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Molecular docking, molecular dynamics simulation, and validation (A) Vina score of molecular docking and BPA binding. The smaller the value, the higher the affinity for binding. (B) Molecular docking diagrams of interactions between BPA and <t>CDKN1B</t> proteins. (C) Molecular dynamics simulation of the BPA-CDKN1B complex. (D) Lysate-based CETSA analyzed the thermal stabilization of CDKN1B with BPA in SKOV3 cell lysates. Two-way ANOVA with post hoc analysis. The experimental data are presented as the mean ± standard error of mean (SEM). ( n = 3, n represents the number of biological replicates) ∗ p < 0.05. RMSD, root-mean-square deviation; Rg, radius of gyration; SASA, solvent accessible surface area; RMSF, Root-mean-square fluctuation.
Cdkn1b Primers Forward Cttcttcgtcagcctcccttcc Reverse Gagtcgcagagccgtgagc, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Sangon Biotech forward reverse primers
Molecular docking, molecular dynamics simulation, and validation (A) Vina score of molecular docking and BPA binding. The smaller the value, the higher the affinity for binding. (B) Molecular docking diagrams of interactions between BPA and <t>CDKN1B</t> proteins. (C) Molecular dynamics simulation of the BPA-CDKN1B complex. (D) Lysate-based CETSA analyzed the thermal stabilization of CDKN1B with BPA in SKOV3 cell lysates. Two-way ANOVA with post hoc analysis. The experimental data are presented as the mean ± standard error of mean (SEM). ( n = 3, n represents the number of biological replicates) ∗ p < 0.05. RMSD, root-mean-square deviation; Rg, radius of gyration; SASA, solvent accessible surface area; RMSF, Root-mean-square fluctuation.
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Molecular docking, molecular dynamics simulation, and validation (A) Vina score of molecular docking and BPA binding. The smaller the value, the higher the affinity for binding. (B) Molecular docking diagrams of interactions between BPA and CDKN1B proteins. (C) Molecular dynamics simulation of the BPA-CDKN1B complex. (D) Lysate-based CETSA analyzed the thermal stabilization of CDKN1B with BPA in SKOV3 cell lysates. Two-way ANOVA with post hoc analysis. The experimental data are presented as the mean ± standard error of mean (SEM). ( n = 3, n represents the number of biological replicates) ∗ p < 0.05. RMSD, root-mean-square deviation; Rg, radius of gyration; SASA, solvent accessible surface area; RMSF, Root-mean-square fluctuation.

Journal: iScience

Article Title: Integrated study reveals molecular mechanisms by which bisphenol A promotes ovarian cancer

doi: 10.1016/j.isci.2026.115768

Figure Lengend Snippet: Molecular docking, molecular dynamics simulation, and validation (A) Vina score of molecular docking and BPA binding. The smaller the value, the higher the affinity for binding. (B) Molecular docking diagrams of interactions between BPA and CDKN1B proteins. (C) Molecular dynamics simulation of the BPA-CDKN1B complex. (D) Lysate-based CETSA analyzed the thermal stabilization of CDKN1B with BPA in SKOV3 cell lysates. Two-way ANOVA with post hoc analysis. The experimental data are presented as the mean ± standard error of mean (SEM). ( n = 3, n represents the number of biological replicates) ∗ p < 0.05. RMSD, root-mean-square deviation; Rg, radius of gyration; SASA, solvent accessible surface area; RMSF, Root-mean-square fluctuation.

Article Snippet: CDKN1B primers Forward:CTTCTTCGTCAGCCTCCCTTCC Reverse:GAGTCGCAGAGCCGTGAGC , Sangon Biotech , N/A.

Techniques: Biomarker Discovery, Binding Assay, Solvent