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Binding of V<sup>IV</sup>O<sup>2+</sup>, V<sup>IV</sup>OL, V<sup>IV</sup>OL<sub>2</sub> and V<sup>V</sup>O<sub>2</sub>L moieties to proteins: X-ray/theoretical characterization and biological implications
Santos, M. F. A., Sciortino, G., Correia, I., Fernandes, A. C. P., Santos-Silva, T., Pisanu, F., … Costa Pessoa, J. (2022). Binding of VIVO2+, VIVOL, VIVOL2 and VVO2L moieties to proteins: X-ray/theoretical characterization and biological implications. Chemistry: A European Journal, 28(40), e202200105 (8 pp.). https://doi.org/10.1002/chem.202200105
Promising non-cytotoxic monosubstituted chalcones to target monoamine oxidase-B
Iacovino, L. G., Pinzi, L., Facchetti, G., Bortolini, B., Christodoulou, M. S., Binda, C., … Dalla Via, L. (2021). Promising non-cytotoxic monosubstituted chalcones to target monoamine oxidase-B. ACS Medicinal Chemistry Letters, 12(7), 1151-1158. https://doi.org/10.1021/acsmedchemlett.1c00238
Structure-activity relationships, biological evaluation and structural studies of novel pyrrolonaphthoxazepines as antitumor agents
Brindisi, M., Ulivieri, C., Alfano, G., Gemma, S., de Asís Balaguer, F., Khan, T., … Brogi, S. (2019). Structure-activity relationships, biological evaluation and structural studies of novel pyrrolonaphthoxazepines as antitumor agents. European Journal of Medicinal Chemistry, 162, 290-320. https://doi.org/10.1016/j.ejmech.2018.11.004
Design, synthesis, structure-activity relationships and X-ray structural studies of novel 1-oxopyrimido[4,5-&lt;em&gt;c&lt;/em&gt;]quinoline-2-acetic acid derivatives as selective and potent inhibitors of human aldose reductase
Crespo, I., Giménez-Dejoz, J., Porté, S., Cousido-Siah, A., Mitschler, A., Podjarny, A., … Farrés, J. (2018). Design, synthesis, structure-activity relationships and X-ray structural studies of novel 1-oxopyrimido[4,5-c]quinoline-2-acetic acid derivatives as selective and potent inhibitors of human aldose reductase. European Journal of Medicinal Chemistry, 152, 160-174. https://doi.org/10.1016/j.ejmech.2018.04.015
Crystal structure of the deglycating enzyme Amadoriase I in its free form and substrate-bound complex
Rigoldi, F., Gautieri, A., Dalle Vedove, A., Lucarelli, A. P., Vesentini, S., & Parisini, E. (2016). Crystal structure of the deglycating enzyme Amadoriase I in its free form and substrate-bound complex. Proteins, 84(6), 744-758. https://doi.org/10.1002/prot.25015
Ribose-protonated DNA base excision repair: a combined theoretical and experimental study
Sadeghian, K., Flaig, D., Blank, I. D., Schneider, S., Strasser, R., Stathis, D., … Ochsenfeld, C. (2014). Ribose-protonated DNA base excision repair: a combined theoretical and experimental study. Angewandte Chemie International Edition, 53(38), 10044-10048. https://doi.org/10.1002/anie.201403334
Crystal structure of HIV-1 reverse transcriptase bound to a non-nucleoside inhibitor with a novel mechanism of action
Freisz, S., Bec, G., Radi, M., Wolff, P., Crespan, E., Angeli, L., … Ennifar, E. (2010). Crystal structure of HIV-1 reverse transcriptase bound to a non-nucleoside inhibitor with a novel mechanism of action. Angewandte Chemie International Edition, 49(10), 1805-1808. https://doi.org/10.1002/anie.200905651