., Paschinger K., Yan S., Wilson I.B.H., Kosma P. (2020) Zwitterionic phosphodiester-substituted neoglycoconjugates as ligands for antibodies and acute phase proteins. ACS Chem. Biol. 15(2), 369-377. doi: 10.1021/acschembio.9b00794

Valli, M., Grillitsch, K., Grunwald-Gruber, C., Tatto, N. E., Hrobath, B., Klug, L., Ivashov, V., Hauzmayer, S., Koller, M., Tir, N., Leisch, F., Gasser, B., Graf, A. B., Altmann, F., Daum, G., Mattanovich, D. (2020) A subcellular proteome atlas of the yeast Komagataella phaffii. FEMS Yeast Res. 20. doi: ARTN foaa00110.1093/femsyr/foaa00

Beihammer, G., Maresch, D., Altmann, F., Strasser, R. (2020) Glycosylphosphatidylinositol-Anchor Synthesis in Plants: A Glycobiology Perspective. Front. Plant Sci. 11. doi: 10.3389/fpls.2020.611188

Baumschabl, M., Prielhofer, R., Mattanovich, D., Steiger, M. G. (2020) Fine-Tuning of Transcription in Pichia pastoris Using dCas9 and RNA Scaffolds. Acs Synth Biol 9, 3202-3209. doi: 10.1021/acssynbio.0c00214

Eckmair B., Jin C., Karlsson N.G., Abed-Navandi D., Wilson I.B.H., Paschinger K. (2020) Glycosylation at an evolutionary nexus: the brittle star Ophiactis savignyi expresses both vertebrate and invertebrate N-glycomic features. J. Biol. Chem. 295(10), 3173-3188. doi: 10.1074/jbc.RA119.011703

Hennicke, J., Schwaigerlehner, L., Grunwald-Gruber, C., Bally, I., Ling, W. L., Thielens, N., Reiser, J. B., Kunert, R. (2020) Transient pentameric IgM fulfill biological function-Effect of expression host and transfection on IgM properties. PLoS One 15. doi: 10.1371/journal.pone.0229992

Sevcnikar, B., Schaffner, I., Chuang, C. Y., Gamon, L., Paumann-Page, M., Hofbauer, S., Davies, M. J., Furtmuller, P. G., Obinger, C. (2020) The leucine-rich repeat domain of human peroxidasin 1 promotes binding to laminin in basement membranes. Arch. Biochem. Biophys. 689. doi: 10.1016/j.abb.2020.108443

Goritzer, K., Goet, I., Duric, S., Maresch, D., Altmann, F., Obinger, C., Strasser, R. (2020) Efficient N-Glycosylation of the Heavy Chain Tailpiece Promotes the Formation of Plant-Produced Dimeric IgA. Front Chem 8. doi: 10.3389/Fchem.2020.00346

Suleiman, E., Mayer, J., Lehner, E., Kohlhauser, B., Katholnig, A., Batzoni, M., Damm, D., Temchura, V., Wagner, A., Uberla, K., Vorauer-Uhl, K. (2020) Conjugation of Native-Like HIV-1 Envelope Trimers onto Liposomes Using EDC/Sulfo-NHS Chemistry: Requirements and Limitations. Pharmaceutics 12. doi: 10.3390/pharmaceutics12100979

Eisenhut, P., Mebrahtu, A., Moradi Barzadd, M., Thalen, N., Klanert, G., Weinguny, M., Sandegren, A., Su, C., Hatton, D., Borth, N., Rockberg, J. (2020) Systematic use of synthetic 5'-UTR RNA structures to tune protein translation improves yield and quality of complex proteins in mammalian cell factories. Nucleic Acids Res. doi: 10.1093/nar/gkaa847

Pascoal, S., Salzer, B., Scheuringer, E., Wenninger-Weinzierl, A., Sturtzel, C., Holter, W., Taschner-Mandl, S., Lehner, M., Distel, M. (2020) A Preclinical Embryonic Zebrafish Xenograft Model to Investigate CAR T Cells in Vivo. Cancers (Basel) 12. doi: 10.3390/Cancers12030567

