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her2 kinase inhibitory activities  (BPS Bioscience)


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    BPS Bioscience her2 kinase inhibitory activities
    Summary of in vitro evaluation of compounds 10, 13, 21 , and 24 .
    Her2 Kinase Inhibitory Activities, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 95/100, based on 69 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/her2 kinase inhibitory activities/product/BPS Bioscience
    Average 95 stars, based on 69 article reviews
    her2 kinase inhibitory activities - by Bioz Stars, 2026-03
    95/100 stars

    Images

    1) Product Images from "Synthesis, Antitumor Activities, and Apoptosis-Inducing Activities of Schiff’s Bases Incorporating Imidazolidine-2,4-dione Scaffold: Molecular Docking Studies and Enzymatic Inhibition Activities"

    Article Title: Synthesis, Antitumor Activities, and Apoptosis-Inducing Activities of Schiff’s Bases Incorporating Imidazolidine-2,4-dione Scaffold: Molecular Docking Studies and Enzymatic Inhibition Activities

    Journal: Pharmaceuticals

    doi: 10.3390/ph18040496

    Summary of in vitro evaluation of compounds 10, 13, 21 , and 24 .
    Figure Legend Snippet: Summary of in vitro evaluation of compounds 10, 13, 21 , and 24 .

    Techniques Used: In Vitro, Inhibition

    Overlay of the redocked (green) and co-crystallized ligand 03Q (yellow) within the HER2 binding site ( A ) and the redocked ligand (green) and co-crystallized ligand Gefitinib (yellow) within the EGFR binding site ( B ). The close alignment of the redocked and co-crystallized ligands validates the docking protocol and confirms the reliability of the binding pose predictions.
    Figure Legend Snippet: Overlay of the redocked (green) and co-crystallized ligand 03Q (yellow) within the HER2 binding site ( A ) and the redocked ligand (green) and co-crystallized ligand Gefitinib (yellow) within the EGFR binding site ( B ). The close alignment of the redocked and co-crystallized ligands validates the docking protocol and confirms the reliability of the binding pose predictions.

    Techniques Used: Binding Assay

    Three-dimensional representation of the HER2 (PDB code: 3PP0) binding site showing compound 24 (depicted in green) in juxtaposition to the co-crystalline ligand (03Q) colored in yellow. The spatial orientations provide insights into their respective interactions and alignments within the active site.
    Figure Legend Snippet: Three-dimensional representation of the HER2 (PDB code: 3PP0) binding site showing compound 24 (depicted in green) in juxtaposition to the co-crystalline ligand (03Q) colored in yellow. The spatial orientations provide insights into their respective interactions and alignments within the active site.

    Techniques Used: Binding Assay

    Molecular docking interactions of compound 24 with HER2 kinase domain (PDB code: 3PP0) and EGFR kinase domain (PDB code: 2ITY). The table delineates the specific interactions between the ligand atoms and both HER2 and EGFR residues separately, including the type of interaction, distance, and estimated binding energy.
    Figure Legend Snippet: Molecular docking interactions of compound 24 with HER2 kinase domain (PDB code: 3PP0) and EGFR kinase domain (PDB code: 2ITY). The table delineates the specific interactions between the ligand atoms and both HER2 and EGFR residues separately, including the type of interaction, distance, and estimated binding energy.

    Techniques Used: Binding Assay

    The Root Mean Square Deviation (RMSD) analysis of compound 24 and the co-crystallized ligand ( A ) Pro-03Q with HER2 and ( B ) Gefitinib with EGFR over 100 ns molecular dynamics simulations. The RMSD plot reflects the structural stability and conformational changes in the protein–ligand complexes, where compound 24 exhibits a stable binding mode comparable to the reference co-crystallized ligands in both the HER2 and EGFR systems.
    Figure Legend Snippet: The Root Mean Square Deviation (RMSD) analysis of compound 24 and the co-crystallized ligand ( A ) Pro-03Q with HER2 and ( B ) Gefitinib with EGFR over 100 ns molecular dynamics simulations. The RMSD plot reflects the structural stability and conformational changes in the protein–ligand complexes, where compound 24 exhibits a stable binding mode comparable to the reference co-crystallized ligands in both the HER2 and EGFR systems.

