Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Nataliya S. Myshakina"'
Publikováno v:
ACS Infect Dis
The ribonuclease H (RNH) activity of HIV-1 reverse transcriptase (RT) is essential for viral replication and can be a target for drug development. Yet, no RNH inhibitor to date has substantial antiviral activity to allow advancement into clinical dev
Autor:
Stefan G. Sarafianos, Nataliya S. Myshakina, Lena Miller, Jing Tang, Andrew D. Huber, Sanjeev Kumar V. Vernekar, Michael A. Parniak, Yue-Lei Chen, Zhengqiang Wang
Publikováno v:
European Journal of Medicinal Chemistry. 133:85-96
Human immunodeficiency virus (HIV) reverse transcriptase (RT) associated ribonuclease H (RNase H) remains the only virally encoded enzymatic function not clinically validated as an antiviral target. 2-Hydroxyisoquinoline-1,3-dione (HID) is known to c
Autor:
I. B. L’vov, Vladimir V. Korochentsev, Vitaliy V. Vovna, Aleksandr A. Komissarov, Nataliya S. Myshakina
Publikováno v:
Journal of Molecular Structure. 1099:579-587
Using ultraviolet photoelectron spectroscopy and electron density functional theory (DFT), we investigated the electronic structure of the d8 complex acetylacetonate Ni(a≿а≿)2 and its NH, S and NCH2-substitutes: nickel bis(acetylacetoneiminate)
Autor:
David Punihaole, Ryan S. Jakubek, Nataliya S. Myshakina, Sanford A. Asher, Steven J. Geib, Elizabeth M. Dahlburg, Zhenmin Hong
Publikováno v:
The Journal of Physical Chemistry B. 119:3931-3939
We investigated the normal mode composition and the aqueous solvation dependence of the primary amide vibrations of propanamide. Infrared, normal Raman, and UV resonance Raman (UVRR) spectroscopy were applied in conjunction with density functional th
Autor:
Jing Tang, Michael A. Parniak, Andrew D. Huber, Jayakanth Kankanala, Daniel J. Wilson, Karen A. Kirby, Stefan G. Sarafianos, Zhengqiang Wang, Sanjeev Kumar V. Vernekar, Bulan Wu, Mary C. Casey, Nataliya S. Myshakina
Publikováno v:
Journal of medicinal chemistry. 60(12)
Human immunodeficiency virus (HIV) reverse transcriptase (RT)-associated ribonuclease H (RNase H) remains the only virally encoded enzymatic function yet to be exploited as an antiviral target. One of the possible challenges may be that targeting HIV
Autor:
Tatiana V Ilina, Michael A. Parniak, Eddy Arnold, Daniel M. Himmel, William C. Ho, Alexander Van Ry, Nataliya S. Myshakina
Publikováno v:
Journal of Molecular Biology. 426:2617-2631
Human immunodeficiency virus (HIV) encodes four essential enzymes: protease, integrase, reverse transcriptase (RT)-associated DNA polymerase, and RT-associated ribonuclease H (RNase H). Current clinically approved anti-AIDS drugs target all HIV enzym
Autor:
Rieko Ishima, Nataliya S. Myshakina, Martin T. Christen, Jinwoo Ahn, Michael A. Parniak, Lakshmi Menon
Publikováno v:
Chemical Biology & Drug Design. 80:706-716
HIV-1 reverse transcriptase (RT) has been an attractive target for the development of antiretroviral agents. Although this enzyme is bi-functional, having both DNA polymerase and ribonuclease H (RNH) activities, there is no clinically approved inhibi
Publikováno v:
The Journal of Physical Chemistry B. 112:11873-11877
The effect of hydrogen bonding on the amide group vibrational spectra has traditionally been rationalized by invoking a resonance model where hydrogen bonding impacts the amide functional group by stabilizing its [(-)O-C=NH (+)] structure over the [O
Autor:
Nataliya S. Myshakina, Tatiana V Ilina, Michael A. Parniak, Venkata Ramana Sirivolu, Sanjeev Kumar V. Vernekar, Zhengqiang Wang
3’-Azidothymidine (AZT) was the first approved antiviral for the treatment of human immunodeficiency virus (HIV). Reported efforts in clicking the 3’-azido group of AZT have not yielded 1,2,3-triazoles active against HIV or any other viruses. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0398dea2e11d802a19ce8827ec88493
https://europepmc.org/articles/PMC4027054/
https://europepmc.org/articles/PMC4027054/
Autor:
I. B. L’vov, Vitaliy I. Vovna, Vladimir V. Korochentsev, Nataliya S. Myshakina, Alexander A. Komissarov
Publikováno v:
Journal of Molecular Structure. 1104:96