Tünde Juhász

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Journal Article
M. Ricci, Horváti, K., Juhász, T., Szigyarto, I., Török, G., Sebák, F., Bodor, A., Homolya, L., Henczkó, J., Pályi, B., Mlinkó, T., Mihály, J., Nizami, B., Yang, Z., Lin, F., Lu, X., Románszki, L., Bóta, A., Varga, Z., Bosze, S., Zsila, F., and Beke-Somfai, T., Anionic food color tartrazine enhances antibacterial efficacy of histatin-derived peptide DHVAR4 by fine-tuning its membrane activity, Quarterly Reviews of Biophysics, vol. 53, 2020.
I. Cs. Szigyártó, Mihály, J., Wacha, A., Bogdán, D., Juhász, T., Kohut, G., Schlosser, G., Zsila, F., Urlacher, V., Varga, Z., Fülöp, F., Bóta, A., Mándity, I., and Beke-Somfai, T., Membrane active Janus-oligomers of β $^\textrm3$ -peptides, Chemical Science, vol. 11, pp. 6868–6881, 2020.
I. Nekkaa, Bogdán, D., Gáti, T., Béni, S., Juhász, T., Palkó, M., Paragi, G., Tóth, G. K., Fülöp, F., and Mándity, I. M., Flow-chemistry enabled efficient synthesis of β-peptides: backbone topology vs. helix formation, Chemical communications, vol. 55, pp. 3061–3064, 2019.
M. Quemé-Peña, Juhász, T., Mihály, J., Szigyártó, I. Csilla, Horváti, K., Bosze, S., Henczkó, J., Pályi, B., Németh, C., Varga, Z., Zsila, F., and Beke-Somfai, T., Manipulating Active Structure and Function of Cationic Antimicrobial Peptide CM15 by the Polysulfonated Drug Suramin: A Step Closer to in vivo Complexity, ChemBioChem, 2019.
G. Kohut, Sieradzan, A., Zsila, F., Juhász, T., Bosze, S., Liwo, A., Samsonov, S. A., and Beke-Somfai, T., The molecular mechanism of structural changes in the antimicrobial peptide CM15 upon complex formation with drug molecule suramin: a computational analysis, Physical Chemistry Chemical Physics, vol. 21, pp. 10644–10659, 2019.
F. Zsila, Juhász, T., Bősze, S., Horváti, K., and Beke-Somfai, T., Hemin and bile pigments are the secondary structure regulators of intrinsically disordered antimicrobial peptides, CHIRALITY, vol. 30, pp. 195–205, 2018.
F. Zsila, Juhász, T., Kohut, G., and Beke-Somfai, T., Heparin and Heparan Sulfate Binding of the Antiparasitic Drug Imidocarb: Circular Dichroism Spectroscopy, Isothermal Titration Calorimetry, and Computational Studies, JOURNAL OF PHYSICAL CHEMISTRY B, vol. 122, pp. 1781–1791, 2018.
T. Juhász, Mihály, J., Kohut, G., Németh, C., Liliom, K., and Beke-Somfai, T., The lipid mediator lysophosphatidic acid induces folding of disordered peptides with basic amphipathic character into rare conformations, Scientific Reports, vol. 8, 2018.
V. Papp-Kádár, Balázs, Z., Nagy, G. N., Juhász, T., Liliom, K., and Vértessy, B. G., Functional Analysis on a Naturally Occurring Variant of the Staphylococcus Aureus Uracil DNA Glycosylase Inhibitor, Periodica Polytechnica Chemical Engineering, 2017.
K. Koprivanacz, Tőke, O., Besztercei, B., Juhász, T., Radnai, L., Merő, B., Mihály, J., Péter, M., Balogh, G., Vígh, L., Buday, L., and Liliom, K., The {SH3} domain of Caskin1 binds to lysophosphatidic acid suggesting a direct role for the lipid in intracellular signaling, Cellular Signalling, vol. 32, pp. 66 - 75, 2017.
K. Koprivanacz, Tőke, O., Besztercei, B., Juhász, T., Radnai, L., Merő, B., Mihály, J., Péter, M., Balogh, G., and Vígh, L., The SH3 domain of Caskin1 binds to lysophosphatidic acid suggesting a direct role for the lipid in intracellular signaling, Cellular signalling, vol. 32, pp. 66–75, 2017.
M. Morawski, Nuytens, K., Juhász, T., Zeitschel, U., Seeger, G., Waelkens, E., Regal, L., Schulz, I., Arendt, T., Szeltner, Z., Creemers, J., and Roßner, S., Cellular and ultra structural evidence for cytoskeletal localization of prolyl endopeptidase-like protein in neurons, NeuroscienceNeuroscience, vol. 242, pp. 128-139, 2013.