    Techniques Used: Binding Assay

    Root Mean Square Fluctuation (RMSF) analysis of backbone Cα atoms for compound 24 and co-crystallized ligands with ( A ) HER2 and ( B ) EGFR. The RMSF profiles reveal the fluctuation patterns across key structural regions, including the glycine-rich loop, αC helix, and activation loop. Compound 24 shows distinct fluctuation patterns compared with the co-crystallized ligands, indicating differential stabilization effects on the kinase domains.
    Figure Legend Snippet: Root Mean Square Fluctuation (RMSF) analysis of backbone Cα atoms for compound 24 and co-crystallized ligands with ( A ) HER2 and ( B ) EGFR. The RMSF profiles reveal the fluctuation patterns across key structural regions, including the glycine-rich loop, αC helix, and activation loop. Compound 24 shows distinct fluctuation patterns compared with the co-crystallized ligands, indicating differential stabilization effects on the kinase domains.

    Techniques Used: Activation Assay

    Radius of gyration (Rg) analysis for compound 24 and the co-crystallized ligand in ( A ) HER2 and ( B ) EGFR. The Rg values reflect the compactness and structural stability of the protein–ligand complexes over the 100 ns molecular dynamics simulation. A slight fluctuation in Rg indicates conformational adjustments upon ligand binding, where compound 24 exhibits a more stable and compact structure compared with the co-crystallized ligand in both HER2 and EGFR.
    Figure Legend Snippet: Radius of gyration (Rg) analysis for compound 24 and the co-crystallized ligand in ( A ) HER2 and ( B ) EGFR. The Rg values reflect the compactness and structural stability of the protein–ligand complexes over the 100 ns molecular dynamics simulation. A slight fluctuation in Rg indicates conformational adjustments upon ligand binding, where compound 24 exhibits a more stable and compact structure compared with the co-crystallized ligand in both HER2 and EGFR.

    Techniques Used: Ligand Binding Assay

    Solvent-Accessible Surface Area (SASA) analysis for compound 24 and co-crystallized ligands with ( A ) HER2 and ( B ) EGFR throughout 100 ns MD simulations. The plot shows the dynamic behavior of the protein–ligand complexes, where compound 24 exhibits reduced the SASA compared with the co-crystallized ligands, indicating tighter binding and potential structural stability in both targets.
    Figure Legend Snippet: Solvent-Accessible Surface Area (SASA) analysis for compound 24 and co-crystallized ligands with ( A ) HER2 and ( B ) EGFR throughout 100 ns MD simulations. The plot shows the dynamic behavior of the protein–ligand complexes, where compound 24 exhibits reduced the SASA compared with the co-crystallized ligands, indicating tighter binding and potential structural stability in both targets.

    Techniques Used: Solvent, Binding Assay



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    her2 kinase inhibitory activities  (BPS Bioscience)
    95
    BPS Bioscience her2 kinase inhibitory activities
    Summary of in vitro evaluation of compounds 10, 13, 21 , and 24 .
    Her2 Kinase Inhibitory Activities, 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
    https://www.bioz.com/result/her2 kinase inhibitory activities/product/BPS Bioscience
    Average 95 stars, based on 1 article reviews
    her2 kinase inhibitory activities - by Bioz Stars, 2026-03
    95/100 stars
    		  Buy from Supplier

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    Summary of in vitro evaluation of compounds 10, 13, 21 , and 24 .

    Journal: Pharmaceuticals

    Article Title: Synthesis, Antitumor Activities, and Apoptosis-Inducing Activities of Schiff’s Bases Incorporating Imidazolidine-2,4-dione Scaffold: Molecular Docking Studies and Enzymatic Inhibition Activities

    doi: 10.3390/ph18040496

    Figure Lengend Snippet: Summary of in vitro evaluation of compounds 10, 13, 21 , and 24 .

    Article Snippet: EGFR and HER2 kinase inhibitory activities were determined based on the manufacturer’s guidelines (EGFR Kinase Assay Kit Catalog no. 40321 and HER2 Kinase Assay Kit Catalog no. 40721, BPS Bioscience, San Diego, CA).

    Techniques: In Vitro, Inhibition

    Overlay of the redocked (green) and co-crystallized ligand 03Q (yellow) within the HER2 binding site ( A ) and the redocked ligand (green) and co-crystallized ligand Gefitinib (yellow) within the EGFR binding site ( B ). The close alignment of the redocked and co-crystallized ligands validates the docking protocol and confirms the reliability of the binding pose predictions.

    Journal: Pharmaceuticals

    Article Title: Synthesis, Antitumor Activities, and Apoptosis-Inducing Activities of Schiff’s Bases Incorporating Imidazolidine-2,4-dione Scaffold: Molecular Docking Studies and Enzymatic Inhibition Activities

    doi: 10.3390/ph18040496

    Figure Lengend Snippet: Overlay of the redocked (green) and co-crystallized ligand 03Q (yellow) within the HER2 binding site ( A ) and the redocked ligand (green) and co-crystallized ligand Gefitinib (yellow) within the EGFR binding site ( B ). The close alignment of the redocked and co-crystallized ligands validates the docking protocol and confirms the reliability of the binding pose predictions.