Zajc, C. U., Salzer, B., Taft, J. M., Reddy, S. T., Lehner, M., Traxlmayr, M. W. (2020) Driving CARs with alternative navigation tools - the potential of engineered binding scaffolds. FEBS J. doi: 10.1111/febs.15523

Herzog, P. L., Borghi, E., Traxlmayr, M. W., Obinger, C., Sikes, H. D., Peterbauer, C. K. (2020) Developing a cell-bound detection system for the screening of oxidase activity using the fluorescent peroxide sensor roGFP2-Orp1. Protein Eng. Des. Sel. 33. doi: 10.1093/protein/gzaa019

Reiter, K., Aguilar, P. P., Grammelhofer, D., Joseph, J., Steppert, P., Jungbauer, A. (2020) Separation of influenza virus-like particles from baculovirus by polymer-grafted anion exchanger. J. Sep. Sci. 43, 2270-2278. doi: 10.1002/jssc.201901215

Aguilar, P. P., Reiter, K., Wetter, V., Steppert, P., Maresch, D., Ling, W. L., Satzer, P., Jungbauer, A. (2020) Capture and purification of Human Immunodeficiency Virus-1 virus-like particles: Convective media vs porous beads. J. Chromatogr. A 1627. doi: 10.1016/J.Chroma.2020.461378

Weinguny, M., Eisenhut, P., Klanert, G., Virgolini, N., Marx, N., Jonsson, A., Ivansson, D., Lovgren, A., Borth, N. (2020) Random epigenetic modulation of CHO cells by repeated knockdown of DNA methyltransferases increases population diversity and enables sorting of cells with higher production capacities. Biotechnol. Bioeng. doi: 10.1002/bit.27493

Weinguny, M., Klanert, G., Eisenhut, P., Jonsson, A., Ivansson, D., Lovgren, A., Borth, N. (2020) Directed evolution approach to enhance efficiency and speed of outgrowth during single cell subcloning of Chinese Hamster Ovary cells. Comput Struct Biotechnol J 18, 1320-1329. doi: 10.1016/j.csbj.2020.05.020

Hamdi, A., Szeliova, D., Ruckerbauer, D. E., Rocha, I., Borth, N., Zanghellini, J. (2020) Key Challenges in Designing CHO Chassis Platforms. Processes 8. Artn 643 doi: 10.3390/Pr8060643

Szeliova, D., Ruckerbauer, D. E., Galleguillos, S. N., Petersen, L. B., Natter, K., Hanscho, M., Troyer, C., Causon, T., Schoeny, H., Christensen, H. B., Lee, D. Y., Lewis, N. E., Koellensperger, G., Hann, S., Nielsen, L. K., Borth, N., Zanghellini, J. (2020) What CHO is made of: Variations in the biomass composition of Chinese hamster ovary cell lines. Metab. Eng. 61, 288-300. doi: 10.1016/j.ymben.2020.06.002

Vanbeselaere J., Jin C., Eckmair B., Wilson I.B.H., Paschinger K. (2020) Sulfated and sialylated N-glycans in the echinoderm Holothuria atra reflect its marine habitat and phylogeny. J. Biol. Chem. 295(10), 3159-3172. doi: 10.1074/jbc.RA119.011701

Pfanzagl, V., Beale, J. H., Michlits, H., Schmidt, D., Gabler, T., Obinger, C., Djinovic-Carugo, K., Hofbauer, S. (2020) X-ray induced photoreduction of heme metal centers rapidly induces active site perturbations in a protein-independent manner. J. Biol. Chem. doi: 10.1074/jbc.RA120.014087

Salzer, B., Schueller, C. M., Zajc, C. U., Peters, T., Schoeber, M. A., Kovacic, B., Buri, M. C., Lobner, E., Dushek, O., Huppa, J. B., Obinger, C., Putz, E. M., Holter, W., Traxlmayr, M. W., Lehner, M. (2020) Engineering AvidCARs for combinatorial antigen recognition and reversible control of CAR function. Nat. Commun. 11, 4166. doi: 10.1038/s41467-020-17970-3