Z. Szeltner, Juhász, T., Szamosi, I., Rea, D., Fülöp, V., Módos, K., Juliano, L., and Polgár, L., The loops facing the active site of prolyl oligopeptidase are crucial components in substrate gating and specificity, Biochimica et Biophysica Acta (BBA) - Proteins and ProteomicsBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol. 1834, no. 1, pp. 98-111, 2013.
K. Kaszuba, Róg, T., Danne, R., Canning, P., Fülöp, V., Juhász, T., Szeltner, Z., Pierre, J. - F. St., García-Horsman, A., Männistö, P. T., Karttunen, M., Hokkanen, J., and Bunker, A., Molecular dynamics, crystallography and mutagenesis studies on the substrate gating mechanism of prolyl oligopeptidase, BiochimieBiochimie, vol. 94, no. 6, pp. 1398-1411, 2012.
Z. Szeltner, Morawski, M., Juhász, T., Szamosi, I., Liliom, K., Csizmók, V., Tölgyesi, F., and Polgár, L., GAP43 shows partial co-localisation but no strong physical interaction with prolyl oligopeptidase, Biochimica et Biophysica Acta (BBA) - Proteins and ProteomicsBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol. 1804, no. 12, pp. 2162-2176, 2010.
D. N. Okamoto, Oliveira, L. C. G., Kondo, M. Y., Cezari, M. H. S., Szeltner, Z., Juhász, T., Juliano, M. A., Polgár, L., Juliano, L., and Gouvea, I. E., Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition, Biological ChemistryBiological Chemistry, vol. 391, no. 12, 2010.
A. L. Kiss, Hornung, B., Rádi, K., Gengeliczki, Z., Sztáray, B., Juhász, T., Szeltner, Z., Harmat, V., and Polgár, L., The Acylaminoacyl Peptidase from Aeropyrum pernix K1 Thought to Be an Exopeptidase Displays Endopeptidase Activity, Journal of Molecular BiologyJournal of Molecular Biology, vol. 368, no. 2, pp. 509-520, 2007.
T. Juhász, Szeltner, Z., and Polgár, L., Truncated prolyl oligopeptidase from Pyrococcus furiosus, Proteins: Structure, Function, and BioinformaticsProteins: Structure, Function, and Bioinformatics, vol. 69, no. 3, pp. 633-643, 2007.
I. E. Gouvea, Judice, W. A. S., Cezari, M. H. S., Juliano, M. A., Juhász, T., Szeltner, Z., Polgár, L., and Juliano, L., Kosmotropic Salt Activation and Substrate Specificity of Poliovirus Protease 3C , BiochemistryBiochemistry, vol. 45, no. 39, pp. 12083-12089, 2006.
T. Juhász, Szeltner, Z., and Polgár, L., Properties of the prolyl oligopeptidase homologue from Pyrococcus furiosus, FEBS LettersFEBS Letters, vol. 580, no. 14, pp. 3493-3497, 2006.
M. Fuxreiter, Magyar, C., Juhász, T., Szeltner, Z., Polgár, L., and Simon, I., Flexibility of prolyl oligopeptidase: Molecular dynamics and molecular framework analysis of the potential substrate pathways, Proteins: Structure, Function, and BioinformaticsProteins: Structure, Function, and Bioinformatics, vol. 60, no. 3, pp. 504-512, 2005.
Z. Szeltner, Alshafee, I., Juhász, T., Parvari, R., and Polgár, L., The PREPL A protein, a new member of the prolyl oligopeptidase family, lacking catalytic activity, Cellular and Molecular Life SciencesCellular and Molecular Life Sciences, vol. 62, no. 19-20, pp. 2376-2381, 2005.
T. Juhász, Szeltner, Z., Fülöp, V., and Polgár, L., Unclosed β-Propellers Display Stable Structures: Implications for Substrate Access to the Active Site of Prolyl Oligopeptidase, Journal of Molecular BiologyJournal of Molecular Biology, vol. 346, no. 3, pp. 907-917, 2005.
Z. Szeltner, Rea, D., Juhász, T., Renner, V., Fülöp, V., and Polgár, L., Concerted Structural Changes in the Peptidase and the Propeller Domains of Prolyl Oligopeptidase are Required for Substrate Binding, Journal of Molecular BiologyJournal of Molecular Biology, vol. 340, no. 3, pp. 627-637, 2004.
T. Juhász, Szeltner, Z., Renner, V., and Polgár, L., Role of the Oxyanion Binding Site and Subsites S1 and S2 in the Catalysis of Oligopeptidase B, a Novel Target for Antimicrobial Chemotherapy, BiochemistryBiochemistry, vol. 41, no. 12, pp. 4096-4106, 2002.

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