Effect of N(4)-Phenyl Substitution in 2-Oxo-1,2-dihydroquinoline-3-carbaldehyde Semicarbazones on the Structure, DNA/Protein Interaction, and Antioxidative and Cytotoxic Activity of Cu(II) Complexes

2011 ◽  
Vol 50 (24) ◽  
pp. 12852-12866 ◽  
Author(s):  
Duraisamy Senthil Raja ◽  
Nattamai S. P. Bhuvanesh ◽  
Karuppannan Natarajan
Keyword(s):  
Cytotoxic Activity ◽  
Protein Interaction ◽  
Dna Protein Interaction

DNA/protein interaction and cytotoxic activity of imidazole terpyridine derived Cu(ii)/Zn(ii) metal complexes

2014 ◽  
Vol 43 (34) ◽  
pp. 13018 ◽  
Author(s):  
V. M. Manikandamathavan ◽  
T. Weyhermüller ◽  
R. P. Parameswari ◽  
M. Sathishkumar ◽  
V. Subramanian ◽  
...  
Keyword(s):  
Metal Complexes ◽  
Cytotoxic Activity ◽  
Protein Interaction ◽  
Dna Protein Interaction

DNA/protein interaction, cytotoxic activity and magnetic properties of amino-alcohol Schiff base derived Cu(ii)/Ni(ii) metal complexes: influence of the nuclearity and metal ions

RSC Advances ◽  
2015 ◽  
Vol 5 (47) ◽  
pp. 37085-37095 ◽  
Author(s):  
Meiju Niu ◽  
Zhen Li ◽  
Huanhuan Li ◽  
Xiao Li ◽  
Jianmin Dou ◽  
...  
Keyword(s):  
Magnetic Properties ◽  
Schiff Base ◽  
Metal Ions ◽  
Metal Complexes ◽  
Cytotoxic Activity ◽  
Protein Interaction ◽  
Amino Alcohol ◽  
Polynuclear Complexes ◽  
Schiff Base Ligands ◽  
Dna Protein Interaction

The reactions of amino-alcohol derived Schiff-base ligands with Cu(ii) and Ni(ii) salts have afforded four novel polynuclear complexes, which exhibited interesting magnetic and cytotoxic properties.

Distinct supramolecular assemblies of Fe(iii) and Ni(ii) complexes constructed from the o-vanillin salicylhydrazone ligand: syntheses, crystal structures, DNA/protein interaction, and antioxidant and cytotoxic activity

2019 ◽  
Vol 43 (21) ◽  
pp. 8024-8043 ◽  
Author(s):  
Yueqin Li ◽  
Yun Li ◽  
Zhiwei Yang ◽  
Fantao Meng ◽  
Nana Wang ◽  
...  
Keyword(s):  
Dna Binding ◽  
Coordination Polymer ◽  
Cytotoxic Activity ◽  
Crystal Structures ◽  
Protein Interaction ◽  
Radical Scavenging ◽  
Dna Binding Protein ◽  
Anticancer Properties ◽  
Dna Protein Interaction

A novel aroylhydrazone ligand-bridged Ni(ii) coordination polymer was reported and its DNA binding, protein interaction, radical scavenging and in vitro anticancer properties were evaluated.

Weakening of DNA-protein interaction in cultured human fibroblasts induced by chemical mutagens

1987 ◽  
Vol 104 (6) ◽  
pp. 1730-1732
Author(s):  
A. I. Gorin ◽  
N. S. Bogomolova ◽  
A. V. Ermakov ◽  
M. I. Freidin ◽  
V. A. Chernov ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Human Fibroblasts ◽  
Chemical Mutagens ◽  
Cultured Human Fibroblasts ◽  
Dna Protein Interaction

Physical manipulation of single-molecule DNA using microbead and its application to analysis of DNA–protein interaction

2009 ◽  
Vol 321 (7) ◽  
pp. 655-658
Author(s):  
Hirofumi Kurita ◽  
Hachiro Yasuda ◽  
Kazunori Takashima ◽  
Shinji Katsura ◽  
Akira Mizuno
Keyword(s):  
Single Molecule ◽  
Protein Interaction ◽  
Dna Protein Interaction ◽  
Physical Manipulation

scholarly journals A model of nonlinear DNA-protein interaction system with Cornell potential and its stability

2017 ◽  
Vol 1 (1) ◽  
pp. 62
Author(s):  
Edy Syahroni ◽  
A Suparmi ◽  
C Cari ◽  
Fuad Anwar
Keyword(s):  
Protein Interaction ◽  
Interaction Model ◽  
The State ◽  
Hamiltonian Equation ◽  
Single Chain ◽  
Cornell Potential ◽  
Interaction System ◽  
Dna Protein Interaction ◽  
Dna Chain ◽  
The Stability

<p class="Abstract">The purpose of this study was to determine the model of a interaction system between the DNA with protein. The interaction system consisted of a molecule of protein bound with a single chain of DNA. The interaction between DNA chain, especially adenine and thymine, and DNA-protein bound to glutamine and adenine. The forms of these bonds are adapted from the hydrogen bonds. The Cornell potential was used to describe both of the interactions. We proposed the Hamiltonian equation to describe the general model of interaction. Interaction system is divided into three parts. The interaction model is satisfied when a protein molecule triggers pulses on a DNA chain. An initial shift in position of protein xm should trigger the shift in position of DNA ym, or alter the state. However, an initial shift in DNA, yn, should not alter the state of a rest protein (i.e. xm = 0), otherwise, the protein would not steadily bind. We also investigated the stability of the model from the DNA-protein interaction with Lyapunov function. The stability of system can be determined when we obtained the equilibrium point.</p>

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