De, S., Rebnegger, C., Moser, J., Tatto, N., Graf, A. B., Mattanovich, D., Gasser, B. (2020) Pseudohyphal differentiation in Komagataella phaffii: investigating the FLO gene family. FEMS Yeast Res 20. doi: 10.1093/femsyr/foaa04

Breslmayr, E., Laurent, C., Scheiblbrandner, S., Jerkovic, A., Heyes, D. J., Oostenbrink, C., Ludwig, R., Hedison, T. M., Scrutton, N. S., Kracher, D. (2020) Protein Conformational Change Is Essential for Reductive Activation of Lytic Polysaccharide Monooxygenase by Cellobiose Dehydrogenase. ACS Catal 10, 4842-4853. doi: 10.1021/acscatal.0c00754

Michlits, H., Lier, B., Pfanzagl, V., Djinovic-Carugo, K., Furtmuller, P. G., Oostenbrink, C., Obinger, C., Hofbauer, S. (2020) Actinobacterial Coproheme Decarboxylases Use Histidine as a Distal Base to Promote Compound I Formation. ACS Catal. 10, 5405-5418. doi: 10.1021/acscatal.0c00411

Zajc, C. U., Dobersberger, M., Schaffner, I., Mlynek, G., Puhringer, D., Salzer, B., Djinovic-Carugo, K., Steinberger, P., De Sousa Linhares, A., Yang, N. J., Obinger, C., Holter, W., Traxlmayr, M. W., Lehner, M. (2020) A conformation-specific ON-switch for controlling CAR T cells with an orally available drug. Proc. Natl. Acad. Sci. U. S. A. 117, 14926-14935. doi: 10.1073/pnas.1911154117

Abrera, A. T., Sutzl, L., Haltrich, D. (2020) Pyranose oxidase: A versatile sugar oxidoreductase for bioelectrochemical applications. Bioelectrochemistry 132, 107409. doi: 10.1016/j.bioelechem.2019.107409

Schutz, G., Haltrich, D., Atanasova, L. (2020) Influence of spore morphology on spectrophotometric quantification of Trichoderma inocula. Biotechniques. doi: 10.2144/btn-2019-0152

Lobner, E., Wachernig, A., Gudipati, V., Mayrhofer, P., Salzer, B., Lehner, M., Huppa, J. B., Kunert, R. (2020) Getting CD19 Into Shape: Expression of Natively Folded "Difficult-to- Express" CD19 for Staining and Stimulation of CAR-T Cells. Front Bioeng Biotechnol 8, 49. doi: 10.3389/fbioe.2020.00049

Schwestka, J., Tschofen, M., Vogt, S., Marcel, S., Grillari, J., Raith, M., Swoboda, I., Stoger, E. (2020) Plant-derived protein bodies as delivery vehicles for recombinant proteins into mammalian cells. Biotechnol. Bioeng. doi: 10.1002/bit.27273

Filandr, F., Kavan, D., Kracher, D., Laurent, C., Ludwig, R. , Man, P., Halada, P. (2020) Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis. Biomolecules 10. doi: 10.3390/biom10020242

Turupcu, A., Blaukopf, M., Kosma, P., Oostenbrink, C. (2020) Molecular Conformations of Di-, Tri-, and Tetra-alpha-(2 -> 8)-Linked Sialic Acid from NMR Spectroscopy and MD Simulations. Int. J. Mol. Sci. 21. doi: Artn 3010.3390/Ijms21010030

Schiavinato, M., Marcet-Houben, M., Dohm, J. C., Gabaldon, T., Himmelbauer, H. (2019) Parental origin of the allotetraploid tobacco Nicotiana benthamiana. Plant J. doi: 10.1111/tpj.14648

Széliová D. , Schoeny H., Knez S., Troyer C., Coman C., Rampler E. , Koellensperger G., Ahrends R., Hann S., Borth N., Zanghellini J. , Ruckerbauer D.E. (2020) Robust analytical methods for the accurate quantification of the total biomass composition of mammalian cells. Methods in Molecular Biology. 2088, 119-160. doi: 10.1007/978-1-0716-0159-4_7

