Comparison of genotype frequencies of SNPs in Wnt pathway genes between ER + breast cancers versus controls.

<p>BC. Breast Cancer; ER+. Estrogen Receptor positive; OR 95% CI. Odds Ratio and 95% Confidence Interval.</p>*<p>P<0.05 was considered significant and are depicted in bold.</p

Description of SNPs present in Wnt pathway genes that were analyzed.

*<p>Source – dbSNP, National Center for Biotechnology Information.</p

Comparison of genotype frequencies of SNPs in Wnt pathway genes between ER- breast cancers versus controls.

<p>BC. Breast Cancer; ER-. Estrogen Receptor negative; OR 95% CI. Odds Ratio and 95% Confidence Interval.</p>*<p>P<0.05 was considered significant and are depicted in bold.</p

Genotype frequencies of Wnt pathway gene polymorphism in breast cancers and Controls.

<p>BC. Breast Cancer; OR 95% CI. Odds Ratio and 95% Confidence Interval.</p>*<p>P<0.05 was considered significant and are depicted in bold.</p

Comparison of genotype frequencies of SNPs in Wnt pathway genes between early on-set Breast cancers (patients age ≤43 years) versus controls.

<p>BC. Breast Cancer; OR 95% CI. Odds Ratio and 95% Confidence Interval.</p>*<p>P<0.05 was considered significant and are depicted in bold.</p

Relative PARP1 mRNA expression in different grades of breast cancer.

<p>(Ct values are plotted ±SEM).</p

The crystal structure domain of human recombinant poly (ADP-ribose) Polymerase (PARP).

<p>(a) Crystal structure domain of the human PARP1 protein structural changes in the regions due to mutation. (b) Wild type structure of PARP1 domain Chain ‘A’ have a point mutation αHelix-5 VAL762 (blue) in a stick representation of the helix region. (c) Mutant type structure of PARP1 domain Chain ‘A’ have a mutation αHelix-5 ALA762 (red) a stick representation of the helix region. (d) Wild and Mutant type structures superimposed of PARP1 domain Chain ‘A’ have wild type residue αHelix-5 VAL762 (red) and mutant residue αHelix-5 ALA762 (blue). Figures (a-d) were made by using CCP4/QTMG.</p

The MD simulation showing truncated octahedron boundary explicit water solvated.

<p>The molecular dynamic simulation used in system calculation are, (a) water box surround the entire protein in middle. The visual inspection also allow to identify the side chain of the histidine residue involved in the hydrogen bonding with surrounding molecules and in that case the δ nitrogen of the histidine (HSB;1-4) was protonated residue.</p

The dbSNP were used to recognize the protein encoded by PARP1 gene (PDB ID: 1uk0) and identified a single mutation residue position.

<p>The Z-score, which indicates overall model quality was -9.51 in (black color). The Z-score plot from the different sources (X-ray, and NMR) was distinguished by various colors (X-ray in pale blue and NMR in dark blue color).</p

Predicted effect of the mutations affecting hBD-3 on protein structure stability.

<p>^apredicted protein thermal stability change (∆∆G in Kcal/mol) of mutation from CUPSAT program.</p><p>^brelative solvent accessibility of the wild type residue computed from PoP MuSiC program.</p><p>^cpridected protein stability change (∆∆G in Kcal/mol) of mutation from PoP MuSiC program.</p><p>Predicted effect of the mutations affecting hBD-3 on protein structure stability.</p