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Thermodynamic and conformational stability-time evolution for the simulated compounds at <t>VEGFR2</t> binding sites. ( A ) Cα-atom VEGFR2 RMSD (Å) trajectories; ( B ) Only compound RMSD (Å) tones; ( C ) Overlaid VEGFR2-compound frames at start, midway, and final simulation times. Ligands (sticks) and respective bounded VEGFR2 proteins (cartoon) are shown in green, yellow, and red colors as per initial, midway, and final extracted frames; ( D ) Bur-SASA (Å) of the simulated ligand-VEGFR2 complexes across time (ns); ( E ) PCA analysis highlighting protein atom projections within space phase along the two most dominant eigenvectors (eigenvector-1 and -2; Å 2 ). Initial and final ensembles conformations are flagged by Star and Dot-labels, respectively.
Vegfr2 Inhibition, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Thermodynamic and conformational stability-time evolution for the simulated compounds at <t>VEGFR2</t> binding sites. ( A ) Cα-atom VEGFR2 RMSD (Å) trajectories; ( B ) Only compound RMSD (Å) tones; ( C ) Overlaid VEGFR2-compound frames at start, midway, and final simulation times. Ligands (sticks) and respective bounded VEGFR2 proteins (cartoon) are shown in green, yellow, and red colors as per initial, midway, and final extracted frames; ( D ) Bur-SASA (Å) of the simulated ligand-VEGFR2 complexes across time (ns); ( E ) PCA analysis highlighting protein atom projections within space phase along the two most dominant eigenvectors (eigenvector-1 and -2; Å 2 ). Initial and final ensembles conformations are flagged by Star and Dot-labels, respectively.
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Thermodynamic and conformational stability-time evolution for the simulated compounds at <t>VEGFR2</t> binding sites. ( A ) Cα-atom VEGFR2 RMSD (Å) trajectories; ( B ) Only compound RMSD (Å) tones; ( C ) Overlaid VEGFR2-compound frames at start, midway, and final simulation times. Ligands (sticks) and respective bounded VEGFR2 proteins (cartoon) are shown in green, yellow, and red colors as per initial, midway, and final extracted frames; ( D ) Bur-SASA (Å) of the simulated ligand-VEGFR2 complexes across time (ns); ( E ) PCA analysis highlighting protein atom projections within space phase along the two most dominant eigenvectors (eigenvector-1 and -2; Å 2 ). Initial and final ensembles conformations are flagged by Star and Dot-labels, respectively.
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Thermodynamic and conformational stability-time evolution for the simulated compounds at <t>VEGFR2</t> binding sites. ( A ) Cα-atom VEGFR2 RMSD (Å) trajectories; ( B ) Only compound RMSD (Å) tones; ( C ) Overlaid VEGFR2-compound frames at start, midway, and final simulation times. Ligands (sticks) and respective bounded VEGFR2 proteins (cartoon) are shown in green, yellow, and red colors as per initial, midway, and final extracted frames; ( D ) Bur-SASA (Å) of the simulated ligand-VEGFR2 complexes across time (ns); ( E ) PCA analysis highlighting protein atom projections within space phase along the two most dominant eigenvectors (eigenvector-1 and -2; Å 2 ). Initial and final ensembles conformations are flagged by Star and Dot-labels, respectively.
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Thermodynamic and conformational stability-time evolution for the simulated compounds at <t>VEGFR2</t> binding sites. ( A ) Cα-atom VEGFR2 RMSD (Å) trajectories; ( B ) Only compound RMSD (Å) tones; ( C ) Overlaid VEGFR2-compound frames at start, midway, and final simulation times. Ligands (sticks) and respective bounded VEGFR2 proteins (cartoon) are shown in green, yellow, and red colors as per initial, midway, and final extracted frames; ( D ) Bur-SASA (Å) of the simulated ligand-VEGFR2 complexes across time (ns); ( E ) PCA analysis highlighting protein atom projections within space phase along the two most dominant eigenvectors (eigenvector-1 and -2; Å 2 ). Initial and final ensembles conformations are flagged by Star and Dot-labels, respectively.
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Thermodynamic and conformational stability-time evolution for the simulated compounds at <t>VEGFR2</t> binding sites. ( A ) Cα-atom VEGFR2 RMSD (Å) trajectories; ( B ) Only compound RMSD (Å) tones; ( C ) Overlaid VEGFR2-compound frames at start, midway, and final simulation times. Ligands (sticks) and respective bounded VEGFR2 proteins (cartoon) are shown in green, yellow, and red colors as per initial, midway, and final extracted frames; ( D ) Bur-SASA (Å) of the simulated ligand-VEGFR2 complexes across time (ns); ( E ) PCA analysis highlighting protein atom projections within space phase along the two most dominant eigenvectors (eigenvector-1 and -2; Å 2 ). Initial and final ensembles conformations are flagged by Star and Dot-labels, respectively.
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BPS Bioscience vegfr2 kinase inhibition assay vegfr2 kdr kinase assay kit
Thermodynamic and conformational stability-time evolution for the simulated compounds at <t>VEGFR2</t> binding sites. ( A ) Cα-atom VEGFR2 RMSD (Å) trajectories; ( B ) Only compound RMSD (Å) tones; ( C ) Overlaid VEGFR2-compound frames at start, midway, and final simulation times. Ligands (sticks) and respective bounded VEGFR2 proteins (cartoon) are shown in green, yellow, and red colors as per initial, midway, and final extracted frames; ( D ) Bur-SASA (Å) of the simulated ligand-VEGFR2 complexes across time (ns); ( E ) PCA analysis highlighting protein atom projections within space phase along the two most dominant eigenvectors (eigenvector-1 and -2; Å 2 ). Initial and final ensembles conformations are flagged by Star and Dot-labels, respectively.
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Thermodynamic and conformational stability-time evolution for the simulated compounds at VEGFR2 binding sites. ( A ) Cα-atom VEGFR2 RMSD (Å) trajectories; ( B ) Only compound RMSD (Å) tones; ( C ) Overlaid VEGFR2-compound frames at start, midway, and final simulation times. Ligands (sticks) and respective bounded VEGFR2 proteins (cartoon) are shown in green, yellow, and red colors as per initial, midway, and final extracted frames; ( D ) Bur-SASA (Å) of the simulated ligand-VEGFR2 complexes across time (ns); ( E ) PCA analysis highlighting protein atom projections within space phase along the two most dominant eigenvectors (eigenvector-1 and -2; Å 2 ). Initial and final ensembles conformations are flagged by Star and Dot-labels, respectively.

