39 articles for thisTarget
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Article Title
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Cell Penetrant Inhibitors of the KDM4 and KDM5 Families of Histone Lysine Demethylases. 1. 3-Amino-4-pyridine Carboxylate Derivatives.
Glaxosmithkline
8-Substituted Pyrido[3,4-d]pyrimidin-4(3H)-one Derivatives As Potent, Cell Permeable, KDM4 (JMJD2) and KDM5 (JARID1) Histone Lysine Demethylase Inhibitors.
The Institute of Cancer Research
Cell Penetrant Inhibitors of the KDM4 and KDM5 Families of Histone Lysine Demethylases. 2. Pyrido[3,4-d]pyrimidin-4(3H)-one Derivatives.
Glaxosmithkline
Novel 5-carboxy-8-HQ based histone demethylase JMJD2A inhibitors: introduction of an additional carboxyl group at the C-2 position of quinoline.
China Pharmaceutical University
KDM4B as a target for prostate cancer: structural analysis and selective inhibition by a novel inhibitor.
National Tsing Hua University
Identification of the KDM2/7 histone lysine demethylase subfamily inhibitor and its antiproliferative activity.
Kyoto Prefectural University of Medicine
Quantitative analysis of histone demethylase probes using fluorescence polarization.
University of Colorado
A small molecule inhibitor of fungal histone acetyltransferase Rtt109.
University of Massachusetts Medical School
Design, synthesis, enzyme-inhibitory activity, and effect on human cancer cells of a novel series of jumonji domain-containing protein 2 histone demethylase inhibitors.
Nagoya City University
Selective inhibitors of the JMJD2 histone demethylases: combined nondenaturing mass spectrometric screening and crystallographic approaches.
University of Oxford
Phenyl-quinoline-xxo-butyric Acid Inhibitors of Histone Lysine Demethylase for the Treatment of Cancer.
Arrival Discovery
Focused Screening Identifies Different Sensitivities of Human TET Oxygenases to the Oncometabolite 2-Hydroxyglutarate.
University of Oxford
Inhibition of AlkB Nucleic Acid Demethylases: Promising New Epigenetic Targets.
University College London
Structure-Based Design of Selective Fat Mass and Obesity Associated Protein (FTO) Inhibitors.
University of Oxford
Recent Advances with KDM4 Inhibitors and Potential Applications.
St. Jude Children'S Research Hospital
Drug discovery of histone lysine demethylases (KDMs) inhibitors (progress from 2018 to present).
Hangzhou Normal University
Design, synthesis and biological evaluation of a novel spiro oxazolidinedione as potent p300/CBP HAT inhibitor for the treatment of ovarian cancer.
China Pharmaceutical University
Discovery of a potent and selective inhibitor of histone lysine demethylase KDM4D.
Nankai University
Discovery of pyrazole derivatives as cellular active inhibitors of histone lysine specific demethylase 5B (KDM5B/JARID1B).
Zhengzhou University
Identification of novel lysine demethylase 5-selective inhibitors by inhibitor-based fragment merging strategy.
Kyoto Prefectural University of Medicine
Identification of ortho-hydroxy anilide as a novel scaffold for lysine demethylase 5 inhibitors.
Kyoto Prefectural University of Medicine
New Modalities, Technologies, and Partnerships in Probe and Lead Generation: Enabling a Mode-of-Action Centric Paradigm.
Astrazeneca
C8-substituted pyrido[3,4-d]pyrimidin-4(3H)-ones: Studies towards the identification of potent, cell penetrant Jumonji C domain containing histone lysine demethylase 4 subfamily (KDM4) inhibitors, compound profiling in cell-based target engagement assays.
Institute of Cancer Research
Optimisation of a triazolopyridine based histone demethylase inhibitor yields a potent and selective KDM2A (FBXL11) inhibitor.
University of Oxford
Structure-Based Engineering of Irreversible Inhibitors against Histone Lysine Demethylase KDM5A.
The University of Texas M.D. Anderson Cancer Center
Targeting lysine specific demethylase 4A (KDM4A) tandem TUDOR domain - A fragment based approach.
Abbvie
Design of KDM4 Inhibitors with Antiproliferative Effects in Cancer Models.
Celgene Quanticel Research
Structure-activity studies of a macrocyclic peptide inhibitor of histone lysine demethylase 4A.
The University of Tokyo
Roles of phosphate recognition in inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IPK1) substrate binding and activation.
Mcgill University