Gassler T., Sauer M., Gasser B. , Egermeier M., Troyer C., Causon T., Hann S., Mattanovich D. , Steiger M. (2020) The industrial yeast Pichia pastoris is converted from a heterotroph into an autotroph capable of growth on CO2. Nat Biotechnol., 38, 210-216. doi: 10.1038/s41587-019-0363-0

Baumann M., Klanert G. , Vcelar S., Weinguny M., Marx N., Borth N. (2020) Genome Variation, the epigenome and cellular phenotypes. Wiley-Blackwell Biotechnology Series: Cell Culture Engineering. Recombinant Protein Production. Eds. Lee G.M., Kildegaard H.F., Lee S.Y., Nielsen J., Stephanopoulos S. doi: 10.1002/9783527811410

Zavec D., Gasser B., Mattanovich D. (2020) Biotechnol Bioeng. Characterization of methanol utilization negative Pichia pastoris for secreted protein production: New cultivation strategies for current and future applications. 117, 1394-1405. doi: 10.1002/bit.27303

Heistinger L., Gasser B., Mattanovich D. (2020) Microbe Profile: Komagataella phaffii: a methanol devouring biotech yeast formerly known as Pichia pastoris. Microbiology (Reading). 166, 614-616. doi: 10.1099/mic.0.000958

Bydlinski N., Coats M.T. , Maresch D., Altmann F., Strasser R., Borth N. (2020) Transfection of glycoprotein encoding mRNA for swift evaluation of N-glycan engineering strategies. Biotechn Progress 36, e2990. doi: 10.1002/btpr.2990

Heistinger L., Gasser B., Mattanovich D. (2020) Komagataella phaffii YPS1-5 encodes the alpha-factor degrading protease Bar1. FEMS Yeast Res. 20, foaa024. doi: 10.1093/femsyr/foaa024

Li J., Rinnerthaler M., Hartl J., Weber M., Karl T., Breitenbach-Koller H., Mülleder M., Vowinckel J., Marx H., Sauer M., Mattanovich D. , Ata Ö., De S. , Greslehner G.P., Geltinger F.., Burhans B, Grant C., Doronina V., Ralser M., Streubel M.K., Grabner C., Jarolim S., Moßhammer C., Gourlay C.W., Hasek J., Cullen P.J., Liti G., Ralser M., Breitenbach M. (2020) Slow growth and increased spontaneous mutation frequency in respiratory deficient afo1- yeast suppressed by a dominant mutation in ATP3. G3 (Bethesda). 10, 4637-4648. doi: 10.1534/g3.120.401537

2019

Hernandez I. , Dhiman H., Klanert G., Jadhav J. , Auer N., Hanscho M., Baumann M., Esteve-Codina A., Dabad M., Gómez J., Alioto T., Merkel A., Raineri E., Heath S., Rico D., Borth N. (2019) Epigenetic regulation of gene expression in Chinese Hamster Ovary cells in response to the changing environment of a batch culture. Biotechn. Bioeng. 116 (3), 677. doi: 10.1002/bit.26891

Klanert G., Bydlinski N. , Agu P., Diendorfer A.B., Hackl M., Hanscho M., Melcher M., Baumann M., Grillari J., Borth N. (2019) Transient manipulation of the expression level of selected growth rate correlating microRNAs does not increase growth rate in CHO-K1 cells (2019) J. Biotechn. 295, 63-70, doi: 10.1016/j.jbiotec.2019.02.011

Abreraa,A.T., Changa, H., Krachera, D.,  Ludwig, R., Haltrich, D. (2019) Characterization of pyranose oxidase variants for bioelectrocatalytic applications. BBA Proteins and Proteomics 1868. doi: 10.1016/j.bbapap.2019.140335

Reiter, K., Aguilar, P. P., Wetter, V., Steppert, P., Tover, A., Jungbauer, A. (2019) Separation of virus-like particles and extracellular vesicles by flow-through and heparin affinity chromatography. J. Chromatogr. A 1588, 77-84. doi: 10.1016/j.chroma.2018.12.035

