Synthesis, cytotoxic activity and DNA interaction studies of new dinuclear platinum(ii) complexes with an aromatic 1,5-naphthyridine bridging ligand: DNA binding mode of polynuclear platinum(ii) complexes in relation to the complex structure

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.

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.


2020 ◽  
Vol 49 (45) ◽  
pp. 16498-16514
Author(s):  
Juliana P. da Silva ◽  
Otávio Fuganti ◽  
M. Gabriela Kramer ◽  
Gianella Facchin ◽  
Lucas E. N. Aquino ◽  
...  

Electrochemical/chemical, cytotoxic and DNA interaction studies of P–NR–P containing ruthenium–cymene complexes [RuCl(η6-p-cymene)(P–NR–P)]X.


2017 ◽  
Vol 46 (11) ◽  
pp. 3611-3622 ◽  
Author(s):  
Héctor J. Lozano ◽  
Natalia Busto ◽  
Gustavo Espino ◽  
Arancha Carbayo ◽  
José M. Leal ◽  
...  

The quinones naphthazarin and quinizarin intercalate into DNA whereas their p-cymene di-ruthenium(ii) complexes bind covalently via interstrand crosslinking.


2013 ◽  
Vol 64 ◽  
pp. 228-238 ◽  
Author(s):  
Violeta Marković ◽  
Ana Janićijević ◽  
Tatjana Stanojković ◽  
Branka Kolundžija ◽  
Dušan Sladić ◽  
...  

2014 ◽  
Vol 21 (26) ◽  
pp. 3081-3094 ◽  
Author(s):  
M. Ashfaq ◽  
T. Najam ◽  
S.S.A. Shah ◽  
M.M. Ahmad ◽  
S. Shaheen ◽  
...  

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 ◽  
...  

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