Publications of BioToP PhD-Students

(Highlighted are BioToP students and BioToP faculty members)


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


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

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

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

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


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


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

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