Zobrazeno 1 - 10
of 246
pro vyhledávání: '"Marjana Novič"'
Autor:
Janja Sluga, Tihomir Tomašič, Marko Anderluh, Martina Hrast Rambaher, Gregor Bajc, Alen Sevšek, Nathaniel I. Martin, Roland J. Pieters, Marjana Novič, Katja Venko
Publikováno v:
Antibiotics, Vol 13, Iss 8, p 751 (2024)
Bacteria are capable of remarkable adaptations to their environment, including undesirable bacterial resistance to antibacterial agents. One of the most serious cases is an infection caused by multidrug-resistant Staphylococcus aureus, which has unfo
Externí odkaz:
https://doaj.org/article/a64f174040894b3aa54b7e163275ddbd
Publikováno v:
International Journal of Molecular Sciences, Vol 25, Iss 8, p 4156 (2024)
Artificial neural networks (ANNs) are nowadays applied as the most efficient methods in the majority of machine learning approaches, including data-driven modeling for assessment of the toxicity of chemicals. We developed a combined neural network me
Externí odkaz:
https://doaj.org/article/8375993fbb444d4dab4c62afb87629ce
Autor:
Ramon Carbó-Dorca
Publikováno v:
Journal of Computational Chemistry. 40:1880-1880
Autor:
Natalja Fjodorova, Marjana Novič, Katja Venko, Bakhtiyor Rasulev, Melek Türker Saçan, Gulcin Tugcu, Safiye Sağ Erdem, Alla P. Toropova, Andrey A. Toropov
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 18, p 14160 (2023)
Fullerene derivatives (FDs) are widely used in nanomaterials production, the pharmaceutical industry and biomedicine. In the present study, we focused on the potential toxic effects of FDs on the aquatic environment. First, we analyzed the binding af
Externí odkaz:
https://doaj.org/article/cf06117e3ca8492fa32f34dea509bca9
Akademický článek
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Autor:
Natalja Fjodorova, Marjana Novič, Katja Venko, Viktor Drgan, Bakhtiyor Rasulev, Melek Türker Saçan, Safiye Sağ Erdem, Gulcin Tugcu, Alla P. Toropova, Andrey A. Toropov
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 20, Iss , Pp 913-924 (2022)
Fullerene derivatives (FDs) belong to a relatively new family of nano-sized organic compounds. They are widely applied in materials science, pharmaceutical industry, and (bio) medicine. This research focused on the study of FDs in terms of their pote
Externí odkaz:
https://doaj.org/article/4ddd56cc32f4403e830d0fcc7923b78c
Autor:
Liadys Mora Lagares, Marjana Novič
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 23, p 14804 (2022)
ABC transporters play a critical role in both drug bioavailability and toxicity, and with the discovery of the P-glycoprotein (P-gp), this became even more evident, as it plays an important role in preventing intracellular accumulation of toxic compo
Externí odkaz:
https://doaj.org/article/024e8d77b92f42239edea16661039945
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 14 (2021)
Besides amyloid fibrils, amyloid pores (APs) represent another mechanism of amyloid induced toxicity. Since hypothesis put forward by Arispe and collegues in 1993 that amyloid-beta makes ion-conducting channels and that Alzheimer's disease may be due
Externí odkaz:
https://doaj.org/article/503d9970a8db4682825636f85eb5c465
Autor:
Jure Borišek, Sara Pintar, Mitja Ogrizek, Simona Golič Grdadolnik, Vesna Hodnik, Dušan Turk, Andrej Perdih, Marjana Novič
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 33, Iss 1, Pp 1239-1247 (2018)
Autolysin E (AtlE) is a cell wall degrading enzyme that catalyzes the hydrolysis of the β-1,4-glycosidic bond between the N-acetylglucosamine and N-acetylmuramic acid units of the bacterial peptidoglycan. Using our recently determined crystal struct
Externí odkaz:
https://doaj.org/article/183744445d2b4e33acfeefddb1bf33c9
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 1, p 362 (2021)
P-Glycoprotein (P-gp) is a transmembrane protein belonging to the ATP binding cassette superfamily of transporters, and it is a xenobiotic efflux pump that limits intracellular drug accumulation by pumping compounds out of cells. P-gp contributes to
Externí odkaz:
https://doaj.org/article/3cdc88b91c1b4abe85a911a567a7dbb2