Фізико-хімічний інститут ім. О.В. Богатського НАН України, Україна

Доктор біологічних наук, професор, головний науковий співробітник, академік НАМН України

 

Профіль Scopus: посилання

Researcher ID: L-2253-2018

ID ORCID: http://orcid.org/0000-0003-1485-128X

 

Selected Publications:

1. Golovenko, M., Reder, A., Zupanets, I., Bezugla, N., Larionov, V., Valivodz`, I. (2023). A Phase I study evaluating the pharmacokinetic profile of a novel oral analgesic propoxazepam. Journal of Pre-Clinical and Clinical Research, 17 (3), 138–144. https://doi.org/10.26444/jpccr/169426
   
   
2. Larionov, V., Golovenko, M., Kyz’min, V., Valivodz’, I., Nefedov, O. (2023). Propoxazepam interaction with cytochromes p450 isoforms based on molecular docking analysis. Reports of the National Academy of Sciences of Ukraine, 3, 96–104.  https://doi.org/10.15407/dopovidi2023.03.096
   
   
3. Golovenko, M. Ya. (2022). Cation channels - molecular targets for potential drugs with an analgesic mechanism of action. Fiziolohichnyĭ Zhurnal, 68 (5), 89–103. https://doi.org/10.15407/fz68.05.089
   
   
4. Golovenko, M. Ya., Reder, A. S., Larionov, V. B., Andronati, S. A., Akisheva, A. S. (2022). Cross-species differential plasma protein binding of Propoxazepam, a novel analgesic agent. Biopolymers and Cell, 37 (6), 459–468. https://doi.org/10.7124/bc.000a68
   
   
5. Golovenko, M. Y., Larionov, V. B., Reder, A. S., Andronati, S. A., Valivodz’, I. P., Yurpalova, T. O. (2018). Pharmacodynamics of Interaction between Propoxazepam and a GABA-Benzodiazepine Receptor-Ionofor Complex. Neurophysiology, 50 (1), 2–10. http://doi.org/10.1007/s11062-018-9711-9
   
   
6. Polishchuk, P. G., Kosinskaya, A. P., Larionov, V. B., Ognichenko, L. N., Kuz’min, V. E., Golovenko, N. Y. (2017). A Ranged Series of Drug Molecule Fragments Defining Their Neuroavailability. Pharmaceutical Chemistry Journal, 51 (1), 35–38. http://doi.org/10.1007/s11094-017-1553-z
   
   
7. Golovenko, M. Y., Larionov, V. B. (2014). Kinetics of hydrolysis of 1,4-benzodiazepine derivative by carboxylesterases in mice organism. The Ukrainian Biochemical Journal, 86 (4), 150–157.  http://doi.org/10.15407/ubj86.04.150