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G. Jakab, Bogdán, D., Mazák, K., Deme, R., Mucsi, Z., Mándity, I. M., Noszál, B., Kállai-Szabó, N., and Antal, I., Physicochemical Profiling of Baicalin Along with the Development and Characterization of Cyclodextrin Inclusion Complexes, AAPS PharmSciTech, vol. 20, no. 8, p. 314, 2019.
A. Jakli, Taushanoff, S., Molnár, M., Bóta, A., Kalman, E., and Varga, Z., Method for preparing anisotropic particles and devices thereof. US Patent 8,263,029, 2012.
C. Jiang, Séquaris, J. - M., Wacha, A., Bóta, A., Vereecken, H., and Klumpp, E., Effect of metal oxide on surface area and pore size of water-dispersible colloids from three German silt loam topsoils, Geoderma, vol. 235-236, pp. 260 - 270, 2014.
J. R. Johansson, Hermansson, E., Nordén, B., Kann, N., and Beke-Somfai, T., δ-Peptides from RuAAC-derived 1,5-disubstituted triazole units, European Journal of Organic Chemistry, vol. 2014, no. 13, pp. 2703 - 2713, 2014.
J. R. Johansson, Beke-Somfai, T., Stålsmeden, A. Said, and Kann, N., Ruthenium-Catalyzed Azide Alkyne Cycloaddition Reaction: Scope, Mechanism, and Applications, Chemical reviews, vol. 116, pp. 14726–14768, 2016.
F. Jonsson, Beke-Somfai, T., Andréasson, J., and Nordén, B., Interactions of a photochromic spiropyran with liposome model membranes, Langmuir, vol. 29, no. 7, pp. 2099 - 2103, 2013.
S. Juhas, Harris, N., Il’kova, G., Rehák, P., Zsila, F., Kogan, F. Yurgenzon, Lahmy, O., Zhuk, R., Gregor, P., and Koppel, J., RX-207, a small molecule inhibitor of protein interaction with glycosaminoglycans (SMIGs), reduces experimentally induced inflammation and increases survival rate in cecal ligation and puncture (CLP)-induced sepsis, Inflammation, vol. 41, pp. 307–314, 2018.
S. Juhas, Harris, N., Il’kova, G., Rehák, P., Zsila, F., Kogan, F. Yurgenzon, Lahmy, O., Zhuk, R., Gregor, P., and Koppel, J., RX-207, a Small Molecule Inhibitor of Protein Interaction with Glycosaminoglycans (SMIGs), Reduces Experimentally Induced Inflammation and Increases Survival Rate in Cecal Ligation and Puncture (CLP)-Induced Sepsis, Inflammation, pp. 1–8, 2017.
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.
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.
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.
L. Juhász, Szilágyi, L., Antus, S., Visy, J., Zsila, F., and Simonyi, M., New insight into the mechanism of hypervalent iodine oxidation of flavanones, Tetrahedron, vol. 58, no. 21, pp. 4261 - 4265, 2002.
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.
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.