    Article Snippet: EGFR and HER2 kinase inhibitory activities were determined based on the manufacturer’s guidelines (EGFR Kinase Assay Kit Catalog no. 40321 and HER2 Kinase Assay Kit Catalog no. 40721, BPS Bioscience, San Diego, CA).

    Techniques: Binding Assay

    Three-dimensional representation of the HER2 (PDB code: 3PP0) binding site showing compound 24 (depicted in green) in juxtaposition to the co-crystalline ligand (03Q) colored in yellow. The spatial orientations provide insights into their respective interactions and alignments within the active site.

    Journal: Pharmaceuticals

    Article Title: Synthesis, Antitumor Activities, and Apoptosis-Inducing Activities of Schiff’s Bases Incorporating Imidazolidine-2,4-dione Scaffold: Molecular Docking Studies and Enzymatic Inhibition Activities

    doi: 10.3390/ph18040496

    Figure Lengend Snippet: Three-dimensional representation of the HER2 (PDB code: 3PP0) binding site showing compound 24 (depicted in green) in juxtaposition to the co-crystalline ligand (03Q) colored in yellow. The spatial orientations provide insights into their respective interactions and alignments within the active site.

    Article Snippet: EGFR and HER2 kinase inhibitory activities were determined based on the manufacturer’s guidelines (EGFR Kinase Assay Kit Catalog no. 40321 and HER2 Kinase Assay Kit Catalog no. 40721, BPS Bioscience, San Diego, CA).

    Techniques: Binding Assay

    Molecular docking interactions of compound 24 with HER2 kinase domain (PDB code: 3PP0) and EGFR kinase domain (PDB code: 2ITY). The table delineates the specific interactions between the ligand atoms and both HER2 and EGFR residues separately, including the type of interaction, distance, and estimated binding energy.

    Journal: Pharmaceuticals

    Article Title: Synthesis, Antitumor Activities, and Apoptosis-Inducing Activities of Schiff’s Bases Incorporating Imidazolidine-2,4-dione Scaffold: Molecular Docking Studies and Enzymatic Inhibition Activities

    doi: 10.3390/ph18040496

    Figure Lengend Snippet: Molecular docking interactions of compound 24 with HER2 kinase domain (PDB code: 3PP0) and EGFR kinase domain (PDB code: 2ITY). The table delineates the specific interactions between the ligand atoms and both HER2 and EGFR residues separately, including the type of interaction, distance, and estimated binding energy.

    Article Snippet: EGFR and HER2 kinase inhibitory activities were determined based on the manufacturer’s guidelines (EGFR Kinase Assay Kit Catalog no. 40321 and HER2 Kinase Assay Kit Catalog no. 40721, BPS Bioscience, San Diego, CA).

    Techniques: Binding Assay

    The Root Mean Square Deviation (RMSD) analysis of compound 24 and the co-crystallized ligand ( A ) Pro-03Q with HER2 and ( B ) Gefitinib with EGFR over 100 ns molecular dynamics simulations. The RMSD plot reflects the structural stability and conformational changes in the protein–ligand complexes, where compound 24 exhibits a stable binding mode comparable to the reference co-crystallized ligands in both the HER2 and EGFR systems.

    Journal: Pharmaceuticals

    Article Title: Synthesis, Antitumor Activities, and Apoptosis-Inducing Activities of Schiff’s Bases Incorporating Imidazolidine-2,4-dione Scaffold: Molecular Docking Studies and Enzymatic Inhibition Activities

    doi: 10.3390/ph18040496

    Figure Lengend Snippet: The Root Mean Square Deviation (RMSD) analysis of compound 24 and the co-crystallized ligand ( A ) Pro-03Q with HER2 and ( B ) Gefitinib with EGFR over 100 ns molecular dynamics simulations. The RMSD plot reflects the structural stability and conformational changes in the protein–ligand complexes, where compound 24 exhibits a stable binding mode comparable to the reference co-crystallized ligands in both the HER2 and EGFR systems.

    Article Snippet: EGFR and HER2 kinase inhibitory activities were determined based on the manufacturer’s guidelines (EGFR Kinase Assay Kit Catalog no. 40321 and HER2 Kinase Assay Kit Catalog no. 40721, BPS Bioscience, San Diego, CA).