Aguilar, P. P., Gonzalez-Dominguez, I., Schneider, T. A., Gotha, F., Cervera, L., Jungbauer, A. (2019) At-line multi-angle light scattering detector for faster process development in enveloped virus-like particle purification. J. Sep. Sci. 42, 2640-2649. doi: 10.1002/jssc.201900441

Nguyen, L. N., Baumann, M., Dhiman, H., Marx, N., Schmieder, V., Hussein, M., Eisenhut, P., Hernandez, I., Koehn, J., Borth, N. (2019) Novel Promoters Derived from Chinese Hamster Ovary Cells via In Silico and In Vitro Analysis. Biotechnol. J. 14. doi: 10.1002/Biot.201900125

Klanert, G., Fernandez, D. J., Weinguny, M., Eisenhut, P., Buhler, E., Melcher, M., Titus, S. A., Diendorfer, A. B., Gludovacz, E., Jadhav, V., Xiao, S., Stern, B., Lal, M., Shiloach, J., Borth, N. (2019) A cross-species whole genome siRNA screen in suspension- cultured Chinese hamster ovary cells identifies novel engineering targets. Sci. Rep. 9. doi: Artn 8689 10.1038/S41598-019-45159-2

Breslmayr, E., Daly, S., Pozgajcic, A., Chang, H. C., Rezic, T., Oostenbrink, C., Ludwig, R. (2019) Improved spectrophotometric assay for lytic polysaccharide monooxygenase. Biotechnol. Biofuels 12. doi: Artn 28310.1186/S13068-019-1624-3

Terlecki-Zaniewicz, L., Pils, V., Bobbili, M. R., Lammermann, I., Perrotta, I., Grillenberger, T., Schwestka, J., Weiss, K., Pum, D., Arcalis, E., Schwingenschuh, S., Birngruber, T., Brandstetter, M., Heuser, T., Schosserer, M., Morizot, F., Mildner, M., Stoger, E., Tschachler, E., Weinmullner, R., Gruber, F., Grillari, J. (2019) Extracellular Vesicles in Human Skin: Cross-Talk from Senescent Fibroblasts to Keratinocytes by miRNAs. J. Invest. Dermatol. 139, 2425-+. doi: 10.1016/j.jid.2019.05.015

Suleiman, E., Damm, D., Batzoni, M., Temchura, V., Wagner, A., Uberla, K., Vorauer-Uhl, K. (2019) Electrostatically Driven Encapsulation of Hydrophilic, Non-Conformational Peptide Epitopes into Liposomes. Pharmaceutics 11. doi: 10.3390/pharmaceutics11110619

Tarazona, A. A. P., Lobner, E., Taubenschmid, Y., Paireder, M., Acosta, J. A. T., Goritzer, K., Steinkellner, H., Mach, L. (2019) Steric Accessibility of the Cleavage Sites Dictates the Proteolytic Vulnerability of the Anti-HIV-1 Antibodies 2F5, 2G12, and PG9 in Plants. Biotechnol. J. doi: Artn190030810.1002/Biot.201900308

Laurent, C., Sun, P., Scheiblbrandner, S., Csarman, F., Cannazza, P., Frommhagen, M., van Berkel, W. J. H., Oostenbrink, C., Kabel, M. A., Ludwig, R. (2019) Influence of Lytic Polysaccharide Monooxygenase Active Site Segments on Activity and Affinity. Int. J. Mol. Sci. 20. doi: 10.3390/ijms20246219

Pfanzagl, V., Bellei, M., Hofbauer, S., Laurent, C. V. F. P., Furtmuller, P. G., Oostenbrink, C., Battistuzzi, G., Obinger, C. (2019) Redox thermodynamics of B-class dye-decolorizing peroxidases. J. Inorg. Biochem. 199. doi: UNSP 11076110.1016/j.jinorgbio.2019.110761

