pyrazolone and benzimidazole

pyrazolone has been researched along with benzimidazole* in 2 studies

Other Studies

2 other study(ies) available for pyrazolone and benzimidazole

Article	Year
Identification of a Novel Benzimidazole Pyrazolone Scaffold That Inhibits KDM4 Lysine Demethylases and Reduces Proliferation of Prostate Cancer Cells. SLAS discovery : advancing life sciences R & D, 2017, Volume: 22, Issue:7 Human lysine demethylase (KDM) enzymes (KDM1-7) constitute an emerging class of therapeutic targets, with activities that support growth and development of metastatic disease. By interacting with and co-activating the androgen receptor, the KDM4 subfamily (KDM4A-E) promotes aggressive phenotypes of prostate cancer (PCa). Knockdown of KDM4 expression or inhibition of KDM4 enzyme activity reduces the proliferation of PCa cell lines and highlights inhibition of lysine demethylation as a possible therapeutic method for PCa treatment. To address this possibility, we screened the ChemBioNet small molecule library for inhibitors of the human KDM4E isoform and identified several compounds with IC Topics: Benzimidazoles; Cell Line, Tumor; Cell Proliferation; Demethylation; Enzyme Inhibitors; Histone Demethylases; Histones; Humans; Hydroxyquinolines; Jumonji Domain-Containing Histone Demethylases; Lysine; Male; PC-3 Cells; Prostatic Neoplasms; Pyrazolones; Receptors, Androgen; Transcription, Genetic	2017
Non-peptide ligand binding to the formyl peptide receptor FPR2--A comparison to peptide ligand binding modes. Bioorganic & medicinal chemistry, 2015, Jul-15, Volume: 23, Issue:14 Ligands of the FPR2 receptor initiate many signaling pathways including activation of phospholipase C, protein kinase C, the mitogen-activated protein kinase, and phosphatidylinositol 3-kinase/protein kinase B pathway. The possible actions include also calcium flux, superoxide generation, as well as migration and proliferation of monocytes. FPR2 activation may induce a pro- and anti-inflammatory effect depending on the ligand type. It is also found that this receptor is involved in tumor growth. Most of currently known FPR2 ligands are agonists since they were designed based on N-formyl peptides, which are natural agonists of formyl receptors. Since the non-peptide drugs are indispensable for effective treatment strategies, we performed a docking study of such ligands employing a generated dual template homology model of the FPR2 receptor. The study revealed different binding modes of particular classes of these drugs. Based on the obtained docking poses we proposed a detailed location of three hydrophobic pockets in orthosteric binding site of FPR2. Our model emphasizes the importance of aromatic stacking, especially with regard to residues His102(3.29) and Phe257(6.51), for binding of FPR2 ligands. We also identified other residues important for non-peptide ligand binding in the binding site of FPR2. Topics: Benzimidazoles; Binding Sites; Hydrophobic and Hydrophilic Interactions; Ligands; Models, Molecular; Molecular Docking Simulation; Phenylurea Compounds; Protein Conformation; Pyrazolones; Pyridazines; Quinazolinones; Receptors, Formyl Peptide; Receptors, Lipoxin; Structure-Activity Relationship	2015

Article

Year

Identification of a Novel Benzimidazole Pyrazolone Scaffold That Inhibits KDM4 Lysine Demethylases and Reduces Proliferation of Prostate Cancer Cells.

SLAS discovery : advancing life sciences R & D, 2017, Volume: 22, Issue:7

Human lysine demethylase (KDM) enzymes (KDM1-7) constitute an emerging class of therapeutic targets, with activities that support growth and development of metastatic disease. By interacting with and co-activating the androgen receptor, the KDM4 subfamily (KDM4A-E) promotes aggressive phenotypes of prostate cancer (PCa). Knockdown of KDM4 expression or inhibition of KDM4 enzyme activity reduces the proliferation of PCa cell lines and highlights inhibition of lysine demethylation as a possible therapeutic method for PCa treatment. To address this possibility, we screened the ChemBioNet small molecule library for inhibitors of the human KDM4E isoform and identified several compounds with IC

Topics: Benzimidazoles; Cell Line, Tumor; Cell Proliferation; Demethylation; Enzyme Inhibitors; Histone Demethylases; Histones; Humans; Hydroxyquinolines; Jumonji Domain-Containing Histone Demethylases; Lysine; Male; PC-3 Cells; Prostatic Neoplasms; Pyrazolones; Receptors, Androgen; Transcription, Genetic

2017

Non-peptide ligand binding to the formyl peptide receptor FPR2--A comparison to peptide ligand binding modes.

Bioorganic & medicinal chemistry, 2015, Jul-15, Volume: 23, Issue:14

Ligands of the FPR2 receptor initiate many signaling pathways including activation of phospholipase C, protein kinase C, the mitogen-activated protein kinase, and phosphatidylinositol 3-kinase/protein kinase B pathway. The possible actions include also calcium flux, superoxide generation, as well as migration and proliferation of monocytes. FPR2 activation may induce a pro- and anti-inflammatory effect depending on the ligand type. It is also found that this receptor is involved in tumor growth. Most of currently known FPR2 ligands are agonists since they were designed based on N-formyl peptides, which are natural agonists of formyl receptors. Since the non-peptide drugs are indispensable for effective treatment strategies, we performed a docking study of such ligands employing a generated dual template homology model of the FPR2 receptor. The study revealed different binding modes of particular classes of these drugs. Based on the obtained docking poses we proposed a detailed location of three hydrophobic pockets in orthosteric binding site of FPR2. Our model emphasizes the importance of aromatic stacking, especially with regard to residues His102(3.29) and Phe257(6.51), for binding of FPR2 ligands. We also identified other residues important for non-peptide ligand binding in the binding site of FPR2.

Topics: Benzimidazoles; Binding Sites; Hydrophobic and Hydrophilic Interactions; Ligands; Models, Molecular; Molecular Docking Simulation; Phenylurea Compounds; Protein Conformation; Pyrazolones; Pyridazines; Quinazolinones; Receptors, Formyl Peptide; Receptors, Lipoxin; Structure-Activity Relationship

2015