    Techniques: Binding Assay

    Root Mean Square Fluctuation (RMSF) analysis of backbone Cα atoms for compound 24 and co-crystallized ligands with ( A ) HER2 and ( B ) EGFR. The RMSF profiles reveal the fluctuation patterns across key structural regions, including the glycine-rich loop, αC helix, and activation loop. Compound 24 shows distinct fluctuation patterns compared with the co-crystallized ligands, indicating differential stabilization effects on the kinase domains.

    Journal: Pharmaceuticals

    Article Title: Synthesis, Antitumor Activities, and Apoptosis-Inducing Activities of Schiff’s Bases Incorporating Imidazolidine-2,4-dione Scaffold: Molecular Docking Studies and Enzymatic Inhibition Activities

    doi: 10.3390/ph18040496

    Figure Lengend Snippet: Root Mean Square Fluctuation (RMSF) analysis of backbone Cα atoms for compound 24 and co-crystallized ligands with ( A ) HER2 and ( B ) EGFR. The RMSF profiles reveal the fluctuation patterns across key structural regions, including the glycine-rich loop, αC helix, and activation loop. Compound 24 shows distinct fluctuation patterns compared with the co-crystallized ligands, indicating differential stabilization effects on the kinase domains.

    Article Snippet: EGFR and HER2 kinase inhibitory activities were determined based on the manufacturer’s guidelines (EGFR Kinase Assay Kit Catalog no. 40321 and HER2 Kinase Assay Kit Catalog no. 40721, BPS Bioscience, San Diego, CA).

    Techniques: Activation Assay

    Radius of gyration (Rg) analysis for compound 24 and the co-crystallized ligand in ( A ) HER2 and ( B ) EGFR. The Rg values reflect the compactness and structural stability of the protein–ligand complexes over the 100 ns molecular dynamics simulation. A slight fluctuation in Rg indicates conformational adjustments upon ligand binding, where compound 24 exhibits a more stable and compact structure compared with the co-crystallized ligand in both HER2 and EGFR.

    Journal: Pharmaceuticals

    Article Title: Synthesis, Antitumor Activities, and Apoptosis-Inducing Activities of Schiff’s Bases Incorporating Imidazolidine-2,4-dione Scaffold: Molecular Docking Studies and Enzymatic Inhibition Activities

    doi: 10.3390/ph18040496

    Figure Lengend Snippet: Radius of gyration (Rg) analysis for compound 24 and the co-crystallized ligand in ( A ) HER2 and ( B ) EGFR. The Rg values reflect the compactness and structural stability of the protein–ligand complexes over the 100 ns molecular dynamics simulation. A slight fluctuation in Rg indicates conformational adjustments upon ligand binding, where compound 24 exhibits a more stable and compact structure compared with the co-crystallized ligand in both HER2 and EGFR.

    Article Snippet: EGFR and HER2 kinase inhibitory activities were determined based on the manufacturer’s guidelines (EGFR Kinase Assay Kit Catalog no. 40321 and HER2 Kinase Assay Kit Catalog no. 40721, BPS Bioscience, San Diego, CA).

    Techniques: Ligand Binding Assay

    Solvent-Accessible Surface Area (SASA) analysis for compound 24 and co-crystallized ligands with ( A ) HER2 and ( B ) EGFR throughout 100 ns MD simulations. The plot shows the dynamic behavior of the protein–ligand complexes, where compound 24 exhibits reduced the SASA compared with the co-crystallized ligands, indicating tighter binding and potential structural stability in both targets.

    Journal: Pharmaceuticals

    Article Title: Synthesis, Antitumor Activities, and Apoptosis-Inducing Activities of Schiff’s Bases Incorporating Imidazolidine-2,4-dione Scaffold: Molecular Docking Studies and Enzymatic Inhibition Activities

    doi: 10.3390/ph18040496

    Figure Lengend Snippet: Solvent-Accessible Surface Area (SASA) analysis for compound 24 and co-crystallized ligands with ( A ) HER2 and ( B ) EGFR throughout 100 ns MD simulations. The plot shows the dynamic behavior of the protein–ligand complexes, where compound 24 exhibits reduced the SASA compared with the co-crystallized ligands, indicating tighter binding and potential structural stability in both targets.

    Article Snippet: EGFR and HER2 kinase inhibitory activities were determined based on the manufacturer’s guidelines (EGFR Kinase Assay Kit Catalog no. 40321 and HER2 Kinase Assay Kit Catalog no. 40721, BPS Bioscience, San Diego, CA).

    Techniques: Solvent, Binding Assay