Gassler, T. ,Heistinger, L., Mattanovich, D., Gasser, B., Prielhofer, R. (2019) CRISPR/Cas9-Mediated Homology-Directed Genome Editing in Pichia pastoris. Methods Mol. Biol. 1923, 211-225. doi: 10.1007/978-1-4939-9024-5_9

Coats, M. T., Bydlinski, N., Maresch, D., Diendorfer, A., Klanert, G., Borth, N. (2019) mRNA Transfection into CHO-Cells Reveals Production Bottlenecks. Biotechnol. J. doi:Artn190019810.1002/Biot.201900198

Pereira Aguilar, P., Schneider, T. A., Wetter, V., Maresch, D., Ling, W. L., Tover, A., Steppert, P., Jungbauer, A. (2019) Polymer-grafted chromatography media for the purification of enveloped virus-like particles, exemplified with HIV-1 gag VLP. Vaccine 37, 7070-7080. doi: 10.1016/j.vaccine.2019.07.001

Göritzer, K., Turupcu, A., Maresch, D., Novak, J., Altmann, F., Oostenbrink, C., Obinger, C., Strasser, R. (2019) Distinct Fc alpha receptor N-glycans modulate the binding affinity to immunoglobulin A (IgA) antibodies. J. Biol. Chem. 294, 13995-14008. doi: 10.1074/jbc.RA119.009954

Paumann-Page, M., Tscheliessnig, R., Sevcnikar, B., Katz, R. S., Schwartz, I., Hofbauer, S., Pfanzagl, V., Furtmuller, P. G., Obinger, C. (2019) Monomeric and homotrimeric solution structures of truncated human peroxidasin 1 variants. Biochimica et biophysica acta. Proteins and proteomics  140249. doi: 10.1016/j.bbapap.2019.07.002

Milazzo, L., Gabler, T., Puhringer, D., Jandova, Z., Maresch, D., Michlits, H., Pfanzagl, V., Djinovic-Carugo, K., Oostenbrink, C., Furtmuller, P. G., Obinger, C., Smulevich, G., Hofbauer, S. (2019) Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Heme b. ACS Catal. 9, 6766-6782. doi: 10.1021/acscatal.9b00963

Schwaigerlehner, L., Mayrhofer, P., Diem, M., Steinfellner, W., Fenech, E., Oostenbrink, C., Kunert, R. (2019) Germinality does not necessarily define mAb expression and thermal stability. Appl. Microbiol. Biotechnol. 103, 7505-7518. doi: 10.1007/s00253-019-09998-3

Hager, F. F., Sutzl, L., Stefanovic, C., Blaukopf, M., Schäffer, C. (2019) Pyruvate Substitutions on Glycoconjugates. Int. J. Mol. Sci. 20. doi: 10.3390/ijms20194929

Olin-Sandoval, V., Yu, J. S. L., Miller-Fleming, L., Alam, M. T., Kamrad, S., Correia-Melo, C., Haas, R., Segal, J., Pena Navarro, D. A., Herrera-Dominguez, L., Mendez-Lucio, O., Vowinckel, J., Mulleder, M., Ralser, M. (2019) Lysine harvesting is an antioxidant strategy and triggers underground polyamine metabolism. Nature 572, 249-+. doi: 10.1038/s41586-019-1442-6

Montero-Morales, L., Maresch, D., Crescioli, S., Castilho, A., Llieva, K. M., Mele, S., Karagiannis, S. N., Altmann, F., Steinkellner, H. (2019) In Planta Glycan Engineering and Functional Activities of IgE Antibodies. Front. Bioeng. Biotechnol. 7. doi: Artn 24210.3389/Fbioe.2019.00242

Ma, S., Laurent, C. V. F. P., Meneghello, M., Tuoriniemi, J., Oostenbrink, C., Gorton, L., Bartlett, P. N., Ludwig, R. (2019) Direct Electron-Transfer Anisotropy of a Site-Specifically Immobilized Cellobiose Dehydrogenase. ACS Catal. 9, 7607-7615. doi: 10.1021/acscatal.9b02014

