74 articles for thisTarget
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Discovery and structure-activity analysis of 4-((5-nitropyrimidin-4-yl)amino)benzimidamide derivatives as novel protein arginine methyltransferase 1 (PRMT1) inhibitors.
Sichuan University
Exploration of cyanine compounds as selective inhibitors of protein arginine methyltransferases: synthesis and biological evaluation.
The University of Georgia
Discovery of a selective, substrate-competitive inhibitor of the lysine methyltransferase SETD8.
University of North Carolina At Chapel Hill
Diamidine compounds for selective inhibition of protein arginine methyltransferase 1.
The University of Georgia
Identification of Potent, Selective, Cell-Active Inhibitors of the Histone Lysine Methyltransferase EZH2.
TBA
Synthesis and evaluation of carbocyanine dyes as PRMT inhibitors and imaging agents.
Georgia State University
Targeting Arginine Methyltransferase PRMT5 for Cancer Therapy: Updated Progress and Novel Strategies.
Sun Yat-Sen University
Structure-Based Design and Characterization of the Highly Potent and Selective Covalent Inhibitors Targeting the Lysine Methyltransferases G9a/GLP.
Sun Yat-Sen University
Discovery of a New-Generation S-Adenosylmethionine-Noncompetitive Covalent Inhibitor Targeting the Lysine Methyltransferase Enhancer of Zeste Homologue 2.
Sun Yat-Sen University
Structural Modification and Pharmacological Evaluation of Substituted Quinoline-5,8-diones as Potent NSD2 Inhibitors.
Shanghai Jiao Tong University
Structure-Based Discovery of Potent CARM1 Inhibitors for Solid Tumor and Cancer Immunology Therapy.
Shanghai Institute of Materia Medica
Structure-Aided Design, Synthesis, and Biological Evaluation of Potent and Selective Non-Nucleoside Inhibitors Targeting Protein Arginine Methyltransferase 5.
Sun Yat-Sen University
Turning Nonselective Inhibitors of Type I Protein Arginine Methyltransferases into Potent and Selective Inhibitors of Protein Arginine Methyltransferase 4 through a Deconstruction-Reconstruction and Fragment-Growing Approach.
Institut De G£N£Tique Et De Biologie Mol£Culaire Et Cellulaire
Fascinating Transformation of SAM-Competitive Protein Methyltransferase Inhibitors from Nucleoside Analogues to Non-Nucleoside Analogues.
Csir-Indian Institute of Chemical Biology
Paradoxical Increase of Permeability and Lipophilicity with the Increasing Topological Polar Surface Area within a Series of PRMT5 Inhibitors.
Novartis Institutes For Biomedical Research
Design and evaluation of achiral, non-atropisomeric 4-(aminomethyl)phthalazin-1(2H)-one derivatives as novel PRMT5/MTA inhibitors.
Mirati Therapeutics
Fragment-Based Discovery of MRTX1719, a Synthetic Lethal Inhibitor of the PRMT5•MTA Complex for the Treatment of
Mirati Therapeutics
Discovery of a potent MLL1 and WDR5 protein-protein interaction inhibitor with in vivo antitumor activity.
China Pharmaceutical University
Discovery of a First-in-Class Inhibitor of the PRMT5-Substrate Adaptor Interaction.
The Broad Institute of Mit and Harvard
5-Aminonaphthalene derivatives as selective nonnucleoside nuclear receptor binding SET domain-protein 2 (NSD2) inhibitors for the treatment of multiple myeloma.
Chinese Academy of Sciences
The Discovery of Two Novel Classes of 5,5-Bicyclic Nucleoside-Derived PRMT5 Inhibitors for the Treatment of Cancer.
Merck
A Chemical Probe for the Methyl Transferase PRMT5 with a Novel Binding Mode.
Janssen Pharmaceutica
Identification of DOT1L inhibitors by structure-based virtual screening adapted from a nucleoside-focused library.
University of Michigan Medical School
Structure and Property Guided Design in the Identification of PRMT5 Tool Compound EPZ015666.
Epizyme
New small molecule inhibitors of histone methyl transferase DOT1L with a nitrile as a non-traditional replacement for heavy halogen atoms.
University College London
Discovery of a Potent and Selective Coactivator Associated Arginine Methyltransferase 1 (CARM1) Inhibitor by Virtual Screening.
University of Toronto
Histone methyl transferases: A class of epigenetic opportunities to counter uncontrolled cell proliferation.
Punjabi University
Design and Synthesis of Potent, Selective Inhibitors of Protein Arginine Methyltransferase 4 against Acute Myeloid Leukemia.
Chinese Academy of Sciences
Nucleoside protein arginine methyltransferase 5 (PRMT5) inhibitors.
Prelude Therapeutics
The development and characterization of a chemical probe targeting PRMT1 over PRMT5.
University of North Florida
Discovery of new potent protein arginine methyltransferase 5 (PRMT5) inhibitors by assembly of key pharmacophores from known inhibitors.
University of Jinan
Discovery of Potent and Selective Covalent Protein Arginine Methyltransferase 5 (PRMT5) Inhibitors.
Prelude Therapeutics
Protein Arginine Methyltransferase 5 (PRMT5) as an Anticancer Target and Its Inhibitor Discovery.
Sun Yat-Sen University
LLY-283, a Potent and Selective Inhibitor of Arginine Methyltransferase 5, PRMT5, with Antitumor Activity.
Lilly Research Laboratories
Development of Potent Type I Protein Arginine Methyltransferase (PRMT) Inhibitors of Leukemia Cell Proliferation.
Zhejiang Sci-Tech University
MULTI-TARGET INHIBITOR TARGETING HDAC AND NAD SYNTHESIS AND USE OF MULTI-TARGET INHIBITOR
Ocean University of China
TRICYCLIC PYRIMIDINES AS CYCLIN-DEPENDENT KINASE 7 (CDK7) INHIBITORS
Janssen Pharmaceutica
4,5,6-trisubstituted indazole derivatives, and preparation method and pharmaceutical use thereof
TBA
Imidazo[4,5-c]pyridine and pyrrolo[2,3-c]pyridine derivatives as SSAO inhibitors
Proximagen
Imidazo[4,5-c]pyridine and pyrrolo[2,3-c]pyridine derivatives as SSAO inhibitors
Proximagen
Kappa opioid receptor antagonists and products and methods related thereto
Blackthorn Therapeutics
Characterization and Noncovalent Inhibition of the Deubiquitinase and deISGylase Activity of SARS-CoV-2 Papain-Like Protease.
University of Georgia
Novel inhibitor of bacterial sphingomyelinase, SMY-540, developed based on three-dimensional structure analysis.
Tokushima Bunri University
Electrostatic Interactions as Mediators in the Allosteric Activation of Protein Kinase A RIa.
University of California San Diego
Laccaic acid A is a direct, DNA-competitive inhibitor of DNA methyltransferase 1.
University of Iowa