DNA interaction studies of a platinum (II) complex containing an antiviral drug, ribavirin: The effect of metal on DNA binding

Author(s):  
Nahid Shahabadi ◽  
Zeinab Mirzaei kalar ◽  
Neda Hosseinpour Moghadam
MedChemComm ◽  
2018 ◽  
Vol 9 (10) ◽  
pp. 1679-1697 ◽  
Author(s):  
Katarina Jakovljević ◽  
Milan D. Joksović ◽  
Ivana Z. Matić ◽  
Nina Petrović ◽  
Tatjana Stanojković ◽  
...  

1,3,4-Thiadiazole compounds containing catechol moiety and chalcone motif are synthesized and examined for antioxidant activity, cytotoxicity and DNA-binding activity.


RSC Advances ◽  
2016 ◽  
Vol 6 (77) ◽  
pp. 73605-73616 ◽  
Author(s):  
Nahid Shahabadi ◽  
Monireh Falsafi ◽  
Foroozan Feizi ◽  
Reza Khodarahmi

The aim of this study was to design and prepare γ-Fe2O3@SiO2-zidovudine magnetic nanoparticles (MNPs) for magnetic guided drug targeting and biological applications.


2018 ◽  
Vol 47 (42) ◽  
pp. 15091-15102 ◽  
Author(s):  
Bata Konovalov ◽  
Marija D. Živković ◽  
Jelena Z. Milovanović ◽  
Dragana B. Djordjević ◽  
Aleksandar N. Arsenijević ◽  
...  

[{Pt(L)Cl}2(μ-1,5-nphe)]2+ complexes have been reported.


2012 ◽  
Vol 31 (5) ◽  
pp. 876-882 ◽  
Author(s):  
Nahid Shahabadi ◽  
Zeinab Mirzaei kalar ◽  
Asad Vaisi-Raygani

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Christopher R. Horne ◽  
Hariprasad Venugopal ◽  
Santosh Panjikar ◽  
David M. Wood ◽  
Amy Henrickson ◽  
...  

AbstractBacteria respond to environmental changes by inducing transcription of some genes and repressing others. Sialic acids, which coat human cell surfaces, are a nutrient source for pathogenic and commensal bacteria. The Escherichia coli GntR-type transcriptional repressor, NanR, regulates sialic acid metabolism, but the mechanism is unclear. Here, we demonstrate that three NanR dimers bind a (GGTATA)3-repeat operator cooperatively and with high affinity. Single-particle cryo-electron microscopy structures reveal the DNA-binding domain is reorganized to engage DNA, while three dimers assemble in close proximity across the (GGTATA)3-repeat operator. Such an interaction allows cooperative protein-protein interactions between NanR dimers via their N-terminal extensions. The effector, N-acetylneuraminate, binds NanR and attenuates the NanR-DNA interaction. The crystal structure of NanR in complex with N-acetylneuraminate reveals a domain rearrangement upon N-acetylneuraminate binding to lock NanR in a conformation that weakens DNA binding. Our data provide a molecular basis for the regulation of bacterial sialic acid metabolism.


2019 ◽  
Vol 496 ◽  
pp. 119048
Author(s):  
Erum Jabeen ◽  
Naveed Kausar Janjua ◽  
Safeer Ahmed ◽  
Iftikhar Tahiri ◽  
Muhammad Kashif ◽  
...  

Polyhedron ◽  
1996 ◽  
Vol 15 (5-6) ◽  
pp. 765-774 ◽  
Author(s):  
Sharada P. Kaiwar ◽  
Alavattam Sreedhara ◽  
Meenakshi S.S. Raghavan ◽  
Chebrolu P. Rao ◽  
Vasant Jadhav ◽  
...  

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