Heissenberger, C., Liendl, L., Nagelreiter, F., Gonskikh, Y., Yang, G., Stelzer, E. M., Krammer, T. L., Micutkova, L., Vogt, S., Kreil, D. P., Sekot, G., Siena, E., Poser, I., Harreither, E., Linder, A., Ehret, V., Helbich, T. H., Grillari-Voglauer, R., Jansen-Dürr, P., Kos, M., Polacek, N., Grillari, J., Schosserer, M. (2019) Loss of the ribosomal RNA methyltransferase NSUN5 impairs global protein synthesis and normal growth. Nucleic Acids Res. doi: 10.1093/nar/gkz1043

Nika, L., Cuadrado-Castano, S., Arunkumar, G. A., Grunwald-Gruber, C., McMahon, M., Koczka, K., Garcia-Sastre, A., Krammer, F., Grabherr, R. (2019) A HER2-Displaying Virus-Like Particle Vaccine Protects from Challenge with Mammary Carcinoma Cells in a Mouse Model. Vaccines-Basel 7. doi: Artn 4110.3390/Vaccines7020041

Sützl, L., Foley, G., Gillam, E. M. J., Boden, M., Haltrich, D. (2019) The GMC superfamily of oxidoreductases revisited: analysis and evolution of fungal GMC oxidoreductases. Biotechnol Biofuels 12, 118. doi: 10.1186/s13068-019-1457-0

Herzog, P. L., Sützl, L., Eisenhut, B., Maresch, D., Haltrich, D., Obinger, C., Peterbauer, C. K. (2019) Versatile Oxidase and Dehydrogenase Activities of Bacterial Pyranose 2-Oxidase Facilitate Redox Cycling with Manganese Peroxidase In Vitro. Appl. Environ. Microbiol. 85. doi: UNSP e00390-19 10.1128/AEM.00390-19

Foley, G., Sützl, L., D'Cunha, S. A., Gillam, E. M., Boden, M. (2019) SeqScrub: a web tool for automatic cleaning and annotation of FASTA file headers for bioinformatic applications. Biotechniques 67, 50-54. doi: 10.2144/btn-2018-0188

Schiavinato, M., Strasser, R., Mach, L., Dohm, J. C., Himmelbauer, H. (2019) Genome and transcriptome characterization of the glycoengineered Nicotiana benthamiana line Delta XT/FT. BMC Genomics 20. doi: Artn 594 10.1186/S12864-019-5960-2

Jandova, Z., Gill, S. C., Lim, N. M., Mobley, D. L., Oostenbrink, C. (2019) Binding Modes and Metabolism of Caffeine. Chem. Res. Toxicol. 32, 1374-1383. doi: 10.1021/acs.chemrestox.9b00030

Jandova, Z., Jespers, W., Sotelo, E., Gutierrez-de-Teran, H., Oostenbrink, C. (2019) Free-Energy Calculations for Bioisosteric Modifications of A3 Adenosine Receptor Antagonists. Int. J. Mol. Sci. 20. doi: 10.3390/ijms20143499

Turupcu, A., Diem, M., Smith, L. J., Oostenbrink, C. (2019) Structural Aspects of the O-glycosylation Linkage in Glycopeptides via MD Simulations and Comparison with NMR Experiments. Chemphyschem 20, 1527-1537. doi: 10.1002/cphc.201900079

Milazzo, L., Gabler, T., Pfanzagl, V., Michlits, H., Furtmuller, P. G., Obinger, C., Hofbauer, S., Smulevich, G. (2019) The hydrogen bonding network of coproheme in coproheme decarboxylase from Listeria monocytogenes: Effect on structure and catalysis. J. Inorg. Biochem. 195, 61-70. doi: 10.1016/j.jinorgbio.2019.03.009

Ilieva, K. M., Fazekas-Singer, J., Bax, H. J., Crescioli, S., Montero-Morales, L., Mele, S., Sow, H. S., Stavraka, C., Josephs, D. H., Spicer, J. F., Steinkellner, H., Jensen-Jarolim, E., Tutt, A. N. J., Karagiannis, S. N. (2019) AllergoOncology: Expression platform development and functional profiling of an anti-HER2 IgE antibody. Allergy. doi: 10.1111/all.13818