Journal: Scientific Reports

Article Title: Exploring market-approved azoles as potential breast cancer therapeutics targeting the VEGFR-2 biotarget

doi: 10.1038/s41598-025-29322-6

Figure Lengend Snippet: Thermodynamic and conformational stability-time evolution for the simulated compounds at VEGFR2 binding sites. ( A ) Cα-atom VEGFR2 RMSD (Å) trajectories; ( B ) Only compound RMSD (Å) tones; ( C ) Overlaid VEGFR2-compound frames at start, midway, and final simulation times. Ligands (sticks) and respective bounded VEGFR2 proteins (cartoon) are shown in green, yellow, and red colors as per initial, midway, and final extracted frames; ( D ) Bur-SASA (Å) of the simulated ligand-VEGFR2 complexes across time (ns); ( E ) PCA analysis highlighting protein atom projections within space phase along the two most dominant eigenvectors (eigenvector-1 and -2; Å 2 ). Initial and final ensembles conformations are flagged by Star and Dot-labels, respectively.

Article Snippet: They were tested for the VEGFR2 inhibition using VEGFR2 Kinase Inhibition Assay Kit Catalog # 40325 BPS Bioscience, San Diego, CA.

Techniques: Binding Assay

ΔRMSF analysis for bounded VEGFR2 proteins in relation to unliganded/apo one. Values are represented as per constituting amino acids (residue range; N -terminus Glu818 to C -terminus Asp1171).

Journal: Scientific Reports

Article Title: Exploring market-approved azoles as potential breast cancer therapeutics targeting the VEGFR-2 biotarget

doi: 10.1038/s41598-025-29322-6

Figure Lengend Snippet: ΔRMSF analysis for bounded VEGFR2 proteins in relation to unliganded/apo one. Values are represented as per constituting amino acids (residue range; N -terminus Glu818 to C -terminus Asp1171).

Article Snippet: They were tested for the VEGFR2 inhibition using VEGFR2 Kinase Inhibition Assay Kit Catalog # 40325 BPS Bioscience, San Diego, CA.

Techniques: Residue

Free-binding energy for the simulated compound-VEGFR2 complexes estimated by MM_PBSA calculation. ( A ) Total free-binding energies and their dissected energy term contributions; ( B ) Residue-wise energy term contributions of the key binding residues of the important structural motifs within the VEGFR2 binding site.

Journal: Scientific Reports

Article Title: Exploring market-approved azoles as potential breast cancer therapeutics targeting the VEGFR-2 biotarget

doi: 10.1038/s41598-025-29322-6

Figure Lengend Snippet: Free-binding energy for the simulated compound-VEGFR2 complexes estimated by MM_PBSA calculation. ( A ) Total free-binding energies and their dissected energy term contributions; ( B ) Residue-wise energy term contributions of the key binding residues of the important structural motifs within the VEGFR2 binding site.

Article Snippet: They were tested for the VEGFR2 inhibition using VEGFR2 Kinase Inhibition Assay Kit Catalog # 40325 BPS Bioscience, San Diego, CA.

Techniques: Binding Assay, Residue