Laurent, C., Breslmayr, E., Tunega, D., Ludwig, R., Oostenbrink, C. (2019) Interaction between Cellobiose Dehydrogenase and Lytic Polysaccharide Monooxygenase. Biochemistry. doi: 10.1021/acs.biochem.8b01178

Koczka, K., Ernst, W., Palmberger, D., Klausberger, M., Nika, L., Grabherr, R. (2019) Development of a Dual-Vector System Utilizing MicroRNA Mimics of the Autographa californica miR-1 for an Inducible Knockdown in Insect Cells. Int. J. Mol. Sci. 20. doi: 10.3390/ijms20030533

Hennicke, J., Reinhart, D., Altmann, F., Kunert, R. (2019) Impact of temperature and pH on recombinant human IgM quality attributes and productivity. N. Biotechnol. doi: 10.1016/j.nbt.2019.01.001

Martini, F., Eckmair, B., Stefanic, S., Jin, C., Garg, M., Yan, S., Jimenez-Castells, C., Hykollari, A., Neupert, C., Venco, L., Varon Silva, D., Wilson, I. B. H., Paschinger, K. (2019) Highly modified and immunoactive N-glycans of the canine heartworm. Nat. Commun. 10, 75. doi: 10.1038/s41467-018-07948-7

2018

Ata Ö., Rebnegger C. , Tatto N.E., Valli M., Mairinger T., Hann S. , Steiger M.G., Çalık P., Mattanovich D. (2018) A single Gal4-like transcription factor activates the Crabtree effect in Komagataella phaffii. Nat Commun. 9,4911. doi: 10.1038/s41467-018-07430-4

Maurer, M., Hansen, N., Oostenbrink, C. (2018) Comparison of free-energy methods using a tripeptide-water model system. J. Comput. Chem. 39, 2226-2242. doi: 10.1002/jcc.25537

Brey, C. U., Proff, J., Teufert, N., Salzer, B., Brozy, J., Munz, M., Pendzialek, J., Ensser, A., Holter, W., Lehner, M. (2018) A gB/CD3 bispecific BiTE antibody construct for targeting Human Cytomegalovirus-infected cells. Sci. Rep. 8, 17453. doi: 10.1038/s41598-018-36055-2

Hykollari, A., Malzl, D., Eckmair, B., Vanbeselaere, J., Scheidl, P., Jin, C., Karlsson, N. G., Wilson, I. B. H., Paschinger, K. (2018) Isomeric Separation and Recognition of Anionic and Zwitterionic N-glycans from Royal Jelly Glycoproteins. Mol. Cell. Proteomics 17, 2177-2196. doi: 10.1074/mcp.RA117.000462

Hernandez, I., Dhiman, H., Klanert, G., Jadhav, V., Auer, N., Hanscho, M., Baumann, M., Esteve-Codina, A., Dabad, M., Gomez, J., Alioto, T., Merkel, A., Raineri, E., Heath, S., Rico, D., Borth, N. (2018) Epigenetic regulation of gene expression in Chinese Hamster Ovary cells in response to the changing environment of a batch culture. Biotechnol. Bioeng. doi: 10.1002/bit.26891

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

Proff, J., Walterskirchen, C., Brey, C., Geyeregger, R., Full, F., Ensser, A., Lehner, M., Holter, W. (2016) Cytomegalovirus-Infected Cells Resist T Cell Mediated Killing in an HLA-Recognition Independent Manner. Front. Microbiol. 7. doi: 10.3389/Fmicb.2016.00844

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

Weilner, S., Skalicky, S., Salzer, B., Keider, V., Wagner, M., Hildner, F., Gabriel, C., Dovjak, P., Pietschmann, P., Grillari-Voglauer, R., Grillari, J., Hackl, M. (2015) Differentially circulating miRNAs after recent osteoporotic fractures can influence osteogenic differentiation. Bone 79, 43-51. doi: 10.1016/j.bone.2015.05.027

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